*** ***
Job options:
ID = 2404111338133657461
JOBID =
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = on
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
CRYST1 101.284 53.455 71.840 90.00 90.00 90.00 P 21 21 2 1
ATOM 1 N HIS B 0 11.671 26.246 41.306 1.00 64.17 N
ATOM 2 CA HIS B 0 10.477 25.445 41.555 1.00 66.90 C
ATOM 3 C HIS B 0 10.847 24.103 42.175 1.00 58.95 C
ATOM 4 O HIS B 0 11.911 23.544 41.874 1.00 54.52 O
ATOM 5 CB HIS B 0 9.691 25.223 40.256 1.00 69.39 C
TER
HETATM 6 CA CA B 1 13.084 13.329 -11.208 1.00 26.86 Ca
ATOM 7 N MET B 1 9.963 23.590 43.032 1.00 56.56 N
ATOM 8 CA MET B 1 10.138 22.259 43.596 1.00 53.39 C
ATOM 9 C MET B 1 9.626 21.188 42.648 1.00 48.46 C
ATOM 10 O MET B 1 8.623 21.370 41.949 1.00 54.09 O
ATOM 11 CB MET B 1 9.427 22.128 44.941 1.00 58.63 C
ATOM 12 CG MET B 1 10.222 22.688 46.111 1.00 58.64 C
ATOM 13 SD MET B 1 9.862 21.803 47.641 1.00 59.47 S
ATOM 14 CE MET B 1 9.862 23.171 48.805 1.00 60.84 C
TER
HETATM 15 CA CA B 2 6.359 -7.487 3.887 1.00 45.13 Ca
ATOM 16 N LYS B 2 10.324 20.062 42.647 1.00 40.61 N
ATOM 17 CA LYS B 2 10.031 18.912 41.811 1.00 41.73 C
ATOM 18 C LYS B 2 9.845 17.682 42.694 1.00 47.89 C
ATOM 19 O LYS B 2 10.498 17.549 43.738 1.00 39.07 O
ATOM 20 CB LYS B 2 11.171 18.683 40.812 1.00 43.48 C
ATOM 21 CG LYS B 2 10.907 17.621 39.775 1.00 51.62 C
ATOM 22 CD LYS B 2 12.106 17.479 38.858 1.00 54.24 C
ATOM 23 CE LYS B 2 11.682 17.109 37.437 1.00 62.50 C
ATOM 24 NZ LYS B 2 12.855 16.702 36.607 1.00 60.39 N1+
ATOM 25 N ARG B 3 8.950 16.779 42.281 1.00 45.26 N
ATOM 26 CA ARG B 3 8.759 15.514 42.989 1.00 40.67 C
ATOM 27 C ARG B 3 8.645 14.375 41.987 1.00 39.52 C
ATOM 28 O ARG B 3 7.760 14.389 41.126 1.00 47.57 O
ATOM 29 CB ARG B 3 7.530 15.561 43.899 1.00 38.24 C
ATOM 30 CG ARG B 3 7.260 14.239 44.606 1.00 39.54 C
ATOM 31 CD ARG B 3 6.317 14.377 45.802 1.00 44.34 C
ATOM 32 NE ARG B 3 5.077 15.053 45.448 1.00 37.23 N
ATOM 33 CZ ARG B 3 4.666 16.191 45.984 1.00 43.06 C
ATOM 34 NH1 ARG B 3 5.320 16.763 46.979 1.00 46.71 N1+
ATOM 35 NH2 ARG B 3 3.557 16.758 45.524 1.00 43.39 N
ATOM 36 N LEU B 4 9.529 13.389 42.104 1.00 38.05 N
ATOM 37 CA LEU B 4 9.566 12.232 41.220 1.00 36.01 C
ATOM 38 C LEU B 4 9.152 10.982 41.982 1.00 33.93 C
ATOM 39 O LEU B 4 9.527 10.806 43.143 1.00 38.20 O
ATOM 40 CB LEU B 4 10.976 12.003 40.659 1.00 40.61 C
ATOM 41 CG LEU B 4 11.724 13.056 39.844 1.00 49.59 C
ATOM 42 CD1 LEU B 4 13.111 12.524 39.485 1.00 40.17 C
ATOM 43 CD2 LEU B 4 10.948 13.403 38.589 1.00 52.67 C
ATOM 44 N THR B 5 8.424 10.095 41.318 1.00 34.88 N
ATOM 45 CA THR B 5 8.082 8.788 41.853 1.00 32.04 C
ATOM 46 C THR B 5 8.535 7.744 40.854 1.00 35.55 C
ATOM 47 O THR B 5 8.205 7.845 39.667 1.00 39.47 O
ATOM 48 CB THR B 5 6.575 8.613 42.076 1.00 31.92 C
ATOM 49 CG2 THR B 5 6.304 7.257 42.652 1.00 30.02 C
ATOM 50 OG1 THR B 5 6.091 9.601 42.978 1.00 34.17 O
ATOM 51 N TYR B 6 9.242 6.722 41.327 1.00 25.59 N
ATOM 52 CA TYR B 6 9.722 5.694 40.423 1.00 33.91 C
ATOM 53 C TYR B 6 9.663 4.330 41.095 1.00 30.95 C
ATOM 54 O TYR B 6 9.580 4.206 42.322 1.00 32.63 O
ATOM 55 CB TYR B 6 11.149 6.005 39.907 1.00 37.64 C
ATOM 56 CG TYR B 6 12.255 5.745 40.920 1.00 34.62 C
ATOM 57 CD1 TYR B 6 12.802 4.475 41.078 1.00 32.05 C
ATOM 58 CD2 TYR B 6 12.761 6.775 41.701 1.00 36.84 C
ATOM 59 CE1 TYR B 6 13.791 4.226 42.007 1.00 29.42 C
ATOM 60 CE2 TYR B 6 13.770 6.541 42.628 1.00 37.13 C
ATOM 61 CZ TYR B 6 14.276 5.259 42.772 1.00 34.45 C
ATOM 62 OH TYR B 6 15.259 5.003 43.703 1.00 33.52 O
ATOM 63 N ILE B 7 9.696 3.298 40.255 1.00 30.39 N
ATOM 64 CA ILE B 7 9.810 1.919 40.696 1.00 32.71 C
ATOM 65 C ILE B 7 10.967 1.287 39.950 1.00 35.80 C
ATOM 66 O ILE B 7 11.317 1.697 38.838 1.00 35.87 O
ATOM 67 CB ILE B 7 8.514 1.112 40.481 1.00 31.98 C
ATOM 68 CG1 ILE B 7 8.097 1.101 39.007 1.00 33.29 C
ATOM 69 CG2 ILE B 7 7.405 1.704 41.304 1.00 34.30 C
ATOM 70 CD1 ILE B 7 6.976 0.117 38.744 1.00 35.84 C
ATOM 71 N SER B 8 11.570 0.287 40.578 1.00 31.72 N
ATOM 72 CA SER B 8 12.712 -0.387 39.997 1.00 39.46 C
ATOM 73 C SER B 8 12.756 -1.791 40.563 1.00 41.83 C
ATOM 74 O SER B 8 11.974 -2.150 41.451 1.00 31.58 O
ATOM 75 CB SER B 8 14.016 0.371 40.283 1.00 42.96 C
ATOM 76 OG SER B 8 14.395 0.216 41.647 1.00 38.39 O
ATOM 77 N LYS B 9 13.716 -2.566 40.074 1.00 34.81 N
ATOM 78 CA LYS B 9 13.865 -3.972 40.407 1.00 38.94 C
ATOM 79 C LYS B 9 15.274 -4.195 40.923 1.00 46.45 C
ATOM 80 O LYS B 9 16.219 -3.576 40.428 1.00 47.19 O
ATOM 81 CB LYS B 9 13.588 -4.844 39.164 1.00 47.25 C
ATOM 82 CG LYS B 9 13.609 -6.348 39.405 1.00 50.79 C
ATOM 83 CD LYS B 9 12.831 -7.114 38.321 1.00 60.73 C
ATOM 84 CE LYS B 9 13.127 -6.575 36.925 1.00 63.59 C
ATOM 85 NZ LYS B 9 13.150 -7.623 35.851 1.00 65.77 N1+
ATOM 86 N PHE B 10 15.413 -5.049 41.940 1.00 42.82 N
ATOM 87 CA PHE B 10 16.743 -5.448 42.383 1.00 37.70 C
ATOM 88 C PHE B 10 17.449 -6.154 41.229 1.00 48.54 C
ATOM 89 O PHE B 10 16.921 -7.115 40.655 1.00 43.32 O
ATOM 90 CB PHE B 10 16.672 -6.396 43.587 1.00 42.42 C
ATOM 91 CG PHE B 10 16.137 -5.778 44.876 1.00 39.83 C
ATOM 92 CD1 PHE B 10 15.395 -4.610 44.885 1.00 36.96 C
ATOM 93 CD2 PHE B 10 16.364 -6.418 46.085 1.00 40.34 C
ATOM 94 CE1 PHE B 10 14.896 -4.087 46.083 1.00 40.77 C
ATOM 95 CE2 PHE B 10 15.875 -5.899 47.281 1.00 42.22 C
ATOM 96 CZ PHE B 10 15.147 -4.732 47.276 1.00 37.15 C
ATOM 97 N SER B 11 18.633 -5.672 40.869 1.00 51.19 N
ATOM 98 CA SER B 11 19.424 -6.360 39.858 1.00 50.11 C
ATOM 99 C SER B 11 20.303 -7.456 40.456 1.00 49.55 C
ATOM 100 O SER B 11 21.081 -8.080 39.729 1.00 64.62 O
ATOM 101 CB SER B 11 20.256 -5.343 39.068 1.00 55.23 C
ATOM 102 OG SER B 11 21.131 -4.625 39.908 1.00 47.37 O
ATOM 103 N ARG B 12 20.177 -7.704 41.754 1.00 43.85 N
ATOM 104 CA ARG B 12 20.829 -8.789 42.477 1.00 46.56 C
ATOM 105 C ARG B 12 20.234 -8.825 43.885 1.00 47.53 C
ATOM 106 O ARG B 12 19.674 -7.829 44.336 1.00 43.99 O
ATOM 107 CB ARG B 12 22.350 -8.582 42.545 1.00 51.90 C
ATOM 108 CG ARG B 12 22.767 -7.259 43.187 1.00 58.83 C
ATOM 109 CD ARG B 12 24.157 -7.355 43.830 1.00 65.53 C
ATOM 110 NE ARG B 12 24.650 -6.062 44.296 1.00 57.67 N
ATOM 111 CZ ARG B 12 24.977 -5.783 45.552 1.00 67.80 C
ATOM 112 NH1 ARG B 12 24.855 -6.683 46.518 1.00 70.66 N1+
ATOM 113 NH2 ARG B 12 25.445 -4.570 45.847 1.00 58.69 N
ATOM 114 N PRO B 13 20.330 -9.955 44.584 1.00 51.85 N
ATOM 115 CA PRO B 13 19.748 -10.027 45.936 1.00 54.58 C
ATOM 116 C PRO B 13 20.375 -9.012 46.887 1.00 56.86 C
ATOM 117 O PRO B 13 21.592 -8.812 46.898 1.00 51.17 O
ATOM 118 CB PRO B 13 20.047 -11.462 46.391 1.00 51.19 C
ATOM 119 CG PRO B 13 20.610 -12.178 45.221 1.00 56.13 C
ATOM 120 CD PRO B 13 20.633 -11.281 44.027 1.00 53.30 C
ATOM 121 N LEU B 14 19.527 -8.374 47.697 1.00 49.60 N
ATOM 122 CA LEU B 14 19.954 -7.399 48.695 1.00 43.79 C
ATOM 123 C LEU B 14 19.327 -7.753 50.034 1.00 51.74 C
ATOM 124 O LEU B 14 18.123 -8.022 50.110 1.00 49.16 O
ATOM 125 CB LEU B 14 19.564 -5.972 48.301 1.00 38.01 C
ATOM 126 CG LEU B 14 20.046 -5.414 46.969 1.00 48.20 C
ATOM 127 CD1 LEU B 14 19.389 -4.082 46.668 1.00 39.03 C
ATOM 128 CD2 LEU B 14 21.560 -5.266 46.990 1.00 49.29 C
ATOM 129 N SER B 15 20.138 -7.749 51.085 1.00 44.44 N
ATOM 130 CA SER B 15 19.655 -8.058 52.419 1.00 43.33 C
ATOM 131 C SER B 15 18.925 -6.859 53.015 1.00 42.25 C
ATOM 132 O SER B 15 18.999 -5.732 52.507 1.00 38.87 O
ATOM 133 CB SER B 15 20.816 -8.438 53.327 1.00 47.53 C
ATOM 134 OG SER B 15 21.678 -7.323 53.470 1.00 41.63 O
ATOM 135 N GLY B 16 18.237 -7.109 54.131 1.00 46.83 N
ATOM 136 CA GLY B 16 17.577 -6.024 54.839 1.00 46.80 C
ATOM 137 C GLY B 16 18.566 -5.015 55.397 1.00 45.61 C
ATOM 138 O GLY B 16 18.328 -3.804 55.337 1.00 38.18 O
ATOM 139 N ASP B 17 19.688 -5.500 55.945 1.00 43.84 N
ATOM 140 CA ASP B 17 20.741 -4.600 56.402 1.00 45.34 C
ATOM 141 C ASP B 17 21.283 -3.754 55.254 1.00 42.85 C
ATOM 142 O ASP B 17 21.550 -2.558 55.424 1.00 44.37 O
ATOM 143 CB ASP B 17 21.865 -5.401 57.060 1.00 50.21 C
ATOM 144 CG ASP B 17 21.570 -5.732 58.511 1.00 54.36 C
ATOM 145 OD1 ASP B 17 20.595 -5.175 59.058 1.00 57.49 O
ATOM 146 OD2 ASP B 17 22.308 -6.542 59.108 1.00 57.94 O1-
ATOM 147 N GLU B 18 21.440 -4.350 54.074 1.00 40.43 N
ATOM 148 CA GLU B 18 21.949 -3.591 52.934 1.00 44.26 C
ATOM 149 C GLU B 18 20.943 -2.555 52.456 1.00 37.96 C
ATOM 150 O GLU B 18 21.329 -1.453 52.046 1.00 36.50 O
ATOM 151 CB GLU B 18 22.343 -4.544 51.803 1.00 45.16 C
ATOM 152 CG GLU B 18 23.730 -5.194 52.027 1.00 50.15 C
ATOM 153 CD GLU B 18 24.086 -6.219 50.965 1.00 61.32 C
ATOM 154 OE1 GLU B 18 23.150 -6.843 50.413 1.00 56.82 O
ATOM 155 OE2 GLU B 18 25.294 -6.407 50.687 1.00 70.61 O1-
ATOM 156 N ILE B 19 19.650 -2.886 52.496 1.00 40.00 N
ATOM 157 CA ILE B 19 18.619 -1.909 52.146 1.00 33.49 C
ATOM 158 C ILE B 19 18.598 -0.778 53.170 1.00 35.51 C
ATOM 159 O ILE B 19 18.467 0.403 52.820 1.00 33.77 O
ATOM 160 CB ILE B 19 17.256 -2.621 52.032 1.00 33.34 C
ATOM 161 CG1 ILE B 19 17.286 -3.601 50.842 1.00 35.82 C
ATOM 162 CG2 ILE B 19 16.101 -1.591 51.933 1.00 27.15 C
ATOM 163 CD1 ILE B 19 16.252 -4.708 50.918 1.00 44.79 C
ATOM 164 N GLU B 20 18.743 -1.131 54.447 1.00 32.18 N
ATOM 165 CA GLU B 20 18.738 -0.166 55.536 1.00 34.41 C
ATOM 166 C GLU B 20 19.871 0.839 55.397 1.00 37.78 C
ATOM 167 O GLU B 20 19.686 2.036 55.656 1.00 33.75 O
ATOM 168 CB GLU B 20 18.853 -0.929 56.855 1.00 36.33 C
ATOM 169 CG GLU B 20 18.813 -0.087 58.106 1.00 44.11 C
ATOM 170 CD GLU B 20 18.822 -0.947 59.363 1.00 56.50 C
ATOM 171 OE1 GLU B 20 19.796 -1.717 59.552 1.00 62.22 O
ATOM 172 OE2 GLU B 20 17.850 -0.860 60.156 1.00 65.45 O1-
ATOM 173 N ALA B 21 21.058 0.368 55.006 1.00 34.04 N
ATOM 174 CA ALA B 21 22.184 1.272 54.829 1.00 36.94 C
ATOM 175 C ALA B 21 21.937 2.238 53.682 1.00 33.50 C
ATOM 176 O ALA B 21 22.224 3.436 53.803 1.00 35.80 O
ATOM 177 CB ALA B 21 23.465 0.473 54.599 1.00 44.16 C
ATOM 178 N ILE B 22 21.413 1.737 52.559 1.00 30.90 N
ATOM 179 CA ILE B 22 21.062 2.622 51.452 1.00 33.12 C
ATOM 180 C ILE B 22 20.162 3.738 51.950 1.00 32.18 C
ATOM 181 O ILE B 22 20.384 4.922 51.666 1.00 33.34 O
ATOM 182 CB ILE B 22 20.396 1.830 50.312 1.00 36.30 C
ATOM 183 CG1 ILE B 22 21.426 0.946 49.599 1.00 37.88 C
ATOM 184 CG2 ILE B 22 19.708 2.765 49.315 1.00 33.12 C
ATOM 185 CD1 ILE B 22 20.823 0.118 48.490 1.00 36.24 C
ATOM 186 N GLY B 23 19.151 3.375 52.735 1.00 36.08 N
ATOM 187 CA GLY B 23 18.238 4.377 53.251 1.00 34.14 C
ATOM 188 C GLY B 23 18.932 5.389 54.141 1.00 34.61 C
ATOM 189 O GLY B 23 18.703 6.597 54.023 1.00 34.92 O
ATOM 190 N AARG B 24 19.797 4.911 55.042 0.58 33.09 N
ATOM 191 N BARG B 24 19.804 4.907 55.035 0.42 33.13 N
ATOM 192 CA AARG B 24 20.457 5.814 55.984 0.58 32.59 C
ATOM 193 CA BARG B 24 20.455 5.795 55.995 0.42 32.62 C
ATOM 194 C AARG B 24 21.456 6.716 55.273 0.58 32.10 C
ATOM 195 C BARG B 24 21.482 6.694 55.310 0.42 32.10 C
ATOM 196 O AARG B 24 21.567 7.906 55.592 0.58 30.23 O
ATOM 197 O BARG B 24 21.631 7.866 55.675 0.42 30.27 O
ATOM 198 CB AARG B 24 21.164 5.024 57.087 0.58 35.62 C
ATOM 199 CB BARG B 24 21.115 4.974 57.111 0.42 35.62 C
ATOM 200 CG AARG B 24 20.246 4.518 58.194 0.58 35.92 C
ATOM 201 CG BARG B 24 20.149 4.123 57.974 0.42 35.62 C
ATOM 202 CD AARG B 24 21.042 4.228 59.462 0.58 36.11 C
ATOM 203 CD BARG B 24 20.462 4.245 59.471 0.42 36.10 C
ATOM 204 NE AARG B 24 21.332 5.450 60.203 0.58 30.68 N
ATOM 205 NE BARG B 24 20.090 3.066 60.254 0.42 36.61 N
ATOM 206 CZ AARG B 24 22.540 5.976 60.382 0.58 32.68 C
ATOM 207 CZ BARG B 24 20.949 2.277 60.892 0.42 36.66 C
ATOM 208 NH1AARG B 24 23.637 5.384 59.924 0.58 17.81 N1+
ATOM 209 NH1BARG B 24 22.255 2.505 60.870 0.42 33.42 N1+
ATOM 210 NH2AARG B 24 22.646 7.131 61.025 0.58 26.50 N
ATOM 211 NH2BARG B 24 20.486 1.241 61.584 0.42 39.17 N
ATOM 212 N ILE B 25 22.192 6.168 54.307 1.00 35.71 N
ATOM 213 CA ILE B 25 23.112 6.996 53.533 1.00 32.07 C
ATOM 214 C ILE B 25 22.334 7.960 52.644 1.00 35.10 C
ATOM 215 O ILE B 25 22.688 9.141 52.540 1.00 32.92 O
ATOM 216 CB ILE B 25 24.092 6.114 52.734 1.00 42.34 C
ATOM 217 CG1 ILE B 25 24.924 5.253 53.696 1.00 45.36 C
ATOM 218 CG2 ILE B 25 25.050 6.961 51.900 1.00 44.14 C
ATOM 219 CD1 ILE B 25 25.750 4.181 53.001 1.00 45.58 C
ATOM 220 N SER B 26 21.217 7.498 52.047 1.00 31.49 N
ATOM 221 CA SER B 26 20.355 8.413 51.290 1.00 34.13 C
ATOM 222 C SER B 26 19.854 9.552 52.169 1.00 28.52 C
ATOM 223 O SER B 26 19.802 10.712 51.739 1.00 29.67 O
ATOM 224 CB SER B 26 19.167 7.654 50.684 1.00 35.39 C
ATOM 225 OG SER B 26 19.625 6.659 49.775 1.00 33.91 O
ATOM 226 N SER B 27 19.461 9.240 53.402 1.00 26.48 N
ATOM 227 CA SER B 27 19.020 10.292 54.305 1.00 24.69 C
ATOM 228 C SER B 27 20.126 11.319 54.526 1.00 28.10 C
ATOM 229 O SER B 27 19.886 12.531 54.478 1.00 29.15 O
ATOM 230 CB SER B 27 18.580 9.683 55.631 1.00 28.91 C
ATOM 231 OG SER B 27 18.097 10.698 56.479 1.00 29.07 O
ATOM 232 N GLN B 28 21.343 10.849 54.789 1.00 29.52 N
ATOM 233 CA AGLN B 28 22.451 11.770 55.030 0.55 30.42 C
ATOM 234 CA BGLN B 28 22.447 11.769 55.033 0.45 30.42 C
ATOM 235 C GLN B 28 22.656 12.699 53.841 1.00 30.82 C
ATOM 236 O GLN B 28 22.739 13.923 54.000 1.00 27.11 O
ATOM 237 CB AGLN B 28 23.734 10.995 55.332 0.55 30.60 C
ATOM 238 CB BGLN B 28 23.718 10.980 55.341 0.45 30.59 C
ATOM 239 CG AGLN B 28 24.943 11.914 55.593 0.55 32.04 C
ATOM 240 CG BGLN B 28 24.920 11.860 55.656 0.45 32.05 C
ATOM 241 CD AGLN B 28 26.207 11.150 55.930 0.55 32.04 C
ATOM 242 CD BGLN B 28 25.902 11.918 54.519 0.45 31.67 C
ATOM 243 NE2AGLN B 28 26.952 11.637 56.918 0.55 31.95 N
ATOM 244 NE2BGLN B 28 26.212 13.123 54.069 0.45 36.75 N
ATOM 245 OE1AGLN B 28 26.511 10.133 55.312 0.55 35.89 O
ATOM 246 OE1BGLN B 28 26.385 10.887 54.049 0.45 33.45 O
ATOM 247 N LYS B 29 22.723 12.132 52.633 1.00 30.76 N
ATOM 248 CA LYS B 29 22.940 12.943 51.437 1.00 32.11 C
ATOM 249 C LYS B 29 21.769 13.866 51.154 1.00 27.41 C
ATOM 250 O LYS B 29 21.962 15.045 50.834 1.00 28.34 O
ATOM 251 CB LYS B 29 23.210 12.036 50.239 1.00 31.26 C
ATOM 252 CG LYS B 29 24.450 11.198 50.456 1.00 39.55 C
ATOM 253 CD LYS B 29 24.788 10.332 49.258 1.00 50.62 C
ATOM 254 CE LYS B 29 26.103 9.602 49.510 1.00 57.28 C
ATOM 255 NZ LYS B 29 26.418 8.606 48.459 1.00 57.63 N1+
ATOM 256 N ASN B 30 20.537 13.363 51.261 1.00 33.11 N
ATOM 257 CA ASN B 30 19.397 14.217 50.950 1.00 31.16 C
ATOM 258 C ASN B 30 19.275 15.367 51.941 1.00 30.18 C
ATOM 259 O ASN B 30 18.831 16.460 51.568 1.00 28.43 O
ATOM 260 CB ASN B 30 18.090 13.403 50.924 1.00 32.57 C
ATOM 261 CG ASN B 30 18.017 12.469 49.732 1.00 32.97 C
ATOM 262 ND2 ASN B 30 17.025 11.588 49.719 1.00 29.88 N
ATOM 263 OD1 ASN B 30 18.837 12.558 48.820 1.00 34.91 O
ATOM 264 N GLN B 31 19.613 15.129 53.220 1.00 28.65 N
ATOM 265 CA GLN B 31 19.597 16.223 54.191 1.00 36.00 C
ATOM 266 C GLN B 31 20.525 17.347 53.751 1.00 30.51 C
ATOM 267 O GLN B 31 20.182 18.527 53.890 1.00 34.38 O
ATOM 268 CB GLN B 31 19.995 15.729 55.591 1.00 23.84 C
ATOM 269 CG GLN B 31 19.780 16.755 56.699 1.00 30.75 C
ATOM 270 CD GLN B 31 20.927 17.769 56.840 1.00 32.82 C
ATOM 271 NE2 GLN B 31 20.606 18.971 57.308 1.00 32.01 N
ATOM 272 OE1 GLN B 31 22.072 17.467 56.537 1.00 32.81 O
ATOM 273 N GLN B 32 21.709 17.000 53.230 1.00 30.03 N
ATOM 274 CA GLN B 32 22.632 18.039 52.773 1.00 36.61 C
ATOM 275 C GLN B 32 22.111 18.752 51.517 1.00 41.31 C
ATOM 276 O GLN B 32 22.514 19.889 51.250 1.00 36.67 O
ATOM 277 CB GLN B 32 24.015 17.446 52.484 1.00 33.37 C
ATOM 278 CG GLN B 32 24.914 17.142 53.727 1.00 37.05 C
ATOM 279 CD GLN B 32 25.226 18.368 54.588 1.00 46.52 C
ATOM 280 NE2 GLN B 32 24.482 18.522 55.697 1.00 38.00 N
ATOM 281 OE1 GLN B 32 26.153 19.130 54.301 1.00 45.62 O
ATOM 282 N ALA B 33 21.222 18.116 50.750 1.00 28.93 N
ATOM 283 CA ALA B 33 20.639 18.699 49.542 1.00 38.22 C
ATOM 284 C ALA B 33 19.294 19.351 49.789 1.00 35.79 C
ATOM 285 O ALA B 33 18.742 19.967 48.877 1.00 42.85 O
ATOM 286 CB ALA B 33 20.488 17.629 48.454 1.00 36.17 C
ATOM 287 N ASN B 34 18.756 19.237 51.001 1.00 39.44 N
ATOM 288 CA ASN B 34 17.425 19.736 51.323 1.00 41.34 C
ATOM 289 C ASN B 34 16.384 19.017 50.463 1.00 42.55 C
ATOM 290 O ASN B 34 15.452 19.619 49.924 1.00 40.72 O
ATOM 291 CB ASN B 34 17.344 21.258 51.168 1.00 48.67 C
ATOM 292 CG ASN B 34 16.038 21.825 51.688 1.00 52.36 C
ATOM 293 ND2 ASN B 34 15.449 22.752 50.938 1.00 50.17 N
ATOM 294 OD1 ASN B 34 15.560 21.425 52.752 1.00 57.69 O
ATOM 295 N VAL B 35 16.570 17.709 50.334 1.00 37.89 N
ATOM 296 CA VAL B 35 15.692 16.816 49.588 1.00 37.90 C
ATOM 297 C VAL B 35 15.010 15.874 50.577 1.00 34.79 C
ATOM 298 O VAL B 35 15.623 15.473 51.574 1.00 31.50 O
ATOM 299 CB VAL B 35 16.522 16.048 48.541 1.00 32.57 C
ATOM 300 CG1 VAL B 35 15.827 14.777 48.102 1.00 31.89 C
ATOM 301 CG2 VAL B 35 16.822 16.951 47.340 1.00 34.44 C
ATOM 302 N THR B 36 13.744 15.533 50.321 1.00 30.32 N
ATOM 303 CA THR B 36 12.995 14.658 51.226 1.00 35.17 C
ATOM 304 C THR B 36 12.327 13.531 50.440 1.00 32.77 C
ATOM 305 O THR B 36 12.287 13.545 49.209 1.00 26.25 O
ATOM 306 CB THR B 36 11.956 15.438 52.060 1.00 31.83 C
ATOM 307 CG2 THR B 36 12.637 16.348 53.074 1.00 31.43 C
ATOM 308 OG1 THR B 36 11.116 16.244 51.228 1.00 31.93 O
ATOM 309 N GLY B 37 11.837 12.518 51.148 1.00 29.32 N
ATOM 310 CA GLY B 37 11.098 11.457 50.466 1.00 24.60 C
ATOM 311 C GLY B 37 11.081 10.160 51.269 1.00 31.06 C
ATOM 312 O GLY B 37 11.364 10.145 52.473 1.00 27.54 O
ATOM 313 N VAL B 38 10.778 9.076 50.560 1.00 24.61 N
ATOM 314 CA VAL B 38 10.527 7.781 51.183 1.00 27.46 C
ATOM 315 C VAL B 38 10.973 6.690 50.222 1.00 27.27 C
ATOM 316 O VAL B 38 10.771 6.789 49.006 1.00 29.94 O
ATOM 317 CB VAL B 38 9.039 7.605 51.571 1.00 28.17 C
ATOM 318 CG1 VAL B 38 8.109 7.733 50.349 1.00 27.53 C
ATOM 319 CG2 VAL B 38 8.809 6.235 52.275 1.00 25.58 C
ATOM 320 N LEU B 39 11.576 5.646 50.776 1.00 27.85 N
ATOM 321 CA LEU B 39 12.032 4.478 50.026 1.00 29.79 C
ATOM 322 C LEU B 39 11.401 3.232 50.630 1.00 35.65 C
ATOM 323 O LEU B 39 11.495 3.010 51.848 1.00 30.30 O
ATOM 324 CB LEU B 39 13.573 4.379 50.051 1.00 30.32 C
ATOM 325 CG LEU B 39 14.303 3.165 49.451 1.00 32.42 C
ATOM 326 CD1 LEU B 39 14.130 3.050 47.949 1.00 31.74 C
ATOM 327 CD2 LEU B 39 15.801 3.197 49.837 1.00 27.91 C
ATOM 328 N LEU B 40 10.728 2.435 49.788 1.00 27.84 N
ATOM 329 CA LEU B 40 10.083 1.210 50.229 1.00 25.56 C
ATOM 330 C LEU B 40 10.557 0.063 49.357 1.00 32.29 C
ATOM 331 O LEU B 40 10.823 0.241 48.168 1.00 30.41 O
ATOM 332 CB LEU B 40 8.522 1.301 50.178 1.00 25.98 C
ATOM 333 CG LEU B 40 7.857 2.513 50.830 1.00 25.55 C
ATOM 334 CD1 LEU B 40 7.680 3.620 49.819 1.00 28.64 C
ATOM 335 CD2 LEU B 40 6.497 2.118 51.435 1.00 27.46 C
ATOM 336 N CYS B 41 10.686 -1.109 49.956 1.00 28.97 N
ATOM 337 CA CYS B 41 11.056 -2.282 49.197 1.00 27.99 C
ATOM 338 C CYS B 41 10.034 -3.364 49.467 1.00 35.87 C
ATOM 339 O CYS B 41 9.447 -3.422 50.547 1.00 32.80 O
ATOM 340 CB CYS B 41 12.461 -2.763 49.544 1.00 27.88 C
ATOM 341 SG CYS B 41 12.608 -3.447 51.182 1.00 37.17 S
ATOM 342 N LEU B 42 9.797 -4.200 48.463 1.00 34.97 N
ATOM 343 CA LEU B 42 8.866 -5.318 48.607 1.00 40.12 C
ATOM 344 C LEU B 42 9.255 -6.371 47.583 1.00 32.49 C
ATOM 345 O LEU B 42 9.099 -6.136 46.380 1.00 37.84 O
ATOM 346 CB LEU B 42 7.417 -4.872 48.408 1.00 35.78 C
ATOM 347 CG LEU B 42 6.351 -5.979 48.354 1.00 36.71 C
ATOM 348 CD1 LEU B 42 6.251 -6.706 49.701 1.00 40.10 C
ATOM 349 CD2 LEU B 42 4.965 -5.422 47.958 1.00 36.10 C
ATOM 350 N ASP B 43 9.788 -7.502 48.055 1.00 33.80 N
ATOM 351 CA ASP B 43 10.034 -8.666 47.199 1.00 42.66 C
ATOM 352 C ASP B 43 10.881 -8.316 45.963 1.00 41.03 C
ATOM 353 O ASP B 43 10.552 -8.670 44.830 1.00 37.06 O
ATOM 354 CB ASP B 43 8.690 -9.288 46.802 1.00 45.01 C
ATOM 355 CG ASP B 43 8.838 -10.622 46.119 1.00 54.36 C
ATOM 356 OD1 ASP B 43 9.135 -11.619 46.812 1.00 53.63 O
ATOM 357 OD2 ASP B 43 8.626 -10.666 44.888 1.00 66.53 O1-
ATOM 358 N GLY B 44 11.992 -7.614 46.188 1.00 38.31 N
ATOM 359 CA GLY B 44 12.896 -7.283 45.102 1.00 37.31 C
ATOM 360 C GLY B 44 12.442 -6.130 44.239 1.00 42.40 C
ATOM 361 O GLY B 44 12.928 -5.974 43.112 1.00 43.41 O
ATOM 362 N ILE B 45 11.511 -5.325 44.730 1.00 37.14 N
ATOM 363 CA ILE B 45 11.058 -4.109 44.075 1.00 33.96 C
ATOM 364 C ILE B 45 11.424 -2.940 44.972 1.00 38.47 C
ATOM 365 O ILE B 45 11.174 -2.986 46.183 1.00 38.23 O
ATOM 366 CB ILE B 45 9.528 -4.121 43.874 1.00 39.87 C
ATOM 367 CG1 ILE B 45 9.048 -5.415 43.217 1.00 42.25 C
ATOM 368 CG2 ILE B 45 9.073 -2.866 43.115 1.00 32.21 C
ATOM 369 CD1 ILE B 45 7.535 -5.626 43.421 1.00 39.89 C
ATOM 370 N PHE B 46 11.965 -1.879 44.388 1.00 31.54 N
ATOM 371 CA PHE B 46 12.103 -0.613 45.092 1.00 35.46 C
ATOM 372 C PHE B 46 11.002 0.334 44.632 1.00 36.61 C
ATOM 373 O PHE B 46 10.660 0.370 43.443 1.00 31.54 O
ATOM 374 CB PHE B 46 13.453 0.049 44.822 1.00 31.82 C
ATOM 375 CG PHE B 46 14.596 -0.530 45.595 1.00 32.71 C
ATOM 376 CD1 PHE B 46 14.573 -0.570 46.977 1.00 31.14 C
ATOM 377 CD2 PHE B 46 15.739 -0.957 44.933 1.00 31.71 C
ATOM 378 CE1 PHE B 46 15.651 -1.092 47.692 1.00 36.01 C
ATOM 379 CE2 PHE B 46 16.836 -1.450 45.640 1.00 34.07 C
ATOM 380 CZ PHE B 46 16.790 -1.526 47.021 1.00 37.30 C
ATOM 381 N PHE B 47 10.449 1.094 45.579 1.00 28.39 N
ATOM 382 CA PHE B 47 9.613 2.252 45.288 1.00 28.99 C
ATOM 383 C PHE B 47 10.260 3.435 45.981 1.00 30.83 C
ATOM 384 O PHE B 47 10.636 3.328 47.154 1.00 31.68 O
ATOM 385 CB PHE B 47 8.167 2.128 45.814 1.00 29.35 C
ATOM 386 CG PHE B 47 7.499 0.801 45.549 1.00 32.50 C
ATOM 387 CD1 PHE B 47 7.727 -0.283 46.386 1.00 36.21 C
ATOM 388 CD2 PHE B 47 6.586 0.655 44.514 1.00 34.08 C
ATOM 389 CE1 PHE B 47 7.090 -1.506 46.174 1.00 35.83 C
ATOM 390 CE2 PHE B 47 5.943 -0.574 44.297 1.00 31.78 C
ATOM 391 CZ PHE B 47 6.196 -1.645 45.130 1.00 35.29 C
ATOM 392 N GLN B 48 10.368 4.561 45.282 1.00 28.20 N
ATOM 393 CA GLN B 48 10.885 5.762 45.916 1.00 29.37 C
ATOM 394 C GLN B 48 10.150 6.994 45.416 1.00 28.44 C
ATOM 395 O GLN B 48 9.817 7.101 44.228 1.00 30.69 O
ATOM 396 CB GLN B 48 12.392 5.946 45.671 1.00 25.45 C
ATOM 397 CG GLN B 48 12.948 7.108 46.485 1.00 28.16 C
ATOM 398 CD GLN B 48 14.453 7.146 46.506 1.00 41.22 C
ATOM 399 NE2 GLN B 48 15.002 7.813 47.508 1.00 41.92 N
ATOM 400 OE1 GLN B 48 15.123 6.565 45.640 1.00 41.87 O
ATOM 401 N ILE B 49 9.883 7.907 46.348 1.00 27.44 N
ATOM 402 CA ILE B 49 9.436 9.260 46.059 1.00 26.40 C
ATOM 403 C ILE B 49 10.549 10.209 46.495 1.00 37.75 C
ATOM 404 O ILE B 49 11.046 10.105 47.622 1.00 28.70 O
ATOM 405 CB ILE B 49 8.119 9.574 46.788 1.00 32.74 C
ATOM 406 CG1 ILE B 49 7.040 8.548 46.399 1.00 32.92 C
ATOM 407 CG2 ILE B 49 7.653 10.998 46.496 1.00 29.69 C
ATOM 408 CD1 ILE B 49 5.767 8.614 47.273 1.00 25.64 C
ATOM 409 N LEU B 50 10.940 11.125 45.610 1.00 32.38 N
ATOM 410 CA LEU B 50 11.946 12.146 45.898 1.00 34.66 C
ATOM 411 C LEU B 50 11.368 13.528 45.636 1.00 38.16 C
ATOM 412 O LEU B 50 10.777 13.754 44.576 1.00 36.43 O
ATOM 413 CB LEU B 50 13.181 11.960 45.018 1.00 40.71 C
ATOM 414 CG LEU B 50 14.324 11.096 45.513 1.00 45.01 C
ATOM 415 CD1 LEU B 50 15.468 11.179 44.518 1.00 39.43 C
ATOM 416 CD2 LEU B 50 14.759 11.587 46.880 1.00 44.90 C
ATOM 417 N GLU B 51 11.572 14.463 46.568 1.00 35.50 N
ATOM 418 CA GLU B 51 11.086 15.825 46.383 1.00 38.25 C
ATOM 419 C GLU B 51 12.125 16.844 46.843 1.00 42.04 C
ATOM 420 O GLU B 51 12.841 16.643 47.829 1.00 36.29 O
ATOM 421 CB GLU B 51 9.760 16.063 47.115 1.00 32.87 C
ATOM 422 CG GLU B 51 9.898 16.043 48.605 1.00 31.88 C
ATOM 423 CD GLU B 51 8.591 15.807 49.340 1.00 40.08 C
ATOM 424 OE1 GLU B 51 7.504 15.879 48.712 1.00 41.97 O
ATOM 425 OE2 GLU B 51 8.660 15.533 50.561 1.00 31.41 O1-
ATOM 426 N GLY B 52 12.189 17.946 46.110 1.00 39.98 N
ATOM 427 CA GLY B 52 13.141 18.994 46.400 1.00 41.55 C
ATOM 428 C GLY B 52 13.278 19.924 45.210 1.00 51.61 C
ATOM 429 O GLY B 52 12.496 19.873 44.261 1.00 46.68 O
ATOM 430 N GLU B 53 14.297 20.774 45.288 1.00 46.33 N
ATOM 431 CA GLU B 53 14.585 21.701 44.204 1.00 51.83 C
ATOM 432 C GLU B 53 14.902 20.929 42.925 1.00 43.74 C
ATOM 433 O GLU B 53 15.656 19.950 42.943 1.00 41.26 O
ATOM 434 CB GLU B 53 15.750 22.613 44.607 1.00 52.15 C
ATOM 435 CG GLU B 53 15.955 23.810 43.699 1.00 57.12 C
ATOM 436 CD GLU B 53 16.828 23.483 42.498 1.00 64.98 C
ATOM 437 OE1 GLU B 53 17.956 22.975 42.705 1.00 67.62 O
ATOM 438 OE2 GLU B 53 16.378 23.719 41.349 1.00 63.63 O1-
ATOM 439 N ALA B 54 14.312 21.376 41.809 1.00 45.38 N
ATOM 440 CA ALA B 54 14.352 20.597 40.564 1.00 51.68 C
ATOM 441 C ALA B 54 15.781 20.245 40.144 1.00 51.25 C
ATOM 442 O ALA B 54 16.071 19.095 39.783 1.00 46.41 O
ATOM 443 CB ALA B 54 13.644 21.363 39.447 1.00 47.69 C
ATOM 444 N GLU B 55 16.686 21.229 40.170 1.00 56.97 N
ATOM 445 CA GLU B 55 18.075 20.970 39.798 1.00 55.59 C
ATOM 446 C GLU B 55 18.696 19.905 40.697 1.00 54.71 C
ATOM 447 O GLU B 55 19.363 18.983 40.213 1.00 53.16 O
ATOM 448 CB GLU B 55 18.882 22.272 39.856 1.00 68.97 C
ATOM 449 CG GLU B 55 20.393 22.121 39.667 1.00 71.12 C
ATOM 450 CD GLU B 55 20.833 22.118 38.201 1.00 85.12 C
ATOM 451 OE1 GLU B 55 20.177 21.459 37.358 1.00 77.28 O
ATOM 452 OE2 GLU B 55 21.862 22.764 37.897 1.00 85.36 O1-
ATOM 453 N LYS B 56 18.480 20.005 42.011 1.00 49.74 N
ATOM 454 CA LYS B 56 19.029 18.996 42.914 1.00 53.67 C
ATOM 455 C LYS B 56 18.382 17.632 42.690 1.00 47.20 C
ATOM 456 O LYS B 56 19.062 16.598 42.736 1.00 46.67 O
ATOM 457 CB LYS B 56 18.859 19.450 44.360 1.00 48.72 C
ATOM 458 CG LYS B 56 19.903 20.484 44.786 1.00 52.46 C
ATOM 459 CD LYS B 56 19.411 21.277 45.978 1.00 46.16 C
ATOM 460 CE LYS B 56 20.536 22.009 46.681 1.00 55.97 C
ATOM 461 NZ LYS B 56 20.182 23.426 46.972 1.00 63.17 N1+
ATOM 462 N ILE B 57 17.069 17.606 42.449 1.00 46.49 N
ATOM 463 CA ILE B 57 16.389 16.334 42.223 1.00 46.28 C
ATOM 464 C ILE B 57 17.007 15.606 41.033 1.00 48.09 C
ATOM 465 O ILE B 57 17.309 14.405 41.107 1.00 44.48 O
ATOM 466 CB ILE B 57 14.874 16.557 42.043 1.00 44.75 C
ATOM 467 CG1 ILE B 57 14.221 16.939 43.373 1.00 42.95 C
ATOM 468 CG2 ILE B 57 14.206 15.294 41.565 1.00 44.59 C
ATOM 469 CD1 ILE B 57 14.515 15.942 44.487 1.00 43.84 C
ATOM 470 N ASP B 58 17.255 16.335 39.931 1.00 49.88 N
ATOM 471 CA ASP B 58 17.768 15.682 38.723 1.00 51.63 C
ATOM 472 C ASP B 58 19.178 15.139 38.937 1.00 52.47 C
ATOM 473 O ASP B 58 19.497 14.036 38.471 1.00 52.37 O
ATOM 474 CB ASP B 58 17.721 16.641 37.525 1.00 54.15 C
ATOM 475 CG ASP B 58 16.281 16.912 37.033 1.00 66.06 C
ATOM 476 OD1 ASP B 58 15.920 18.096 36.826 1.00 66.11 O
ATOM 477 OD2 ASP B 58 15.503 15.946 36.860 1.00 62.18 O1-
ATOM 478 N ARG B 59 20.030 15.884 39.649 1.00 50.11 N
ATOM 479 CA ARG B 59 21.365 15.380 39.967 1.00 48.44 C
ATOM 480 C ARG B 59 21.280 14.045 40.682 1.00 49.35 C
ATOM 481 O ARG B 59 21.956 13.079 40.304 1.00 44.53 O
ATOM 482 CB ARG B 59 22.136 16.388 40.827 1.00 57.33 C
ATOM 483 CG ARG B 59 22.249 17.792 40.239 1.00 65.94 C
ATOM 484 CD ARG B 59 23.344 17.848 39.169 1.00 65.76 C
ATOM 485 NE ARG B 59 22.859 17.583 37.816 1.00 65.37 N
ATOM 486 CZ ARG B 59 21.825 18.177 37.230 1.00 64.09 C
ATOM 487 NH1 ARG B 59 21.212 19.213 37.780 1.00 60.62 N1+
ATOM 488 NH2 ARG B 59 21.419 17.740 36.042 1.00 60.50 N
ATOM 489 N ILE B 60 20.428 13.969 41.711 1.00 43.34 N
ATOM 490 CA ILE B 60 20.289 12.735 42.476 1.00 43.13 C
ATOM 491 C ILE B 60 19.721 11.633 41.599 1.00 42.88 C
ATOM 492 O ILE B 60 20.180 10.480 41.634 1.00 38.87 O
ATOM 493 CB ILE B 60 19.411 12.979 43.717 1.00 46.83 C
ATOM 494 CG1 ILE B 60 20.132 13.895 44.708 1.00 42.43 C
ATOM 495 CG2 ILE B 60 19.063 11.661 44.384 1.00 33.05 C
ATOM 496 CD1 ILE B 60 19.225 14.465 45.754 1.00 45.97 C
ATOM 497 N TYR B 61 18.718 11.967 40.785 1.00 44.41 N
ATOM 498 CA TYR B 61 18.065 10.921 40.012 1.00 47.25 C
ATOM 499 C TYR B 61 18.996 10.388 38.937 1.00 47.47 C
ATOM 500 O TYR B 61 19.002 9.179 38.662 1.00 45.61 O
ATOM 501 CB TYR B 61 16.764 11.440 39.412 1.00 49.78 C
ATOM 502 CG TYR B 61 15.963 10.358 38.747 1.00 50.46 C
ATOM 503 CD1 TYR B 61 15.901 10.254 37.363 1.00 39.50 C
ATOM 504 CD2 TYR B 61 15.286 9.406 39.513 1.00 48.93 C
ATOM 505 CE1 TYR B 61 15.159 9.256 36.752 1.00 45.32 C
ATOM 506 CE2 TYR B 61 14.546 8.396 38.909 1.00 47.71 C
ATOM 507 CZ TYR B 61 14.483 8.331 37.524 1.00 49.13 C
ATOM 508 OH TYR B 61 13.756 7.331 36.920 1.00 53.26 O
ATOM 509 N GLU B 62 19.818 11.271 38.349 1.00 48.37 N
ATOM 510 CA GLU B 62 20.894 10.828 37.462 1.00 45.93 C
ATOM 511 C GLU B 62 21.793 9.810 38.155 1.00 43.62 C
ATOM 512 O GLU B 62 22.141 8.772 37.579 1.00 49.24 O
ATOM 513 CB GLU B 62 21.724 12.024 36.999 1.00 52.71 C
ATOM 514 CG GLU B 62 21.184 12.738 35.787 1.00 66.58 C
ATOM 515 CD GLU B 62 22.252 13.569 35.110 1.00 72.96 C
ATOM 516 OE1 GLU B 62 23.428 13.454 35.515 1.00 74.79 O
ATOM 517 OE2 GLU B 62 21.920 14.322 34.171 1.00 83.38 O1-
ATOM 518 N ARG B 63 22.181 10.096 39.402 1.00 43.93 N
ATOM 519 CA ARG B 63 23.004 9.153 40.153 1.00 38.89 C
ATOM 520 C ARG B 63 22.257 7.858 40.415 1.00 45.10 C
ATOM 521 O ARG B 63 22.826 6.767 40.282 1.00 42.02 O
ATOM 522 CB ARG B 63 23.453 9.787 41.468 1.00 46.80 C
ATOM 523 CG ARG B 63 24.907 10.156 41.511 1.00 45.20 C
ATOM 524 CD ARG B 63 25.346 10.634 42.881 1.00 54.53 C
ATOM 525 NE ARG B 63 24.873 11.981 43.176 1.00 56.84 N
ATOM 526 CZ ARG B 63 24.136 12.319 44.225 1.00 57.31 C
ATOM 527 NH1 ARG B 63 23.773 11.429 45.136 1.00 50.98 N1+
ATOM 528 NH2 ARG B 63 23.774 13.592 44.376 1.00 50.35 N
ATOM 529 N ILE B 64 20.978 7.962 40.798 1.00 44.42 N
ATOM 530 CA ILE B 64 20.158 6.777 41.050 1.00 46.57 C
ATOM 531 C ILE B 64 20.067 5.912 39.797 1.00 43.46 C
ATOM 532 O ILE B 64 20.248 4.688 39.853 1.00 47.00 O
ATOM 533 CB ILE B 64 18.764 7.197 41.556 1.00 45.42 C
ATOM 534 CG1 ILE B 64 18.872 7.764 42.979 1.00 44.67 C
ATOM 535 CG2 ILE B 64 17.787 6.028 41.504 1.00 41.33 C
ATOM 536 CD1 ILE B 64 17.640 8.508 43.438 1.00 42.55 C
ATOM 537 N LEU B 65 19.796 6.533 38.647 1.00 35.44 N
ATOM 538 CA LEU B 65 19.738 5.777 37.391 1.00 48.10 C
ATOM 539 C LEU B 65 20.990 4.931 37.174 1.00 49.02 C
ATOM 540 O LEU B 65 20.901 3.787 36.706 1.00 48.59 O
ATOM 541 CB LEU B 65 19.540 6.727 36.212 1.00 46.97 C
ATOM 542 CG LEU B 65 18.179 7.416 36.149 1.00 48.83 C
ATOM 543 CD1 LEU B 65 18.186 8.529 35.109 1.00 52.22 C
ATOM 544 CD2 LEU B 65 17.073 6.406 35.864 1.00 42.12 C
ATOM 545 N ALA B 66 22.162 5.467 37.541 1.00 38.37 N
ATOM 546 CA ALA B 66 23.454 4.814 37.351 1.00 48.38 C
ATOM 547 C ALA B 66 23.789 3.768 38.410 1.00 50.04 C
ATOM 548 O ALA B 66 24.761 3.025 38.227 1.00 51.92 O
ATOM 549 CB ALA B 66 24.576 5.861 37.335 1.00 42.76 C
ATOM 550 N ASP B 67 23.046 3.701 39.517 1.00 47.57 N
ATOM 551 CA ASP B 67 23.366 2.748 40.575 1.00 45.93 C
ATOM 552 C ASP B 67 23.170 1.311 40.078 1.00 54.75 C
ATOM 553 O ASP B 67 22.076 0.929 39.643 1.00 50.50 O
ATOM 554 CB ASP B 67 22.508 3.031 41.806 1.00 38.06 C
ATOM 555 CG ASP B 67 22.993 2.317 43.023 1.00 36.97 C
ATOM 556 OD1 ASP B 67 23.209 1.088 42.961 1.00 42.35 O
ATOM 557 OD2 ASP B 67 23.158 2.979 44.073 1.00 47.54 O1-
ATOM 558 N GLU B 68 24.234 0.507 40.166 1.00 53.56 N
ATOM 559 CA GLU B 68 24.206 -0.857 39.643 1.00 57.67 C
ATOM 560 C GLU B 68 23.254 -1.763 40.402 1.00 54.12 C
ATOM 561 O GLU B 68 22.881 -2.822 39.883 1.00 50.68 O
ATOM 562 CB GLU B 68 25.608 -1.475 39.682 1.00 53.16 C
ATOM 563 CG GLU B 68 26.691 -0.593 39.073 1.00 74.96 C
ATOM 564 CD GLU B 68 27.997 -1.343 38.821 1.00 88.10 C
ATOM 565 OE1 GLU B 68 28.874 -1.349 39.718 1.00 79.26 O
ATOM 566 OE2 GLU B 68 28.136 -1.934 37.726 1.00 89.44 O1-
ATOM 567 N ARG B 69 22.859 -1.378 41.614 1.00 53.42 N
ATOM 568 CA ARG B 69 22.136 -2.274 42.503 1.00 47.86 C
ATOM 569 C ARG B 69 20.661 -2.421 42.139 1.00 47.95 C
ATOM 570 O ARG B 69 19.972 -3.263 42.735 1.00 41.57 O
ATOM 571 CB ARG B 69 22.295 -1.783 43.943 1.00 44.96 C
ATOM 572 CG ARG B 69 23.740 -1.795 44.401 1.00 47.38 C
ATOM 573 CD ARG B 69 23.900 -1.117 45.731 1.00 45.42 C
ATOM 574 NE ARG B 69 23.593 0.309 45.666 1.00 44.95 N
ATOM 575 CZ ARG B 69 23.895 1.161 46.636 1.00 37.53 C
ATOM 576 NH1 ARG B 69 24.498 0.755 47.742 1.00 34.05 N1+
ATOM 577 NH2 ARG B 69 23.586 2.448 46.494 1.00 38.32 N
ATOM 578 N HIS B 70 20.160 -1.650 41.173 1.00 42.12 N
ATOM 579 CA HIS B 70 18.821 -1.909 40.672 1.00 47.35 C
ATOM 580 C HIS B 70 18.755 -1.621 39.174 1.00 53.05 C
ATOM 581 O HIS B 70 19.630 -0.964 38.599 1.00 48.35 O
ATOM 582 CB HIS B 70 17.761 -1.117 41.464 1.00 41.13 C
ATOM 583 CG HIS B 70 17.869 0.368 41.333 1.00 42.69 C
ATOM 584 CD2 HIS B 70 18.808 1.153 40.755 1.00 36.92 C
ATOM 585 ND1 HIS B 70 16.902 1.223 41.820 1.00 38.73 N
ATOM 586 CE1 HIS B 70 17.253 2.471 41.567 1.00 38.58 C
ATOM 587 NE2 HIS B 70 18.404 2.456 40.919 1.00 41.06 N
ATOM 588 N THR B 71 17.686 -2.130 38.553 1.00 48.16 N
ATOM 589 CA THR B 71 17.484 -2.098 37.112 1.00 48.79 C
ATOM 590 C THR B 71 16.020 -1.823 36.799 1.00 51.87 C
ATOM 591 O THR B 71 15.157 -1.803 37.688 1.00 45.36 O
ATOM 592 CB THR B 71 17.930 -3.418 36.451 1.00 49.81 C
ATOM 593 CG2 THR B 71 16.885 -4.511 36.625 1.00 53.28 C
ATOM 594 OG1 THR B 71 18.185 -3.203 35.058 1.00 53.58 O
ATOM 595 N ASP B 72 15.759 -1.619 35.507 1.00 48.23 N
ATOM 596 CA ASP B 72 14.427 -1.374 34.969 1.00 44.45 C
ATOM 597 C ASP B 72 13.728 -0.246 35.719 1.00 50.64 C
ATOM 598 O ASP B 72 12.593 -0.382 36.182 1.00 47.27 O
ATOM 599 CB ASP B 72 13.591 -2.652 34.991 1.00 58.48 C
ATOM 600 CG ASP B 72 14.286 -3.792 34.297 1.00 59.92 C
ATOM 601 OD1 ASP B 72 15.227 -3.511 33.527 1.00 61.55 O
ATOM 602 OD2 ASP B 72 13.883 -4.957 34.494 1.00 63.35 O1-
ATOM 603 N ILE B 73 14.426 0.880 35.835 1.00 43.10 N
ATOM 604 CA ILE B 73 13.923 2.019 36.591 1.00 50.13 C
ATOM 605 C ILE B 73 12.907 2.776 35.745 1.00 49.15 C
ATOM 606 O ILE B 73 13.254 3.322 34.693 1.00 54.34 O
ATOM 607 CB ILE B 73 15.069 2.939 37.025 1.00 36.70 C
ATOM 608 CG1 ILE B 73 16.101 2.161 37.852 1.00 43.33 C
ATOM 609 CG2 ILE B 73 14.526 4.117 37.813 1.00 39.99 C
ATOM 610 CD1 ILE B 73 17.537 2.677 37.686 1.00 46.34 C
ATOM 611 N LEU B 74 11.657 2.830 36.220 1.00 41.78 N
ATOM 612 CA LEU B 74 10.552 3.473 35.515 1.00 44.71 C
ATOM 613 C LEU B 74 9.954 4.586 36.369 1.00 41.06 C
ATOM 614 O LEU B 74 9.409 4.322 37.447 1.00 40.59 O
ATOM 615 CB LEU B 74 9.471 2.450 35.161 1.00 42.78 C
ATOM 616 CG LEU B 74 8.264 3.092 34.475 1.00 48.39 C
ATOM 617 CD1 LEU B 74 8.631 3.485 33.043 1.00 50.63 C
ATOM 618 CD2 LEU B 74 7.062 2.157 34.496 1.00 46.25 C
ATOM 619 N CYS B 75 10.031 5.820 35.877 1.00 40.11 N
ATOM 620 CA CYS B 75 9.415 6.968 36.544 1.00 38.93 C
ATOM 621 C CYS B 75 7.909 6.984 36.288 1.00 45.65 C
ATOM 622 O CYS B 75 7.465 7.219 35.158 1.00 39.47 O
ATOM 623 CB CYS B 75 10.050 8.264 36.057 1.00 39.83 C
ATOM 624 SG CYS B 75 9.252 9.750 36.683 1.00 49.48 S
ATOM 625 N LEU B 76 7.117 6.779 37.344 1.00 37.41 N
ATOM 626 CA LEU B 76 5.662 6.768 37.211 1.00 38.52 C
ATOM 627 C LEU B 76 5.072 8.169 37.156 1.00 43.01 C
ATOM 628 O LEU B 76 4.055 8.389 36.489 1.00 42.54 O
ATOM 629 CB LEU B 76 5.028 6.010 38.375 1.00 42.51 C
ATOM 630 CG LEU B 76 5.483 4.572 38.555 1.00 41.83 C
ATOM 631 CD1 LEU B 76 4.918 4.019 39.841 1.00 38.48 C
ATOM 632 CD2 LEU B 76 5.053 3.761 37.364 1.00 42.11 C
ATOM 633 N LYS B 77 5.674 9.122 37.852 1.00 43.24 N
ATOM 634 CA LYS B 77 5.090 10.447 37.959 1.00 40.37 C
ATOM 635 C LYS B 77 6.206 11.447 38.150 1.00 38.70 C
ATOM 636 O LYS B 77 7.147 11.191 38.904 1.00 40.67 O
ATOM 637 CB LYS B 77 4.116 10.544 39.134 1.00 39.45 C
ATOM 638 CG LYS B 77 3.493 11.912 39.277 1.00 37.69 C
ATOM 639 CD LYS B 77 2.604 11.982 40.489 1.00 45.65 C
ATOM 640 CE LYS B 77 1.241 11.455 40.187 1.00 50.62 C
ATOM 641 NZ LYS B 77 0.268 11.945 41.201 1.00 59.16 N1+
ATOM 642 N SER B 78 6.084 12.594 37.496 1.00 41.82 N
ATOM 643 CA SER B 78 7.051 13.673 37.651 1.00 41.12 C
ATOM 644 C SER B 78 6.283 14.973 37.819 1.00 45.90 C
ATOM 645 O SER B 78 5.699 15.473 36.854 1.00 53.53 O
ATOM 646 CB SER B 78 7.996 13.748 36.453 1.00 42.69 C
ATOM 647 OG SER B 78 8.753 14.933 36.512 1.00 52.12 O
ATOM 648 N GLU B 79 6.281 15.521 39.032 1.00 41.53 N
ATOM 649 CA GLU B 79 5.571 16.756 39.329 1.00 41.59 C
ATOM 650 C GLU B 79 6.541 17.926 39.318 1.00 51.21 C
ATOM 651 O GLU B 79 7.659 17.825 39.831 1.00 52.78 O
ATOM 652 CB GLU B 79 4.869 16.681 40.688 1.00 44.67 C
ATOM 653 CG GLU B 79 3.838 15.572 40.814 1.00 48.14 C
ATOM 654 CD GLU B 79 3.504 15.246 42.268 1.00 49.02 C
ATOM 655 OE1 GLU B 79 2.705 15.993 42.870 1.00 39.74 O
ATOM 656 OE2 GLU B 79 4.066 14.261 42.812 1.00 42.18 O1-
ATOM 657 N VAL B 80 6.110 19.031 38.717 1.00 54.84 N
ATOM 658 CA VAL B 80 6.878 20.265 38.692 1.00 51.24 C
ATOM 659 C VAL B 80 6.060 21.339 39.390 1.00 56.55 C
ATOM 660 O VAL B 80 4.858 21.180 39.628 1.00 56.43 O
ATOM 661 CB VAL B 80 7.250 20.696 37.258 1.00 67.19 C
ATOM 662 CG1 VAL B 80 8.138 19.643 36.598 1.00 56.29 C
ATOM 663 CG2 VAL B 80 5.984 20.932 36.432 1.00 50.41 C
ATOM 664 N GLU B 81 6.733 22.440 39.729 1.00 59.34 N
ATOM 665 CA GLU B 81 6.106 23.556 40.437 1.00 62.08 C
ATOM 666 C GLU B 81 5.276 23.054 41.616 1.00 56.87 C
ATOM 667 O GLU B 81 4.096 23.378 41.762 1.00 55.73 O
ATOM 668 CB GLU B 81 5.244 24.395 39.491 1.00 72.84 C
ATOM 669 CG GLU B 81 6.016 25.229 38.473 1.00 77.47 C
ATOM 670 CD GLU B 81 5.103 25.806 37.396 1.00 91.70 C
ATOM 671 OE1 GLU B 81 4.374 25.020 36.745 1.00 86.18 O
ATOM 672 OE2 GLU B 81 5.097 27.046 37.216 1.00 93.74 O1-
ATOM 673 N VAL B 82 5.901 22.231 42.452 1.00 51.53 N
ATOM 674 CA VAL B 82 5.206 21.628 43.584 1.00 50.20 C
ATOM 675 C VAL B 82 5.096 22.653 44.704 1.00 49.08 C
ATOM 676 O VAL B 82 6.081 23.311 45.060 1.00 52.53 O
ATOM 677 CB VAL B 82 5.936 20.363 44.055 1.00 52.39 C
ATOM 678 CG1 VAL B 82 5.564 20.042 45.490 1.00 52.33 C
ATOM 679 CG2 VAL B 82 5.620 19.201 43.126 1.00 49.28 C
ATOM 680 N GLN B 83 3.893 22.798 45.262 1.00 49.16 N
ATOM 681 CA GLN B 83 3.679 23.844 46.257 1.00 53.78 C
ATOM 682 C GLN B 83 4.220 23.464 47.636 1.00 60.39 C
ATOM 683 O GLN B 83 4.802 24.312 48.324 1.00 57.58 O
ATOM 684 CB GLN B 83 2.194 24.196 46.326 1.00 57.13 C
ATOM 685 CG GLN B 83 1.715 25.036 45.141 1.00 66.24 C
ATOM 686 CD GLN B 83 2.850 25.819 44.493 1.00 65.01 C
ATOM 687 NE2 GLN B 83 3.205 26.954 45.091 1.00 65.79 N
ATOM 688 OE1 GLN B 83 3.405 25.406 43.473 1.00 67.09 O
ATOM 689 N GLU B 84 4.041 22.215 48.071 1.00 60.28 N
ATOM 690 CA GLU B 84 4.555 21.823 49.376 1.00 57.79 C
ATOM 691 C GLU B 84 4.978 20.362 49.359 1.00 50.42 C
ATOM 692 O GLU B 84 4.519 19.564 48.537 1.00 43.63 O
ATOM 693 CB GLU B 84 3.539 22.054 50.505 1.00 62.79 C
ATOM 694 CG GLU B 84 2.406 21.060 50.577 1.00 59.30 C
ATOM 695 CD GLU B 84 1.123 21.579 49.943 1.00 84.68 C
ATOM 696 OE1 GLU B 84 1.208 22.422 49.022 1.00 81.89 O
ATOM 697 OE2 GLU B 84 0.026 21.153 50.381 1.00 94.05 O1-
ATOM 698 N ARG B 85 5.859 20.024 50.301 1.00 39.20 N
ATOM 699 CA ARG B 85 6.410 18.683 50.406 1.00 38.22 C
ATOM 700 C ARG B 85 5.388 17.713 50.985 1.00 35.50 C
ATOM 701 O ARG B 85 4.561 18.077 51.826 1.00 44.05 O
ATOM 702 CB ARG B 85 7.666 18.690 51.283 1.00 39.77 C
ATOM 703 CG ARG B 85 8.765 19.597 50.767 1.00 36.40 C
ATOM 704 CD ARG B 85 9.888 19.779 51.766 1.00 41.91 C
ATOM 705 NE ARG B 85 10.959 20.564 51.161 1.00 42.88 N
ATOM 706 CZ ARG B 85 12.023 20.046 50.562 1.00 39.70 C
ATOM 707 NH1 ARG B 85 12.233 18.739 50.532 1.00 35.89 N1+
ATOM 708 NH2 ARG B 85 12.889 20.859 49.964 1.00 41.03 N
ATOM 709 N MET B 86 5.451 16.464 50.519 1.00 33.73 N
ATOM 710 CA MET B 86 4.669 15.408 51.150 1.00 34.88 C
ATOM 711 C MET B 86 5.354 14.868 52.397 1.00 41.52 C
ATOM 712 O MET B 86 4.674 14.419 53.324 1.00 35.40 O
ATOM 713 CB MET B 86 4.435 14.253 50.186 1.00 35.12 C
ATOM 714 CG MET B 86 3.039 14.242 49.560 1.00 45.52 C
ATOM 715 SD MET B 86 2.983 13.351 47.986 1.00 56.32 S
ATOM 716 CE MET B 86 1.333 13.818 47.393 1.00 37.30 C
ATOM 717 N PHE B 87 6.685 14.898 52.439 1.00 30.10 N
ATOM 718 CA PHE B 87 7.453 14.226 53.481 1.00 31.18 C
ATOM 719 C PHE B 87 8.465 15.188 54.099 1.00 28.79 C
ATOM 720 O PHE B 87 9.664 14.906 54.141 1.00 28.21 O
ATOM 721 CB PHE B 87 8.121 12.980 52.896 1.00 27.69 C
ATOM 722 CG PHE B 87 7.161 12.083 52.140 1.00 35.06 C
ATOM 723 CD1 PHE B 87 6.181 11.365 52.827 1.00 28.23 C
ATOM 724 CD2 PHE B 87 7.224 11.960 50.754 1.00 30.99 C
ATOM 725 CE1 PHE B 87 5.292 10.525 52.160 1.00 26.88 C
ATOM 726 CE2 PHE B 87 6.332 11.121 50.066 1.00 28.52 C
ATOM 727 CZ PHE B 87 5.377 10.396 50.770 1.00 30.65 C
ATOM 728 N PRO B 88 8.001 16.334 54.619 1.00 33.82 N
ATOM 729 CA PRO B 88 8.948 17.405 55.000 1.00 33.05 C
ATOM 730 C PRO B 88 9.976 17.007 56.052 1.00 35.67 C
ATOM 731 O PRO B 88 11.085 17.559 56.057 1.00 34.45 O
ATOM 732 CB PRO B 88 8.022 18.516 55.511 1.00 29.56 C
ATOM 733 CG PRO B 88 6.792 17.800 55.954 1.00 29.76 C
ATOM 734 CD PRO B 88 6.613 16.670 54.992 1.00 32.33 C
ATOM 735 N ASP B 89 9.664 16.064 56.935 1.00 30.15 N
ATOM 736 CA ASP B 89 10.607 15.680 57.977 1.00 34.21 C
ATOM 737 C ASP B 89 11.396 14.428 57.633 1.00 35.16 C
ATOM 738 O ASP B 89 12.111 13.909 58.485 1.00 29.21 O
ATOM 739 CB ASP B 89 9.865 15.508 59.298 1.00 36.12 C
ATOM 740 CG ASP B 89 9.168 16.780 59.714 1.00 38.79 C
ATOM 741 OD1 ASP B 89 9.862 17.822 59.756 1.00 41.22 O
ATOM 742 OD2 ASP B 89 7.941 16.750 59.932 1.00 40.62 O1-
ATOM 743 N TRP B 90 11.282 13.924 56.410 1.00 24.78 N
ATOM 744 CA TRP B 90 11.956 12.689 56.012 1.00 25.22 C
ATOM 745 C TRP B 90 12.997 13.026 54.952 1.00 29.26 C
ATOM 746 O TRP B 90 12.669 13.077 53.768 1.00 33.24 O
ATOM 747 CB TRP B 90 10.949 11.654 55.460 1.00 24.74 C
ATOM 748 CG TRP B 90 9.903 11.179 56.409 1.00 30.72 C
ATOM 749 CD1 TRP B 90 9.798 11.458 57.748 1.00 26.01 C
ATOM 750 CD2 TRP B 90 8.811 10.303 56.095 1.00 27.91 C
ATOM 751 CE2 TRP B 90 8.080 10.102 57.287 1.00 29.26 C
ATOM 752 CE3 TRP B 90 8.383 9.668 54.919 1.00 26.76 C
ATOM 753 NE1 TRP B 90 8.703 10.823 58.277 1.00 25.47 N
ATOM 754 CZ2 TRP B 90 6.934 9.288 57.340 1.00 27.67 C
ATOM 755 CZ3 TRP B 90 7.239 8.841 54.976 1.00 29.86 C
ATOM 756 CH2 TRP B 90 6.529 8.674 56.176 1.00 28.03 C
ATOM 757 N SER B 91 14.249 13.259 55.353 1.00 32.27 N
ATOM 758 CA SER B 91 15.292 13.368 54.339 1.00 29.02 C
ATOM 759 C SER B 91 15.312 12.113 53.478 1.00 28.80 C
ATOM 760 O SER B 91 15.372 12.194 52.248 1.00 27.08 O
ATOM 761 CB SER B 91 16.659 13.610 54.989 1.00 24.42 C
ATOM 762 OG SER B 91 16.674 14.864 55.659 1.00 28.94 O
ATOM 763 N MET B 92 15.289 10.940 54.111 1.00 26.82 N
ATOM 764 CA MET B 92 14.884 9.711 53.432 1.00 29.18 C
ATOM 765 C MET B 92 14.358 8.757 54.496 1.00 30.21 C
ATOM 766 O MET B 92 15.117 8.329 55.366 1.00 30.91 O
ATOM 767 CB MET B 92 16.025 9.032 52.657 1.00 30.74 C
ATOM 768 CG MET B 92 15.506 7.815 51.849 1.00 33.56 C
ATOM 769 SD MET B 92 14.018 8.022 50.797 1.00 35.47 S
ATOM 770 CE MET B 92 14.095 9.709 50.188 1.00 32.54 C
ATOM 771 N GLN B 93 13.074 8.413 54.430 1.00 29.28 N
ATOM 772 CA GLN B 93 12.497 7.400 55.317 1.00 27.93 C
ATOM 773 C GLN B 93 12.455 6.066 54.596 1.00 29.32 C
ATOM 774 O GLN B 93 11.959 5.985 53.470 1.00 32.74 O
ATOM 775 CB GLN B 93 11.081 7.772 55.753 1.00 27.06 C
ATOM 776 CG GLN B 93 10.350 6.705 56.567 1.00 25.80 C
ATOM 777 CD GLN B 93 10.806 6.631 58.026 1.00 29.02 C
ATOM 778 NE2 GLN B 93 10.219 5.707 58.772 1.00 26.44 N
ATOM 779 OE1 GLN B 93 11.676 7.386 58.470 1.00 26.20 O
ATOM 780 N THR B 94 12.906 5.016 55.267 1.00 28.09 N
ATOM 781 CA THR B 94 13.024 3.696 54.670 1.00 29.25 C
ATOM 782 C THR B 94 12.011 2.748 55.298 1.00 33.13 C
ATOM 783 O THR B 94 11.893 2.672 56.528 1.00 30.14 O
ATOM 784 CB THR B 94 14.451 3.189 54.844 1.00 33.51 C
ATOM 785 CG2 THR B 94 14.621 1.790 54.238 1.00 29.22 C
ATOM 786 OG1 THR B 94 15.326 4.116 54.184 1.00 35.76 O
ATOM 787 N ILE B 95 11.249 2.061 54.452 1.00 30.16 N
ATOM 788 CA ILE B 95 10.150 1.205 54.890 1.00 28.43 C
ATOM 789 C ILE B 95 10.333 -0.134 54.194 1.00 31.09 C
ATOM 790 O ILE B 95 9.981 -0.280 53.020 1.00 28.55 O
ATOM 791 CB ILE B 95 8.778 1.801 54.562 1.00 29.90 C
ATOM 792 CG1 ILE B 95 8.624 3.198 55.181 1.00 27.59 C
ATOM 793 CG2 ILE B 95 7.667 0.877 55.034 1.00 24.50 C
ATOM 794 CD1 ILE B 95 7.268 3.865 54.817 1.00 24.25 C
ATOM 795 N ASN B 96 10.865 -1.114 54.913 1.00 33.04 N
ATOM 796 CA ASN B 96 11.031 -2.457 54.374 1.00 38.20 C
ATOM 797 C ASN B 96 9.723 -3.207 54.575 1.00 37.33 C
ATOM 798 O ASN B 96 9.389 -3.589 55.701 1.00 33.05 O
ATOM 799 CB ASN B 96 12.191 -3.183 55.052 1.00 34.64 C
ATOM 800 CG ASN B 96 12.502 -4.528 54.395 1.00 43.82 C
ATOM 801 ND2 ASN B 96 13.780 -4.781 54.132 1.00 43.99 N
ATOM 802 OD1 ASN B 96 11.600 -5.326 54.123 1.00 40.21 O
ATOM 803 N LEU B 97 8.981 -3.416 53.482 1.00 32.45 N
ATOM 804 CA LEU B 97 7.701 -4.099 53.592 1.00 29.38 C
ATOM 805 C LEU B 97 7.848 -5.597 53.786 1.00 32.69 C
ATOM 806 O LEU B 97 6.951 -6.221 54.359 1.00 30.93 O
ATOM 807 CB LEU B 97 6.845 -3.814 52.361 1.00 32.03 C
ATOM 808 CG LEU B 97 6.463 -2.343 52.357 1.00 32.71 C
ATOM 809 CD1 LEU B 97 5.890 -1.956 51.010 1.00 32.75 C
ATOM 810 CD2 LEU B 97 5.484 -2.089 53.504 1.00 28.66 C
ATOM 811 N ASP B 98 8.944 -6.196 53.314 1.00 31.04 N
ATOM 812 CA ASP B 98 9.156 -7.620 53.559 1.00 34.08 C
ATOM 813 C ASP B 98 9.108 -7.922 55.042 1.00 34.59 C
ATOM 814 O ASP B 98 8.483 -8.900 55.468 1.00 45.04 O
ATOM 815 CB ASP B 98 10.498 -8.073 52.980 1.00 29.11 C
ATOM 816 CG ASP B 98 10.545 -7.970 51.483 1.00 35.16 C
ATOM 817 OD1 ASP B 98 9.619 -8.483 50.827 1.00 35.19 O
ATOM 818 OD2 ASP B 98 11.494 -7.337 50.956 1.00 42.77 O1-
ATOM 819 N GLU B 99 9.755 -7.086 55.841 1.00 38.26 N
ATOM 820 CA GLU B 99 9.809 -7.288 57.282 1.00 38.54 C
ATOM 821 C GLU B 99 8.567 -6.785 58.001 1.00 34.84 C
ATOM 822 O GLU B 99 8.397 -7.071 59.189 1.00 36.57 O
ATOM 823 CB GLU B 99 11.053 -6.600 57.841 1.00 37.69 C
ATOM 824 CG GLU B 99 12.338 -7.141 57.215 1.00 47.42 C
ATOM 825 CD GLU B 99 13.589 -6.395 57.654 1.00 46.10 C
ATOM 826 OE1 GLU B 99 13.548 -5.715 58.703 1.00 55.21 O
ATOM 827 OE2 GLU B 99 14.614 -6.502 56.942 1.00 51.57 O1-
ATOM 828 N ASN B 100 7.686 -6.064 57.330 1.00 32.95 N
ATOM 829 CA ASN B 100 6.523 -5.550 58.035 1.00 37.26 C
ATOM 830 C ASN B 100 5.483 -6.654 58.159 1.00 31.04 C
ATOM 831 O ASN B 100 5.204 -7.358 57.186 1.00 36.53 O
ATOM 832 CB ASN B 100 5.943 -4.339 57.314 1.00 38.50 C
ATOM 833 CG ASN B 100 4.888 -3.636 58.142 1.00 37.97 C
ATOM 834 ND2 ASN B 100 5.265 -2.516 58.761 1.00 28.82 N
ATOM 835 OD1 ASN B 100 3.749 -4.104 58.239 1.00 32.90 O
ATOM 836 N THR B 101 4.923 -6.814 59.360 1.00 34.91 N
ATOM 837 CA THR B 101 3.900 -7.824 59.632 1.00 41.55 C
ATOM 838 C THR B 101 2.614 -7.208 60.180 1.00 38.20 C
ATOM 839 O THR B 101 1.808 -7.915 60.780 1.00 37.59 O
ATOM 840 CB THR B 101 4.414 -8.891 60.611 1.00 43.37 C
ATOM 841 CG2 THR B 101 5.738 -9.488 60.150 1.00 41.70 C
ATOM 842 OG1 THR B 101 4.595 -8.320 61.916 1.00 43.45 O
ATOM 843 N ASP B 102 2.416 -5.906 60.001 1.00 33.90 N
ATOM 844 CA ASP B 102 1.240 -5.254 60.550 1.00 30.84 C
ATOM 845 C ASP B 102 -0.024 -5.780 59.873 1.00 35.08 C
ATOM 846 O ASP B 102 -0.063 -6.006 58.658 1.00 31.34 O
ATOM 847 CB ASP B 102 1.334 -3.739 60.365 1.00 26.29 C
ATOM 848 CG ASP B 102 2.486 -3.125 61.142 1.00 35.53 C
ATOM 849 OD1 ASP B 102 3.081 -3.819 61.996 1.00 38.65 O
ATOM 850 OD2 ASP B 102 2.854 -1.971 60.833 1.00 33.16 O1-
ATOM 851 N PHE B 103 -1.075 -5.903 60.678 1.00 30.86 N
ATOM 852 CA PHE B 103 -2.327 -6.531 60.267 1.00 33.36 C
ATOM 853 C PHE B 103 -2.899 -5.924 58.990 1.00 30.21 C
ATOM 854 O PHE B 103 -3.312 -6.647 58.079 1.00 32.70 O
ATOM 855 CB PHE B 103 -3.344 -6.392 61.399 1.00 29.07 C
ATOM 856 CG PHE B 103 -4.667 -7.015 61.096 1.00 30.91 C
ATOM 857 CD1 PHE B 103 -4.843 -8.393 61.224 1.00 32.78 C
ATOM 858 CD2 PHE B 103 -5.728 -6.242 60.668 1.00 31.59 C
ATOM 859 CE1 PHE B 103 -6.069 -8.970 60.949 1.00 30.04 C
ATOM 860 CE2 PHE B 103 -6.955 -6.816 60.407 1.00 33.53 C
ATOM 861 CZ PHE B 103 -7.119 -8.180 60.541 1.00 32.11 C
ATOM 862 N LEU B 104 -3.024 -4.596 58.949 1.00 28.88 N
ATOM 863 CA LEU B 104 -3.638 -3.954 57.802 1.00 28.79 C
ATOM 864 C LEU B 104 -2.681 -3.851 56.620 1.00 29.74 C
ATOM 865 O LEU B 104 -3.136 -3.828 55.471 1.00 33.01 O
ATOM 866 CB LEU B 104 -4.150 -2.563 58.173 1.00 30.79 C
ATOM 867 CG LEU B 104 -5.349 -2.499 59.134 1.00 33.92 C
ATOM 868 CD1 LEU B 104 -5.536 -1.088 59.627 1.00 40.98 C
ATOM 869 CD2 LEU B 104 -6.628 -3.002 58.460 1.00 31.75 C
ATOM 870 N ILE B 105 -1.368 -3.780 56.878 1.00 26.94 N
ATOM 871 CA ILE B 105 -0.409 -3.674 55.783 1.00 30.08 C
ATOM 872 C ILE B 105 -0.305 -4.965 54.964 1.00 28.37 C
ATOM 873 O ILE B 105 0.061 -4.910 53.783 1.00 30.78 O
ATOM 874 CB ILE B 105 0.964 -3.213 56.328 1.00 32.09 C
ATOM 875 CG1 ILE B 105 0.906 -1.726 56.699 1.00 34.51 C
ATOM 876 CG2 ILE B 105 2.060 -3.409 55.309 1.00 28.36 C
ATOM 877 CD1 ILE B 105 2.215 -1.159 57.236 1.00 30.85 C
ATOM 878 N ARG B 106 -0.648 -6.124 55.532 1.00 23.73 N
ATOM 879 CA ARG B 106 -0.523 -7.370 54.772 1.00 27.65 C
ATOM 880 C ARG B 106 -1.321 -7.374 53.468 1.00 30.24 C
ATOM 881 O ARG B 106 -0.724 -7.663 52.415 1.00 30.75 O
ATOM 882 CB ARG B 106 -0.876 -8.572 55.653 1.00 30.20 C
ATOM 883 CG ARG B 106 -0.556 -9.910 54.965 1.00 39.23 C
ATOM 884 CD ARG B 106 -0.891 -11.130 55.804 1.00 33.47 C
ATOM 885 NE ARG B 106 -2.320 -11.355 55.990 1.00 39.42 N
ATOM 886 CZ ARG B 106 -3.045 -12.181 55.248 1.00 40.24 C
ATOM 887 NH1 ARG B 106 -2.547 -12.758 54.165 1.00 35.96 N1+
ATOM 888 NH2 ARG B 106 -4.296 -12.437 55.604 1.00 37.03 N
ATOM 889 N PRO B 107 -2.633 -7.075 53.439 1.00 29.34 N
ATOM 890 CA PRO B 107 -3.328 -7.054 52.134 1.00 30.18 C
ATOM 891 C PRO B 107 -2.877 -5.911 51.243 1.00 31.14 C
ATOM 892 O PRO B 107 -2.947 -6.022 50.015 1.00 28.37 O
ATOM 893 CB PRO B 107 -4.804 -6.909 52.521 1.00 29.19 C
ATOM 894 CG PRO B 107 -4.752 -6.172 53.821 1.00 28.79 C
ATOM 895 CD PRO B 107 -3.548 -6.728 54.541 1.00 29.33 C
ATOM 896 N ILE B 108 -2.411 -4.809 51.828 1.00 30.81 N
ATOM 897 CA ILE B 108 -1.872 -3.721 51.024 1.00 31.33 C
ATOM 898 C ILE B 108 -0.630 -4.189 50.265 1.00 30.28 C
ATOM 899 O ILE B 108 -0.446 -3.863 49.082 1.00 29.37 O
ATOM 900 CB ILE B 108 -1.578 -2.501 51.914 1.00 35.84 C
ATOM 901 CG1 ILE B 108 -2.865 -1.977 52.561 1.00 29.09 C
ATOM 902 CG2 ILE B 108 -0.933 -1.424 51.095 1.00 38.25 C
ATOM 903 CD1 ILE B 108 -2.599 -0.970 53.690 1.00 32.08 C
ATOM 904 N LYS B 109 0.221 -4.993 50.915 1.00 31.84 N
ATOM 905 CA LYS B 109 1.403 -5.522 50.233 1.00 33.60 C
ATOM 906 C LYS B 109 1.016 -6.376 49.028 1.00 35.79 C
ATOM 907 O LYS B 109 1.617 -6.264 47.952 1.00 36.27 O
ATOM 908 CB LYS B 109 2.263 -6.325 51.212 1.00 30.31 C
ATOM 909 CG LYS B 109 3.089 -5.468 52.150 1.00 30.20 C
ATOM 910 CD LYS B 109 3.597 -6.259 53.362 1.00 29.29 C
ATOM 911 CE LYS B 109 4.417 -7.481 52.968 1.00 34.15 C
ATOM 912 NZ LYS B 109 4.867 -8.141 54.223 1.00 28.20 N1+
ATOM 913 N VAL B 110 0.024 -7.251 49.190 1.00 35.81 N
ATOM 914 CA VAL B 110 -0.394 -8.098 48.073 1.00 31.42 C
ATOM 915 C VAL B 110 -0.867 -7.237 46.911 1.00 35.21 C
ATOM 916 O VAL B 110 -0.533 -7.502 45.752 1.00 35.64 O
ATOM 917 CB VAL B 110 -1.499 -9.077 48.513 1.00 32.13 C
ATOM 918 CG1 VAL B 110 -2.091 -9.768 47.283 1.00 34.36 C
ATOM 919 CG2 VAL B 110 -0.972 -10.083 49.521 1.00 32.84 C
ATOM 920 N LEU B 111 -1.638 -6.182 47.210 1.00 31.70 N
ATOM 921 CA LEU B 111 -2.147 -5.264 46.188 1.00 34.87 C
ATOM 922 C LEU B 111 -1.026 -4.462 45.532 1.00 32.24 C
ATOM 923 O LEU B 111 -1.002 -4.295 44.305 1.00 35.07 O
ATOM 924 CB LEU B 111 -3.169 -4.327 46.833 1.00 36.65 C
ATOM 925 CG LEU B 111 -3.984 -3.322 46.045 1.00 40.55 C
ATOM 926 CD1 LEU B 111 -5.008 -4.041 45.182 1.00 43.42 C
ATOM 927 CD2 LEU B 111 -4.674 -2.384 47.028 1.00 37.50 C
ATOM 928 N LEU B 112 -0.118 -3.907 46.341 1.00 34.55 N
ATOM 929 CA LEU B 112 1.079 -3.274 45.799 1.00 34.28 C
ATOM 930 C LEU B 112 1.799 -4.203 44.833 1.00 31.60 C
ATOM 931 O LEU B 112 2.178 -3.805 43.729 1.00 34.20 O
ATOM 932 CB LEU B 112 2.026 -2.874 46.934 1.00 35.97 C
ATOM 933 CG LEU B 112 1.849 -1.522 47.601 1.00 37.24 C
ATOM 934 CD1 LEU B 112 2.959 -1.354 48.649 1.00 38.51 C
ATOM 935 CD2 LEU B 112 1.866 -0.391 46.554 1.00 36.02 C
ATOM 936 N GLN B 113 2.020 -5.450 45.243 1.00 40.31 N
ATOM 937 CA GLN B 113 2.743 -6.369 44.373 1.00 37.67 C
ATOM 938 C GLN B 113 1.976 -6.591 43.074 1.00 39.62 C
ATOM 939 O GLN B 113 2.545 -6.517 41.981 1.00 38.78 O
ATOM 940 CB GLN B 113 2.989 -7.692 45.087 1.00 39.04 C
ATOM 941 CG GLN B 113 3.723 -8.681 44.209 1.00 48.18 C
ATOM 942 CD GLN B 113 4.980 -9.199 44.849 1.00 51.69 C
ATOM 943 NE2 GLN B 113 6.113 -8.965 44.200 1.00 54.70 N
ATOM 944 OE1 GLN B 113 4.940 -9.798 45.923 1.00 59.49 O
ATOM 945 N THR B 114 0.668 -6.822 43.181 1.00 35.87 N
ATOM 946 CA THR B 114 -0.140 -7.120 42.004 1.00 36.75 C
ATOM 947 C THR B 114 -0.195 -5.932 41.050 1.00 37.36 C
ATOM 948 O THR B 114 -0.081 -6.105 39.833 1.00 34.83 O
ATOM 949 CB THR B 114 -1.537 -7.538 42.448 1.00 37.48 C
ATOM 950 CG2 THR B 114 -2.486 -7.609 41.268 1.00 33.52 C
ATOM 951 OG1 THR B 114 -1.456 -8.828 43.058 1.00 39.84 O
ATOM 952 N LEU B 115 -0.356 -4.715 41.586 1.00 32.57 N
ATOM 953 CA LEU B 115 -0.404 -3.525 40.740 1.00 34.68 C
ATOM 954 C LEU B 115 0.912 -3.312 40.011 1.00 41.44 C
ATOM 955 O LEU B 115 0.931 -2.838 38.868 1.00 37.77 O
ATOM 956 CB LEU B 115 -0.716 -2.294 41.588 1.00 32.35 C
ATOM 957 CG LEU B 115 -2.139 -1.795 41.743 1.00 42.95 C
ATOM 958 CD1 LEU B 115 -2.162 -0.756 42.863 1.00 40.45 C
ATOM 959 CD2 LEU B 115 -2.603 -1.179 40.435 1.00 45.03 C
ATOM 960 N THR B 116 2.027 -3.618 40.682 1.00 36.66 N
ATOM 961 CA THR B 116 3.349 -3.447 40.096 1.00 30.08 C
ATOM 962 C THR B 116 3.596 -4.465 38.990 1.00 39.49 C
ATOM 963 O THR B 116 4.093 -4.116 37.914 1.00 41.83 O
ATOM 964 CB THR B 116 4.417 -3.577 41.195 1.00 41.62 C
ATOM 965 CG2 THR B 116 5.810 -3.499 40.613 1.00 32.80 C
ATOM 966 OG1 THR B 116 4.260 -2.522 42.153 1.00 41.91 O
ATOM 967 N GLU B 117 3.285 -5.742 39.248 1.00 38.77 N
ATOM 968 CA GLU B 117 3.430 -6.761 38.209 1.00 41.38 C
ATOM 969 C GLU B 117 2.545 -6.442 37.009 1.00 42.05 C
ATOM 970 O GLU B 117 2.976 -6.557 35.857 1.00 37.57 O
ATOM 971 CB GLU B 117 3.077 -8.143 38.766 1.00 40.42 C
ATOM 972 CG GLU B 117 4.032 -8.662 39.826 1.00 45.93 C
ATOM 973 CD GLU B 117 3.447 -9.823 40.625 1.00 52.91 C
ATOM 974 OE1 GLU B 117 2.257 -10.166 40.412 1.00 59.59 O
ATOM 975 OE2 GLU B 117 4.174 -10.371 41.481 1.00 54.95 O1-
ATOM 976 N SER B 118 1.303 -6.032 37.263 1.00 37.42 N
ATOM 977 CA SER B 118 0.420 -5.639 36.172 1.00 39.96 C
ATOM 978 C SER B 118 1.028 -4.485 35.388 1.00 44.43 C
ATOM 979 O SER B 118 1.121 -4.525 34.156 1.00 47.12 O
ATOM 980 CB SER B 118 -0.954 -5.258 36.733 1.00 37.91 C
ATOM 981 OG SER B 118 -1.827 -4.836 35.697 1.00 48.18 O
ATOM 982 N HIS B 119 1.483 -3.463 36.102 1.00 44.23 N
ATOM 983 CA HIS B 119 2.112 -2.313 35.468 1.00 42.90 C
ATOM 984 C HIS B 119 3.296 -2.718 34.599 1.00 43.37 C
ATOM 985 O HIS B 119 3.551 -2.101 33.558 1.00 45.21 O
ATOM 986 CB HIS B 119 2.568 -1.337 36.543 1.00 41.70 C
ATOM 987 CG HIS B 119 2.645 0.065 36.063 1.00 40.16 C
ATOM 988 CD2 HIS B 119 1.811 1.115 36.251 1.00 40.77 C
ATOM 989 ND1 HIS B 119 3.646 0.504 35.228 1.00 35.65 N
ATOM 990 CE1 HIS B 119 3.442 1.778 34.944 1.00 49.25 C
ATOM 991 NE2 HIS B 119 2.334 2.171 35.549 1.00 47.76 N
ATOM 992 N ARG B 120 4.044 -3.741 35.018 1.00 45.56 N
ATOM 993 CA ARG B 120 5.191 -4.195 34.231 1.00 38.21 C
ATOM 994 C ARG B 120 4.749 -4.909 32.958 1.00 47.51 C
ATOM 995 O ARG B 120 5.408 -4.802 31.915 1.00 48.48 O
ATOM 996 CB ARG B 120 6.061 -5.116 35.076 1.00 43.25 C
ATOM 997 CG ARG B 120 6.777 -4.434 36.231 1.00 45.89 C
ATOM 998 CD ARG B 120 7.596 -3.247 35.757 1.00 49.69 C
ATOM 999 NE ARG B 120 8.772 -3.107 36.602 1.00 58.67 N
ATOM 1000 CZ ARG B 120 9.733 -2.210 36.437 1.00 55.26 C
ATOM 1001 NH1 ARG B 120 9.691 -1.317 35.457 1.00 48.60 N1+
ATOM 1002 NH2 ARG B 120 10.775 -2.227 37.263 1.00 44.19 N
ATOM 1003 N ILE B 121 3.650 -5.659 33.025 1.00 47.68 N
ATOM 1004 CA ILE B 121 3.071 -6.233 31.815 1.00 47.49 C
ATOM 1005 C ILE B 121 2.717 -5.126 30.832 1.00 48.23 C
ATOM 1006 O ILE B 121 3.185 -5.111 29.687 1.00 44.08 O
ATOM 1007 CB ILE B 121 1.846 -7.097 32.166 1.00 50.47 C
ATOM 1008 CG1 ILE B 121 2.272 -8.254 33.077 1.00 48.66 C
ATOM 1009 CG2 ILE B 121 1.154 -7.593 30.909 1.00 51.86 C
ATOM 1010 CD1 ILE B 121 1.289 -9.410 33.118 1.00 55.32 C
ATOM 1011 N LEU B 122 1.897 -4.171 31.281 1.00 49.89 N
ATOM 1012 CA LEU B 122 1.454 -3.072 30.425 1.00 51.74 C
ATOM 1013 C LEU B 122 2.613 -2.306 29.816 1.00 54.29 C
ATOM 1014 O LEU B 122 2.483 -1.747 28.718 1.00 53.40 O
ATOM 1015 CB LEU B 122 0.583 -2.103 31.226 1.00 52.87 C
ATOM 1016 CG LEU B 122 -0.920 -2.222 31.026 1.00 55.21 C
ATOM 1017 CD1 LEU B 122 -1.369 -3.666 31.228 1.00 54.91 C
ATOM 1018 CD2 LEU B 122 -1.620 -1.292 31.999 1.00 57.84 C
ATOM 1019 N GLU B 123 3.740 -2.248 30.524 1.00 47.85 N
ATOM 1020 CA GLU B 123 4.895 -1.499 30.054 1.00 48.37 C
ATOM 1021 C GLU B 123 5.491 -2.118 28.792 1.00 54.33 C
ATOM 1022 O GLU B 123 6.025 -1.396 27.939 1.00 53.35 O
ATOM 1023 CB GLU B 123 5.928 -1.432 31.183 1.00 43.37 C
ATOM 1024 CG GLU B 123 7.083 -0.497 30.963 1.00 56.93 C
ATOM 1025 CD GLU B 123 8.235 -0.790 31.917 1.00 68.79 C
ATOM 1026 OE1 GLU B 123 7.972 -1.350 33.010 1.00 60.54 O
ATOM 1027 OE2 GLU B 123 9.397 -0.478 31.567 1.00 64.45 O1-
ATOM 1028 N LYS B 124 5.413 -3.446 28.659 1.00 46.91 N
ATOM 1029 CA LYS B 124 5.884 -4.117 27.453 1.00 49.72 C
ATOM 1030 C LYS B 124 4.985 -3.855 26.255 1.00 47.56 C
ATOM 1031 O LYS B 124 5.435 -4.001 25.116 1.00 49.25 O
ATOM 1032 CB LYS B 124 5.978 -5.624 27.699 1.00 50.33 C
ATOM 1033 CG LYS B 124 7.036 -6.029 28.710 1.00 46.43 C
ATOM 1034 CD LYS B 124 8.383 -5.456 28.301 1.00 58.59 C
ATOM 1035 CE LYS B 124 9.473 -5.874 29.262 1.00 59.19 C
ATOM 1036 NZ LYS B 124 9.474 -7.349 29.374 1.00 59.85 N1+
ATOM 1037 N TYR B 125 3.725 -3.488 26.485 1.00 46.10 N
ATOM 1038 CA TYR B 125 2.733 -3.358 25.429 1.00 47.42 C
ATOM 1039 C TYR B 125 2.387 -1.907 25.118 1.00 46.42 C
ATOM 1040 O TYR B 125 1.402 -1.658 24.420 1.00 47.88 O
ATOM 1041 CB TYR B 125 1.472 -4.140 25.803 1.00 43.95 C
ATOM 1042 CG TYR B 125 1.662 -5.637 25.778 1.00 42.60 C
ATOM 1043 CD1 TYR B 125 2.173 -6.313 26.874 1.00 43.87 C
ATOM 1044 CD2 TYR B 125 1.343 -6.376 24.652 1.00 46.20 C
ATOM 1045 CE1 TYR B 125 2.365 -7.678 26.850 1.00 42.66 C
ATOM 1046 CE2 TYR B 125 1.528 -7.744 24.617 1.00 36.09 C
ATOM 1047 CZ TYR B 125 2.035 -8.392 25.717 1.00 51.98 C
ATOM 1048 OH TYR B 125 2.215 -9.760 25.680 1.00 56.24 O
ATOM 1049 N THR B 126 3.166 -0.946 25.625 1.00 50.47 N
ATOM 1050 CA THR B 126 3.042 0.470 25.284 1.00 61.61 C
ATOM 1051 C THR B 126 4.365 1.000 24.748 1.00 63.67 C
ATOM 1052 O THR B 126 5.438 0.452 25.025 1.00 66.82 O
ATOM 1053 CB THR B 126 2.636 1.347 26.488 1.00 60.43 C
ATOM 1054 CG2 THR B 126 1.383 0.860 27.129 1.00 56.98 C
ATOM 1055 OG1 THR B 126 3.686 1.353 27.461 1.00 52.39 O
ATOM 1056 N GLN B 127 4.282 2.105 23.984 1.00 67.80 N
ATOM 1057 CA GLN B 127 5.504 2.710 23.464 1.00 65.27 C
ATOM 1058 C GLN B 127 6.269 3.402 24.592 1.00 66.74 C
ATOM 1059 O GLN B 127 5.661 4.080 25.429 1.00 63.64 O
ATOM 1060 CB GLN B 127 5.191 3.732 22.372 1.00 62.92 C
ATOM 1061 CG GLN B 127 4.986 3.227 20.921 1.00 62.87 C
ATOM 1062 CD GLN B 127 5.710 1.926 20.554 1.00 66.20 C
ATOM 1063 NE2 GLN B 127 7.024 1.868 20.799 1.00 60.48 N
ATOM 1064 OE1 GLN B 127 5.090 0.994 20.030 1.00 70.04 O
ATOM 1065 N PRO B 128 7.603 3.255 24.632 1.00 64.13 N
ATOM 1066 CA PRO B 128 8.402 3.992 25.623 1.00 65.34 C
ATOM 1067 C PRO B 128 8.374 5.503 25.446 1.00 61.43 C
ATOM 1068 O PRO B 128 8.945 6.219 26.269 1.00 68.20 O
ATOM 1069 CB PRO B 128 9.817 3.439 25.409 1.00 68.45 C
ATOM 1070 CG PRO B 128 9.599 2.074 24.827 1.00 69.74 C
ATOM 1071 CD PRO B 128 8.381 2.198 23.963 1.00 66.24 C
ATOM 1072 N SER B 129 7.728 6.014 24.393 1.00 65.88 N
ATOM 1073 CA SER B 129 7.594 7.460 24.258 1.00 65.64 C
ATOM 1074 C SER B 129 6.506 8.032 25.162 1.00 57.72 C
ATOM 1075 O SER B 129 6.567 9.220 25.495 1.00 55.38 O
ATOM 1076 CB SER B 129 7.318 7.843 22.799 1.00 59.93 C
ATOM 1077 OG SER B 129 6.032 7.409 22.396 1.00 66.43 O
ATOM 1078 N ILE B 130 5.523 7.224 25.574 1.00 56.61 N
ATOM 1079 CA ILE B 130 4.549 7.701 26.559 1.00 54.49 C
ATOM 1080 C ILE B 130 5.214 7.863 27.926 1.00 59.15 C
ATOM 1081 O ILE B 130 4.930 8.817 28.663 1.00 56.99 O
ATOM 1082 CB ILE B 130 3.317 6.770 26.616 1.00 61.53 C
ATOM 1083 CG1 ILE B 130 2.265 7.158 25.558 1.00 64.45 C
ATOM 1084 CG2 ILE B 130 2.648 6.799 27.987 1.00 58.69 C
ATOM 1085 CD1 ILE B 130 2.733 7.136 24.105 1.00 60.50 C
ATOM 1086 N PHE B 131 6.129 6.955 28.275 1.00 55.21 N
ATOM 1087 CA PHE B 131 6.870 7.109 29.522 1.00 58.00 C
ATOM 1088 C PHE B 131 7.822 8.291 29.465 1.00 58.36 C
ATOM 1089 O PHE B 131 8.050 8.948 30.490 1.00 53.44 O
ATOM 1090 CB PHE B 131 7.638 5.830 29.852 1.00 59.70 C
ATOM 1091 CG PHE B 131 6.760 4.623 29.992 1.00 63.42 C
ATOM 1092 CD1 PHE B 131 5.770 4.587 30.965 1.00 56.43 C
ATOM 1093 CD2 PHE B 131 6.916 3.530 29.151 1.00 66.97 C
ATOM 1094 CE1 PHE B 131 4.953 3.483 31.098 1.00 58.60 C
ATOM 1095 CE2 PHE B 131 6.100 2.422 29.275 1.00 63.29 C
ATOM 1096 CZ PHE B 131 5.115 2.398 30.254 1.00 58.73 C
ATOM 1097 N LYS B 132 8.390 8.570 28.287 1.00 60.51 N
ATOM 1098 CA LYS B 132 9.227 9.754 28.130 1.00 61.24 C
ATOM 1099 C LYS B 132 8.421 11.019 28.375 1.00 57.47 C
ATOM 1100 O LYS B 132 8.878 11.928 29.077 1.00 59.56 O
ATOM 1101 CB LYS B 132 9.862 9.776 26.737 1.00 59.57 C
ATOM 1102 N ILE B 133 7.210 11.086 27.818 1.00 53.81 N
ATOM 1103 CA ILE B 133 6.310 12.201 28.105 1.00 59.96 C
ATOM 1104 C ILE B 133 6.030 12.284 29.602 1.00 54.74 C
ATOM 1105 O ILE B 133 5.982 13.376 30.177 1.00 60.97 O
ATOM 1106 CB ILE B 133 5.005 12.064 27.290 1.00 56.94 C
ATOM 1107 CG1 ILE B 133 5.267 12.258 25.791 1.00 61.29 C
ATOM 1108 CG2 ILE B 133 3.957 13.060 27.757 1.00 62.59 C
ATOM 1109 CD1 ILE B 133 4.259 11.541 24.896 1.00 55.36 C
ATOM 1110 N ILE B 134 5.866 11.133 30.255 1.00 54.48 N
ATOM 1111 CA ILE B 134 5.518 11.109 31.675 1.00 59.79 C
ATOM 1112 C ILE B 134 6.690 11.587 32.526 1.00 63.73 C
ATOM 1113 O ILE B 134 6.520 12.404 33.440 1.00 63.26 O
ATOM 1114 CB ILE B 134 5.069 9.697 32.085 1.00 54.41 C
ATOM 1115 CG1 ILE B 134 3.626 9.457 31.643 1.00 51.33 C
ATOM 1116 CG2 ILE B 134 5.221 9.510 33.589 1.00 52.50 C
ATOM 1117 CD1 ILE B 134 3.268 7.993 31.506 1.00 46.83 C
ATOM 1118 N SER B 135 7.895 11.077 32.243 1.00 61.45 N
ATOM 1119 CA SER B 135 9.095 11.488 32.967 1.00 64.41 C
ATOM 1120 C SER B 135 9.365 12.983 32.851 1.00 68.18 C
ATOM 1121 O SER B 135 10.048 13.549 33.713 1.00 73.21 O
ATOM 1122 CB SER B 135 10.303 10.714 32.447 1.00 64.99 C
ATOM 1123 OG SER B 135 10.052 9.321 32.498 1.00 71.13 O
ATOM 1124 N GLN B 136 8.860 13.627 31.800 1.00 68.07 N
ATOM 1125 CA GLN B 136 9.025 15.060 31.594 1.00 64.33 C
ATOM 1126 C GLN B 136 8.014 15.895 32.370 1.00 66.39 C
ATOM 1127 O GLN B 136 8.086 17.128 32.326 1.00 69.21 O
ATOM 1128 CB GLN B 136 8.940 15.375 30.096 1.00 68.87 C
ATOM 1129 CG GLN B 136 10.146 14.868 29.307 1.00 70.31 C
ATOM 1130 CD GLN B 136 9.909 14.838 27.811 1.00 72.65 C
ATOM 1131 NE2 GLN B 136 10.911 14.380 27.059 1.00 69.03 N
ATOM 1132 OE1 GLN B 136 8.838 15.223 27.334 1.00 74.68 O
ATOM 1133 N GLY B 137 7.087 15.264 33.084 1.00 62.25 N
ATOM 1134 CA GLY B 137 6.155 15.994 33.913 1.00 64.34 C
ATOM 1135 C GLY B 137 4.860 16.378 33.247 1.00 65.20 C
ATOM 1136 O GLY B 137 4.213 17.330 33.696 1.00 66.19 O
ATOM 1137 N THR B 138 4.454 15.672 32.191 1.00 66.20 N
ATOM 1138 CA THR B 138 3.250 16.015 31.445 1.00 73.70 C
ATOM 1139 C THR B 138 2.414 14.762 31.211 1.00 70.68 C
ATOM 1140 O THR B 138 2.947 13.715 30.826 1.00 65.94 O
ATOM 1141 CB THR B 138 3.594 16.695 30.105 1.00 68.80 C
ATOM 1142 CG2 THR B 138 4.185 18.088 30.339 1.00 62.82 C
ATOM 1143 OG1 THR B 138 4.538 15.899 29.381 1.00 70.86 O
ATOM 1144 N ASN B 139 1.115 14.870 31.460 1.00 67.07 N
ATOM 1145 CA ASN B 139 0.202 13.771 31.190 1.00 66.51 C
ATOM 1146 C ASN B 139 0.057 13.621 29.682 1.00 63.36 C
ATOM 1147 O ASN B 139 -0.374 14.575 29.018 1.00 62.40 O
ATOM 1148 CB ASN B 139 -1.153 14.036 31.847 1.00 62.66 C
ATOM 1149 CG ASN B 139 -2.083 12.822 31.811 1.00 61.67 C
ATOM 1150 ND2 ASN B 139 -2.900 12.691 32.849 1.00 57.72 N
ATOM 1151 OD1 ASN B 139 -2.085 12.029 30.863 1.00 61.62 O
ATOM 1152 N PRO B 140 0.421 12.469 29.098 1.00 67.76 N
ATOM 1153 CA PRO B 140 0.238 12.279 27.645 1.00 62.69 C
ATOM 1154 C PRO B 140 -1.189 12.525 27.158 1.00 65.06 C
ATOM 1155 O PRO B 140 -1.375 12.928 26.000 1.00 56.40 O
ATOM 1156 CB PRO B 140 0.664 10.824 27.407 1.00 64.10 C
ATOM 1157 CG PRO B 140 1.277 10.331 28.679 1.00 63.33 C
ATOM 1158 CD PRO B 140 1.141 11.367 29.751 1.00 66.74 C
ATOM 1159 N LEU B 141 -2.207 12.301 27.999 1.00 64.58 N
ATOM 1160 CA LEU B 141 -3.578 12.629 27.627 1.00 58.65 C
ATOM 1161 C LEU B 141 -3.819 14.131 27.510 1.00 61.33 C
ATOM 1162 O LEU B 141 -4.867 14.532 26.991 1.00 60.53 O
ATOM 1163 CB LEU B 141 -4.553 12.034 28.645 1.00 65.50 C
ATOM 1164 CG LEU B 141 -4.576 10.509 28.793 1.00 65.90 C
ATOM 1165 CD1 LEU B 141 -5.356 10.115 30.042 1.00 59.68 C
ATOM 1166 CD2 LEU B 141 -5.179 9.850 27.551 1.00 56.38 C
ATOM 1167 N ASN B 142 -2.880 14.965 27.967 1.00 64.65 N
ATOM 1168 CA ASN B 142 -3.042 16.412 27.955 1.00 66.60 C
ATOM 1169 C ASN B 142 -2.245 17.109 26.860 1.00 65.29 C
ATOM 1170 O ASN B 142 -2.306 18.338 26.759 1.00 65.55 O
ATOM 1171 CB ASN B 142 -2.652 17.001 29.316 1.00 69.72 C
ATOM 1172 CG ASN B 142 -3.636 16.632 30.415 1.00 70.62 C
ATOM 1173 ND2 ASN B 142 -4.899 16.447 30.039 1.00 67.58 N
ATOM 1174 OD1 ASN B 142 -3.260 16.496 31.585 1.00 64.80 O
ATOM 1175 N ILE B 143 -1.494 16.365 26.045 1.00 61.97 N
ATOM 1176 CA ILE B 143 -0.762 16.973 24.939 1.00 62.84 C
ATOM 1177 C ILE B 143 -1.739 17.630 23.973 1.00 56.99 C
ATOM 1178 O ILE B 143 -2.714 17.009 23.534 1.00 56.16 O
ATOM 1179 CB ILE B 143 0.100 15.914 24.234 1.00 61.12 C
ATOM 1180 CG1 ILE B 143 1.056 15.261 25.234 1.00 67.65 C
ATOM 1181 CG2 ILE B 143 0.850 16.518 23.048 1.00 61.22 C
ATOM 1182 CD1 ILE B 143 2.338 16.043 25.471 1.00 64.22 C
ATOM 1183 N ARG B 144 -1.481 18.952 23.639 1.00 59.10 N
ATOM 1184 CA ARG B 144 -2.265 19.709 22.672 1.00 54.81 C
ATOM 1185 C ARG B 144 -1.715 19.497 21.262 1.00 55.40 C
ATOM 1186 O ARG B 144 -0.513 19.270 21.083 1.00 53.82 O
ATOM 1187 CB ARG B 144 -2.247 21.196 23.013 1.00 55.47 C
ATOM 1188 N PRO B 145 -2.577 19.578 20.248 1.00 50.75 N
ATOM 1189 CA PRO B 145 -2.173 19.168 18.894 1.00 46.95 C
ATOM 1190 C PRO B 145 -1.061 20.025 18.298 1.00 42.16 C
ATOM 1191 O PRO B 145 -1.059 21.250 18.422 1.00 45.27 O
ATOM 1192 CB PRO B 145 -3.472 19.291 18.082 1.00 40.46 C
ATOM 1193 CG PRO B 145 -4.443 20.036 18.960 1.00 45.36 C
ATOM 1194 CD PRO B 145 -4.032 19.770 20.363 1.00 45.98 C
ATOM 1195 N LYS B 146 -0.125 19.356 17.618 1.00 36.30 N
ATOM 1196 CA LYS B 146 1.036 19.976 16.984 1.00 35.55 C
ATOM 1197 C LYS B 146 1.375 19.248 15.686 1.00 32.47 C
ATOM 1198 O LYS B 146 1.393 18.016 15.652 1.00 37.06 O
ATOM 1199 CB LYS B 146 2.250 19.931 17.937 1.00 39.74 C
ATOM 1200 CG LYS B 146 3.189 21.137 17.906 1.00 48.38 C
ATOM 1201 CD LYS B 146 4.207 21.068 19.069 1.00 47.51 C
ATOM 1202 CE LYS B 146 5.285 19.987 18.880 1.00 61.08 C
ATOM 1203 NZ LYS B 146 6.366 20.044 19.934 1.00 57.54 N1+
ATOM 1204 N ALA B 147 1.645 20.003 14.623 1.00 29.66 N
ATOM 1205 CA ALA B 147 2.189 19.431 13.397 1.00 33.98 C
ATOM 1206 C ALA B 147 3.709 19.499 13.470 1.00 37.20 C
ATOM 1207 O ALA B 147 4.269 20.558 13.771 1.00 32.76 O
ATOM 1208 CB ALA B 147 1.696 20.174 12.158 1.00 34.16 C
ATOM 1209 N VAL B 148 4.370 18.366 13.232 1.00 35.42 N
ATOM 1210 CA AVAL B 148 5.823 18.288 13.292 0.52 34.22 C
ATOM 1211 CA BVAL B 148 5.825 18.260 13.313 0.48 34.24 C
ATOM 1212 C VAL B 148 6.310 17.468 12.108 1.00 37.42 C
ATOM 1213 O VAL B 148 5.762 16.404 11.804 1.00 35.66 O
ATOM 1214 CB AVAL B 148 6.306 17.673 14.620 0.52 38.13 C
ATOM 1215 CB BVAL B 148 6.301 17.570 14.611 0.48 38.09 C
ATOM 1216 CG1AVAL B 148 5.572 16.387 14.899 0.52 34.89 C
ATOM 1217 CG1BVAL B 148 7.776 17.879 14.867 0.48 34.65 C
ATOM 1218 CG2AVAL B 148 7.814 17.450 14.596 0.52 34.81 C
ATOM 1219 CG2BVAL B 148 5.453 17.973 15.822 0.48 35.21 C
ATOM 1220 N GLU B 149 7.332 17.965 11.432 1.00 40.42 N
ATOM 1221 CA GLU B 149 7.915 17.204 10.338 1.00 37.44 C
ATOM 1222 C GLU B 149 8.881 16.174 10.915 1.00 34.22 C
ATOM 1223 O GLU B 149 9.708 16.502 11.771 1.00 38.55 O
ATOM 1224 CB GLU B 149 8.642 18.125 9.368 1.00 44.91 C
ATOM 1225 CG GLU B 149 8.406 17.770 7.915 1.00 48.85 C
ATOM 1226 CD GLU B 149 9.136 18.707 6.979 1.00 61.17 C
ATOM 1227 OE1 GLU B 149 8.698 18.834 5.810 1.00 72.61 O
ATOM 1228 OE2 GLU B 149 10.159 19.293 7.408 1.00 60.03 O1-
ATOM 1229 N LYS B 150 8.747 14.925 10.482 1.00 30.65 N
ATOM 1230 CA LYS B 150 9.617 13.852 10.913 1.00 29.25 C
ATOM 1231 C LYS B 150 10.193 13.143 9.703 1.00 33.22 C
ATOM 1232 O LYS B 150 9.620 13.160 8.610 1.00 29.99 O
ATOM 1233 CB LYS B 150 8.887 12.806 11.765 1.00 30.84 C
ATOM 1234 CG LYS B 150 8.132 13.336 12.979 1.00 29.09 C
ATOM 1235 CD LYS B 150 9.067 13.628 14.110 1.00 30.26 C
ATOM 1236 CE LYS B 150 8.296 13.638 15.439 1.00 43.22 C
ATOM 1237 NZ LYS B 150 9.090 14.281 16.516 1.00 39.70 N1+
ATOM 1238 N ILE B 151 11.322 12.484 9.924 1.00 25.08 N
ATOM 1239 CA ILE B 151 11.777 11.459 8.999 1.00 32.56 C
ATOM 1240 C ILE B 151 11.046 10.185 9.366 1.00 29.38 C
ATOM 1241 O ILE B 151 11.120 9.737 10.513 1.00 30.85 O
ATOM 1242 CB ILE B 151 13.299 11.258 9.096 1.00 32.63 C
ATOM 1243 CG1 ILE B 151 14.036 12.589 8.896 1.00 32.36 C
ATOM 1244 CG2 ILE B 151 13.754 10.220 8.069 1.00 25.67 C
ATOM 1245 CD1 ILE B 151 13.949 13.116 7.502 1.00 35.00 C
ATOM 1246 N VAL B 152 10.352 9.585 8.409 1.00 23.00 N
ATOM 1247 CA VAL B 152 9.618 8.355 8.664 1.00 24.12 C
ATOM 1248 C VAL B 152 10.373 7.181 8.057 1.00 22.67 C
ATOM 1249 O VAL B 152 10.766 7.219 6.888 1.00 24.56 O
ATOM 1250 CB VAL B 152 8.178 8.417 8.132 1.00 29.96 C
ATOM 1251 CG1 VAL B 152 7.422 7.236 8.662 1.00 30.32 C
ATOM 1252 CG2 VAL B 152 7.511 9.713 8.584 1.00 33.32 C
ATOM 1253 N PHE B 153 10.526 6.134 8.855 1.00 23.05 N
ATOM 1254 CA PHE B 153 11.247 4.912 8.544 1.00 27.30 C
ATOM 1255 C PHE B 153 10.220 3.795 8.399 1.00 23.76 C
ATOM 1256 O PHE B 153 9.374 3.616 9.282 1.00 25.67 O
ATOM 1257 CB PHE B 153 12.241 4.635 9.689 1.00 24.88 C
ATOM 1258 CG PHE B 153 12.919 3.289 9.639 1.00 22.76 C
ATOM 1259 CD1 PHE B 153 12.230 2.129 9.969 1.00 19.75 C
ATOM 1260 CD2 PHE B 153 14.281 3.197 9.331 1.00 22.81 C
ATOM 1261 CE1 PHE B 153 12.841 0.898 9.938 1.00 25.03 C
ATOM 1262 CE2 PHE B 153 14.919 1.971 9.318 1.00 21.68 C
ATOM 1263 CZ PHE B 153 14.209 0.814 9.626 1.00 26.03 C
ATOM 1264 N PHE B 154 10.278 3.066 7.283 1.00 18.92 N
ATOM 1265 CA PHE B 154 9.500 1.846 7.072 1.00 21.61 C
ATOM 1266 C PHE B 154 10.447 0.758 6.600 1.00 24.86 C
ATOM 1267 O PHE B 154 11.093 0.906 5.561 1.00 23.91 O
ATOM 1268 CB PHE B 154 8.407 2.028 6.009 1.00 23.19 C
ATOM 1269 CG PHE B 154 7.310 2.927 6.415 1.00 28.76 C
ATOM 1270 CD1 PHE B 154 6.315 2.487 7.270 1.00 28.14 C
ATOM 1271 CD2 PHE B 154 7.255 4.222 5.936 1.00 28.57 C
ATOM 1272 CE1 PHE B 154 5.280 3.333 7.633 1.00 34.84 C
ATOM 1273 CE2 PHE B 154 6.208 5.062 6.287 1.00 30.68 C
ATOM 1274 CZ PHE B 154 5.240 4.622 7.136 1.00 26.89 C
ATOM 1275 N SER B 155 10.506 -0.341 7.326 1.00 24.43 N
ATOM 1276 CA SER B 155 11.211 -1.517 6.846 1.00 26.51 C
ATOM 1277 C SER B 155 10.250 -2.696 6.836 1.00 28.82 C
ATOM 1278 O SER B 155 9.285 -2.726 7.597 1.00 30.48 O
ATOM 1279 CB SER B 155 12.423 -1.838 7.720 1.00 27.53 C
ATOM 1280 OG SER B 155 12.004 -2.258 9.015 1.00 30.71 O
ATOM 1281 N ASP B 156 10.516 -3.689 5.985 1.00 25.55 N
ATOM 1282 CA ASP B 156 9.711 -4.898 6.038 1.00 24.29 C
ATOM 1283 C ASP B 156 10.584 -6.096 5.669 1.00 31.27 C
ATOM 1284 O ASP B 156 11.776 -5.963 5.365 1.00 27.31 O
ATOM 1285 CB ASP B 156 8.456 -4.740 5.164 1.00 27.32 C
ATOM 1286 CG ASP B 156 8.697 -5.034 3.697 1.00 31.51 C
ATOM 1287 OD1 ASP B 156 9.712 -4.598 3.116 1.00 38.52 O
ATOM 1288 OD2 ASP B 156 7.834 -5.712 3.113 1.00 41.46 O1-
ATOM 1289 N ILE B 157 9.996 -7.284 5.749 1.00 26.58 N
ATOM 1290 CA ILE B 157 10.727 -8.530 5.574 1.00 25.32 C
ATOM 1291 C ILE B 157 10.496 -9.000 4.150 1.00 26.39 C
ATOM 1292 O ILE B 157 9.351 -9.117 3.723 1.00 27.50 O
ATOM 1293 CB ILE B 157 10.265 -9.598 6.580 1.00 28.83 C
ATOM 1294 CG1 ILE B 157 10.646 -9.195 8.014 1.00 25.00 C
ATOM 1295 CG2 ILE B 157 10.921 -10.946 6.220 1.00 23.39 C
ATOM 1296 CD1 ILE B 157 10.293 -10.248 9.070 1.00 25.90 C
ATOM 1297 N VAL B 158 11.577 -9.264 3.410 1.00 27.42 N
ATOM 1298 CA VAL B 158 11.425 -9.692 2.021 1.00 28.66 C
ATOM 1299 C VAL B 158 10.753 -11.049 1.995 1.00 28.52 C
ATOM 1300 O VAL B 158 11.145 -11.964 2.726 1.00 26.32 O
ATOM 1301 CB VAL B 158 12.776 -9.735 1.308 1.00 28.92 C
ATOM 1302 CG1 VAL B 158 12.588 -10.309 -0.133 1.00 29.22 C
ATOM 1303 CG2 VAL B 158 13.400 -8.341 1.304 1.00 23.24 C
ATOM 1304 N SER B 159 9.675 -11.157 1.215 1.00 27.74 N
ATOM 1305 CA SER B 159 9.028 -12.438 0.978 1.00 30.69 C
ATOM 1306 C SER B 159 8.558 -13.063 2.286 1.00 27.83 C
ATOM 1307 O SER B 159 8.665 -14.268 2.497 1.00 30.08 O
ATOM 1308 CB SER B 159 9.976 -13.369 0.221 1.00 33.67 C
ATOM 1309 OG SER B 159 9.249 -14.301 -0.542 1.00 48.29 O
ATOM 1310 N PHE B 160 8.013 -12.230 3.172 1.00 23.10 N
ATOM 1311 CA PHE B 160 7.592 -12.727 4.471 1.00 29.24 C
ATOM 1312 C PHE B 160 6.563 -13.845 4.368 1.00 28.95 C
ATOM 1313 O PHE B 160 6.554 -14.752 5.206 1.00 30.85 O
ATOM 1314 CB PHE B 160 7.008 -11.601 5.295 1.00 30.27 C
ATOM 1315 CG PHE B 160 6.405 -12.072 6.547 1.00 35.93 C
ATOM 1316 CD1 PHE B 160 7.214 -12.425 7.608 1.00 34.59 C
ATOM 1317 CD2 PHE B 160 5.031 -12.203 6.669 1.00 37.06 C
ATOM 1318 CE1 PHE B 160 6.654 -12.884 8.776 1.00 39.26 C
ATOM 1319 CE2 PHE B 160 4.478 -12.673 7.838 1.00 40.63 C
ATOM 1320 CZ PHE B 160 5.292 -12.999 8.889 1.00 30.95 C
ATOM 1321 N SER B 161 5.680 -13.791 3.365 1.00 29.03 N
ATOM 1322 CA SER B 161 4.638 -14.799 3.244 1.00 37.37 C
ATOM 1323 C SER B 161 5.221 -16.191 3.047 1.00 35.16 C
ATOM 1324 O SER B 161 4.584 -17.177 3.424 1.00 35.48 O
ATOM 1325 CB SER B 161 3.704 -14.444 2.084 1.00 36.26 C
ATOM 1326 OG SER B 161 4.472 -14.112 0.942 1.00 39.65 O
ATOM 1327 N THR B 162 6.430 -16.294 2.469 1.00 30.29 N
ATOM 1328 CA THR B 162 7.069 -17.603 2.307 1.00 31.30 C
ATOM 1329 C THR B 162 7.398 -18.242 3.654 1.00 32.70 C
ATOM 1330 O THR B 162 7.252 -19.456 3.821 1.00 36.81 O
ATOM 1331 CB THR B 162 8.345 -17.483 1.468 1.00 31.83 C
ATOM 1332 CG2 THR B 162 8.891 -18.852 1.111 1.00 35.34 C
ATOM 1333 OG1 THR B 162 8.081 -16.749 0.274 1.00 37.37 O
ATOM 1334 N PHE B 163 7.873 -17.455 4.620 1.00 31.02 N
ATOM 1335 CA PHE B 163 8.110 -18.014 5.949 1.00 33.61 C
ATOM 1336 C PHE B 163 6.840 -18.645 6.504 1.00 36.36 C
ATOM 1337 O PHE B 163 6.831 -19.821 6.898 1.00 30.07 O
ATOM 1338 CB PHE B 163 8.611 -16.931 6.901 1.00 28.07 C
ATOM 1339 CG PHE B 163 9.987 -16.413 6.573 1.00 28.04 C
ATOM 1340 CD1 PHE B 163 10.172 -15.516 5.548 1.00 20.83 C
ATOM 1341 CD2 PHE B 163 11.098 -16.841 7.297 1.00 25.64 C
ATOM 1342 CE1 PHE B 163 11.435 -15.036 5.254 1.00 31.92 C
ATOM 1343 CE2 PHE B 163 12.365 -16.373 7.008 1.00 24.89 C
ATOM 1344 CZ PHE B 163 12.540 -15.471 5.985 1.00 25.72 C
ATOM 1345 N ALA B 164 5.751 -17.867 6.535 1.00 28.67 N
ATOM 1346 CA ALA B 164 4.488 -18.367 7.066 1.00 40.18 C
ATOM 1347 C ALA B 164 4.032 -19.617 6.327 1.00 34.59 C
ATOM 1348 O ALA B 164 3.488 -20.540 6.936 1.00 41.19 O
ATOM 1349 CB ALA B 164 3.419 -17.276 6.984 1.00 39.18 C
ATOM 1350 N GLU B 165 4.272 -19.678 5.021 1.00 35.14 N
ATOM 1351 CA GLU B 165 3.815 -20.824 4.252 1.00 38.46 C
ATOM 1352 C GLU B 165 4.685 -22.056 4.447 1.00 41.63 C
ATOM 1353 O GLU B 165 4.188 -23.175 4.291 1.00 43.08 O
ATOM 1354 CB GLU B 165 3.746 -20.459 2.769 1.00 36.53 C
ATOM 1355 CG GLU B 165 2.510 -19.636 2.413 1.00 43.24 C
ATOM 1356 CD GLU B 165 2.700 -18.760 1.190 1.00 54.32 C
ATOM 1357 OE1 GLU B 165 3.794 -18.802 0.581 1.00 54.34 O
ATOM 1358 OE2 GLU B 165 1.745 -18.024 0.842 1.00 59.86 O1-
ATOM 1359 N LYS B 166 5.965 -21.896 4.778 1.00 35.52 N
ATOM 1360 CA LYS B 166 6.860 -23.044 4.789 1.00 36.13 C
ATOM 1361 C LYS B 166 7.304 -23.492 6.171 1.00 38.54 C
ATOM 1362 O LYS B 166 7.817 -24.608 6.303 1.00 35.38 O
ATOM 1363 CB LYS B 166 8.100 -22.748 3.942 1.00 36.05 C
ATOM 1364 CG LYS B 166 7.756 -22.392 2.533 1.00 38.66 C
ATOM 1365 CD LYS B 166 8.549 -23.207 1.527 1.00 51.94 C
ATOM 1366 CE LYS B 166 8.037 -22.953 0.112 1.00 44.70 C
ATOM 1367 NZ LYS B 166 7.479 -24.197 -0.488 1.00 60.44 N1+
ATOM 1368 N LEU B 167 7.126 -22.672 7.191 1.00 35.38 N
ATOM 1369 CA LEU B 167 7.667 -23.002 8.494 1.00 30.33 C
ATOM 1370 C LEU B 167 6.543 -23.187 9.497 1.00 34.85 C
ATOM 1371 O LEU B 167 5.500 -22.535 9.388 1.00 35.50 O
ATOM 1372 CB LEU B 167 8.589 -21.900 9.028 1.00 36.09 C
ATOM 1373 CG LEU B 167 9.798 -21.436 8.231 1.00 32.51 C
ATOM 1374 CD1 LEU B 167 10.563 -20.383 9.035 1.00 32.44 C
ATOM 1375 CD2 LEU B 167 10.680 -22.642 7.940 1.00 39.43 C
ATOM 1376 N PRO B 168 6.743 -24.024 10.509 1.00 40.11 N
ATOM 1377 CA PRO B 168 5.811 -24.032 11.632 1.00 37.64 C
ATOM 1378 C PRO B 168 5.729 -22.653 12.268 1.00 39.06 C
ATOM 1379 O PRO B 168 6.681 -21.868 12.256 1.00 37.68 O
ATOM 1380 CB PRO B 168 6.409 -25.067 12.589 1.00 42.67 C
ATOM 1381 CG PRO B 168 7.816 -25.220 12.167 1.00 43.44 C
ATOM 1382 CD PRO B 168 7.866 -24.954 10.712 1.00 36.82 C
ATOM 1383 N VAL B 169 4.556 -22.369 12.821 1.00 37.28 N
ATOM 1384 CA VAL B 169 4.216 -21.027 13.269 1.00 30.35 C
ATOM 1385 C VAL B 169 5.163 -20.535 14.358 1.00 33.16 C
ATOM 1386 O VAL B 169 5.500 -19.345 14.404 1.00 31.17 O
ATOM 1387 CB VAL B 169 2.740 -21.034 13.722 1.00 34.04 C
ATOM 1388 CG1 VAL B 169 2.563 -21.938 14.925 1.00 34.81 C
ATOM 1389 CG2 VAL B 169 2.270 -19.643 14.031 1.00 36.71 C
ATOM 1390 N GLU B 170 5.638 -21.431 15.229 1.00 35.75 N
ATOM 1391 CA GLU B 170 6.546 -20.998 16.286 1.00 32.14 C
ATOM 1392 C GLU B 170 7.857 -20.474 15.706 1.00 33.46 C
ATOM 1393 O GLU B 170 8.479 -19.568 16.283 1.00 31.25 O
ATOM 1394 CB GLU B 170 6.811 -22.139 17.276 1.00 39.31 C
ATOM 1395 CG GLU B 170 7.273 -23.454 16.644 1.00 45.65 C
ATOM 1396 CD GLU B 170 6.137 -24.393 16.231 1.00 52.91 C
ATOM 1397 OE1 GLU B 170 4.940 -24.025 16.336 1.00 51.73 O
ATOM 1398 OE2 GLU B 170 6.457 -25.524 15.793 1.00 62.76 O1-
ATOM 1399 N GLU B 171 8.264 -20.999 14.552 1.00 36.31 N
ATOM 1400 CA GLU B 171 9.510 -20.577 13.917 1.00 33.27 C
ATOM 1401 C GLU B 171 9.356 -19.256 13.164 1.00 37.12 C
ATOM 1402 O GLU B 171 10.315 -18.468 13.106 1.00 30.81 O
ATOM 1403 CB GLU B 171 10.006 -21.680 12.979 1.00 36.04 C
ATOM 1404 CG GLU B 171 10.767 -22.793 13.718 1.00 43.66 C
ATOM 1405 CD GLU B 171 11.226 -23.923 12.809 1.00 61.87 C
ATOM 1406 OE1 GLU B 171 11.105 -25.096 13.220 1.00 70.97 O
ATOM 1407 OE2 GLU B 171 11.759 -23.644 11.707 1.00 55.71 O1-
ATOM 1408 N VAL B 172 8.177 -19.008 12.573 1.00 28.24 N
ATOM 1409 CA VAL B 172 7.863 -17.686 12.026 1.00 30.76 C
ATOM 1410 C VAL B 172 7.957 -16.631 13.114 1.00 27.17 C
ATOM 1411 O VAL B 172 8.569 -15.568 12.934 1.00 31.10 O
ATOM 1412 CB VAL B 172 6.458 -17.675 11.384 1.00 34.91 C
ATOM 1413 CG1 VAL B 172 6.170 -16.317 10.799 1.00 28.02 C
ATOM 1414 CG2 VAL B 172 6.312 -18.746 10.314 1.00 27.82 C
ATOM 1415 N VAL B 173 7.304 -16.884 14.247 1.00 26.57 N
ATOM 1416 CA VAL B 173 7.391 -15.940 15.352 1.00 24.82 C
ATOM 1417 C VAL B 173 8.849 -15.705 15.732 1.00 25.92 C
ATOM 1418 O VAL B 173 9.265 -14.570 15.989 1.00 29.96 O
ATOM 1419 CB VAL B 173 6.561 -16.450 16.542 1.00 27.05 C
ATOM 1420 CG1 VAL B 173 6.972 -15.744 17.842 1.00 27.79 C
ATOM 1421 CG2 VAL B 173 5.096 -16.226 16.255 1.00 31.13 C
ATOM 1422 N SER B 174 9.646 -16.771 15.789 1.00 27.99 N
ATOM 1423 CA SER B 174 11.042 -16.602 16.167 1.00 30.16 C
ATOM 1424 C SER B 174 11.764 -15.684 15.185 1.00 28.57 C
ATOM 1425 O SER B 174 12.494 -14.775 15.600 1.00 29.08 O
ATOM 1426 CB SER B 174 11.729 -17.963 16.250 1.00 35.62 C
ATOM 1427 OG SER B 174 13.081 -17.811 16.639 1.00 36.90 O
ATOM 1428 N VAL B 175 11.517 -15.858 13.879 1.00 26.80 N
ATOM 1429 CA VAL B 175 12.164 -15.005 12.877 1.00 27.02 C
ATOM 1430 C VAL B 175 11.695 -13.558 12.998 1.00 28.37 C
ATOM 1431 O VAL B 175 12.505 -12.629 12.946 1.00 24.74 O
ATOM 1432 CB VAL B 175 11.922 -15.553 11.462 1.00 26.82 C
ATOM 1433 CG1 VAL B 175 12.373 -14.546 10.419 1.00 28.65 C
ATOM 1434 CG2 VAL B 175 12.687 -16.856 11.290 1.00 31.70 C
ATOM 1435 N VAL B 176 10.384 -13.323 13.121 1.00 26.94 N
ATOM 1436 CA VAL B 176 9.949 -11.928 13.145 1.00 25.31 C
ATOM 1437 C VAL B 176 10.474 -11.246 14.396 1.00 25.02 C
ATOM 1438 O VAL B 176 10.837 -10.070 14.369 1.00 28.24 O
ATOM 1439 CB VAL B 176 8.414 -11.805 13.015 1.00 34.97 C
ATOM 1440 CG1 VAL B 176 7.910 -12.594 11.846 1.00 29.07 C
ATOM 1441 CG2 VAL B 176 7.702 -12.211 14.279 1.00 27.50 C
ATOM 1442 N ASN B 177 10.552 -11.985 15.509 1.00 31.08 N
ATOM 1443 CA ASN B 177 11.085 -11.411 16.741 1.00 31.20 C
ATOM 1444 C ASN B 177 12.553 -11.045 16.590 1.00 26.86 C
ATOM 1445 O ASN B 177 12.984 -9.994 17.070 1.00 31.04 O
ATOM 1446 CB ASN B 177 10.897 -12.381 17.909 1.00 33.42 C
ATOM 1447 CG ASN B 177 9.467 -12.414 18.422 1.00 33.50 C
ATOM 1448 ND2 ASN B 177 9.238 -13.220 19.456 1.00 31.72 N
ATOM 1449 OD1 ASN B 177 8.580 -11.721 17.908 1.00 30.95 O
ATOM 1450 N SER B 178 13.344 -11.917 15.959 1.00 27.49 N
ATOM 1451 CA SER B 178 14.742 -11.582 15.706 1.00 29.02 C
ATOM 1452 C SER B 178 14.839 -10.323 14.858 1.00 30.51 C
ATOM 1453 O SER B 178 15.712 -9.477 15.082 1.00 24.98 O
ATOM 1454 CB SER B 178 15.461 -12.734 15.004 1.00 27.99 C
ATOM 1455 OG SER B 178 15.632 -13.852 15.854 1.00 31.45 O
ATOM 1456 N TYR B 179 13.936 -10.187 13.879 1.00 26.33 N
ATOM 1457 CA TYR B 179 13.920 -9.024 13.000 1.00 19.06 C
ATOM 1458 C TYR B 179 13.519 -7.775 13.756 1.00 26.44 C
ATOM 1459 O TYR B 179 14.214 -6.754 13.698 1.00 26.95 O
ATOM 1460 CB TYR B 179 12.948 -9.274 11.844 1.00 22.35 C
ATOM 1461 CG TYR B 179 12.764 -8.095 10.928 1.00 24.30 C
ATOM 1462 CD1 TYR B 179 13.806 -7.665 10.141 1.00 24.61 C
ATOM 1463 CD2 TYR B 179 11.552 -7.425 10.846 1.00 30.72 C
ATOM 1464 CE1 TYR B 179 13.668 -6.606 9.297 1.00 35.22 C
ATOM 1465 CE2 TYR B 179 11.405 -6.339 9.979 1.00 31.09 C
ATOM 1466 CZ TYR B 179 12.472 -5.951 9.218 1.00 22.20 C
ATOM 1467 OH TYR B 179 12.405 -4.881 8.351 1.00 38.06 O
ATOM 1468 N PHE B 180 12.389 -7.831 14.472 1.00 21.94 N
ATOM 1469 CA PHE B 180 11.962 -6.658 15.228 1.00 22.55 C
ATOM 1470 C PHE B 180 13.008 -6.252 16.255 1.00 24.57 C
ATOM 1471 O PHE B 180 13.179 -5.060 16.521 1.00 26.51 O
ATOM 1472 CB PHE B 180 10.630 -6.921 15.938 1.00 27.30 C
ATOM 1473 CG PHE B 180 9.440 -6.935 15.035 1.00 30.92 C
ATOM 1474 CD1 PHE B 180 9.428 -6.227 13.850 1.00 29.99 C
ATOM 1475 CD2 PHE B 180 8.330 -7.682 15.369 1.00 26.31 C
ATOM 1476 CE1 PHE B 180 8.305 -6.243 13.016 1.00 30.81 C
ATOM 1477 CE2 PHE B 180 7.207 -7.700 14.544 1.00 32.56 C
ATOM 1478 CZ PHE B 180 7.202 -6.980 13.367 1.00 28.39 C
ATOM 1479 N SER B 181 13.729 -7.214 16.833 1.00 28.16 N
ATOM 1480 CA SER B 181 14.719 -6.850 17.848 1.00 28.14 C
ATOM 1481 C SER B 181 15.883 -6.081 17.233 1.00 26.63 C
ATOM 1482 O SER B 181 16.345 -5.081 17.800 1.00 25.12 O
ATOM 1483 CB SER B 181 15.230 -8.105 18.550 1.00 33.99 C
ATOM 1484 OG SER B 181 14.208 -8.661 19.359 1.00 38.54 O
ATOM 1485 N VAL B 182 16.368 -6.539 16.073 1.00 23.67 N
ATOM 1486 CA VAL B 182 17.497 -5.882 15.408 1.00 26.02 C
ATOM 1487 C VAL B 182 17.121 -4.456 15.055 1.00 27.02 C
ATOM 1488 O VAL B 182 17.849 -3.504 15.361 1.00 25.65 O
ATOM 1489 CB VAL B 182 17.927 -6.672 14.152 1.00 25.95 C
ATOM 1490 CG1 VAL B 182 18.872 -5.824 13.251 1.00 27.02 C
ATOM 1491 CG2 VAL B 182 18.592 -7.968 14.528 1.00 28.45 C
ATOM 1492 N CYS B 183 15.952 -4.293 14.428 1.00 24.71 N
ATOM 1493 CA CYS B 183 15.508 -2.971 14.001 1.00 25.23 C
ATOM 1494 C CYS B 183 15.357 -2.048 15.193 1.00 23.35 C
ATOM 1495 O CYS B 183 15.892 -0.933 15.198 1.00 29.23 O
ATOM 1496 CB CYS B 183 14.184 -3.081 13.231 1.00 23.18 C
ATOM 1497 SG CYS B 183 14.369 -4.002 11.650 1.00 24.66 S
ATOM 1498 N THR B 184 14.645 -2.509 16.228 1.00 23.13 N
ATOM 1499 CA THR B 184 14.307 -1.640 17.351 1.00 25.76 C
ATOM 1500 C THR B 184 15.552 -1.160 18.099 1.00 26.37 C
ATOM 1501 O THR B 184 15.662 0.032 18.436 1.00 28.72 O
ATOM 1502 CB THR B 184 13.340 -2.374 18.290 1.00 26.24 C
ATOM 1503 CG2 THR B 184 13.035 -1.517 19.506 1.00 35.48 C
ATOM 1504 OG1 THR B 184 12.118 -2.659 17.580 1.00 29.54 O
ATOM 1505 N ALA B 185 16.509 -2.062 18.344 1.00 27.44 N
ATOM 1506 CA ALA B 185 17.739 -1.680 19.049 1.00 31.04 C
ATOM 1507 C ALA B 185 18.526 -0.627 18.278 1.00 24.33 C
ATOM 1508 O ALA B 185 18.981 0.365 18.856 1.00 26.84 O
ATOM 1509 CB ALA B 185 18.617 -2.903 19.292 1.00 31.18 C
ATOM 1510 N ILE B 186 18.656 -0.798 16.960 1.00 25.88 N
ATOM 1511 CA ILE B 186 19.469 0.134 16.184 1.00 27.61 C
ATOM 1512 C ILE B 186 18.771 1.482 16.034 1.00 27.87 C
ATOM 1513 O ILE B 186 19.409 2.538 16.154 1.00 26.74 O
ATOM 1514 CB ILE B 186 19.835 -0.486 14.826 1.00 25.83 C
ATOM 1515 CG1 ILE B 186 20.782 -1.666 15.039 1.00 29.50 C
ATOM 1516 CG2 ILE B 186 20.530 0.533 13.927 1.00 25.01 C
ATOM 1517 CD1 ILE B 186 21.126 -2.373 13.757 1.00 27.79 C
ATOM 1518 N ILE B 187 17.462 1.478 15.746 1.00 24.48 N
ATOM 1519 CA ILE B 187 16.714 2.737 15.643 1.00 24.84 C
ATOM 1520 C ILE B 187 16.820 3.532 16.941 1.00 24.93 C
ATOM 1521 O ILE B 187 17.080 4.745 16.936 1.00 26.31 O
ATOM 1522 CB ILE B 187 15.245 2.460 15.274 1.00 27.13 C
ATOM 1523 CG1 ILE B 187 15.142 2.044 13.812 1.00 22.31 C
ATOM 1524 CG2 ILE B 187 14.360 3.701 15.518 1.00 27.27 C
ATOM 1525 CD1 ILE B 187 13.802 1.433 13.486 1.00 22.72 C
ATOM 1526 N THR B 188 16.636 2.851 18.074 1.00 23.59 N
ATOM 1527 CA THR B 188 16.738 3.515 19.372 1.00 30.08 C
ATOM 1528 C THR B 188 18.147 4.032 19.616 1.00 30.22 C
ATOM 1529 O THR B 188 18.332 5.178 20.035 1.00 30.24 O
ATOM 1530 CB THR B 188 16.329 2.551 20.481 1.00 31.28 C
ATOM 1531 CG2 THR B 188 16.376 3.248 21.828 1.00 41.55 C
ATOM 1532 OG1 THR B 188 15.003 2.075 20.224 1.00 30.22 O
ATOM 1533 N ARG B 189 19.160 3.202 19.343 1.00 27.31 N
ATOM 1534 CA ARG B 189 20.542 3.657 19.468 1.00 32.48 C
ATOM 1535 C ARG B 189 20.771 4.938 18.678 1.00 32.90 C
ATOM 1536 O ARG B 189 21.517 5.825 19.118 1.00 30.42 O
ATOM 1537 CB ARG B 189 21.502 2.555 19.004 1.00 37.57 C
ATOM 1538 CG ARG B 189 22.939 2.807 19.386 1.00 42.17 C
ATOM 1539 CD ARG B 189 23.907 2.543 18.254 1.00 53.04 C
ATOM 1540 NE ARG B 189 23.900 1.159 17.787 1.00 53.88 N
ATOM 1541 CZ ARG B 189 23.994 0.802 16.510 1.00 49.20 C
ATOM 1542 NH1 ARG B 189 23.959 1.700 15.533 1.00 46.86 N1+
ATOM 1543 NH2 ARG B 189 24.138 -0.485 16.205 1.00 51.19 N
ATOM 1544 N GLN B 190 20.122 5.066 17.516 1.00 27.15 N
ATOM 1545 CA GLN B 190 20.360 6.198 16.627 1.00 25.59 C
ATOM 1546 C GLN B 190 19.437 7.376 16.907 1.00 26.35 C
ATOM 1547 O GLN B 190 19.445 8.360 16.152 1.00 30.23 O
ATOM 1548 CB GLN B 190 20.226 5.748 15.174 1.00 29.47 C
ATOM 1549 CG GLN B 190 21.422 4.894 14.710 1.00 26.43 C
ATOM 1550 CD GLN B 190 22.726 5.678 14.646 1.00 38.38 C
ATOM 1551 NE2 GLN B 190 23.842 4.968 14.775 1.00 39.36 N
ATOM 1552 OE1 GLN B 190 22.732 6.900 14.482 1.00 33.53 O
ATOM 1553 N GLY B 191 18.673 7.315 17.990 1.00 29.06 N
ATOM 1554 CA GLY B 191 17.854 8.424 18.423 1.00 28.84 C
ATOM 1555 C GLY B 191 16.477 8.480 17.813 1.00 32.26 C
ATOM 1556 O GLY B 191 15.784 9.489 17.982 1.00 34.06 O
ATOM 1557 N GLY B 192 16.070 7.455 17.073 1.00 31.31 N
ATOM 1558 CA GLY B 192 14.719 7.381 16.570 1.00 28.72 C
ATOM 1559 C GLY B 192 13.842 6.634 17.538 1.00 33.15 C
ATOM 1560 O GLY B 192 14.285 6.129 18.564 1.00 30.80 O
ATOM 1561 N GLU B 193 12.565 6.540 17.198 1.00 29.74 N
ATOM 1562 CA GLU B 193 11.658 5.757 18.029 1.00 37.37 C
ATOM 1563 C GLU B 193 10.731 4.936 17.145 1.00 33.54 C
ATOM 1564 O GLU B 193 10.189 5.446 16.158 1.00 27.09 O
ATOM 1565 CB GLU B 193 10.848 6.652 18.982 1.00 34.87 C
ATOM 1566 CG GLU B 193 9.786 7.538 18.325 1.00 47.47 C
ATOM 1567 CD GLU B 193 9.500 8.836 19.107 1.00 69.79 C
ATOM 1568 OE1 GLU B 193 8.513 8.865 19.877 1.00 73.45 O
ATOM 1569 OE2 GLU B 193 10.256 9.826 18.947 1.00 70.49 O1-
ATOM 1570 N VAL B 194 10.560 3.665 17.494 1.00 25.01 N
ATOM 1571 CA VAL B 194 9.611 2.810 16.794 1.00 28.53 C
ATOM 1572 C VAL B 194 8.210 3.174 17.274 1.00 36.34 C
ATOM 1573 O VAL B 194 7.953 3.229 18.484 1.00 32.29 O
ATOM 1574 CB VAL B 194 9.934 1.322 17.045 1.00 31.16 C
ATOM 1575 CG1 VAL B 194 8.779 0.424 16.598 1.00 30.52 C
ATOM 1576 CG2 VAL B 194 11.208 0.914 16.319 1.00 29.44 C
ATOM 1577 N THR B 195 7.308 3.477 16.338 1.00 33.44 N
ATOM 1578 CA THR B 195 5.944 3.820 16.714 1.00 29.67 C
ATOM 1579 C THR B 195 4.984 2.663 16.599 1.00 35.70 C
ATOM 1580 O THR B 195 4.047 2.587 17.392 1.00 33.41 O
ATOM 1581 CB THR B 195 5.390 4.974 15.878 1.00 43.62 C
ATOM 1582 CG2 THR B 195 6.056 6.216 16.276 1.00 35.62 C
ATOM 1583 OG1 THR B 195 5.608 4.721 14.483 1.00 42.98 O
ATOM 1584 N LYS B 196 5.189 1.758 15.647 1.00 32.23 N
ATOM 1585 CA LYS B 196 4.349 0.574 15.610 1.00 35.81 C
ATOM 1586 C LYS B 196 4.908 -0.433 14.622 1.00 30.73 C
ATOM 1587 O LYS B 196 5.721 -0.110 13.759 1.00 27.75 O
ATOM 1588 CB LYS B 196 2.905 0.915 15.238 1.00 39.10 C
ATOM 1589 CG LYS B 196 2.752 1.635 13.936 1.00 30.38 C
ATOM 1590 CD LYS B 196 1.337 2.239 13.826 1.00 41.15 C
ATOM 1591 CE LYS B 196 1.047 3.196 14.978 1.00 36.91 C
ATOM 1592 NZ LYS B 196 -0.280 3.858 14.898 1.00 34.65 N1+
ATOM 1593 N PHE B 197 4.446 -1.659 14.776 1.00 25.29 N
ATOM 1594 CA PHE B 197 4.596 -2.710 13.794 1.00 28.12 C
ATOM 1595 C PHE B 197 3.290 -2.821 13.019 1.00 32.60 C
ATOM 1596 O PHE B 197 2.212 -2.875 13.619 1.00 30.57 O
ATOM 1597 CB PHE B 197 4.927 -4.035 14.481 1.00 26.92 C
ATOM 1598 CG PHE B 197 6.132 -3.964 15.383 1.00 33.09 C
ATOM 1599 CD1 PHE B 197 7.313 -3.355 14.951 1.00 29.29 C
ATOM 1600 CD2 PHE B 197 6.078 -4.477 16.670 1.00 32.59 C
ATOM 1601 CE1 PHE B 197 8.433 -3.280 15.796 1.00 32.35 C
ATOM 1602 CE2 PHE B 197 7.187 -4.401 17.513 1.00 37.08 C
ATOM 1603 CZ PHE B 197 8.360 -3.810 17.073 1.00 34.18 C
ATOM 1604 N ILE B 198 3.386 -2.821 11.699 1.00 30.42 N
ATOM 1605 CA ILE B 198 2.243 -3.062 10.824 1.00 31.06 C
ATOM 1606 C ILE B 198 2.554 -4.367 10.110 1.00 28.71 C
ATOM 1607 O ILE B 198 3.326 -4.375 9.146 1.00 25.64 O
ATOM 1608 CB ILE B 198 2.028 -1.920 9.827 1.00 35.68 C
ATOM 1609 CG1 ILE B 198 1.998 -0.565 10.534 1.00 33.53 C
ATOM 1610 CG2 ILE B 198 0.754 -2.138 9.041 1.00 29.86 C
ATOM 1611 CD1 ILE B 198 2.481 0.568 9.621 1.00 30.79 C
ATOM 1612 N GLY B 199 1.991 -5.468 10.590 1.00 27.16 N
ATOM 1613 CA GLY B 199 2.445 -6.764 10.125 1.00 25.92 C
ATOM 1614 C GLY B 199 3.954 -6.894 10.316 1.00 28.41 C
ATOM 1615 O GLY B 199 4.500 -6.591 11.382 1.00 23.19 O
ATOM 1616 N ASP B 200 4.652 -7.336 9.277 1.00 29.11 N
ATOM 1617 CA ASP B 200 6.110 -7.432 9.344 1.00 24.45 C
ATOM 1618 C ASP B 200 6.794 -6.101 9.098 1.00 27.72 C
ATOM 1619 O ASP B 200 8.024 -6.061 8.985 1.00 28.26 O
ATOM 1620 CB ASP B 200 6.627 -8.459 8.331 1.00 26.52 C
ATOM 1621 CG ASP B 200 6.264 -8.097 6.910 1.00 30.72 C
ATOM 1622 OD1 ASP B 200 5.079 -7.889 6.635 1.00 27.74 O
ATOM 1623 OD2 ASP B 200 7.169 -8.013 6.063 1.00 30.06 O1-
ATOM 1624 N CYS B 201 6.040 -5.016 8.995 1.00 26.01 N
ATOM 1625 CA CYS B 201 6.616 -3.701 8.750 1.00 24.53 C
ATOM 1626 C CYS B 201 6.903 -2.959 10.055 1.00 29.67 C
ATOM 1627 O CYS B 201 6.032 -2.836 10.925 1.00 28.41 O
ATOM 1628 CB CYS B 201 5.685 -2.876 7.866 1.00 28.48 C
ATOM 1629 SG CYS B 201 6.210 -1.183 7.753 1.00 35.16 S
ATOM 1630 N VAL B 202 8.135 -2.478 10.188 1.00 24.28 N
ATOM 1631 CA VAL B 202 8.551 -1.623 11.293 1.00 27.93 C
ATOM 1632 C VAL B 202 8.387 -0.174 10.861 1.00 25.18 C
ATOM 1633 O VAL B 202 8.972 0.241 9.857 1.00 26.50 O
ATOM 1634 CB VAL B 202 10.012 -1.907 11.689 1.00 28.29 C
ATOM 1635 CG1 VAL B 202 10.493 -0.899 12.687 1.00 26.12 C
ATOM 1636 CG2 VAL B 202 10.151 -3.312 12.253 1.00 27.60 C
ATOM 1637 N MET B 203 7.618 0.604 11.625 1.00 24.12 N
ATOM 1638 CA MET B 203 7.420 2.029 11.375 1.00 21.03 C
ATOM 1639 C MET B 203 8.089 2.850 12.478 1.00 24.25 C
ATOM 1640 O MET B 203 7.875 2.590 13.666 1.00 27.31 O
ATOM 1641 CB MET B 203 5.923 2.370 11.316 1.00 25.66 C
ATOM 1642 CG MET B 203 5.638 3.849 11.046 1.00 26.00 C
ATOM 1643 SD MET B 203 3.821 4.188 11.039 1.00 34.47 S
ATOM 1644 CE MET B 203 3.856 5.969 11.043 1.00 34.25 C
ATOM 1645 N ALA B 204 8.859 3.869 12.095 1.00 22.08 N
ATOM 1646 CA ALA B 204 9.617 4.617 13.089 1.00 24.64 C
ATOM 1647 C ALA B 204 9.751 6.066 12.651 1.00 25.61 C
ATOM 1648 O ALA B 204 9.608 6.411 11.475 1.00 25.04 O
ATOM 1649 CB ALA B 204 11.011 4.011 13.325 1.00 22.57 C
ATOM 1650 N TYR B 205 10.014 6.912 13.624 1.00 20.77 N
ATOM 1651 CA TYR B 205 10.214 8.327 13.394 1.00 25.04 C
ATOM 1652 C TYR B 205 11.614 8.707 13.811 1.00 26.05 C
ATOM 1653 O TYR B 205 12.122 8.207 14.810 1.00 25.23 O
ATOM 1654 CB TYR B 205 9.246 9.173 14.210 1.00 28.03 C
ATOM 1655 CG TYR B 205 7.806 9.062 13.808 1.00 31.89 C
ATOM 1656 CD1 TYR B 205 7.438 8.953 12.476 1.00 28.94 C
ATOM 1657 CD2 TYR B 205 6.805 9.041 14.775 1.00 34.59 C
ATOM 1658 CE1 TYR B 205 6.081 8.852 12.106 1.00 30.22 C
ATOM 1659 CE2 TYR B 205 5.459 8.935 14.424 1.00 35.86 C
ATOM 1660 CZ TYR B 205 5.111 8.830 13.090 1.00 38.09 C
ATOM 1661 OH TYR B 205 3.789 8.719 12.752 1.00 40.00 O
ATOM 1662 N PHE B 206 12.208 9.608 13.056 1.00 28.61 N
ATOM 1663 CA PHE B 206 13.369 10.372 13.466 1.00 28.98 C
ATOM 1664 C PHE B 206 12.965 11.840 13.423 1.00 31.98 C
ATOM 1665 O PHE B 206 12.078 12.207 12.657 1.00 32.17 O
ATOM 1666 CB PHE B 206 14.565 10.096 12.533 1.00 25.52 C
ATOM 1667 CG PHE B 206 15.165 8.726 12.700 1.00 23.83 C
ATOM 1668 CD1 PHE B 206 14.600 7.616 12.079 1.00 23.92 C
ATOM 1669 CD2 PHE B 206 16.303 8.547 13.486 1.00 26.42 C
ATOM 1670 CE1 PHE B 206 15.161 6.351 12.241 1.00 23.94 C
ATOM 1671 CE2 PHE B 206 16.867 7.274 13.653 1.00 28.24 C
ATOM 1672 CZ PHE B 206 16.298 6.183 13.027 1.00 25.05 C
ATOM 1673 N ASP B 207 13.585 12.675 14.264 1.00 30.83 N
ATOM 1674 CA ASP B 207 13.369 14.117 14.181 1.00 34.63 C
ATOM 1675 C ASP B 207 13.624 14.608 12.760 1.00 34.25 C
ATOM 1676 O ASP B 207 14.438 14.045 12.028 1.00 35.14 O
ATOM 1677 CB ASP B 207 14.296 14.866 15.144 1.00 39.73 C
ATOM 1678 CG ASP B 207 13.910 14.679 16.604 1.00 44.93 C
ATOM 1679 OD1 ASP B 207 12.768 14.245 16.868 1.00 45.90 O
ATOM 1680 OD2 ASP B 207 14.750 14.980 17.491 1.00 55.19 O1-
ATOM 1681 N GLY B 208 12.921 15.675 12.363 1.00 32.45 N
ATOM 1682 CA GLY B 208 12.995 16.126 10.984 1.00 30.35 C
ATOM 1683 C GLY B 208 14.380 16.550 10.537 1.00 37.68 C
ATOM 1684 O GLY B 208 14.665 16.547 9.335 1.00 41.92 O
ATOM 1685 N ASP B 209 15.249 16.915 11.473 1.00 38.93 N
ATOM 1686 CA ASP B 209 16.613 17.297 11.149 1.00 39.26 C
ATOM 1687 C ASP B 209 17.610 16.157 11.346 1.00 39.60 C
ATOM 1688 O ASP B 209 18.819 16.385 11.244 1.00 44.18 O
ATOM 1689 CB ASP B 209 17.026 18.524 11.976 1.00 42.37 C
ATOM 1690 CG ASP B 209 17.161 18.225 13.468 1.00 52.76 C
ATOM 1691 OD1 ASP B 209 16.369 17.421 14.011 1.00 57.51 O
ATOM 1692 OD2 ASP B 209 18.063 18.807 14.110 1.00 63.69 O1-
ATOM 1693 N CYS B 210 17.146 14.929 11.572 1.00 36.31 N
ATOM 1694 CA CYS B 210 18.047 13.817 11.862 1.00 32.17 C
ATOM 1695 C CYS B 210 18.099 12.783 10.742 1.00 29.36 C
ATOM 1696 O CYS B 210 18.199 11.584 10.998 1.00 25.96 O
ATOM 1697 CB CYS B 210 17.678 13.147 13.177 1.00 33.41 C
ATOM 1698 SG CYS B 210 18.018 14.155 14.617 1.00 43.79 S
ATOM 1699 N ALA B 211 18.077 13.243 9.489 1.00 29.04 N
ATOM 1700 CA ALA B 211 18.148 12.319 8.360 1.00 34.11 C
ATOM 1701 C ALA B 211 19.442 11.520 8.378 1.00 25.00 C
ATOM 1702 O ALA B 211 19.455 10.347 7.996 1.00 24.27 O
ATOM 1703 CB ALA B 211 18.028 13.075 7.031 1.00 25.41 C
ATOM 1704 N ASP B 212 20.541 12.150 8.794 1.00 25.07 N
ATOM 1705 CA ASP B 212 21.820 11.445 8.862 1.00 31.52 C
ATOM 1706 C ASP B 212 21.723 10.231 9.771 1.00 25.58 C
ATOM 1707 O ASP B 212 22.269 9.169 9.460 1.00 27.49 O
ATOM 1708 CB ASP B 212 22.914 12.388 9.348 1.00 32.37 C
ATOM 1709 CG ASP B 212 23.248 13.453 8.334 1.00 35.11 C
ATOM 1710 OD1 ASP B 212 23.565 13.096 7.184 1.00 36.68 O
ATOM 1711 OD2 ASP B 212 23.186 14.654 8.683 1.00 40.11 O1-
ATOM 1712 N GLN B 213 20.995 10.366 10.887 1.00 26.68 N
ATOM 1713 CA GLN B 213 20.836 9.270 11.833 1.00 23.67 C
ATOM 1714 C GLN B 213 19.926 8.190 11.269 1.00 26.08 C
ATOM 1715 O GLN B 213 20.141 6.995 11.501 1.00 28.69 O
ATOM 1716 CB GLN B 213 20.258 9.802 13.152 1.00 23.69 C
ATOM 1717 CG GLN B 213 21.275 10.509 14.067 1.00 31.84 C
ATOM 1718 CD GLN B 213 21.829 11.776 13.461 1.00 41.74 C
ATOM 1719 NE2 GLN B 213 23.159 11.872 13.418 1.00 37.94 N
ATOM 1720 OE1 GLN B 213 21.076 12.664 13.020 1.00 39.85 O
ATOM 1721 N ALA B 214 18.871 8.596 10.568 1.00 25.76 N
ATOM 1722 CA ALA B 214 17.991 7.618 9.935 1.00 25.11 C
ATOM 1723 C ALA B 214 18.731 6.824 8.862 1.00 22.80 C
ATOM 1724 O ALA B 214 18.526 5.614 8.733 1.00 25.05 O
ATOM 1725 CB ALA B 214 16.763 8.315 9.342 1.00 20.66 C
ATOM 1726 N ILE B 215 19.588 7.483 8.078 1.00 20.55 N
ATOM 1727 CA ILE B 215 20.373 6.748 7.088 1.00 21.73 C
ATOM 1728 C ILE B 215 21.355 5.806 7.772 1.00 23.88 C
ATOM 1729 O ILE B 215 21.497 4.637 7.381 1.00 22.46 O
ATOM 1730 CB ILE B 215 21.091 7.714 6.128 1.00 24.35 C
ATOM 1731 CG1 ILE B 215 20.067 8.439 5.229 1.00 25.63 C
ATOM 1732 CG2 ILE B 215 22.073 6.950 5.230 1.00 21.65 C
ATOM 1733 CD1 ILE B 215 20.631 9.724 4.571 1.00 24.22 C
ATOM 1734 N GLN B 216 22.042 6.288 8.805 1.00 26.46 N
ATOM 1735 CA GLN B 216 22.989 5.426 9.506 1.00 27.82 C
ATOM 1736 C GLN B 216 22.272 4.241 10.123 1.00 24.13 C
ATOM 1737 O GLN B 216 22.746 3.104 10.040 1.00 24.72 O
ATOM 1738 CB GLN B 216 23.729 6.213 10.593 1.00 21.92 C
ATOM 1739 CG GLN B 216 24.880 5.450 11.191 1.00 27.00 C
ATOM 1740 CD GLN B 216 25.976 5.254 10.167 1.00 31.64 C
ATOM 1741 NE2 GLN B 216 26.111 4.034 9.675 1.00 29.36 N
ATOM 1742 OE1 GLN B 216 26.659 6.210 9.783 1.00 35.10 O
ATOM 1743 N ALA B 217 21.122 4.489 10.752 1.00 22.47 N
ATOM 1744 CA ALA B 217 20.339 3.384 11.299 1.00 23.86 C
ATOM 1745 C ALA B 217 19.997 2.365 10.226 1.00 20.94 C
ATOM 1746 O ALA B 217 20.121 1.158 10.452 1.00 22.07 O
ATOM 1747 CB ALA B 217 19.069 3.909 11.972 1.00 20.67 C
ATOM 1748 N SER B 218 19.589 2.825 9.042 1.00 18.84 N
ATOM 1749 CA SER B 218 19.246 1.897 7.962 1.00 21.05 C
ATOM 1750 C SER B 218 20.440 1.052 7.548 1.00 22.42 C
ATOM 1751 O SER B 218 20.329 -0.171 7.381 1.00 20.27 O
ATOM 1752 CB SER B 218 18.718 2.685 6.763 1.00 20.16 C
ATOM 1753 OG SER B 218 17.559 3.424 7.135 1.00 22.77 O
ATOM 1754 N LEU B 219 21.590 1.696 7.346 1.00 20.58 N
ATOM 1755 CA LEU B 219 22.792 0.954 6.981 1.00 26.78 C
ATOM 1756 C LEU B 219 23.173 -0.035 8.072 1.00 22.03 C
ATOM 1757 O LEU B 219 23.524 -1.187 7.783 1.00 25.90 O
ATOM 1758 CB LEU B 219 23.927 1.937 6.699 1.00 23.98 C
ATOM 1759 CG LEU B 219 23.650 2.756 5.431 1.00 27.86 C
ATOM 1760 CD1 LEU B 219 24.623 3.921 5.295 1.00 28.05 C
ATOM 1761 CD2 LEU B 219 23.713 1.860 4.209 1.00 27.04 C
ATOM 1762 N ASP B 220 23.116 0.396 9.339 1.00 24.11 N
ATOM 1763 CA ASP B 220 23.486 -0.491 10.434 1.00 26.51 C
ATOM 1764 C ASP B 220 22.560 -1.699 10.494 1.00 25.16 C
ATOM 1765 O ASP B 220 23.013 -2.827 10.723 1.00 23.51 O
ATOM 1766 CB ASP B 220 23.473 0.266 11.765 1.00 29.48 C
ATOM 1767 CG ASP B 220 24.677 1.194 11.921 1.00 33.03 C
ATOM 1768 OD1 ASP B 220 25.569 1.178 11.037 1.00 35.13 O
ATOM 1769 OD2 ASP B 220 24.720 1.955 12.910 1.00 35.24 O1-
ATOM 1770 N ILE B 221 21.265 -1.497 10.240 1.00 24.16 N
ATOM 1771 CA ILE B 221 20.344 -2.630 10.239 1.00 24.32 C
ATOM 1772 C ILE B 221 20.715 -3.611 9.139 1.00 20.36 C
ATOM 1773 O ILE B 221 20.755 -4.828 9.353 1.00 24.65 O
ATOM 1774 CB ILE B 221 18.887 -2.146 10.098 1.00 22.60 C
ATOM 1775 CG1 ILE B 221 18.451 -1.456 11.389 1.00 20.42 C
ATOM 1776 CG2 ILE B 221 17.979 -3.319 9.805 1.00 21.44 C
ATOM 1777 CD1 ILE B 221 17.015 -0.881 11.300 1.00 25.27 C
ATOM 1778 N LEU B 222 20.975 -3.097 7.942 1.00 21.25 N
ATOM 1779 CA LEU B 222 21.337 -3.971 6.840 1.00 25.46 C
ATOM 1780 C LEU B 222 22.627 -4.714 7.153 1.00 24.79 C
ATOM 1781 O LEU B 222 22.732 -5.920 6.903 1.00 27.39 O
ATOM 1782 CB LEU B 222 21.460 -3.168 5.542 1.00 24.45 C
ATOM 1783 CG LEU B 222 20.147 -2.537 5.041 1.00 25.78 C
ATOM 1784 CD1 LEU B 222 20.366 -1.758 3.757 1.00 31.81 C
ATOM 1785 CD2 LEU B 222 19.048 -3.584 4.857 1.00 26.35 C
ATOM 1786 N MET B 223 23.606 -4.011 7.723 1.00 21.75 N
ATOM 1787 CA AMET B 223 24.860 -4.658 8.106 0.49 27.49 C
ATOM 1788 CA BMET B 223 24.855 -4.659 8.098 0.51 27.34 C
ATOM 1789 C MET B 223 24.619 -5.766 9.119 1.00 26.26 C
ATOM 1790 O MET B 223 25.188 -6.857 9.006 1.00 25.59 O
ATOM 1791 CB AMET B 223 25.850 -3.632 8.682 0.49 29.58 C
ATOM 1792 CB BMET B 223 25.816 -3.608 8.655 0.51 29.58 C
ATOM 1793 CG AMET B 223 26.824 -4.232 9.725 0.49 33.21 C
ATOM 1794 CG BMET B 223 27.177 -4.118 9.025 0.51 33.49 C
ATOM 1795 SD AMET B 223 28.008 -3.071 10.470 0.49 37.18 S
ATOM 1796 SD BMET B 223 28.285 -2.710 9.036 0.51 37.20 S
ATOM 1797 CE AMET B 223 26.952 -2.188 11.622 0.49 33.49 C
ATOM 1798 CE BMET B 223 28.315 -2.287 7.303 0.51 34.83 C
ATOM 1799 N GLU B 224 23.772 -5.508 10.121 1.00 22.29 N
ATOM 1800 CA GLU B 224 23.545 -6.512 11.157 1.00 21.50 C
ATOM 1801 C GLU B 224 22.757 -7.697 10.632 1.00 26.44 C
ATOM 1802 O GLU B 224 22.956 -8.827 11.094 1.00 22.80 O
ATOM 1803 CB GLU B 224 22.814 -5.893 12.358 1.00 26.28 C
ATOM 1804 CG GLU B 224 23.649 -4.874 13.074 1.00 36.12 C
ATOM 1805 CD GLU B 224 24.788 -5.509 13.852 1.00 44.00 C
ATOM 1806 OE1 GLU B 224 24.697 -6.719 14.170 1.00 50.53 O
ATOM 1807 OE2 GLU B 224 25.773 -4.802 14.142 1.00 48.90 O1-
ATOM 1808 N LEU B 225 21.844 -7.473 9.684 1.00 24.19 N
ATOM 1809 CA LEU B 225 21.121 -8.613 9.139 1.00 21.62 C
ATOM 1810 C LEU B 225 22.038 -9.475 8.274 1.00 20.85 C
ATOM 1811 O LEU B 225 21.915 -10.701 8.282 1.00 24.92 O
ATOM 1812 CB LEU B 225 19.889 -8.132 8.360 1.00 24.67 C
ATOM 1813 CG LEU B 225 18.720 -7.607 9.225 1.00 22.74 C
ATOM 1814 CD1 LEU B 225 17.599 -7.065 8.315 1.00 20.22 C
ATOM 1815 CD2 LEU B 225 18.160 -8.676 10.144 1.00 23.23 C
ATOM 1816 N GLU B 226 22.985 -8.866 7.551 1.00 25.46 N
ATOM 1817 CA GLU B 226 23.972 -9.667 6.821 1.00 25.83 C
ATOM 1818 C GLU B 226 24.791 -10.522 7.780 1.00 23.65 C
ATOM 1819 O GLU B 226 25.000 -11.721 7.540 1.00 25.51 O
ATOM 1820 CB GLU B 226 24.907 -8.776 5.999 1.00 22.21 C
ATOM 1821 CG GLU B 226 26.050 -9.524 5.277 1.00 25.86 C
ATOM 1822 CD GLU B 226 25.564 -10.319 4.060 1.00 36.16 C
ATOM 1823 OE1 GLU B 226 26.069 -11.443 3.799 1.00 49.22 O
ATOM 1824 OE2 GLU B 226 24.662 -9.822 3.350 1.00 46.45 O1-
ATOM 1825 N ILE B 227 25.236 -9.934 8.887 1.00 22.97 N
ATOM 1826 CA ILE B 227 25.979 -10.706 9.885 1.00 24.56 C
ATOM 1827 C ILE B 227 25.107 -11.803 10.462 1.00 24.61 C
ATOM 1828 O ILE B 227 25.557 -12.944 10.651 1.00 25.46 O
ATOM 1829 CB ILE B 227 26.526 -9.781 10.990 1.00 20.32 C
ATOM 1830 CG1 ILE B 227 27.635 -8.884 10.438 1.00 29.18 C
ATOM 1831 CG2 ILE B 227 27.042 -10.607 12.164 1.00 30.46 C
ATOM 1832 CD1 ILE B 227 27.917 -7.659 11.271 1.00 29.19 C
ATOM 1833 N LEU B 228 23.840 -11.481 10.746 1.00 27.03 N
ATOM 1834 CA LEU B 228 22.912 -12.487 11.256 1.00 27.33 C
ATOM 1835 C LEU B 228 22.742 -13.648 10.275 1.00 26.49 C
ATOM 1836 O LEU B 228 22.787 -14.821 10.673 1.00 25.43 O
ATOM 1837 CB LEU B 228 21.565 -11.839 11.563 1.00 24.78 C
ATOM 1838 CG LEU B 228 20.607 -12.723 12.334 1.00 31.23 C
ATOM 1839 CD1 LEU B 228 21.191 -13.067 13.734 1.00 26.14 C
ATOM 1840 CD2 LEU B 228 19.262 -11.999 12.485 1.00 29.15 C
ATOM 1841 N ARG B 229 22.513 -13.344 8.990 1.00 23.54 N
ATOM 1842 CA ARG B 229 22.400 -14.413 7.989 1.00 26.37 C
ATOM 1843 C ARG B 229 23.667 -15.267 7.947 1.00 26.34 C
ATOM 1844 O ARG B 229 23.603 -16.501 7.864 1.00 24.99 O
ATOM 1845 CB ARG B 229 22.149 -13.835 6.588 1.00 23.63 C
ATOM 1846 CG ARG B 229 20.783 -13.228 6.352 1.00 22.66 C
ATOM 1847 CD ARG B 229 20.576 -12.930 4.881 1.00 22.94 C
ATOM 1848 NE ARG B 229 21.389 -11.816 4.397 1.00 25.39 N
ATOM 1849 CZ ARG B 229 21.044 -10.542 4.527 1.00 24.61 C
ATOM 1850 NH1 ARG B 229 19.929 -10.188 5.157 1.00 22.23 N1+
ATOM 1851 NH2 ARG B 229 21.808 -9.605 3.983 1.00 23.05 N
ATOM 1852 N ASN B 230 24.829 -14.620 7.936 1.00 22.67 N
ATOM 1853 CA ASN B 230 26.061 -15.372 7.740 1.00 28.24 C
ATOM 1854 C ASN B 230 26.356 -16.272 8.933 1.00 29.39 C
ATOM 1855 O ASN B 230 26.933 -17.347 8.767 1.00 26.46 O
ATOM 1856 CB ASN B 230 27.241 -14.434 7.505 1.00 29.76 C
ATOM 1857 CG ASN B 230 27.091 -13.607 6.268 1.00 32.09 C
ATOM 1858 ND2 ASN B 230 27.830 -12.515 6.208 1.00 33.34 N
ATOM 1859 OD1 ASN B 230 26.314 -13.934 5.370 1.00 34.07 O
ATOM 1860 N SER B 231 25.949 -15.862 10.130 1.00 26.78 N
ATOM 1861 CA SER B 231 26.429 -16.491 11.344 1.00 31.62 C
ATOM 1862 C SER B 231 25.420 -17.453 11.953 1.00 28.06 C
ATOM 1863 O SER B 231 25.743 -18.123 12.934 1.00 28.53 O
ATOM 1864 CB SER B 231 26.826 -15.412 12.349 1.00 27.45 C
ATOM 1865 OG SER B 231 25.679 -14.695 12.765 1.00 32.31 O
ATOM 1866 N ALA B 232 24.230 -17.568 11.368 1.00 27.29 N
ATOM 1867 CA ALA B 232 23.195 -18.439 11.890 1.00 30.37 C
ATOM 1868 C ALA B 232 23.592 -19.909 11.768 1.00 29.93 C
ATOM 1869 O ALA B 232 24.424 -20.274 10.930 1.00 31.68 O
ATOM 1870 CB ALA B 232 21.878 -18.191 11.146 1.00 30.12 C
ATOM 1871 N PRO B 233 23.000 -20.774 12.593 1.00 32.67 N
ATOM 1872 CA PRO B 233 23.268 -22.212 12.476 1.00 31.73 C
ATOM 1873 C PRO B 233 22.908 -22.737 11.098 1.00 35.40 C
ATOM 1874 O PRO B 233 22.092 -22.155 10.379 1.00 34.62 O
ATOM 1875 CB PRO B 233 22.376 -22.830 13.564 1.00 32.55 C
ATOM 1876 CG PRO B 233 22.180 -21.738 14.562 1.00 36.21 C
ATOM 1877 CD PRO B 233 22.174 -20.456 13.776 1.00 34.45 C
ATOM 1878 N GLU B 234 23.547 -23.851 10.717 1.00 32.41 N
ATOM 1879 CA GLU B 234 23.188 -24.503 9.466 1.00 30.80 C
ATOM 1880 C GLU B 234 21.685 -24.764 9.438 1.00 28.02 C
ATOM 1881 O GLU B 234 21.109 -25.208 10.430 1.00 33.05 O
ATOM 1882 CB GLU B 234 23.956 -25.823 9.296 1.00 31.73 C
ATOM 1883 CG GLU B 234 25.442 -25.637 9.104 1.00 50.66 C
ATOM 1884 CD GLU B 234 26.195 -26.913 8.713 1.00 51.30 C
ATOM 1885 OE1 GLU B 234 25.549 -27.936 8.385 1.00 57.00 O
ATOM 1886 OE2 GLU B 234 27.448 -26.877 8.755 1.00 59.75 O1-
ATOM 1887 N GLY B 235 21.045 -24.465 8.307 1.00 31.64 N
ATOM 1888 CA GLY B 235 19.623 -24.739 8.163 1.00 30.41 C
ATOM 1889 C GLY B 235 18.686 -23.802 8.903 1.00 32.04 C
ATOM 1890 O GLY B 235 17.477 -24.048 8.920 1.00 34.25 O
ATOM 1891 N SER B 236 19.206 -22.737 9.525 1.00 33.90 N
ATOM 1892 CA SER B 236 18.385 -21.795 10.272 1.00 30.34 C
ATOM 1893 C SER B 236 17.580 -20.911 9.320 1.00 35.26 C
ATOM 1894 O SER B 236 18.086 -20.495 8.276 1.00 26.43 O
ATOM 1895 CB SER B 236 19.242 -20.912 11.163 1.00 31.12 C
ATOM 1896 OG SER B 236 18.534 -19.729 11.492 1.00 29.59 O
ATOM 1897 N PRO B 237 16.325 -20.599 9.661 1.00 32.66 N
ATOM 1898 CA PRO B 237 15.549 -19.684 8.811 1.00 29.49 C
ATOM 1899 C PRO B 237 16.141 -18.298 8.763 1.00 25.49 C
ATOM 1900 O PRO B 237 15.922 -17.588 7.775 1.00 28.85 O
ATOM 1901 CB PRO B 237 14.154 -19.667 9.465 1.00 28.01 C
ATOM 1902 CG PRO B 237 14.094 -20.906 10.300 1.00 33.97 C
ATOM 1903 CD PRO B 237 15.530 -21.138 10.776 1.00 30.01 C
ATOM 1904 N LEU B 238 16.906 -17.895 9.784 1.00 23.65 N
ATOM 1905 CA LEU B 238 17.503 -16.563 9.759 1.00 26.46 C
ATOM 1906 C LEU B 238 18.440 -16.370 8.577 1.00 27.07 C
ATOM 1907 O LEU B 238 18.690 -15.222 8.188 1.00 26.85 O
ATOM 1908 CB LEU B 238 18.226 -16.282 11.073 1.00 22.88 C
ATOM 1909 CG LEU B 238 17.350 -16.396 12.326 1.00 29.39 C
ATOM 1910 CD1 LEU B 238 18.169 -16.167 13.597 1.00 28.61 C
ATOM 1911 CD2 LEU B 238 16.250 -15.357 12.264 1.00 27.98 C
ATOM 1912 N ARG B 239 18.926 -17.451 7.960 1.00 23.75 N
ATOM 1913 CA ARG B 239 19.825 -17.283 6.819 1.00 29.75 C
ATOM 1914 C ARG B 239 19.142 -16.593 5.634 1.00 28.35 C
ATOM 1915 O ARG B 239 19.835 -16.028 4.773 1.00 27.26 O
ATOM 1916 CB ARG B 239 20.427 -18.650 6.422 1.00 27.25 C
ATOM 1917 CG ARG B 239 21.307 -18.647 5.161 1.00 28.87 C
ATOM 1918 CD ARG B 239 22.464 -19.664 5.226 1.00 27.61 C
ATOM 1919 NE ARG B 239 23.430 -19.278 6.245 1.00 24.53 N
ATOM 1920 CZ ARG B 239 23.522 -19.846 7.442 1.00 26.96 C
ATOM 1921 NH1 ARG B 239 22.851 -20.952 7.741 1.00 22.64 N1+
ATOM 1922 NH2 ARG B 239 24.294 -19.286 8.369 1.00 25.91 N
ATOM 1923 N VAL B 240 17.806 -16.588 5.570 1.00 26.59 N
ATOM 1924 CA VAL B 240 17.133 -15.941 4.447 1.00 25.54 C
ATOM 1925 C VAL B 240 16.240 -14.810 4.934 1.00 34.77 C
ATOM 1926 O VAL B 240 15.247 -14.449 4.274 1.00 27.02 O
ATOM 1927 CB VAL B 240 16.344 -16.955 3.582 1.00 27.82 C
ATOM 1928 CG1 VAL B 240 17.324 -17.807 2.745 1.00 31.53 C
ATOM 1929 CG2 VAL B 240 15.471 -17.856 4.446 1.00 29.42 C
ATOM 1930 N LEU B 241 16.595 -14.239 6.085 1.00 28.80 N
ATOM 1931 CA LEU B 241 15.928 -13.038 6.572 1.00 25.75 C
ATOM 1932 C LEU B 241 16.582 -11.812 5.934 1.00 21.99 C
ATOM 1933 O LEU B 241 17.748 -11.502 6.196 1.00 26.31 O
ATOM 1934 CB LEU B 241 15.974 -12.981 8.094 1.00 22.52 C
ATOM 1935 CG LEU B 241 15.449 -11.727 8.774 1.00 25.52 C
ATOM 1936 CD1 LEU B 241 13.987 -11.465 8.351 1.00 21.64 C
ATOM 1937 CD2 LEU B 241 15.578 -11.828 10.305 1.00 24.41 C
ATOM 1938 N TYR B 242 15.838 -11.137 5.074 1.00 24.93 N
ATOM 1939 CA TYR B 242 16.287 -9.955 4.359 1.00 24.28 C
ATOM 1940 C TYR B 242 15.315 -8.822 4.620 1.00 26.46 C
ATOM 1941 O TYR B 242 14.112 -9.043 4.748 1.00 24.87 O
ATOM 1942 CB TYR B 242 16.363 -10.187 2.837 1.00 23.24 C
ATOM 1943 CG TYR B 242 17.419 -11.178 2.393 1.00 28.45 C
ATOM 1944 CD1 TYR B 242 17.161 -12.531 2.354 1.00 28.21 C
ATOM 1945 CD2 TYR B 242 18.672 -10.741 1.994 1.00 20.30 C
ATOM 1946 CE1 TYR B 242 18.140 -13.437 1.926 1.00 24.78 C
ATOM 1947 CE2 TYR B 242 19.653 -11.627 1.587 1.00 27.06 C
ATOM 1948 CZ TYR B 242 19.377 -12.971 1.547 1.00 25.22 C
ATOM 1949 OH TYR B 242 20.359 -13.855 1.150 1.00 32.32 O
ATOM 1950 N SER B 243 15.813 -7.596 4.625 1.00 25.27 N
ATOM 1951 CA SER B 243 14.907 -6.471 4.798 1.00 29.97 C
ATOM 1952 C SER B 243 14.968 -5.506 3.622 1.00 29.15 C
ATOM 1953 O SER B 243 16.010 -5.363 2.978 1.00 29.86 O
ATOM 1954 CB SER B 243 15.224 -5.728 6.082 1.00 27.01 C
ATOM 1955 OG SER B 243 14.281 -4.715 6.299 1.00 30.46 O
ATOM 1956 N GLY B 244 13.833 -4.848 3.339 1.00 20.85 N
ATOM 1957 CA GLY B 244 13.819 -3.626 2.555 1.00 22.95 C
ATOM 1958 C GLY B 244 13.591 -2.461 3.502 1.00 27.50 C
ATOM 1959 O GLY B 244 12.907 -2.607 4.499 1.00 26.22 O
ATOM 1960 N ILE B 245 14.170 -1.293 3.201 1.00 20.17 N
ATOM 1961 CA ILE B 245 13.994 -0.129 4.068 1.00 23.58 C
ATOM 1962 C ILE B 245 13.692 1.100 3.222 1.00 23.18 C
ATOM 1963 O ILE B 245 14.394 1.365 2.242 1.00 25.56 O
ATOM 1964 CB ILE B 245 15.241 0.132 4.928 1.00 25.04 C
ATOM 1965 CG1 ILE B 245 15.609 -1.087 5.765 1.00 23.29 C
ATOM 1966 CG2 ILE B 245 15.052 1.397 5.788 1.00 22.19 C
ATOM 1967 CD1 ILE B 245 16.777 -0.817 6.734 1.00 26.00 C
ATOM 1968 N GLY B 246 12.687 1.868 3.616 1.00 21.19 N
ATOM 1969 CA GLY B 246 12.355 3.108 2.922 1.00 19.24 C
ATOM 1970 C GLY B 246 12.310 4.260 3.898 1.00 20.48 C
ATOM 1971 O GLY B 246 11.817 4.116 5.008 1.00 22.45 O
ATOM 1972 N LEU B 247 12.836 5.412 3.476 1.00 19.45 N
ATOM 1973 CA LEU B 247 12.766 6.618 4.304 1.00 22.01 C
ATOM 1974 C LEU B 247 12.083 7.729 3.524 1.00 23.66 C
ATOM 1975 O LEU B 247 12.320 7.892 2.323 1.00 21.04 O
ATOM 1976 CB LEU B 247 14.151 7.132 4.757 1.00 23.10 C
ATOM 1977 CG LEU B 247 15.146 6.126 5.317 1.00 25.64 C
ATOM 1978 CD1 LEU B 247 16.526 6.799 5.522 1.00 21.18 C
ATOM 1979 CD2 LEU B 247 14.624 5.522 6.592 1.00 25.22 C
ATOM 1980 N ALA B 248 11.216 8.480 4.207 1.00 23.10 N
ATOM 1981 CA ALA B 248 10.603 9.660 3.621 1.00 24.75 C
ATOM 1982 C ALA B 248 10.459 10.702 4.716 1.00 29.72 C
ATOM 1983 O ALA B 248 10.725 10.426 5.886 1.00 30.37 O
ATOM 1984 CB ALA B 248 9.240 9.327 2.979 1.00 26.88 C
ATOM 1985 N LYS B 249 10.071 11.918 4.337 1.00 27.56 N
ATOM 1986 CA LYS B 249 9.627 12.898 5.321 1.00 34.22 C
ATOM 1987 C LYS B 249 8.111 12.930 5.351 1.00 39.14 C
ATOM 1988 O LYS B 249 7.450 12.809 4.311 1.00 34.03 O
ATOM 1989 CB LYS B 249 10.162 14.301 5.040 1.00 34.85 C
ATOM 1990 CG LYS B 249 11.645 14.410 5.186 1.00 38.75 C
ATOM 1991 CD LYS B 249 12.171 15.838 5.133 1.00 37.93 C
ATOM 1992 CE LYS B 249 12.216 16.488 6.499 1.00 44.60 C
ATOM 1993 NZ LYS B 249 13.183 17.626 6.479 1.00 43.43 N1+
ATOM 1994 N GLY B 250 7.561 13.084 6.544 1.00 34.66 N
ATOM 1995 CA GLY B 250 6.120 13.124 6.702 1.00 36.05 C
ATOM 1996 C GLY B 250 5.727 14.187 7.702 1.00 38.08 C
ATOM 1997 O GLY B 250 6.464 14.492 8.641 1.00 36.09 O
ATOM 1998 N LYS B 251 4.560 14.774 7.477 1.00 44.34 N
ATOM 1999 CA LYS B 251 3.998 15.709 8.438 1.00 36.98 C
ATOM 2000 C LYS B 251 3.171 14.873 9.397 1.00 33.05 C
ATOM 2001 O LYS B 251 2.110 14.359 9.028 1.00 42.22 O
ATOM 2002 CB LYS B 251 3.150 16.774 7.754 1.00 40.18 C
ATOM 2003 CG LYS B 251 2.339 17.614 8.753 1.00 52.17 C
ATOM 2004 CD LYS B 251 1.172 18.352 8.081 1.00 52.16 C
ATOM 2005 CE LYS B 251 -0.171 17.900 8.651 1.00 44.41 C
ATOM 2006 NZ LYS B 251 -0.513 16.460 8.321 1.00 49.64 N1+
ATOM 2007 N VAL B 252 3.663 14.689 10.603 1.00 27.12 N
ATOM 2008 CA VAL B 252 2.910 13.939 11.573 1.00 37.23 C
ATOM 2009 C VAL B 252 2.213 14.943 12.475 1.00 34.47 C
ATOM 2010 O VAL B 252 2.572 16.122 12.539 1.00 31.71 O
ATOM 2011 CB VAL B 252 3.777 12.937 12.368 1.00 37.36 C
ATOM 2012 CG1 VAL B 252 5.041 12.632 11.601 1.00 38.93 C
ATOM 2013 CG2 VAL B 252 4.033 13.408 13.770 1.00 33.42 C
ATOM 2014 N ILE B 253 1.158 14.483 13.126 1.00 33.43 N
ATOM 2015 CA ILE B 253 0.423 15.292 14.083 1.00 32.92 C
ATOM 2016 C ILE B 253 0.587 14.628 15.436 1.00 34.86 C
ATOM 2017 O ILE B 253 0.303 13.433 15.580 1.00 36.50 O
ATOM 2018 CB ILE B 253 -1.060 15.433 13.693 1.00 34.30 C
ATOM 2019 CG1 ILE B 253 -1.188 16.188 12.377 1.00 35.14 C
ATOM 2020 CG2 ILE B 253 -1.827 16.168 14.777 1.00 35.62 C
ATOM 2021 CD1 ILE B 253 -2.607 16.237 11.844 1.00 34.52 C
ATOM 2022 N GLU B 254 1.103 15.382 16.406 1.00 39.31 N
ATOM 2023 CA GLU B 254 1.137 14.961 17.798 1.00 36.81 C
ATOM 2024 C GLU B 254 -0.112 15.489 18.523 1.00 42.11 C
ATOM 2025 O GLU B 254 -0.635 16.557 18.194 1.00 36.19 O
ATOM 2026 CB GLU B 254 2.433 15.453 18.459 1.00 44.61 C
ATOM 2027 CG GLU B 254 3.711 14.901 17.772 1.00 43.87 C
ATOM 2028 CD GLU B 254 5.049 15.336 18.400 1.00 54.79 C
ATOM 2029 OE1 GLU B 254 5.122 16.444 18.992 1.00 54.12 O
ATOM 2030 OE2 GLU B 254 6.032 14.549 18.300 1.00 48.00 O1-
ATOM 2031 N GLY B 255 -0.628 14.701 19.460 1.00 42.50 N
ATOM 2032 CA GLY B 255 -1.829 15.081 20.180 1.00 40.58 C
ATOM 2033 C GLY B 255 -2.411 13.907 20.946 1.00 41.41 C
ATOM 2034 O GLY B 255 -1.805 12.838 21.035 1.00 43.29 O
ATOM 2035 N ASN B 256 -3.600 14.144 21.514 1.00 34.66 N
ATOM 2036 CA ASN B 256 -4.402 13.098 22.165 1.00 38.35 C
ATOM 2037 C ASN B 256 -5.382 12.572 21.119 1.00 39.11 C
ATOM 2038 O ASN B 256 -6.470 13.117 20.922 1.00 35.48 O
ATOM 2039 CB ASN B 256 -5.119 13.632 23.406 1.00 45.38 C
ATOM 2040 CG ASN B 256 -5.874 12.536 24.181 1.00 50.36 C
ATOM 2041 ND2 ASN B 256 -6.791 12.954 25.041 1.00 58.28 N
ATOM 2042 OD1 ASN B 256 -5.627 11.341 24.014 1.00 46.78 O
ATOM 2043 N ILE B 257 -4.981 11.495 20.448 1.00 40.18 N
ATOM 2044 CA ILE B 257 -5.638 11.005 19.244 1.00 40.19 C
ATOM 2045 C ILE B 257 -6.209 9.624 19.513 1.00 40.60 C
ATOM 2046 O ILE B 257 -5.552 8.785 20.134 1.00 35.44 O
ATOM 2047 CB ILE B 257 -4.655 10.962 18.053 1.00 41.28 C
ATOM 2048 CG1 ILE B 257 -4.129 12.369 17.729 1.00 36.90 C
ATOM 2049 CG2 ILE B 257 -5.301 10.291 16.852 1.00 37.50 C
ATOM 2050 CD1 ILE B 257 -2.642 12.406 17.388 1.00 33.35 C
ATOM 2051 N GLY B 258 -7.424 9.379 19.036 1.00 32.88 N
ATOM 2052 CA GLY B 258 -7.952 8.039 19.154 1.00 34.72 C
ATOM 2053 C GLY B 258 -9.413 7.997 19.513 1.00 36.56 C
ATOM 2054 O GLY B 258 -10.148 8.956 19.255 1.00 44.72 O
ATOM 2055 N SER B 259 -9.843 6.906 20.141 1.00 44.98 N
ATOM 2056 CA SER B 259 -11.259 6.582 20.249 1.00 44.85 C
ATOM 2057 C SER B 259 -11.804 6.689 21.668 1.00 53.86 C
ATOM 2058 O SER B 259 -12.914 6.207 21.920 1.00 62.65 O
ATOM 2059 CB SER B 259 -11.492 5.168 19.724 1.00 42.92 C
ATOM 2060 OG SER B 259 -10.756 4.231 20.497 1.00 45.04 O
ATOM 2061 N GLU B 260 -11.051 7.276 22.603 1.00 49.29 N
ATOM 2062 CA GLU B 260 -11.406 7.271 24.026 1.00 66.01 C
ATOM 2063 C GLU B 260 -11.307 5.861 24.610 1.00 62.75 C
ATOM 2064 O GLU B 260 -10.825 5.690 25.736 1.00 66.36 O
ATOM 2065 CB GLU B 260 -12.803 7.865 24.269 1.00 69.71 C
ATOM 2066 N LEU B 261 -11.753 4.846 23.866 1.00 55.87 N
ATOM 2067 CA LEU B 261 -11.326 3.476 24.131 1.00 60.51 C
ATOM 2068 C LEU B 261 -9.803 3.406 23.998 1.00 62.67 C
ATOM 2069 O LEU B 261 -9.094 3.246 24.997 1.00 60.19 O
ATOM 2070 CB LEU B 261 -12.017 2.491 23.168 1.00 63.40 C
ATOM 2071 CG LEU B 261 -11.763 0.967 23.250 1.00 68.44 C
ATOM 2072 CD1 LEU B 261 -13.054 0.144 23.054 1.00 57.19 C
ATOM 2073 CD2 LEU B 261 -10.690 0.498 22.263 1.00 68.28 C
ATOM 2074 N LYS B 262 -9.290 3.572 22.779 1.00 57.76 N
ATOM 2075 CA LYS B 262 -7.866 3.463 22.481 1.00 47.99 C
ATOM 2076 C LYS B 262 -7.288 4.799 22.037 1.00 50.43 C
ATOM 2077 O LYS B 262 -7.887 5.494 21.208 1.00 44.66 O
ATOM 2078 CB LYS B 262 -7.615 2.408 21.411 1.00 54.81 C
ATOM 2079 CG LYS B 262 -6.161 2.325 20.984 1.00 54.77 C
ATOM 2080 CD LYS B 262 -5.405 1.282 21.753 1.00 61.96 C
ATOM 2081 CE LYS B 262 -4.078 1.846 22.208 1.00 54.77 C
ATOM 2082 NZ LYS B 262 -3.498 2.748 21.173 1.00 48.96 N1+
ATOM 2083 N ARG B 263 -6.119 5.143 22.584 1.00 46.31 N
ATOM 2084 CA ARG B 263 -5.479 6.428 22.359 1.00 41.04 C
ATOM 2085 C ARG B 263 -4.080 6.209 21.812 1.00 49.04 C
ATOM 2086 O ARG B 263 -3.507 5.120 21.923 1.00 45.68 O
ATOM 2087 CB ARG B 263 -5.395 7.265 23.654 1.00 44.59 C
ATOM 2088 CG ARG B 263 -6.739 7.840 24.123 1.00 43.95 C
ATOM 2089 CD ARG B 263 -7.240 8.891 23.145 1.00 50.08 C
ATOM 2090 NE ARG B 263 -8.463 9.557 23.577 1.00 60.02 N
ATOM 2091 CZ ARG B 263 -8.985 10.620 22.974 1.00 61.66 C
ATOM 2092 NH1 ARG B 263 -8.401 11.175 21.920 1.00 55.94 N1+
ATOM 2093 NH2 ARG B 263 -10.130 11.129 23.427 1.00 60.50 N
ATOM 2094 N ASP B 264 -3.543 7.270 21.211 1.00 38.50 N
ATOM 2095 CA ASP B 264 -2.141 7.338 20.830 1.00 43.25 C
ATOM 2096 C ASP B 264 -1.741 8.802 20.810 1.00 40.55 C
ATOM 2097 O ASP B 264 -2.577 9.708 20.906 1.00 40.29 O
ATOM 2098 CB ASP B 264 -1.862 6.673 19.475 1.00 49.57 C
ATOM 2099 CG ASP B 264 -0.389 6.264 19.307 1.00 52.88 C
ATOM 2100 OD1 ASP B 264 0.522 6.988 19.782 1.00 54.83 O
ATOM 2101 OD2 ASP B 264 -0.144 5.195 18.709 1.00 64.65 O1-
ATOM 2102 N TYR B 265 -0.440 9.018 20.701 1.00 45.29 N
ATOM 2103 CA TYR B 265 0.160 10.335 20.814 1.00 45.99 C
ATOM 2104 C TYR B 265 0.484 10.923 19.432 1.00 36.83 C
ATOM 2105 O TYR B 265 0.744 12.127 19.308 1.00 38.99 O
ATOM 2106 CB TYR B 265 1.401 10.189 21.733 1.00 47.20 C
ATOM 2107 CG TYR B 265 2.581 11.103 21.536 1.00 47.89 C
ATOM 2108 CD1 TYR B 265 2.430 12.487 21.572 1.00 59.18 C
ATOM 2109 CD2 TYR B 265 3.853 10.585 21.286 1.00 54.74 C
ATOM 2110 CE1 TYR B 265 3.526 13.336 21.399 1.00 57.27 C
ATOM 2111 CE2 TYR B 265 4.950 11.420 21.102 1.00 52.79 C
ATOM 2112 CZ TYR B 265 4.777 12.798 21.162 1.00 59.10 C
ATOM 2113 OH TYR B 265 5.847 13.651 20.977 1.00 71.92 O
ATOM 2114 N THR B 266 0.395 10.121 18.375 1.00 38.83 N
ATOM 2115 CA THR B 266 0.818 10.580 17.059 1.00 32.31 C
ATOM 2116 C THR B 266 -0.072 9.981 15.968 1.00 32.42 C
ATOM 2117 O THR B 266 -0.676 8.921 16.142 1.00 31.70 O
ATOM 2118 CB THR B 266 2.293 10.222 16.861 1.00 30.28 C
ATOM 2119 CG2 THR B 266 2.453 8.728 16.770 1.00 30.70 C
ATOM 2120 OG1 THR B 266 2.790 10.860 15.683 1.00 52.05 O
ATOM 2121 N ILE B 267 -0.145 10.677 14.836 1.00 30.32 N
ATOM 2122 CA ILE B 267 -0.794 10.170 13.619 1.00 31.54 C
ATOM 2123 C ILE B 267 -0.027 10.701 12.411 1.00 29.09 C
ATOM 2124 O ILE B 267 0.296 11.891 12.341 1.00 34.16 O
ATOM 2125 CB ILE B 267 -2.296 10.549 13.523 1.00 28.44 C
ATOM 2126 CG1 ILE B 267 -2.939 9.937 12.272 1.00 32.41 C
ATOM 2127 CG2 ILE B 267 -2.515 12.054 13.459 1.00 24.74 C
ATOM 2128 CD1 ILE B 267 -4.469 9.916 12.339 1.00 34.51 C
ATOM 2129 N LEU B 268 0.277 9.807 11.470 1.00 30.36 N
ATOM 2130 CA LEU B 268 0.802 10.157 10.149 1.00 31.27 C
ATOM 2131 C LEU B 268 -0.242 9.758 9.108 1.00 27.11 C
ATOM 2132 O LEU B 268 -0.394 8.571 8.798 1.00 26.02 O
ATOM 2133 CB LEU B 268 2.131 9.451 9.881 1.00 28.48 C
ATOM 2134 CG LEU B 268 2.651 9.566 8.445 1.00 31.21 C
ATOM 2135 CD1 LEU B 268 3.155 10.960 8.187 1.00 33.86 C
ATOM 2136 CD2 LEU B 268 3.797 8.553 8.185 1.00 29.81 C
ATOM 2137 N GLY B 269 -0.958 10.742 8.575 1.00 30.75 N
ATOM 2138 CA GLY B 269 -1.971 10.440 7.573 1.00 34.52 C
ATOM 2139 C GLY B 269 -1.371 9.714 6.381 1.00 32.82 C
ATOM 2140 O GLY B 269 -0.274 10.039 5.920 1.00 36.66 O
ATOM 2141 N ASP B 270 -2.077 8.677 5.915 1.00 35.64 N
ATOM 2142 CA ASP B 270 -1.671 7.915 4.715 1.00 43.72 C
ATOM 2143 C ASP B 270 -0.317 7.219 4.898 1.00 38.76 C
ATOM 2144 O ASP B 270 0.440 7.024 3.934 1.00 32.59 O
ATOM 2145 CB ASP B 270 -1.642 8.804 3.465 1.00 45.99 C
ATOM 2146 CG ASP B 270 -3.009 9.409 3.145 1.00 46.05 C
ATOM 2147 OD1 ASP B 270 -4.047 8.811 3.523 1.00 41.43 O
ATOM 2148 OD2 ASP B 270 -3.036 10.495 2.529 1.00 43.67 O1-
ATOM 2149 N ALA B 271 -0.007 6.860 6.148 1.00 32.92 N
ATOM 2150 CA ALA B 271 1.131 5.995 6.438 1.00 26.37 C
ATOM 2151 C ALA B 271 1.044 4.678 5.665 1.00 30.44 C
ATOM 2152 O ALA B 271 2.062 4.168 5.170 1.00 29.32 O
ATOM 2153 CB ALA B 271 1.193 5.724 7.948 1.00 30.19 C
ATOM 2154 N VAL B 272 -0.168 4.115 5.565 1.00 28.27 N
ATOM 2155 CA VAL B 272 -0.418 2.895 4.789 1.00 30.01 C
ATOM 2156 C VAL B 272 0.165 3.014 3.387 1.00 34.87 C
ATOM 2157 O VAL B 272 0.850 2.107 2.893 1.00 27.62 O
ATOM 2158 CB VAL B 272 -1.932 2.606 4.723 1.00 39.55 C
ATOM 2159 CG1 VAL B 272 -2.268 1.675 3.538 1.00 30.89 C
ATOM 2160 CG2 VAL B 272 -2.403 2.006 6.010 1.00 34.50 C
ATOM 2161 N ASN B 273 -0.100 4.136 2.730 1.00 27.97 N
ATOM 2162 CA ASN B 273 0.252 4.262 1.321 1.00 35.97 C
ATOM 2163 C ASN B 273 1.727 4.592 1.131 1.00 27.58 C
ATOM 2164 O ASN B 273 2.343 4.121 0.172 1.00 28.43 O
ATOM 2165 CB ASN B 273 -0.644 5.318 0.679 1.00 34.54 C
ATOM 2166 CG ASN B 273 -2.118 5.101 1.030 1.00 48.50 C
ATOM 2167 ND2 ASN B 273 -2.582 5.807 2.071 1.00 39.85 N
ATOM 2168 OD1 ASN B 273 -2.813 4.267 0.414 1.00 48.33 O
ATOM 2169 N VAL B 274 2.308 5.411 2.015 1.00 27.58 N
ATOM 2170 CA VAL B 274 3.748 5.647 1.959 1.00 22.78 C
ATOM 2171 C VAL B 274 4.509 4.342 2.195 1.00 30.40 C
ATOM 2172 O VAL B 274 5.474 4.030 1.479 1.00 30.26 O
ATOM 2173 CB VAL B 274 4.157 6.745 2.957 1.00 29.01 C
ATOM 2174 CG1 VAL B 274 5.672 6.853 3.052 1.00 29.05 C
ATOM 2175 CG2 VAL B 274 3.542 8.088 2.571 1.00 27.26 C
ATOM 2176 N ALA B 275 4.077 3.542 3.174 1.00 22.75 N
ATOM 2177 CA ALA B 275 4.741 2.252 3.404 1.00 29.42 C
ATOM 2178 C ALA B 275 4.620 1.351 2.180 1.00 30.64 C
ATOM 2179 O ALA B 275 5.613 0.784 1.707 1.00 25.21 O
ATOM 2180 CB ALA B 275 4.148 1.543 4.621 1.00 24.69 C
ATOM 2181 N ALA B 276 3.398 1.222 1.643 1.00 25.00 N
ATOM 2182 CA ALA B 276 3.180 0.359 0.488 1.00 28.82 C
ATOM 2183 C ALA B 276 4.023 0.798 -0.704 1.00 23.97 C
ATOM 2184 O ALA B 276 4.586 -0.040 -1.411 1.00 27.98 O
ATOM 2185 CB ALA B 276 1.700 0.348 0.125 1.00 26.51 C
ATOM 2186 N ARG B 277 4.147 2.109 -0.927 1.00 26.14 N
ATOM 2187 CA ARG B 277 4.924 2.592 -2.061 1.00 25.42 C
ATOM 2188 C ARG B 277 6.425 2.405 -1.857 1.00 32.03 C
ATOM 2189 O ARG B 277 7.153 2.150 -2.822 1.00 25.05 O
ATOM 2190 CB ARG B 277 4.600 4.056 -2.341 1.00 28.85 C
ATOM 2191 CG ARG B 277 3.356 4.209 -3.194 1.00 43.04 C
ATOM 2192 CD ARG B 277 2.547 5.426 -2.833 1.00 47.98 C
ATOM 2193 NE ARG B 277 1.132 5.217 -3.137 1.00 60.12 N
ATOM 2194 CZ ARG B 277 0.157 6.035 -2.763 1.00 58.65 C
ATOM 2195 NH1 ARG B 277 0.402 7.113 -2.036 1.00 53.09 N1+
ATOM 2196 NH2 ARG B 277 -1.099 5.754 -3.113 1.00 67.71 N
ATOM 2197 N LEU B 278 6.909 2.572 -0.627 1.00 23.53 N
ATOM 2198 CA LEU B 278 8.310 2.299 -0.344 1.00 26.05 C
ATOM 2199 C LEU B 278 8.631 0.818 -0.520 1.00 25.99 C
ATOM 2200 O LEU B 278 9.696 0.461 -1.039 1.00 26.23 O
ATOM 2201 CB LEU B 278 8.659 2.776 1.075 1.00 24.73 C
ATOM 2202 CG LEU B 278 8.677 4.309 1.178 1.00 21.45 C
ATOM 2203 CD1 LEU B 278 8.696 4.732 2.631 1.00 22.77 C
ATOM 2204 CD2 LEU B 278 9.881 4.879 0.404 1.00 25.56 C
ATOM 2205 N GLU B 279 7.736 -0.059 -0.073 1.00 26.75 N
ATOM 2206 CA GLU B 279 7.939 -1.486 -0.282 1.00 31.52 C
ATOM 2207 C GLU B 279 7.973 -1.828 -1.761 1.00 28.89 C
ATOM 2208 O GLU B 279 8.762 -2.681 -2.180 1.00 30.42 O
ATOM 2209 CB GLU B 279 6.846 -2.285 0.420 1.00 32.54 C
ATOM 2210 CG GLU B 279 7.014 -2.351 1.911 1.00 36.82 C
ATOM 2211 CD GLU B 279 6.057 -3.354 2.550 1.00 43.76 C
ATOM 2212 OE1 GLU B 279 5.551 -4.234 1.810 1.00 42.93 O
ATOM 2213 OE2 GLU B 279 5.837 -3.275 3.794 1.00 35.35 O1-
ATOM 2214 N ALA B 280 7.124 -1.184 -2.572 1.00 27.02 N
ATOM 2215 CA ALA B 280 7.154 -1.465 -4.010 1.00 29.28 C
ATOM 2216 C ALA B 280 8.495 -1.079 -4.594 1.00 29.58 C
ATOM 2217 O ALA B 280 9.017 -1.764 -5.484 1.00 32.31 O
ATOM 2218 CB ALA B 280 6.028 -0.735 -4.753 1.00 28.90 C
ATOM 2219 N LEU B 281 9.096 -0.009 -4.078 1.00 28.48 N
ATOM 2220 CA LEU B 281 10.363 0.447 -4.640 1.00 24.69 C
ATOM 2221 C LEU B 281 11.521 -0.467 -4.255 1.00 29.98 C
ATOM 2222 O LEU B 281 12.403 -0.733 -5.079 1.00 26.96 O
ATOM 2223 CB LEU B 281 10.630 1.877 -4.199 1.00 24.50 C
ATOM 2224 CG LEU B 281 9.933 2.972 -4.995 1.00 33.22 C
ATOM 2225 CD1 LEU B 281 9.937 4.241 -4.174 1.00 30.92 C
ATOM 2226 CD2 LEU B 281 10.677 3.218 -6.311 1.00 30.70 C
ATOM 2227 N THR B 282 11.571 -0.936 -3.008 1.00 28.40 N
ATOM 2228 CA THR B 282 12.687 -1.803 -2.648 1.00 31.75 C
ATOM 2229 C THR B 282 12.624 -3.105 -3.436 1.00 32.25 C
ATOM 2230 O THR B 282 13.662 -3.629 -3.862 1.00 42.78 O
ATOM 2231 CB THR B 282 12.730 -2.090 -1.140 1.00 28.54 C
ATOM 2232 CG2 THR B 282 12.922 -0.816 -0.309 1.00 24.90 C
ATOM 2233 OG1 THR B 282 11.532 -2.760 -0.731 1.00 27.01 O
ATOM 2234 N ARG B 283 11.414 -3.629 -3.659 1.00 29.35 N
ATOM 2235 CA ARG B 283 11.250 -4.815 -4.506 1.00 30.22 C
ATOM 2236 C ARG B 283 11.646 -4.518 -5.946 1.00 34.87 C
ATOM 2237 O ARG B 283 12.375 -5.287 -6.578 1.00 39.08 O
ATOM 2238 CB ARG B 283 9.800 -5.298 -4.480 1.00 33.26 C
ATOM 2239 CG ARG B 283 9.248 -5.555 -3.100 1.00 44.52 C
ATOM 2240 CD ARG B 283 9.862 -6.792 -2.471 1.00 50.89 C
ATOM 2241 NE ARG B 283 10.030 -6.676 -1.022 1.00 56.37 N
ATOM 2242 CZ ARG B 283 9.085 -6.319 -0.154 1.00 45.93 C
ATOM 2243 NH1 ARG B 283 7.831 -6.105 -0.525 1.00 57.67 N1+
ATOM 2244 NH2 ARG B 283 9.402 -6.206 1.130 1.00 48.62 N
ATOM 2245 N GLN B 284 11.173 -3.395 -6.477 1.00 35.19 N
ATOM 2246 CA GLN B 284 11.361 -3.097 -7.892 1.00 40.07 C
ATOM 2247 C GLN B 284 12.809 -2.759 -8.214 1.00 46.35 C
ATOM 2248 O GLN B 284 13.289 -3.089 -9.304 1.00 44.76 O
ATOM 2249 CB GLN B 284 10.425 -1.956 -8.307 1.00 40.11 C
ATOM 2250 CG GLN B 284 10.445 -1.617 -9.791 1.00 40.84 C
ATOM 2251 CD GLN B 284 11.224 -0.358 -10.094 1.00 42.71 C
ATOM 2252 NE2 GLN B 284 12.302 -0.494 -10.877 1.00 45.71 N
ATOM 2253 OE1 GLN B 284 10.865 0.733 -9.631 1.00 40.75 O
ATOM 2254 N LEU B 285 13.514 -2.114 -7.291 1.00 38.35 N
ATOM 2255 CA LEU B 285 14.844 -1.594 -7.563 1.00 42.95 C
ATOM 2256 C LEU B 285 15.954 -2.553 -7.194 1.00 44.90 C
ATOM 2257 O LEU B 285 17.123 -2.256 -7.478 1.00 47.75 O
ATOM 2258 CB LEU B 285 15.060 -0.280 -6.816 1.00 33.74 C
ATOM 2259 CG LEU B 285 14.272 0.875 -7.428 1.00 39.68 C
ATOM 2260 CD1 LEU B 285 14.302 2.089 -6.496 1.00 30.69 C
ATOM 2261 CD2 LEU B 285 14.858 1.204 -8.798 1.00 41.33 C
ATOM 2262 N SER B 286 15.628 -3.685 -6.578 1.00 46.08 N
ATOM 2263 CA SER B 286 16.651 -4.586 -6.061 1.00 55.84 C
ATOM 2264 C SER B 286 17.628 -3.809 -5.187 1.00 50.79 C
ATOM 2265 O SER B 286 18.839 -4.022 -5.220 1.00 49.46 O
ATOM 2266 CB SER B 286 17.380 -5.305 -7.198 1.00 60.35 C
ATOM 2267 OG SER B 286 16.467 -5.719 -8.206 1.00 58.58 O
ATOM 2268 N GLN B 287 17.091 -2.863 -4.423 1.00 48.49 N
ATOM 2269 CA GLN B 287 17.905 -2.013 -3.568 1.00 47.48 C
ATOM 2270 C GLN B 287 17.335 -2.077 -2.169 1.00 35.16 C
ATOM 2271 O GLN B 287 16.141 -1.845 -1.976 1.00 43.61 O
ATOM 2272 CB GLN B 287 17.933 -0.570 -4.061 1.00 43.85 C
ATOM 2273 CG GLN B 287 19.218 0.137 -3.685 1.00 48.31 C
ATOM 2274 CD GLN B 287 20.189 0.235 -4.827 1.00 46.20 C
ATOM 2275 NE2 GLN B 287 21.416 0.638 -4.502 1.00 53.62 N
ATOM 2276 OE1 GLN B 287 19.853 -0.042 -6.000 1.00 39.14 O
ATOM 2277 N ALA B 288 18.168 -2.434 -1.198 1.00 28.93 N
ATOM 2278 CA ALA B 288 17.629 -2.676 0.132 1.00 28.96 C
ATOM 2279 C ALA B 288 17.238 -1.387 0.840 1.00 28.37 C
ATOM 2280 O ALA B 288 16.488 -1.430 1.812 1.00 34.47 O
ATOM 2281 CB ALA B 288 18.644 -3.452 0.976 1.00 26.64 C
ATOM 2282 N LEU B 289 17.763 -0.255 0.407 1.00 24.73 N
ATOM 2283 CA LEU B 289 17.522 1.015 1.053 1.00 25.32 C
ATOM 2284 C LEU B 289 17.177 2.017 -0.026 1.00 29.06 C
ATOM 2285 O LEU B 289 17.938 2.171 -0.989 1.00 24.50 O
ATOM 2286 CB LEU B 289 18.750 1.476 1.834 1.00 25.38 C
ATOM 2287 CG LEU B 289 18.680 2.891 2.404 1.00 23.28 C
ATOM 2288 CD1 LEU B 289 17.553 3.063 3.420 1.00 19.31 C
ATOM 2289 CD2 LEU B 289 20.035 3.211 3.039 1.00 23.66 C
ATOM 2290 N VAL B 290 16.018 2.664 0.111 1.00 19.68 N
ATOM 2291 CA VAL B 290 15.611 3.745 -0.777 1.00 23.42 C
ATOM 2292 C VAL B 290 15.130 4.903 0.086 1.00 23.40 C
ATOM 2293 O VAL B 290 14.623 4.704 1.191 1.00 25.55 O
ATOM 2294 CB VAL B 290 14.517 3.317 -1.796 1.00 21.54 C
ATOM 2295 CG1 VAL B 290 14.984 2.098 -2.600 1.00 21.45 C
ATOM 2296 CG2 VAL B 290 13.151 3.058 -1.109 1.00 21.09 C
ATOM 2297 N PHE B 291 15.331 6.131 -0.398 1.00 19.73 N
ATOM 2298 CA PHE B 291 14.783 7.269 0.318 1.00 21.93 C
ATOM 2299 C PHE B 291 14.539 8.391 -0.668 1.00 22.63 C
ATOM 2300 O PHE B 291 15.088 8.417 -1.774 1.00 22.37 O
ATOM 2301 CB PHE B 291 15.667 7.740 1.497 1.00 19.45 C
ATOM 2302 CG PHE B 291 17.137 7.814 1.184 1.00 19.95 C
ATOM 2303 CD1 PHE B 291 17.690 8.968 0.649 1.00 21.08 C
ATOM 2304 CD2 PHE B 291 17.975 6.743 1.476 1.00 19.06 C
ATOM 2305 CE1 PHE B 291 19.040 9.034 0.354 1.00 20.79 C
ATOM 2306 CE2 PHE B 291 19.333 6.792 1.176 1.00 21.57 C
ATOM 2307 CZ PHE B 291 19.865 7.938 0.610 1.00 25.07 C
ATOM 2308 N SER B 292 13.675 9.304 -0.256 1.00 24.65 N
ATOM 2309 CA SER B 292 13.220 10.387 -1.108 1.00 28.98 C
ATOM 2310 C SER B 292 14.242 11.519 -1.161 1.00 27.07 C
ATOM 2311 O SER B 292 15.121 11.641 -0.317 1.00 23.79 O
ATOM 2312 CB SER B 292 11.906 10.939 -0.585 1.00 27.21 C
ATOM 2313 OG SER B 292 12.124 11.477 0.704 1.00 25.77 O
ATOM 2314 N SER B 293 14.060 12.374 -2.159 1.00 25.86 N
ATOM 2315 CA SER B 293 14.837 13.588 -2.323 1.00 27.57 C
ATOM 2316 C SER B 293 14.838 14.439 -1.069 1.00 26.29 C
ATOM 2317 O SER B 293 15.881 14.980 -0.683 1.00 30.75 O
ATOM 2318 CB SER B 293 14.261 14.393 -3.493 1.00 27.06 C
ATOM 2319 OG SER B 293 14.974 15.590 -3.655 1.00 33.46 O
ATOM 2320 N GLU B 294 13.671 14.608 -0.442 1.00 24.21 N
ATOM 2321 CA GLU B 294 13.598 15.409 0.776 1.00 29.84 C
ATOM 2322 C GLU B 294 14.523 14.863 1.860 1.00 29.98 C
ATOM 2323 O GLU B 294 15.202 15.632 2.542 1.00 31.41 O
ATOM 2324 CB GLU B 294 12.159 15.477 1.284 1.00 31.55 C
ATOM 2325 CG GLU B 294 11.303 16.521 0.584 1.00 39.18 C
ATOM 2326 CD GLU B 294 9.826 16.397 0.929 1.00 46.36 C
ATOM 2327 OE1 GLU B 294 9.464 15.497 1.715 1.00 51.07 O
ATOM 2328 OE2 GLU B 294 9.020 17.199 0.408 1.00 56.57 O1-
ATOM 2329 N VAL B 295 14.558 13.541 2.035 1.00 29.12 N
ATOM 2330 CA VAL B 295 15.477 12.948 3.007 1.00 28.03 C
ATOM 2331 C VAL B 295 16.914 13.217 2.582 1.00 30.63 C
ATOM 2332 O VAL B 295 17.736 13.723 3.362 1.00 31.14 O
ATOM 2333 CB VAL B 295 15.207 11.438 3.159 1.00 20.72 C
ATOM 2334 CG1 VAL B 295 16.317 10.767 3.990 1.00 22.47 C
ATOM 2335 CG2 VAL B 295 13.863 11.181 3.834 1.00 19.99 C
ATOM 2336 N LYS B 296 17.221 12.896 1.325 1.00 24.01 N
ATOM 2337 CA LYS B 296 18.573 13.015 0.791 1.00 29.49 C
ATOM 2338 C LYS B 296 19.112 14.422 0.980 1.00 32.71 C
ATOM 2339 O LYS B 296 20.254 14.609 1.432 1.00 34.56 O
ATOM 2340 CB LYS B 296 18.564 12.610 -0.698 1.00 23.35 C
ATOM 2341 CG LYS B 296 19.911 12.696 -1.416 1.00 31.87 C
ATOM 2342 CD LYS B 296 20.004 13.920 -2.270 1.00 28.28 C
ATOM 2343 CE LYS B 296 21.273 13.915 -3.129 1.00 32.71 C
ATOM 2344 NZ LYS B 296 21.434 15.265 -3.763 1.00 34.72 N1+
ATOM 2345 N ASN B 297 18.290 15.428 0.686 1.00 31.99 N
ATOM 2346 CA ASN B 297 18.743 16.802 0.828 1.00 33.46 C
ATOM 2347 C ASN B 297 18.628 17.337 2.254 1.00 39.96 C
ATOM 2348 O ASN B 297 19.236 18.373 2.559 1.00 39.99 O
ATOM 2349 CB ASN B 297 18.001 17.675 -0.190 1.00 37.71 C
ATOM 2350 CG ASN B 297 18.486 17.408 -1.615 1.00 41.17 C
ATOM 2351 ND2 ASN B 297 17.652 16.760 -2.433 1.00 35.48 N
ATOM 2352 OD1 ASN B 297 19.615 17.760 -1.963 1.00 46.21 O
ATOM 2353 N SER B 298 17.935 16.641 3.156 1.00 34.14 N
ATOM 2354 CA SER B 298 18.030 17.020 4.566 1.00 35.60 C
ATOM 2355 C SER B 298 19.310 16.525 5.222 1.00 34.84 C
ATOM 2356 O SER B 298 19.757 17.105 6.220 1.00 33.80 O
ATOM 2357 CB SER B 298 16.850 16.477 5.357 1.00 32.48 C
ATOM 2358 OG SER B 298 15.737 17.328 5.236 1.00 56.80 O
ATOM 2359 N ALA B 299 19.903 15.458 4.699 1.00 33.90 N
ATOM 2360 CA ALA B 299 21.150 14.948 5.248 1.00 29.84 C
ATOM 2361 C ALA B 299 22.232 16.016 5.179 1.00 40.19 C
ATOM 2362 O ALA B 299 22.267 16.824 4.250 1.00 46.18 O
ATOM 2363 CB ALA B 299 21.588 13.700 4.477 1.00 33.31 C
ATOM 2364 N THR B 300 23.126 16.026 6.176 1.00 37.48 N
ATOM 2365 CA THR B 300 24.289 16.914 6.129 1.00 42.61 C
ATOM 2366 C THR B 300 25.600 16.204 5.837 1.00 42.20 C
ATOM 2367 O THR B 300 26.527 16.841 5.333 1.00 43.98 O
ATOM 2368 CB THR B 300 24.462 17.675 7.448 1.00 39.17 C
ATOM 2369 CG2 THR B 300 23.267 18.538 7.708 1.00 35.36 C
ATOM 2370 OG1 THR B 300 24.607 16.742 8.527 1.00 40.85 O
ATOM 2371 N LYS B 301 25.721 14.922 6.159 1.00 37.17 N
ATOM 2372 CA LYS B 301 27.003 14.269 5.970 1.00 35.21 C
ATOM 2373 C LYS B 301 27.190 13.900 4.508 1.00 37.04 C
ATOM 2374 O LYS B 301 26.243 13.887 3.716 1.00 35.11 O
ATOM 2375 CB LYS B 301 27.142 13.030 6.854 1.00 32.04 C
ATOM 2376 CG LYS B 301 26.909 13.265 8.349 1.00 41.74 C
ATOM 2377 CD LYS B 301 27.246 12.003 9.153 1.00 37.76 C
ATOM 2378 CE LYS B 301 26.908 12.142 10.635 1.00 52.36 C
ATOM 2379 NZ LYS B 301 27.579 13.301 11.262 1.00 58.52 N1+
ATOM 2380 N SER B 302 28.436 13.599 4.147 1.00 40.56 N
ATOM 2381 CA SER B 302 28.772 13.357 2.745 1.00 35.98 C
ATOM 2382 C SER B 302 28.558 11.886 2.391 1.00 35.21 C
ATOM 2383 O SER B 302 29.481 11.136 2.072 1.00 30.76 O
ATOM 2384 CB SER B 302 30.195 13.817 2.463 1.00 43.79 C
ATOM 2385 OG SER B 302 30.261 15.220 2.623 1.00 51.61 O
ATOM 2386 N TRP B 303 27.285 11.491 2.407 1.00 30.55 N
ATOM 2387 CA TRP B 303 26.911 10.137 2.025 1.00 25.58 C
ATOM 2388 C TRP B 303 27.194 9.908 0.545 1.00 21.42 C
ATOM 2389 O TRP B 303 27.112 10.827 -0.270 1.00 26.80 O
ATOM 2390 CB TRP B 303 25.427 9.912 2.297 1.00 23.76 C
ATOM 2391 CG TRP B 303 25.066 10.030 3.751 1.00 28.20 C
ATOM 2392 CD1 TRP B 303 24.468 11.092 4.372 1.00 29.21 C
ATOM 2393 CD2 TRP B 303 25.302 9.049 4.769 1.00 23.38 C
ATOM 2394 CE2 TRP B 303 24.789 9.566 5.980 1.00 28.93 C
ATOM 2395 CE3 TRP B 303 25.887 7.778 4.771 1.00 25.26 C
ATOM 2396 NE1 TRP B 303 24.288 10.815 5.713 1.00 28.32 N
ATOM 2397 CZ2 TRP B 303 24.850 8.855 7.182 1.00 29.79 C
ATOM 2398 CZ3 TRP B 303 25.927 7.062 5.958 1.00 25.89 C
ATOM 2399 CH2 TRP B 303 25.419 7.607 7.149 1.00 27.56 C
ATOM 2400 N ASN B 304 27.494 8.657 0.193 1.00 23.18 N
ATOM 2401 CA ASN B 304 27.735 8.287 -1.200 1.00 24.29 C
ATOM 2402 C ASN B 304 26.397 8.037 -1.903 1.00 27.03 C
ATOM 2403 O ASN B 304 26.049 6.913 -2.271 1.00 25.55 O
ATOM 2404 CB ASN B 304 28.652 7.075 -1.277 1.00 29.42 C
ATOM 2405 CG ASN B 304 29.960 7.281 -0.504 1.00 38.73 C
ATOM 2406 ND2 ASN B 304 30.478 6.215 0.084 1.00 30.99 N
ATOM 2407 OD1 ASN B 304 30.474 8.393 -0.425 1.00 35.25 O
ATOM 2408 N PHE B 305 25.653 9.135 -2.097 1.00 28.63 N
ATOM 2409 CA PHE B 305 24.308 9.083 -2.673 1.00 23.34 C
ATOM 2410 C PHE B 305 24.354 8.609 -4.118 1.00 26.90 C
ATOM 2411 O PHE B 305 25.263 8.963 -4.871 1.00 24.58 O
ATOM 2412 CB PHE B 305 23.644 10.463 -2.651 1.00 22.70 C
ATOM 2413 CG PHE B 305 23.307 10.988 -1.280 1.00 24.34 C
ATOM 2414 CD1 PHE B 305 22.474 10.276 -0.422 1.00 21.63 C
ATOM 2415 CD2 PHE B 305 23.789 12.227 -0.868 1.00 24.29 C
ATOM 2416 CE1 PHE B 305 22.151 10.778 0.832 1.00 25.84 C
ATOM 2417 CE2 PHE B 305 23.488 12.727 0.393 1.00 26.60 C
ATOM 2418 CZ PHE B 305 22.665 12.022 1.238 1.00 24.07 C
ATOM 2419 N ILE B 306 23.345 7.838 -4.521 1.00 24.68 N
ATOM 2420 CA ILE B 306 23.153 7.496 -5.926 1.00 24.94 C
ATOM 2421 C ILE B 306 21.682 7.710 -6.286 1.00 24.63 C
ATOM 2422 O ILE B 306 20.788 7.304 -5.534 1.00 25.33 O
ATOM 2423 CB ILE B 306 23.599 6.049 -6.220 1.00 22.22 C
ATOM 2424 CG1 ILE B 306 23.422 5.710 -7.717 1.00 24.23 C
ATOM 2425 CG2 ILE B 306 22.883 5.032 -5.296 1.00 22.46 C
ATOM 2426 CD1 ILE B 306 24.244 4.520 -8.157 1.00 27.31 C
ATOM 2427 N TRP B 307 21.430 8.382 -7.413 1.00 24.42 N
ATOM 2428 CA TRP B 307 20.072 8.527 -7.929 1.00 24.60 C
ATOM 2429 C TRP B 307 19.638 7.223 -8.596 1.00 27.44 C
ATOM 2430 O TRP B 307 20.404 6.639 -9.375 1.00 24.73 O
ATOM 2431 CB TRP B 307 19.990 9.693 -8.926 1.00 28.54 C
ATOM 2432 CG TRP B 307 18.596 9.872 -9.498 1.00 26.77 C
ATOM 2433 CD1 TRP B 307 17.584 10.636 -8.986 1.00 28.08 C
ATOM 2434 CD2 TRP B 307 18.069 9.248 -10.681 1.00 25.02 C
ATOM 2435 CE2 TRP B 307 16.733 9.679 -10.822 1.00 28.67 C
ATOM 2436 CE3 TRP B 307 18.596 8.357 -11.626 1.00 26.24 C
ATOM 2437 NE1 TRP B 307 16.461 10.532 -9.781 1.00 25.73 N
ATOM 2438 CZ2 TRP B 307 15.914 9.256 -11.882 1.00 27.77 C
ATOM 2439 CZ3 TRP B 307 17.780 7.935 -12.674 1.00 31.88 C
ATOM 2440 CH2 TRP B 307 16.448 8.382 -12.786 1.00 22.56 C
ATOM 2441 N LEU B 308 18.412 6.764 -8.299 1.00 19.98 N
ATOM 2442 CA LEU B 308 17.903 5.500 -8.824 1.00 26.19 C
ATOM 2443 C LEU B 308 16.762 5.653 -9.824 1.00 28.62 C
ATOM 2444 O LEU B 308 16.796 5.029 -10.886 1.00 28.21 O
ATOM 2445 CB LEU B 308 17.450 4.593 -7.676 1.00 27.37 C
ATOM 2446 CG LEU B 308 18.548 4.229 -6.679 1.00 32.10 C
ATOM 2447 CD1 LEU B 308 17.972 3.310 -5.637 1.00 29.92 C
ATOM 2448 CD2 LEU B 308 19.697 3.552 -7.414 1.00 25.61 C
ATOM 2449 N THR B 309 15.743 6.446 -9.509 1.00 25.34 N
ATOM 2450 CA THR B 309 14.515 6.527 -10.296 1.00 25.21 C
ATOM 2451 C THR B 309 13.666 7.651 -9.708 1.00 29.92 C
ATOM 2452 O THR B 309 13.989 8.207 -8.653 1.00 28.02 O
ATOM 2453 CB THR B 309 13.744 5.185 -10.286 1.00 31.13 C
ATOM 2454 CG2 THR B 309 13.083 4.960 -8.919 1.00 30.37 C
ATOM 2455 OG1 THR B 309 12.720 5.190 -11.299 1.00 30.77 O
ATOM 2456 N ASP B 310 12.608 8.026 -10.441 1.00 31.39 N
ATOM 2457 CA ASP B 310 11.451 8.740 -9.907 1.00 24.33 C
ATOM 2458 C ASP B 310 10.352 7.800 -9.455 1.00 25.77 C
ATOM 2459 O ASP B 310 10.134 6.736 -10.037 1.00 30.62 O
ATOM 2460 CB ASP B 310 10.854 9.727 -10.915 1.00 28.22 C
ATOM 2461 CG ASP B 310 11.703 10.942 -11.129 1.00 29.69 C
ATOM 2462 OD1 ASP B 310 12.716 10.893 -11.838 1.00 26.00 O
ATOM 2463 OD2 ASP B 310 11.208 12.017 -10.696 1.00 31.13 O1-
ATOM 2464 N SER B 311 9.627 8.236 -8.431 1.00 29.08 N
ATOM 2465 CA SER B 311 8.420 7.546 -8.016 1.00 30.29 C
ATOM 2466 C SER B 311 7.461 8.581 -7.444 1.00 33.79 C
ATOM 2467 O SER B 311 7.720 9.790 -7.446 1.00 33.68 O
ATOM 2468 CB SER B 311 8.746 6.438 -7.010 1.00 33.38 C
ATOM 2469 OG SER B 311 7.655 5.541 -6.865 1.00 42.06 O
ATOM 2470 N GLU B 312 6.335 8.102 -6.957 1.00 30.96 N
ATOM 2471 CA GLU B 312 5.423 8.957 -6.230 1.00 37.23 C
ATOM 2472 C GLU B 312 5.167 8.248 -4.911 1.00 38.96 C
ATOM 2473 O GLU B 312 4.973 7.029 -4.896 1.00 43.44 O
ATOM 2474 CB GLU B 312 4.151 9.190 -7.043 1.00 35.61 C
ATOM 2475 CG GLU B 312 3.420 10.451 -6.630 1.00 51.03 C
ATOM 2476 CD GLU B 312 2.660 10.270 -5.331 1.00 55.88 C
ATOM 2477 OE1 GLU B 312 2.354 9.100 -4.997 1.00 54.51 O
ATOM 2478 OE2 GLU B 312 2.412 11.286 -4.629 1.00 51.10 O1-
ATOM 2479 N LEU B 313 5.250 8.981 -3.804 1.00 33.68 N
ATOM 2480 CA LEU B 313 5.060 8.357 -2.504 1.00 38.57 C
ATOM 2481 C LEU B 313 3.802 8.817 -1.782 1.00 47.25 C
ATOM 2482 O LEU B 313 3.227 8.041 -1.011 1.00 45.05 O
ATOM 2483 CB LEU B 313 6.279 8.608 -1.606 1.00 41.57 C
ATOM 2484 CG LEU B 313 7.611 7.985 -2.046 1.00 40.93 C
ATOM 2485 CD1 LEU B 313 8.677 8.244 -0.995 1.00 37.17 C
ATOM 2486 CD2 LEU B 313 7.464 6.486 -2.310 1.00 32.47 C
ATOM 2487 N LYS B 314 3.334 10.037 -2.040 1.00 43.18 N
ATOM 2488 CA LYS B 314 2.306 10.664 -1.217 1.00 48.76 C
ATOM 2489 C LYS B 314 0.896 10.523 -1.789 1.00 56.55 C
ATOM 2490 O LYS B 314 -0.067 10.942 -1.137 1.00 54.13 O
ATOM 2491 CB LYS B 314 2.648 12.145 -1.021 1.00 46.90 C
ATOM 2492 CG LYS B 314 4.012 12.384 -0.339 1.00 44.10 C
ATOM 2493 CD LYS B 314 4.101 11.741 1.040 1.00 52.60 C
ATOM 2494 CE LYS B 314 5.456 12.041 1.709 1.00 50.86 C
ATOM 2495 NZ LYS B 314 5.681 13.506 1.906 1.00 52.97 N1+
ATOM 2496 N GLY B 315 0.745 9.928 -2.972 1.00 55.94 N
ATOM 2497 CA GLY B 315 -0.530 9.936 -3.662 1.00 61.47 C
ATOM 2498 C GLY B 315 -0.847 11.237 -4.365 1.00 53.17 C
ATOM 2499 O GLY B 315 -1.935 11.364 -4.938 1.00 65.21 O
ATOM 2500 N LYS B 316 0.051 12.215 -4.305 1.00 55.11 N
ATOM 2501 CA LYS B 316 -0.033 13.420 -5.117 1.00 61.41 C
ATOM 2502 C LYS B 316 0.330 13.061 -6.561 1.00 52.99 C
ATOM 2503 O LYS B 316 0.532 11.896 -6.920 1.00 59.59 O
ATOM 2504 CB LYS B 316 0.897 14.495 -4.556 1.00 65.42 C
ATOM 2505 CG LYS B 316 0.496 15.047 -3.191 1.00 63.82 C
ATOM 2506 CD LYS B 316 -0.617 16.079 -3.326 1.00 69.52 C
ATOM 2507 CE LYS B 316 -0.863 16.817 -2.021 1.00 68.84 C
ATOM 2508 NZ LYS B 316 -1.167 15.877 -0.905 1.00 61.58 N1+
ATOM 2509 N SER B 317 0.446 14.068 -7.412 1.00 48.10 N
ATOM 2510 CA SER B 317 0.988 13.845 -8.743 1.00 55.48 C
ATOM 2511 C SER B 317 2.463 14.228 -8.833 1.00 54.43 C
ATOM 2512 O SER B 317 3.038 14.190 -9.926 1.00 49.16 O
ATOM 2513 CB SER B 317 0.170 14.614 -9.779 1.00 56.00 C
ATOM 2514 OG SER B 317 0.031 15.969 -9.388 1.00 66.02 O
ATOM 2515 N GLU B 318 3.086 14.589 -7.711 1.00 45.54 N
ATOM 2516 CA GLU B 318 4.471 15.044 -7.717 1.00 51.17 C
ATOM 2517 C GLU B 318 5.411 13.855 -7.891 1.00 36.10 C
ATOM 2518 O GLU B 318 5.379 12.908 -7.103 1.00 41.95 O
ATOM 2519 CB GLU B 318 4.779 15.798 -6.427 1.00 53.08 C
ATOM 2520 CG GLU B 318 3.931 17.049 -6.242 1.00 60.10 C
ATOM 2521 CD GLU B 318 4.347 18.181 -7.167 1.00 71.42 C
ATOM 2522 OE1 GLU B 318 3.824 18.250 -8.305 1.00 76.39 O
ATOM 2523 OE2 GLU B 318 5.195 19.005 -6.758 1.00 72.42 O1-
ATOM 2524 N SER B 319 6.218 13.889 -8.940 1.00 31.30 N
ATOM 2525 CA SER B 319 7.243 12.879 -9.180 1.00 31.58 C
ATOM 2526 C SER B 319 8.508 13.250 -8.420 1.00 32.42 C
ATOM 2527 O SER B 319 9.110 14.291 -8.698 1.00 30.22 O
ATOM 2528 CB SER B 319 7.552 12.785 -10.669 1.00 28.84 C
ATOM 2529 OG SER B 319 8.445 11.721 -10.941 1.00 30.35 O
ATOM 2530 N ILE B 320 8.932 12.402 -7.490 1.00 28.75 N
ATOM 2531 CA ILE B 320 10.079 12.752 -6.655 1.00 28.57 C
ATOM 2532 C ILE B 320 11.245 11.823 -6.971 1.00 34.24 C
ATOM 2533 O ILE B 320 11.059 10.662 -7.359 1.00 28.51 O
ATOM 2534 CB ILE B 320 9.757 12.686 -5.152 1.00 35.23 C
ATOM 2535 CG1 ILE B 320 9.428 11.252 -4.770 1.00 34.60 C
ATOM 2536 CG2 ILE B 320 8.592 13.633 -4.814 1.00 38.64 C
ATOM 2537 CD1 ILE B 320 9.425 11.022 -3.290 1.00 44.01 C
ATOM 2538 N ASP B 321 12.461 12.339 -6.775 1.00 25.68 N
ATOM 2539 CA ASP B 321 13.669 11.562 -7.005 1.00 24.56 C
ATOM 2540 C ASP B 321 13.852 10.580 -5.865 1.00 25.99 C
ATOM 2541 O ASP B 321 13.716 10.955 -4.699 1.00 26.32 O
ATOM 2542 CB ASP B 321 14.893 12.474 -7.096 1.00 28.11 C
ATOM 2543 CG ASP B 321 14.843 13.410 -8.303 1.00 34.16 C
ATOM 2544 OD1 ASP B 321 14.590 12.924 -9.418 1.00 27.85 O
ATOM 2545 OD2 ASP B 321 15.052 14.636 -8.139 1.00 29.26 O1-
ATOM 2546 N ILE B 322 14.144 9.323 -6.204 1.00 24.62 N
ATOM 2547 CA ILE B 322 14.440 8.270 -5.236 1.00 25.67 C
ATOM 2548 C ILE B 322 15.939 8.007 -5.276 1.00 29.03 C
ATOM 2549 O ILE B 322 16.513 7.814 -6.358 1.00 26.69 O
ATOM 2550 CB ILE B 322 13.659 6.971 -5.521 1.00 24.18 C
ATOM 2551 CG1 ILE B 322 12.148 7.195 -5.535 1.00 24.59 C
ATOM 2552 CG2 ILE B 322 13.974 5.908 -4.436 1.00 24.35 C
ATOM 2553 CD1 ILE B 322 11.625 7.894 -4.264 1.00 27.19 C
ATOM 2554 N TYR B 323 16.571 8.009 -4.104 1.00 22.72 N
ATOM 2555 CA TYR B 323 18.002 7.816 -3.966 1.00 23.19 C
ATOM 2556 C TYR B 323 18.285 6.596 -3.112 1.00 22.92 C
ATOM 2557 O TYR B 323 17.419 6.115 -2.385 1.00 23.98 O
ATOM 2558 CB TYR B 323 18.678 9.028 -3.310 1.00 21.98 C
ATOM 2559 CG TYR B 323 18.589 10.275 -4.143 1.00 26.87 C
ATOM 2560 CD1 TYR B 323 17.472 11.082 -4.077 1.00 28.61 C
ATOM 2561 CD2 TYR B 323 19.626 10.648 -4.992 1.00 26.63 C
ATOM 2562 CE1 TYR B 323 17.374 12.232 -4.828 1.00 24.14 C
ATOM 2563 CE2 TYR B 323 19.543 11.799 -5.754 1.00 29.37 C
ATOM 2564 CZ TYR B 323 18.405 12.584 -5.669 1.00 29.73 C
ATOM 2565 OH TYR B 323 18.296 13.733 -6.406 1.00 30.25 O
ATOM 2566 N SER B 324 19.531 6.126 -3.172 1.00 25.35 N
ATOM 2567 CA SER B 324 20.038 5.198 -2.159 1.00 22.67 C
ATOM 2568 C SER B 324 21.479 5.588 -1.819 1.00 26.04 C
ATOM 2569 O SER B 324 21.944 6.682 -2.149 1.00 25.77 O
ATOM 2570 CB SER B 324 19.928 3.751 -2.659 1.00 26.07 C
ATOM 2571 OG SER B 324 20.317 2.827 -1.665 1.00 25.94 O
ATOM 2572 N ILE B 325 22.174 4.693 -1.122 1.00 25.79 N
ATOM 2573 CA ILE B 325 23.610 4.798 -0.858 1.00 28.55 C
ATOM 2574 C ILE B 325 24.284 3.760 -1.727 1.00 29.14 C
ATOM 2575 O ILE B 325 23.847 2.606 -1.759 1.00 31.62 O
ATOM 2576 CB ILE B 325 23.954 4.542 0.620 1.00 32.05 C
ATOM 2577 CG1 ILE B 325 23.199 5.487 1.556 1.00 28.69 C
ATOM 2578 CG2 ILE B 325 25.459 4.614 0.853 1.00 30.83 C
ATOM 2579 CD1 ILE B 325 23.572 6.915 1.398 1.00 29.95 C
ATOM 2580 N ASP B 326 25.348 4.153 -2.418 1.00 21.70 N
ATOM 2581 CA ASP B 326 26.114 3.220 -3.243 1.00 29.73 C
ATOM 2582 C ASP B 326 27.308 2.774 -2.410 1.00 38.71 C
ATOM 2583 O ASP B 326 28.244 3.543 -2.194 1.00 32.07 O
ATOM 2584 CB ASP B 326 26.536 3.871 -4.559 1.00 31.12 C
ATOM 2585 CG ASP B 326 27.298 2.918 -5.477 1.00 35.57 C
ATOM 2586 OD1 ASP B 326 27.052 1.698 -5.429 1.00 34.89 O
ATOM 2587 OD2 ASP B 326 28.134 3.397 -6.265 1.00 31.63 O1-
ATOM 2588 N ASN B 327 27.237 1.553 -1.882 1.00 38.86 N
ATOM 2589 CA ASN B 327 28.368 0.884 -1.251 1.00 38.65 C
ATOM 2590 C ASN B 327 28.247 -0.600 -1.566 1.00 44.06 C
ATOM 2591 O ASN B 327 27.359 -1.020 -2.311 1.00 37.00 O
ATOM 2592 CB ASN B 327 28.438 1.142 0.263 1.00 42.71 C
ATOM 2593 CG ASN B 327 27.153 0.773 0.999 1.00 45.80 C
ATOM 2594 ND2 ASN B 327 26.927 1.414 2.155 1.00 40.05 N
ATOM 2595 OD1 ASN B 327 26.376 -0.066 0.544 1.00 46.21 O
ATOM 2596 N GLU B 328 29.142 -1.404 -0.986 1.00 50.77 N
ATOM 2597 CA GLU B 328 29.217 -2.814 -1.361 1.00 50.20 C
ATOM 2598 C GLU B 328 27.946 -3.549 -0.974 1.00 45.71 C
ATOM 2599 O GLU B 328 27.495 -4.454 -1.686 1.00 52.27 O
ATOM 2600 CB GLU B 328 30.437 -3.456 -0.694 1.00 59.58 C
ATOM 2601 CG GLU B 328 31.030 -4.676 -1.401 1.00 59.43 C
ATOM 2602 CD GLU B 328 32.366 -5.088 -0.782 1.00 62.51 C
ATOM 2603 OE1 GLU B 328 32.545 -4.837 0.436 1.00 59.36 O
ATOM 2604 OE2 GLU B 328 33.228 -5.652 -1.506 1.00 59.91 O1-
ATOM 2605 N MET B 329 27.337 -3.135 0.127 1.00 47.99 N
ATOM 2606 CA MET B 329 26.179 -3.828 0.666 1.00 47.80 C
ATOM 2607 C MET B 329 24.959 -3.641 -0.224 1.00 56.31 C
ATOM 2608 O MET B 329 24.181 -4.581 -0.434 1.00 55.37 O
ATOM 2609 CB MET B 329 25.919 -3.287 2.059 1.00 45.69 C
ATOM 2610 CG MET B 329 24.631 -3.692 2.714 1.00 49.56 C
ATOM 2611 SD MET B 329 24.964 -3.503 4.484 1.00 59.10 S
ATOM 2612 CE MET B 329 26.467 -2.516 4.439 1.00 51.57 C
ATOM 2613 N THR B 330 24.769 -2.429 -0.745 1.00 50.52 N
ATOM 2614 CA THR B 330 23.615 -2.145 -1.585 1.00 51.34 C
ATOM 2615 C THR B 330 23.842 -2.516 -3.047 1.00 53.63 C
ATOM 2616 O THR B 330 22.900 -2.415 -3.839 1.00 44.18 O
ATOM 2617 CB THR B 330 23.248 -0.659 -1.484 1.00 47.60 C
ATOM 2618 CG2 THR B 330 23.144 -0.212 -0.027 1.00 42.37 C
ATOM 2619 OG1 THR B 330 24.262 0.122 -2.134 1.00 48.32 O
ATOM 2620 N ARG B 331 25.059 -2.933 -3.426 1.00 48.19 N
ATOM 2621 CA ARG B 331 25.343 -3.331 -4.809 1.00 50.64 C
ATOM 2622 C ARG B 331 24.945 -4.793 -5.004 1.00 55.12 C
ATOM 2623 O ARG B 331 25.774 -5.706 -5.011 1.00 64.78 O
ATOM 2624 CB ARG B 331 26.810 -3.099 -5.156 1.00 47.27 C
ATOM 2625 CG ARG B 331 27.203 -1.625 -5.311 1.00 47.73 C
ATOM 2626 CD ARG B 331 28.696 -1.446 -5.679 1.00 44.37 C
ATOM 2627 NE ARG B 331 29.159 -0.086 -5.413 1.00 40.47 N
ATOM 2628 CZ ARG B 331 30.185 0.228 -4.627 1.00 48.70 C
ATOM 2629 NH1 ARG B 331 30.979 -0.700 -4.119 1.00 40.21 N1+
ATOM 2630 NH2 ARG B 331 30.429 1.510 -4.357 1.00 39.06 N
ATOM 2631 N LYS B 332 23.643 -5.011 -5.190 1.00 68.61 N
ATOM 2632 CA LYS B 332 23.061 -6.344 -5.273 1.00 62.24 C
ATOM 2633 C LYS B 332 22.392 -6.559 -6.627 1.00 63.75 C
ATOM 2634 O LYS B 332 22.015 -5.609 -7.324 1.00 66.31 O
ATOM 2635 CB LYS B 332 22.049 -6.576 -4.142 1.00 55.51 C
ATOM 2636 CG LYS B 332 22.694 -6.676 -2.762 1.00 58.66 C
ATOM 2637 CD LYS B 332 23.810 -7.713 -2.754 1.00 56.10 C
ATOM 2638 CE LYS B 332 24.715 -7.553 -1.539 1.00 56.71 C
ATOM 2639 NZ LYS B 332 26.139 -7.871 -1.890 1.00 59.02 N1+
ATOM 2640 N SER B 333 22.253 -7.835 -6.994 1.00 69.12 N
ATOM 2641 CA SER B 333 21.634 -8.256 -8.251 1.00 72.31 C
ATOM 2642 C SER B 333 20.290 -8.905 -7.951 1.00 74.90 C
ATOM 2643 O SER B 333 20.238 -9.953 -7.296 1.00 74.70 O
ATOM 2644 CB SER B 333 22.528 -9.235 -9.015 1.00 62.51 C
ATOM 2645 OG SER B 333 23.613 -8.564 -9.625 1.00 63.62 O
ATOM 2646 N SER B 334 19.215 -8.289 -8.438 1.00 84.11 N
ATOM 2647 CA SER B 334 17.854 -8.777 -8.210 1.00 74.82 C
ATOM 2648 C SER B 334 17.588 -9.082 -6.735 1.00 73.89 C
ATOM 2649 O SER B 334 18.263 -8.563 -5.838 1.00 77.34 O
ATOM 2650 CB SER B 334 17.583 -10.024 -9.060 1.00 70.42 C
ATOM 2651 OG SER B 334 16.254 -10.480 -8.871 1.00 84.03 O
ATOM 2652 N GLY B 336 14.545 -9.077 -6.930 1.00 75.90 N
ATOM 2653 CA GLY B 336 13.410 -9.362 -7.790 1.00 64.64 C
ATOM 2654 C GLY B 336 12.758 -10.691 -7.467 1.00 66.26 C
ATOM 2655 O GLY B 336 12.659 -11.088 -6.304 1.00 64.30 O
ATOM 2656 N LEU B 337 12.297 -11.393 -8.500 1.00 63.80 N
ATOM 2657 CA LEU B 337 11.720 -12.709 -8.264 1.00 69.33 C
ATOM 2658 C LEU B 337 12.783 -13.742 -7.907 1.00 69.13 C
ATOM 2659 O LEU B 337 12.439 -14.790 -7.349 1.00 55.92 O
ATOM 2660 CB LEU B 337 10.906 -13.164 -9.486 1.00 71.43 C
ATOM 2661 CG LEU B 337 11.526 -13.148 -10.888 1.00 76.65 C
ATOM 2662 CD1 LEU B 337 12.400 -14.375 -11.141 1.00 83.05 C
ATOM 2663 CD2 LEU B 337 10.448 -13.032 -11.958 1.00 69.62 C
ATOM 2664 N GLU B 338 14.062 -13.469 -8.216 1.00 69.55 N
ATOM 2665 CA GLU B 338 15.131 -14.387 -7.830 1.00 71.34 C
ATOM 2666 C GLU B 338 15.260 -14.467 -6.311 1.00 58.48 C
ATOM 2667 O GLU B 338 15.459 -15.553 -5.756 1.00 56.16 O
ATOM 2668 CB GLU B 338 16.469 -13.962 -8.452 1.00 68.97 C
ATOM 2669 CG GLU B 338 17.621 -14.954 -8.172 1.00 75.14 C
ATOM 2670 CD GLU B 338 18.969 -14.565 -8.812 1.00 77.93 C
ATOM 2671 OE1 GLU B 338 19.236 -14.996 -9.957 1.00 77.80 O
ATOM 2672 OE2 GLU B 338 19.788 -13.882 -8.150 1.00 73.35 O1-
ATOM 2673 N ILE B 339 15.144 -13.332 -5.620 1.00 52.40 N
ATOM 2674 CA ILE B 339 15.191 -13.371 -4.161 1.00 58.33 C
ATOM 2675 C ILE B 339 14.022 -14.182 -3.620 1.00 51.58 C
ATOM 2676 O ILE B 339 14.184 -15.003 -2.710 1.00 43.21 O
ATOM 2677 CB ILE B 339 15.211 -11.947 -3.573 1.00 52.88 C
ATOM 2678 CG1 ILE B 339 16.086 -11.030 -4.423 1.00 61.07 C
ATOM 2679 CG2 ILE B 339 15.706 -11.980 -2.139 1.00 50.00 C
ATOM 2680 CD1 ILE B 339 17.566 -11.254 -4.220 1.00 63.63 C
ATOM 2681 N ALA B 340 12.830 -13.986 -4.186 1.00 56.01 N
ATOM 2682 CA ALA B 340 11.658 -14.703 -3.696 1.00 46.35 C
ATOM 2683 C ALA B 340 11.843 -16.205 -3.835 1.00 47.17 C
ATOM 2684 O ALA B 340 11.574 -16.962 -2.893 1.00 42.72 O
ATOM 2685 CB ALA B 340 10.409 -14.249 -4.447 1.00 46.03 C
ATOM 2686 N ARG B 341 12.313 -16.649 -5.011 1.00 51.84 N
ATOM 2687 CA ARG B 341 12.474 -18.077 -5.287 1.00 51.30 C
ATOM 2688 C ARG B 341 13.583 -18.694 -4.441 1.00 47.31 C
ATOM 2689 O ARG B 341 13.479 -19.858 -4.031 1.00 41.42 O
ATOM 2690 CB ARG B 341 12.771 -18.287 -6.773 1.00 56.79 C
ATOM 2691 CG ARG B 341 12.980 -19.737 -7.177 1.00 58.01 C
ATOM 2692 CD ARG B 341 13.014 -19.894 -8.701 1.00 70.28 C
ATOM 2693 NE ARG B 341 14.028 -19.043 -9.319 1.00 80.46 N
ATOM 2694 CZ ARG B 341 13.765 -17.973 -10.061 1.00 81.60 C
ATOM 2695 NH1 ARG B 341 12.522 -17.605 -10.330 1.00 80.72 N1+
ATOM 2696 NH2 ARG B 341 14.774 -17.254 -10.546 1.00 80.05 N
ATOM 2697 N ASN B 342 14.665 -17.937 -4.203 1.00 35.53 N
ATOM 2698 CA ASN B 342 15.740 -18.398 -3.326 1.00 44.51 C
ATOM 2699 C ASN B 342 15.226 -18.697 -1.922 1.00 38.34 C
ATOM 2700 O ASN B 342 15.456 -19.786 -1.382 1.00 37.34 O
ATOM 2701 CB ASN B 342 16.858 -17.347 -3.275 1.00 40.48 C
ATOM 2702 CG ASN B 342 17.976 -17.712 -2.290 1.00 59.00 C
ATOM 2703 ND2 ASN B 342 18.466 -18.948 -2.385 1.00 61.43 N
ATOM 2704 OD1 ASN B 342 18.385 -16.895 -1.447 1.00 52.73 O
ATOM 2705 N ILE B 343 14.528 -17.735 -1.311 1.00 44.17 N
ATOM 2706 CA ILE B 343 14.017 -17.931 0.047 1.00 38.34 C
ATOM 2707 C ILE B 343 13.171 -19.191 0.124 1.00 36.52 C
ATOM 2708 O ILE B 343 13.351 -20.027 1.018 1.00 34.14 O
ATOM 2709 CB ILE B 343 13.231 -16.694 0.511 1.00 41.18 C
ATOM 2710 CG1 ILE B 343 14.139 -15.468 0.492 1.00 35.91 C
ATOM 2711 CG2 ILE B 343 12.571 -16.934 1.873 1.00 30.88 C
ATOM 2712 CD1 ILE B 343 13.380 -14.155 0.491 1.00 44.77 C
ATOM 2713 N GLY B 344 12.262 -19.368 -0.837 1.00 33.73 N
ATOM 2714 CA GLY B 344 11.355 -20.505 -0.769 1.00 36.43 C
ATOM 2715 C GLY B 344 12.078 -21.828 -0.926 1.00 43.43 C
ATOM 2716 O GLY B 344 11.817 -22.783 -0.184 1.00 37.61 O
ATOM 2717 N HIS B 345 13.017 -21.892 -1.876 1.00 39.45 N
ATOM 2718 CA HIS B 345 13.812 -23.098 -2.054 1.00 38.67 C
ATOM 2719 C HIS B 345 14.561 -23.448 -0.767 1.00 39.88 C
ATOM 2720 O HIS B 345 14.566 -24.606 -0.334 1.00 39.52 O
ATOM 2721 CB HIS B 345 14.783 -22.895 -3.219 1.00 41.29 C
ATOM 2722 CG HIS B 345 15.495 -24.139 -3.642 1.00 52.10 C
ATOM 2723 CD2 HIS B 345 16.723 -24.618 -3.322 1.00 63.58 C
ATOM 2724 ND1 HIS B 345 14.926 -25.074 -4.480 1.00 63.72 N
ATOM 2725 CE1 HIS B 345 15.780 -26.066 -4.673 1.00 67.29 C
ATOM 2726 NE2 HIS B 345 16.875 -25.818 -3.976 1.00 62.83 N
ATOM 2727 N TYR B 346 15.172 -22.452 -0.125 1.00 32.58 N
ATOM 2728 CA TYR B 346 15.917 -22.713 1.104 1.00 33.17 C
ATOM 2729 C TYR B 346 14.992 -23.167 2.224 1.00 32.91 C
ATOM 2730 O TYR B 346 15.301 -24.116 2.951 1.00 37.07 O
ATOM 2731 CB TYR B 346 16.689 -21.457 1.517 1.00 31.68 C
ATOM 2732 CG TYR B 346 17.455 -21.589 2.808 1.00 27.57 C
ATOM 2733 CD1 TYR B 346 16.860 -21.293 4.026 1.00 29.58 C
ATOM 2734 CD2 TYR B 346 18.796 -21.992 2.806 1.00 36.09 C
ATOM 2735 CE1 TYR B 346 17.563 -21.398 5.209 1.00 28.90 C
ATOM 2736 CE2 TYR B 346 19.512 -22.115 3.994 1.00 30.98 C
ATOM 2737 CZ TYR B 346 18.887 -21.823 5.192 1.00 31.94 C
ATOM 2738 OH TYR B 346 19.585 -21.920 6.377 1.00 27.19 O
ATOM 2739 N LEU B 347 13.866 -22.474 2.408 1.00 32.88 N
ATOM 2740 CA LEU B 347 12.997 -22.803 3.535 1.00 38.67 C
ATOM 2741 C LEU B 347 12.293 -24.139 3.321 1.00 38.42 C
ATOM 2742 O LEU B 347 11.998 -24.843 4.291 1.00 39.67 O
ATOM 2743 CB LEU B 347 11.992 -21.672 3.762 1.00 37.69 C
ATOM 2744 CG LEU B 347 12.571 -20.330 4.220 1.00 27.23 C
ATOM 2745 CD1 LEU B 347 11.465 -19.296 4.343 1.00 32.53 C
ATOM 2746 CD2 LEU B 347 13.254 -20.500 5.553 1.00 29.13 C
ATOM 2747 N GLU B 348 12.057 -24.519 2.063 1.00 36.46 N
ATOM 2748 CA GLU B 348 11.489 -25.831 1.775 1.00 46.25 C
ATOM 2749 C GLU B 348 12.349 -26.969 2.324 1.00 49.97 C
ATOM 2750 O GLU B 348 11.818 -28.029 2.678 1.00 56.06 O
ATOM 2751 CB GLU B 348 11.314 -25.986 0.266 1.00 47.61 C
ATOM 2752 CG GLU B 348 10.637 -27.277 -0.169 1.00 58.92 C
ATOM 2753 CD GLU B 348 9.206 -27.384 0.316 1.00 60.75 C
ATOM 2754 OE1 GLU B 348 8.567 -26.328 0.508 1.00 64.08 O
ATOM 2755 OE2 GLU B 348 8.720 -28.523 0.517 1.00 65.98 O1-
ATOM 2756 N ARG B 349 13.670 -26.779 2.411 1.00 46.87 N
ATOM 2757 CA ARG B 349 14.592 -27.862 2.742 1.00 48.57 C
ATOM 2758 C ARG B 349 15.125 -27.803 4.170 1.00 49.51 C
ATOM 2759 O ARG B 349 16.220 -28.313 4.431 1.00 56.29 O
ATOM 2760 CB ARG B 349 15.757 -27.881 1.756 1.00 50.05 C
ATOM 2761 CG ARG B 349 15.428 -28.616 0.483 1.00 61.31 C
ATOM 2762 CD ARG B 349 15.930 -27.887 -0.744 1.00 66.94 C
ATOM 2763 NE ARG B 349 15.218 -28.348 -1.928 1.00 70.35 N
ATOM 2764 CZ ARG B 349 14.101 -27.796 -2.383 1.00 69.22 C
ATOM 2765 NH1 ARG B 349 13.563 -26.740 -1.792 1.00 60.16 N1+
ATOM 2766 NH2 ARG B 349 13.507 -28.316 -3.455 1.00 69.26 N
ATOM 2767 N VAL B 350 14.385 -27.207 5.101 1.00 52.64 N
ATOM 2768 CA VAL B 350 14.793 -27.187 6.514 1.00 56.36 C
ATOM 2769 C VAL B 350 13.606 -27.438 7.451 1.00 65.53 C
ATOM 2770 O VAL B 350 13.720 -28.234 8.392 1.00 76.97 O
ATOM 2771 CB VAL B 350 15.482 -25.857 6.902 1.00 50.95 C
ATOM 2772 CG1 VAL B 350 16.769 -25.644 6.104 1.00 47.74 C
ATOM 2773 CG2 VAL B 350 14.526 -24.663 6.757 1.00 42.89 C
ATOM 2774 OXT VAL B 350 12.515 -26.862 7.312 1.00 63.12 O1-
TER
HETATM 2775 P FMN B 400 27.906 10.096 45.675 1.00101.99 P
HETATM 2776 O1P FMN B 400 27.475 11.545 45.791 1.00 86.46 O
HETATM 2777 O2P FMN B 400 29.048 9.833 46.639 1.00 94.32 O1-
HETATM 2778 O3P FMN B 400 28.338 9.810 44.245 1.00 80.22 O
HETATM 2779 C5' FMN B 400 26.175 8.145 45.207 1.00 67.94 C
HETATM 2780 O5' FMN B 400 26.650 9.153 46.074 1.00 80.03 O
HETATM 2781 C4' FMN B 400 24.769 7.730 45.625 1.00 53.32 C
HETATM 2782 O4' FMN B 400 23.909 8.847 45.583 1.00 50.07 O
HETATM 2783 C3' FMN B 400 24.292 6.654 44.670 1.00 50.93 C
HETATM 2784 O3' FMN B 400 24.856 5.428 45.102 1.00 50.83 O
HETATM 2785 C2' FMN B 400 22.751 6.611 44.584 1.00 40.39 C
HETATM 2786 O2' FMN B 400 22.368 5.853 43.451 1.00 44.38 O
HETATM 2787 C1' FMN B 400 22.183 6.025 45.864 1.00 42.67 C
HETATM 2788 N1 FMN B 400 21.272 8.619 46.803 1.00 35.67 N
HETATM 2789 C2 FMN B 400 20.865 9.855 47.254 1.00 39.03 C
HETATM 2790 O2 FMN B 400 21.685 10.759 47.397 1.00 37.49 O
HETATM 2791 N3 FMN B 400 19.525 10.094 47.532 1.00 36.26 N
HETATM 2792 C4 FMN B 400 18.582 9.097 47.354 1.00 38.24 C
HETATM 2793 C4A FMN B 400 18.997 7.857 46.907 1.00 35.99 C
HETATM 2794 O4 FMN B 400 17.386 9.289 47.606 1.00 32.55 O
HETATM 2795 C5A FMN B 400 18.456 5.635 46.286 1.00 37.72 C
HETATM 2796 N5 FMN B 400 18.056 6.876 46.734 1.00 35.35 N
HETATM 2797 C6 FMN B 400 17.517 4.641 46.106 1.00 34.12 C
HETATM 2798 C7 FMN B 400 17.887 3.389 45.654 1.00 35.58 C
HETATM 2799 C7M FMN B 400 16.831 2.334 45.481 1.00 38.53 C
HETATM 2800 C8 FMN B 400 19.216 3.121 45.374 1.00 36.44 C
HETATM 2801 C8M FMN B 400 19.624 1.764 44.883 1.00 42.42 C
HETATM 2802 C9 FMN B 400 20.170 4.119 45.539 1.00 35.49 C
HETATM 2803 C9A FMN B 400 19.789 5.379 45.993 1.00 38.39 C
HETATM 2804 C10 FMN B 400 20.345 7.613 46.620 1.00 39.87 C
HETATM 2805 N10 FMN B 400 20.737 6.366 46.159 1.00 40.32 N
HETATM 2806 O HOH S 3 -0.097 -6.663 12.494 1.00 20.43 O
HETATM 2807 O HOH S 4 18.753 -7.272 4.224 1.00 25.18 O
HETATM 2808 O HOH S 5 11.799 14.618 -9.729 1.00 25.71 O
HETATM 2809 O HOH S 6 13.212 9.640 -13.920 1.00 26.77 O
HETATM 2810 O HOH S 7 21.390 -6.744 4.631 1.00 24.91 O
HETATM 2811 O HOH S 8 16.331 5.891 55.896 1.00 32.75 O
HETATM 2812 O HOH S 9 9.606 12.765 1.231 1.00 24.73 O
HETATM 2813 O HOH S 10 13.472 -12.400 4.068 1.00 27.67 O
HETATM 2814 O HOH S 11 10.517 -2.348 1.992 1.00 28.37 O
HETATM 2815 O HOH S 12 -2.587 5.550 6.679 1.00 29.09 O
HETATM 2816 O HOH S 13 27.694 13.287 -0.589 1.00 26.50 O
HETATM 2817 O HOH S 14 16.119 15.212 -6.147 1.00 31.65 O
HETATM 2818 O HOH S 15 2.175 -6.233 56.944 1.00 34.29 O
HETATM 2819 O HOH S 16 15.032 12.893 -12.741 1.00 29.01 O
HETATM 2820 O HOH S 17 27.535 -6.587 7.332 1.00 29.95 O
HETATM 2821 O HOH S 18 23.628 -9.543 13.694 1.00 30.06 O
HETATM 2822 O HOH S 20 23.727 -12.906 3.093 1.00 29.16 O
HETATM 2823 O HOH S 21 23.236 14.841 56.690 1.00 26.13 O
HETATM 2824 O HOH S 22 12.509 14.968 -6.004 1.00 29.77 O
HETATM 2825 O HOH S 23 15.646 11.492 16.112 1.00 29.95 O
HETATM 2826 O HOH S 24 3.891 9.820 44.159 1.00 34.04 O
HETATM 2827 O HOH S 25 20.981 -16.121 2.375 1.00 37.73 O
HETATM 2828 O HOH S 26 15.441 10.930 57.035 1.00 30.85 O
HETATM 2829 O HOH S 27 -5.361 11.249 1.849 1.00 34.23 O
HETATM 2830 O HOH S 28 29.083 9.742 56.639 1.00 32.69 O
HETATM 2831 O HOH S 29 18.008 10.793 15.862 1.00 34.36 O
HETATM 2832 O HOH S 30 28.358 -5.539 14.317 1.00 34.32 O
HETATM 2833 O HOH S 31 2.712 -6.316 13.497 1.00 32.21 O
HETATM 2834 O HOH S 32 21.707 8.720 58.024 1.00 27.79 O
HETATM 2835 O HOH S 35 -0.391 -5.911 63.532 1.00 39.46 O
HETATM 2836 O HOH S 36 14.197 15.429 -11.298 1.00 31.54 O
HETATM 2837 O HOH S 38 20.609 14.305 -8.119 1.00 36.16 O
HETATM 2838 O HOH S 39 20.901 14.917 9.685 1.00 37.40 O
HETATM 2839 O HOH S 41 -2.308 -2.611 61.267 1.00 31.49 O
HETATM 2840 O HOH S 42 16.266 4.656 -13.435 1.00 32.25 O
HETATM 2841 O HOH S 43 13.682 17.604 57.094 1.00 38.72 O
HETATM 2842 O HOH S 44 27.960 6.891 2.211 1.00 30.06 O
HETATM 2843 O HOH S 45 7.052 -13.517 -2.166 1.00 51.44 O
HETATM 2844 O HOH S 46 26.932 3.223 13.469 1.00 42.90 O
HETATM 2845 O HOH S 47 16.994 17.046 59.332 1.00 36.67 O
HETATM 2846 O HOH S 48 15.647 -3.285 55.631 1.00 36.17 O
HETATM 2847 O HOH S 49 1.291 0.044 60.539 1.00 37.16 O
HETATM 2848 O HOH S 50 10.006 2.684 58.493 1.00 36.49 O
HETATM 2849 O HOH S 52 -0.676 13.153 9.882 1.00 44.19 O
HETATM 2850 O HOH S 53 5.691 12.415 41.660 1.00 43.32 O
HETATM 2851 O HOH S 54 12.479 17.840 60.073 1.00 46.52 O
HETATM 2852 O HOH S 55 16.146 16.864 54.093 1.00 32.98 O
HETATM 2853 O HOH S 56 19.148 12.490 -12.706 1.00 40.05 O
HETATM 2854 O HOH S 57 15.580 15.529 57.820 1.00 42.62 O
HETATM 2855 O HOH S 59 21.866 -8.438 15.811 1.00 36.05 O
HETATM 2856 O HOH S 60 0.707 12.466 6.524 1.00 38.23 O
HETATM 2857 O HOH S 61 17.281 -17.388 17.120 1.00 35.94 O
HETATM 2858 O HOH S 62 -4.458 16.567 21.392 1.00 43.48 O
HETATM 2859 O HOH S 63 18.035 -6.885 2.209 1.00 37.73 O
HETATM 2860 O HOH S 64 23.821 15.916 49.207 1.00 31.94 O
HETATM 2861 O HOH S 65 17.925 -20.135 14.024 1.00 34.47 O
HETATM 2862 O HOH S 66 13.688 4.986 -13.701 1.00 34.57 O
HETATM 2863 O HOH S 67 14.037 -7.152 52.747 1.00 37.88 O
HETATM 2864 O HOH S 68 11.174 14.072 -1.792 1.00 31.34 O
HETATM 2865 O HOH S 69 23.368 8.921 18.305 1.00 52.07 O
HETATM 2866 O HOH S 70 2.586 -8.739 55.551 1.00 40.89 O
HETATM 2867 O HOH S 71 27.196 8.125 54.866 1.00 39.01 O
HETATM 2868 O HOH S 72 24.290 1.007 -5.072 1.00 42.92 O
HETATM 2869 O HOH S 74 1.414 22.859 14.868 1.00 41.12 O
HETATM 2870 O HOH S 75 15.936 6.891 20.838 1.00 39.90 O
HETATM 2871 O HOH S 76 24.929 9.665 11.112 1.00 41.67 O
HETATM 2872 O HOH S 78 1.435 -11.201 23.671 1.00 47.37 O
HETATM 2873 O HOH S 79 20.277 11.086 58.184 1.00 38.48 O
HETATM 2874 O HOH S 80 19.514 -18.957 15.571 1.00 39.41 O
HETATM 2875 O HOH S 81 24.443 8.757 13.415 1.00 40.37 O
HETATM 2876 O HOH S 82 21.922 -26.605 12.925 1.00 45.14 O
HETATM 2877 O HOH S 83 5.521 -5.139 61.478 1.00 37.06 O
HETATM 2878 O HOH S 86 27.076 0.058 8.795 1.00 40.66 O
HETATM 2879 O HOH S 87 25.169 7.723 17.770 1.00 55.85 O
HETATM 2880 O HOH S 88 28.394 3.742 2.560 1.00 42.51 O
HETATM 2881 O HOH S 89 3.223 -20.971 9.339 1.00 40.84 O
HETATM 2882 O HOH S 90 23.012 15.381 46.384 1.00 41.94 O
HETATM 2883 O HOH S 91 24.051 -7.859 54.321 1.00 44.84 O
HETATM 2884 O HOH S 92 13.496 7.111 34.091 1.00 51.52 O
HETATM 2885 O HOH S 93 22.184 -1.650 57.674 1.00 38.93 O
HETATM 2886 O HOH S 95 8.743 -18.975 18.918 1.00 31.28 O
HETATM 2887 O HOH S 99 -4.583 -2.197 62.691 1.00 38.43 O
HETATM 2888 O HOH S 104 3.693 -2.451 -1.900 1.00 38.84 O
HETATM 2889 O HOH S 105 18.076 -13.614 16.619 1.00 39.02 O
HETATM 2890 O HOH S 106 -15.335 4.717 20.593 1.00 39.48 O
HETATM 2891 O HOH S 108 15.295 -18.794 13.685 1.00 38.87 O
HETATM 2892 O HOH S 109 32.661 5.423 1.890 1.00 40.78 O
HETATM 2893 O HOH S 110 20.557 13.488 -10.924 1.00 39.83 O
HETATM 2894 O HOH S 112 6.102 -10.337 53.523 1.00 44.54 O
HETATM 2895 O HOH S 113 24.830 -11.767 14.785 1.00 33.91 O
HETATM 2896 O HOH S 114 26.841 11.234 -4.104 1.00 33.98 O
HETATM 2897 O HOH S 116 17.947 19.685 57.204 1.00 49.12 O
HETATM 2898 O HOH S 117 16.288 11.574 19.802 1.00 48.57 O
HETATM 2899 O HOH S 118 20.490 18.692 -4.118 1.00 50.69 O
HETATM 2900 O HOH S 119 11.194 16.178 -3.575 1.00 36.04 O
HETATM 2901 O HOH S 120 18.373 -23.054 13.582 1.00 44.10 O
HETATM 2902 O HOH S 121 21.360 13.488 58.372 1.00 29.25 O
HETATM 2903 O HOH S 124 -0.930 -3.459 63.146 1.00 49.08 O
HETATM 2904 O HOH S 125 17.746 19.333 54.815 1.00 47.96 O
HETATM 2905 O HOH S 126 21.063 19.045 -0.228 1.00 53.56 O
HETATM 2906 O HOH S 127 -1.720 5.031 16.697 1.00 47.48 O
HETATM 2907 O HOH S 128 20.470 -15.147 16.776 1.00 38.69 O
HETATM 2908 O HOH S 129 12.070 -0.564 57.522 1.00 39.47 O
HETATM 2909 O HOH S 130 0.417 -10.760 45.114 1.00 48.48 O
HETATM 2910 O HOH S 131 23.665 -0.755 51.121 1.00 38.63 O
HETATM 2911 O HOH S 132 0.739 11.072 2.838 1.00 51.63 O
HETATM 2912 O HOH S 133 7.710 -2.174 59.643 1.00 39.92 O
HETATM 2913 O HOH S 135 29.042 6.662 53.863 1.00 37.63 O
HETATM 2914 O HOH S 136 24.292 18.496 48.546 1.00 41.99 O
HETATM 2915 O HOH S 138 18.157 -5.526 33.541 1.00 61.05 O
HETATM 2916 O HOH S 139 23.132 20.250 47.041 1.00 53.49 O
HETATM 2917 O HOH S 140 0.658 -21.177 10.005 1.00 41.50 O
HETATM 2918 O HOH S 141 7.539 13.859 56.627 1.00 36.15 O
HETATM 2919 O HOH S 142 15.124 -16.669 15.667 1.00 36.43 O
HETATM 2920 O HOH S 143 -3.957 -2.468 65.589 1.00 44.77 O
HETATM 2921 O HOH S 144 25.524 -24.694 12.268 1.00 43.49 O
HETATM 2922 O HOH S 145 9.343 -3.289 58.298 1.00 43.10 O
HETATM 2923 O HOH S 148 26.504 6.260 14.555 1.00 41.21 O
HETATM 2924 O HOH S 151 -0.107 20.366 25.512 1.00 56.68 O
HETATM 2925 O HOH S 152 -3.381 -9.348 58.100 1.00 34.44 O
HETATM 2926 O HOH S 154 1.825 -10.977 46.929 1.00 52.00 O
HETATM 2927 O HOH S 157 -0.239 -12.233 52.670 1.00 44.06 O
HETATM 2928 O HOH S 159 9.015 16.816 -7.823 1.00 43.69 O
HETATM 2929 O HOH S 160 7.719 -10.066 50.715 1.00 44.46 O
HETATM 2930 O HOH S 161 14.783 3.608 29.403 1.00 56.36 O
HETATM 2931 O HOH S 163 2.352 7.080 14.228 1.00 42.56 O
HETATM 2932 O HOH S 165 4.273 12.673 35.012 1.00 49.34 O
HETATM 2933 O HOH S 166 4.951 11.886 58.597 1.00 38.37 O
HETATM 2934 O HOH S 172 25.177 7.113 56.687 1.00 34.53 O
HETATM 2935 O HOH S 180 18.789 -25.536 0.270 1.00 36.68 O
HETATM 2936 O HOH S 181 9.637 -0.350 3.199 1.00 33.71 O
HETATM 2937 O HOH S 182 19.944 -3.231 -7.492 1.00 43.19 O
HETATM 2938 O HOH S 184 18.877 -30.114 4.293 1.00 51.42 O
HETATM 2939 O HOH S 185 11.989 -5.103 -0.064 1.00 33.92 O
HETATM 2940 O HOH S 189 22.244 -5.622 15.550 1.00 43.71 O
HETATM 2941 O HOH S 190 24.521 -4.955 16.990 1.00 45.70 O
HETATM 2942 O HOH S 191 17.102 24.468 48.758 1.00 50.14 O
HETATM 2943 O HOH S 192 24.506 4.730 57.344 1.00 41.86 O
HETATM 2944 O HOH S 194 22.542 -1.562 18.513 1.00 47.29 O
HETATM 2945 O HOH S 195 7.049 -9.260 2.537 1.00 33.86 O
HETATM 2946 O HOH S 196 4.663 -5.341 4.636 1.00 33.66 O
HETATM 2947 O HOH S 198 4.694 -6.387 2.730 1.00 34.79 O
HETATM 2948 O HOH S 199 21.952 -5.652 2.287 1.00 43.21 O
HETATM 2949 O HOH S 201 10.547 3.217 60.995 1.00 40.80 O
HETATM 2950 O HOH S 202 3.084 13.024 4.567 1.00 45.23 O
HETATM 2951 O HOH S 203 7.744 12.689 -0.843 1.00 44.18 O
HETATM 2952 O HOH S 204 32.305 2.770 0.795 1.00 48.89 O
HETATM 2953 O HOH S 205 20.953 -2.295 61.886 1.00 55.32 O
HETATM 2954 O HOH S 206 13.704 -14.685 18.159 1.00 34.41 O
HETATM 2955 O HOH S 207 -7.206 1.180 62.654 1.00 41.69 O
HETATM 2956 O HOH S 209 22.156 18.346 2.196 1.00 43.97 O
HETATM 2957 O HOH S 210 15.720 0.371 57.037 1.00 44.24 O
HETATM 2958 O HOH S 212 19.908 26.621 46.940 1.00 59.47 O
HETATM 2959 O HOH S 213 15.737 21.162 47.749 1.00 37.21 O
HETATM 2960 O HOH S 220 25.489 -2.419 53.445 1.00 54.02 O
HETATM 2961 O HOH S 221 22.479 -4.159 62.252 1.00 66.28 O
HETATM 2962 O HOH S 227 17.400 23.042 47.417 1.00 49.57 O
HETATM 2963 O HOH S 232 5.535 14.731 58.366 1.00 45.60 O
HETATM 2964 O HOH S 233 2.112 13.671 59.235 1.00 51.42 O
HETATM 2965 O HOH S 234 6.739 -8.893 41.599 1.00 60.41 O
HETATM 2966 O HOH S 235 9.031 -8.780 42.063 1.00 60.80 O
HETATM 2967 O HOH S 240 8.417 -9.210 -0.871 1.00 41.42 O
HETATM 2968 O HOH S 241 0.376 -19.117 5.410 1.00 54.12 O
HETATM 2969 O HOH S 242 2.654 -24.535 12.390 1.00 41.55 O
HETATM 2970 O HOH S 243 14.473 -12.518 19.218 1.00 41.43 O
HETATM 2971 O HOH S 245 19.482 0.535 21.470 1.00 38.56 O
HETATM 2972 O HOH S 246 20.046 2.710 22.610 1.00 40.09 O
HETATM 2973 O HOH S 247 2.888 -2.086 17.137 1.00 37.86 O
HETATM 2974 O HOH S 249 17.356 15.849 8.479 1.00 46.89 O
HETATM 2975 O HOH S 250 20.878 15.423 15.547 1.00 59.98 O
HETATM 2976 O HOH S 251 28.682 9.385 6.340 1.00 42.06 O
HETATM 2977 O HOH S 252 30.747 14.274 6.134 1.00 52.55 O
HETATM 2978 O HOH S 257 22.292 -2.558 -6.188 1.00 53.80 O
HETATM 2979 O HOH S 260 18.959 -0.505 -8.666 1.00 54.97 O
HETATM 2980 O HOH S 261 15.142 18.434 2.067 1.00 45.82 O
HETATM 2981 O HOH S 271 18.637 -7.244 -3.554 1.00 62.79 O
HETATM 2982 O HOH S 274 5.302 -7.094 1.011 1.00 38.13 O
HETATM 2983 O HOH S 276 25.581 -11.031 -2.225 1.00 41.85 O
HETATM 2984 O HOH S 277 20.363 -9.320 -4.410 1.00 67.08 O
HETATM 2985 O HOH S 278 27.419 11.903 51.903 1.00 52.32 O
HETATM 2986 O HOH S 281 25.327 -2.208 14.857 1.00 52.03 O
HETATM 2987 O HOH S 284 17.590 13.152 -11.553 1.00 45.35 O
HETATM 2988 O HOH S 285 -1.817 -10.687 62.330 1.00 49.39 O
HETATM 2989 O HOH S 286 -6.255 -2.817 66.089 1.00 41.45 O
HETATM 2990 O HOH S 296 11.971 -14.999 20.004 1.00 50.17 O
HETATM 2991 O HOH S 297 12.143 -10.999 20.652 1.00 51.33 O
HETATM 2992 O HOH S 299 18.002 2.279 -10.819 1.00 38.26 O
HETATM 2993 O HOH S 300 18.364 -3.218 61.576 1.00 50.90 O
HETATM 2994 O HOH S 301 8.037 0.886 64.167 1.00 55.34 O
HETATM 2995 O HOH S 315 29.517 3.997 0.094 1.00 44.81 O
HETATM 2996 O HOH S 316 20.031 -8.196 56.385 1.00 51.10 O
HETATM 2997 O HOH S 317 1.737 -10.686 57.931 1.00 57.21 O
HETATM 2998 O HOH S 318 -0.746 -10.618 59.695 1.00 51.70 O
HETATM 2999 O HOH S 319 1.333 -9.815 51.999 1.00 38.27 O
HETATM 3000 O HOH S 320 13.021 -19.739 13.431 1.00 42.45 O
HETATM 3001 O HOH S 321 17.838 -10.516 16.716 1.00 40.87 O
HETATM 3002 O HOH S 322 15.983 -2.497 21.769 1.00 45.18 O
HETATM 3003 O HOH S 323 14.245 18.978 -0.481 1.00 43.72 O
HETATM 3004 O HOH S 324 22.565 16.053 0.907 1.00 41.28 O
ATOM 3005 N HIS B 0 -11.671 -26.246 41.306 1.00 64.17 B000 N
ATOM 3006 CA HIS B 0 -10.477 -25.445 41.555 1.00 66.90 B000 C
ATOM 3007 C HIS B 0 -10.847 -24.103 42.175 1.00 58.95 B000 C
ATOM 3008 O HIS B 0 -11.911 -23.544 41.874 1.00 54.52 B000 O
ATOM 3009 CB HIS B 0 -9.691 -25.223 40.256 1.00 69.39 B000 C
TER
HETATM 3010 CA CA B 1 -13.084 -13.329 -11.208 1.00 26.86 B000Ca
ATOM 3011 N MET B 1 -9.963 -23.590 43.032 1.00 56.56 B000 N
ATOM 3012 CA MET B 1 -10.138 -22.259 43.596 1.00 53.39 B000 C
ATOM 3013 C MET B 1 -9.626 -21.188 42.648 1.00 48.46 B000 C
ATOM 3014 O MET B 1 -8.623 -21.370 41.949 1.00 54.09 B000 O
ATOM 3015 CB MET B 1 -9.427 -22.128 44.941 1.00 58.63 B000 C
ATOM 3016 CG MET B 1 -10.222 -22.688 46.111 1.00 58.64 B000 C
ATOM 3017 SD MET B 1 -9.862 -21.803 47.641 1.00 59.47 B000 S
ATOM 3018 CE MET B 1 -9.862 -23.171 48.805 1.00 60.84 B000 C
TER
HETATM 3019 CA CA B 2 -6.359 7.487 3.887 1.00 45.13 B000Ca
ATOM 3020 N LYS B 2 -10.324 -20.062 42.647 1.00 40.61 B000 N
ATOM 3021 CA LYS B 2 -10.031 -18.912 41.811 1.00 41.73 B000 C
ATOM 3022 C LYS B 2 -9.845 -17.682 42.694 1.00 47.89 B000 C
ATOM 3023 O LYS B 2 -10.498 -17.549 43.738 1.00 39.07 B000 O
ATOM 3024 CB LYS B 2 -11.171 -18.683 40.812 1.00 43.48 B000 C
ATOM 3025 CG LYS B 2 -10.907 -17.621 39.775 1.00 51.62 B000 C
ATOM 3026 CD LYS B 2 -12.106 -17.479 38.858 1.00 54.24 B000 C
ATOM 3027 CE LYS B 2 -11.682 -17.109 37.437 1.00 62.50 B000 C
ATOM 3028 NZ LYS B 2 -12.855 -16.702 36.607 1.00 60.39 B000 N1+
ATOM 3029 N ARG B 3 -8.950 -16.779 42.281 1.00 45.26 B000 N
ATOM 3030 CA ARG B 3 -8.759 -15.514 42.989 1.00 40.67 B000 C
ATOM 3031 C ARG B 3 -8.645 -14.375 41.987 1.00 39.52 B000 C
ATOM 3032 O ARG B 3 -7.760 -14.389 41.126 1.00 47.57 B000 O
ATOM 3033 CB ARG B 3 -7.530 -15.561 43.899 1.00 38.24 B000 C
ATOM 3034 CG ARG B 3 -7.260 -14.239 44.606 1.00 39.54 B000 C
ATOM 3035 CD ARG B 3 -6.317 -14.377 45.802 1.00 44.34 B000 C
ATOM 3036 NE ARG B 3 -5.077 -15.053 45.448 1.00 37.23 B000 N
ATOM 3037 CZ ARG B 3 -4.666 -16.191 45.984 1.00 43.06 B000 C
ATOM 3038 NH1 ARG B 3 -5.320 -16.763 46.979 1.00 46.71 B000 N1+
ATOM 3039 NH2 ARG B 3 -3.557 -16.758 45.524 1.00 43.39 B000 N
TER
HETATM 3040 O HOH B 3 0.097 6.663 12.494 1.00 20.43 B000 O
HETATM 3041 O HOH B 4 -18.753 7.272 4.224 1.00 25.18 B000 O
ATOM 3042 N LEU B 4 -9.529 -13.389 42.104 1.00 38.05 B000 N
ATOM 3043 CA LEU B 4 -9.566 -12.232 41.220 1.00 36.01 B000 C
ATOM 3044 C LEU B 4 -9.152 -10.982 41.982 1.00 33.93 B000 C
ATOM 3045 O LEU B 4 -9.527 -10.806 43.143 1.00 38.20 B000 O
ATOM 3046 CB LEU B 4 -10.976 -12.003 40.659 1.00 40.61 B000 C
ATOM 3047 CG LEU B 4 -11.724 -13.056 39.844 1.00 49.59 B000 C
ATOM 3048 CD1 LEU B 4 -13.111 -12.524 39.485 1.00 40.17 B000 C
ATOM 3049 CD2 LEU B 4 -10.948 -13.403 38.589 1.00 52.67 B000 C
TER
HETATM 3050 O HOH B 5 -11.799 -14.618 -9.729 1.00 25.71 B000 O
ATOM 3051 N THR B 5 -8.424 -10.095 41.318 1.00 34.88 B000 N
ATOM 3052 CA THR B 5 -8.082 -8.788 41.853 1.00 32.04 B000 C
ATOM 3053 C THR B 5 -8.535 -7.744 40.854 1.00 35.55 B000 C
ATOM 3054 O THR B 5 -8.205 -7.845 39.667 1.00 39.47 B000 O
ATOM 3055 CB THR B 5 -6.575 -8.613 42.076 1.00 31.92 B000 C
ATOM 3056 CG2 THR B 5 -6.304 -7.257 42.652 1.00 30.02 B000 C
ATOM 3057 OG1 THR B 5 -6.091 -9.601 42.978 1.00 34.17 B000 O
TER
HETATM 3058 O HOH B 6 -13.212 -9.640 -13.920 1.00 26.77 B000 O
ATOM 3059 N TYR B 6 -9.242 -6.722 41.327 1.00 25.59 B000 N
ATOM 3060 CA TYR B 6 -9.722 -5.694 40.423 1.00 33.91 B000 C
ATOM 3061 C TYR B 6 -9.663 -4.330 41.095 1.00 30.95 B000 C
ATOM 3062 O TYR B 6 -9.580 -4.206 42.322 1.00 32.63 B000 O
ATOM 3063 CB TYR B 6 -11.149 -6.005 39.907 1.00 37.64 B000 C
ATOM 3064 CG TYR B 6 -12.255 -5.745 40.920 1.00 34.62 B000 C
ATOM 3065 CD1 TYR B 6 -12.802 -4.475 41.078 1.00 32.05 B000 C
ATOM 3066 CD2 TYR B 6 -12.761 -6.775 41.701 1.00 36.84 B000 C
ATOM 3067 CE1 TYR B 6 -13.791 -4.226 42.007 1.00 29.42 B000 C
ATOM 3068 CE2 TYR B 6 -13.770 -6.541 42.628 1.00 37.13 B000 C
ATOM 3069 CZ TYR B 6 -14.276 -5.259 42.772 1.00 34.45 B000 C
ATOM 3070 OH TYR B 6 -15.259 -5.003 43.703 1.00 33.52 B000 O
TER
HETATM 3071 O HOH B 7 -21.390 6.744 4.631 1.00 24.91 B000 O
ATOM 3072 N ILE B 7 -9.696 -3.298 40.255 1.00 30.39 B000 N
ATOM 3073 CA ILE B 7 -9.810 -1.919 40.696 1.00 32.71 B000 C
ATOM 3074 C ILE B 7 -10.967 -1.287 39.950 1.00 35.80 B000 C
ATOM 3075 O ILE B 7 -11.317 -1.697 38.838 1.00 35.87 B000 O
ATOM 3076 CB ILE B 7 -8.514 -1.112 40.481 1.00 31.98 B000 C
ATOM 3077 CG1 ILE B 7 -8.097 -1.101 39.007 1.00 33.29 B000 C
ATOM 3078 CG2 ILE B 7 -7.405 -1.704 41.304 1.00 34.30 B000 C
ATOM 3079 CD1 ILE B 7 -6.976 -0.117 38.744 1.00 35.84 B000 C
TER
HETATM 3080 O HOH B 8 -16.331 -5.891 55.896 1.00 32.75 B000 O
ATOM 3081 N SER B 8 -11.570 -0.287 40.578 1.00 31.72 B000 N
ATOM 3082 CA SER B 8 -12.712 0.387 39.997 1.00 39.46 B000 C
ATOM 3083 C SER B 8 -12.756 1.791 40.563 1.00 41.83 B000 C
ATOM 3084 O SER B 8 -11.974 2.150 41.451 1.00 31.58 B000 O
ATOM 3085 CB SER B 8 -14.016 -0.371 40.283 1.00 42.96 B000 C
ATOM 3086 OG SER B 8 -14.395 -0.216 41.647 1.00 38.39 B000 O
TER
HETATM 3087 O HOH B 9 -9.606 -12.765 1.231 1.00 24.73 B000 O
ATOM 3088 N LYS B 9 -13.716 2.566 40.074 1.00 34.81 B000 N
ATOM 3089 CA LYS B 9 -13.865 3.972 40.407 1.00 38.94 B000 C
ATOM 3090 C LYS B 9 -15.274 4.195 40.923 1.00 46.45 B000 C
ATOM 3091 O LYS B 9 -16.219 3.576 40.428 1.00 47.19 B000 O
ATOM 3092 CB LYS B 9 -13.588 4.844 39.164 1.00 47.25 B000 C
ATOM 3093 CG LYS B 9 -13.609 6.348 39.405 1.00 50.79 B000 C
ATOM 3094 CD LYS B 9 -12.831 7.114 38.321 1.00 60.73 B000 C
ATOM 3095 CE LYS B 9 -13.127 6.575 36.925 1.00 63.59 B000 C
ATOM 3096 NZ LYS B 9 -13.150 7.623 35.851 1.00 65.77 B000 N1+
TER
HETATM 3097 O HOH B 10 -13.472 12.400 4.068 1.00 27.67 B000 O
ATOM 3098 N PHE B 10 -15.413 5.049 41.940 1.00 42.82 B000 N
ATOM 3099 CA PHE B 10 -16.743 5.448 42.383 1.00 37.70 B000 C
ATOM 3100 C PHE B 10 -17.449 6.154 41.229 1.00 48.54 B000 C
ATOM 3101 O PHE B 10 -16.921 7.115 40.655 1.00 43.32 B000 O
ATOM 3102 CB PHE B 10 -16.672 6.396 43.587 1.00 42.42 B000 C
ATOM 3103 CG PHE B 10 -16.137 5.778 44.876 1.00 39.83 B000 C
ATOM 3104 CD1 PHE B 10 -15.395 4.610 44.885 1.00 36.96 B000 C
ATOM 3105 CD2 PHE B 10 -16.364 6.418 46.085 1.00 40.34 B000 C
ATOM 3106 CE1 PHE B 10 -14.896 4.087 46.083 1.00 40.77 B000 C
ATOM 3107 CE2 PHE B 10 -15.875 5.899 47.281 1.00 42.22 B000 C
ATOM 3108 CZ PHE B 10 -15.147 4.732 47.276 1.00 37.15 B000 C
TER
HETATM 3109 O HOH B 11 -10.517 2.348 1.992 1.00 28.37 B000 O
ATOM 3110 N SER B 11 -18.633 5.672 40.869 1.00 51.19 B000 N
ATOM 3111 CA SER B 11 -19.424 6.360 39.858 1.00 50.11 B000 C
ATOM 3112 C SER B 11 -20.303 7.456 40.456 1.00 49.55 B000 C
ATOM 3113 O SER B 11 -21.081 8.080 39.729 1.00 64.62 B000 O
ATOM 3114 CB SER B 11 -20.256 5.343 39.068 1.00 55.23 B000 C
ATOM 3115 OG SER B 11 -21.131 4.625 39.908 1.00 47.37 B000 O
ATOM 3116 N ARG B 12 -20.177 7.704 41.754 1.00 43.85 B000 N
ATOM 3117 CA ARG B 12 -20.829 8.789 42.477 1.00 46.56 B000 C
ATOM 3118 C ARG B 12 -20.234 8.825 43.885 1.00 47.53 B000 C
ATOM 3119 O ARG B 12 -19.674 7.829 44.336 1.00 43.99 B000 O
ATOM 3120 CB ARG B 12 -22.350 8.582 42.545 1.00 51.90 B000 C
ATOM 3121 CG ARG B 12 -22.767 7.259 43.187 1.00 58.83 B000 C
ATOM 3122 CD ARG B 12 -24.157 7.355 43.830 1.00 65.53 B000 C
ATOM 3123 NE ARG B 12 -24.650 6.062 44.296 1.00 57.67 B000 N
ATOM 3124 CZ ARG B 12 -24.977 5.783 45.552 1.00 67.80 B000 C
ATOM 3125 NH1 ARG B 12 -24.855 6.683 46.518 1.00 70.66 B000 N1+
ATOM 3126 NH2 ARG B 12 -25.445 4.570 45.847 1.00 58.69 B000 N
TER
HETATM 3127 O HOH B 12 2.587 -5.550 6.679 1.00 29.09 B000 O
HETATM 3128 O HOH B 13 -27.694 -13.287 -0.589 1.00 26.50 B000 O
ATOM 3129 N PRO B 13 -20.330 9.955 44.584 1.00 51.85 B000 N
ATOM 3130 CA PRO B 13 -19.748 10.027 45.936 1.00 54.58 B000 C
ATOM 3131 C PRO B 13 -20.375 9.012 46.887 1.00 56.86 B000 C
ATOM 3132 O PRO B 13 -21.592 8.812 46.898 1.00 51.17 B000 O
ATOM 3133 CB PRO B 13 -20.047 11.462 46.391 1.00 51.19 B000 C
ATOM 3134 CG PRO B 13 -20.610 12.178 45.221 1.00 56.13 B000 C
ATOM 3135 CD PRO B 13 -20.633 11.281 44.027 1.00 53.30 B000 C
TER
HETATM 3136 O HOH B 14 -16.119 -15.212 -6.147 1.00 31.65 B000 O
ATOM 3137 N LEU B 14 -19.527 8.374 47.697 1.00 49.60 B000 N
ATOM 3138 CA LEU B 14 -19.954 7.399 48.695 1.00 43.79 B000 C
ATOM 3139 C LEU B 14 -19.327 7.753 50.034 1.00 51.74 B000 C
ATOM 3140 O LEU B 14 -18.123 8.022 50.110 1.00 49.16 B000 O
ATOM 3141 CB LEU B 14 -19.564 5.972 48.301 1.00 38.01 B000 C
ATOM 3142 CG LEU B 14 -20.046 5.414 46.969 1.00 48.20 B000 C
ATOM 3143 CD1 LEU B 14 -19.389 4.082 46.668 1.00 39.03 B000 C
ATOM 3144 CD2 LEU B 14 -21.560 5.266 46.990 1.00 49.29 B000 C
TER
HETATM 3145 O HOH B 15 -2.175 6.233 56.944 1.00 34.29 B000 O
ATOM 3146 N SER B 15 -20.138 7.749 51.085 1.00 44.44 B000 N
ATOM 3147 CA SER B 15 -19.655 8.058 52.419 1.00 43.33 B000 C
ATOM 3148 C SER B 15 -18.925 6.859 53.015 1.00 42.25 B000 C
ATOM 3149 O SER B 15 -18.999 5.732 52.507 1.00 38.87 B000 O
ATOM 3150 CB SER B 15 -20.816 8.438 53.327 1.00 47.53 B000 C
ATOM 3151 OG SER B 15 -21.678 7.323 53.470 1.00 41.63 B000 O
ATOM 3152 N GLY B 16 -18.237 7.109 54.131 1.00 46.83 B000 N
ATOM 3153 CA GLY B 16 -17.577 6.024 54.839 1.00 46.80 B000 C
ATOM 3154 C GLY B 16 -18.566 5.015 55.397 1.00 45.61 B000 C
ATOM 3155 O GLY B 16 -18.328 3.804 55.337 1.00 38.18 B000 O
TER
HETATM 3156 O HOH B 16 -15.032 -12.893 -12.741 1.00 29.01 B000 O
ATOM 3157 N ASP B 17 -19.688 5.500 55.945 1.00 43.84 B000 N
ATOM 3158 CA ASP B 17 -20.741 4.600 56.402 1.00 45.34 B000 C
ATOM 3159 C ASP B 17 -21.283 3.754 55.254 1.00 42.85 B000 C
ATOM 3160 O ASP B 17 -21.550 2.558 55.424 1.00 44.37 B000 O
ATOM 3161 CB ASP B 17 -21.865 5.401 57.060 1.00 50.21 B000 C
ATOM 3162 CG ASP B 17 -21.570 5.732 58.511 1.00 54.36 B000 C
ATOM 3163 OD1 ASP B 17 -20.595 5.175 59.058 1.00 57.49 B000 O
ATOM 3164 OD2 ASP B 17 -22.308 6.542 59.108 1.00 57.94 B000 O1-
TER
HETATM 3165 O HOH B 17 -27.535 6.587 7.332 1.00 29.95 B000 O
ATOM 3166 N GLU B 18 -21.440 4.350 54.074 1.00 40.43 B000 N
ATOM 3167 CA GLU B 18 -21.949 3.591 52.934 1.00 44.26 B000 C
ATOM 3168 C GLU B 18 -20.943 2.555 52.456 1.00 37.96 B000 C
ATOM 3169 O GLU B 18 -21.329 1.453 52.046 1.00 36.50 B000 O
ATOM 3170 CB GLU B 18 -22.343 4.544 51.803 1.00 45.16 B000 C
ATOM 3171 CG GLU B 18 -23.730 5.194 52.027 1.00 50.15 B000 C
ATOM 3172 CD GLU B 18 -24.086 6.219 50.965 1.00 61.32 B000 C
ATOM 3173 OE1 GLU B 18 -23.150 6.843 50.413 1.00 56.82 B000 O
ATOM 3174 OE2 GLU B 18 -25.294 6.407 50.687 1.00 70.61 B000 O1-
TER
HETATM 3175 O HOH B 18 -23.628 9.543 13.694 1.00 30.06 B000 O
ATOM 3176 N ILE B 19 -19.650 2.886 52.496 1.00 40.00 B000 N
ATOM 3177 CA ILE B 19 -18.619 1.909 52.146 1.00 33.49 B000 C
ATOM 3178 C ILE B 19 -18.598 0.778 53.170 1.00 35.51 B000 C
ATOM 3179 O ILE B 19 -18.467 -0.403 52.820 1.00 33.77 B000 O
ATOM 3180 CB ILE B 19 -17.256 2.621 52.032 1.00 33.34 B000 C
ATOM 3181 CG1 ILE B 19 -17.286 3.601 50.842 1.00 35.82 B000 C
ATOM 3182 CG2 ILE B 19 -16.101 1.591 51.933 1.00 27.15 B000 C
ATOM 3183 CD1 ILE B 19 -16.252 4.708 50.918 1.00 44.79 B000 C
ATOM 3184 N GLU B 20 -18.743 1.131 54.447 1.00 32.18 B000 N
ATOM 3185 CA GLU B 20 -18.738 0.166 55.536 1.00 34.41 B000 C
ATOM 3186 C GLU B 20 -19.871 -0.839 55.397 1.00 37.78 B000 C
ATOM 3187 O GLU B 20 -19.686 -2.036 55.656 1.00 33.75 B000 O
ATOM 3188 CB GLU B 20 -18.853 0.929 56.855 1.00 36.33 B000 C
ATOM 3189 CG GLU B 20 -18.813 0.087 58.106 1.00 44.11 B000 C
ATOM 3190 CD GLU B 20 -18.822 0.947 59.363 1.00 56.50 B000 C
ATOM 3191 OE1 GLU B 20 -19.796 1.717 59.552 1.00 62.22 B000 O
ATOM 3192 OE2 GLU B 20 -17.850 0.860 60.156 1.00 65.45 B000 O1-
TER
HETATM 3193 O HOH B 20 -23.727 12.906 3.093 1.00 29.16 B000 O
ATOM 3194 N ALA B 21 -21.058 -0.368 55.006 1.00 34.04 B000 N
ATOM 3195 CA ALA B 21 -22.184 -1.272 54.829 1.00 36.94 B000 C
ATOM 3196 C ALA B 21 -21.937 -2.238 53.682 1.00 33.50 B000 C
ATOM 3197 O ALA B 21 -22.224 -3.436 53.803 1.00 35.80 B000 O
ATOM 3198 CB ALA B 21 -23.465 -0.473 54.599 1.00 44.16 B000 C
TER
HETATM 3199 O HOH B 21 -23.236 -14.841 56.690 1.00 26.13 B000 O
HETATM 3200 O HOH B 22 -12.509 -14.968 -6.004 1.00 29.77 B000 O
ATOM 3201 N ILE B 22 -21.413 -1.737 52.559 1.00 30.90 B000 N
ATOM 3202 CA ILE B 22 -21.062 -2.622 51.452 1.00 33.12 B000 C
ATOM 3203 C ILE B 22 -20.162 -3.738 51.950 1.00 32.18 B000 C
ATOM 3204 O ILE B 22 -20.384 -4.922 51.666 1.00 33.34 B000 O
ATOM 3205 CB ILE B 22 -20.396 -1.830 50.312 1.00 36.30 B000 C
ATOM 3206 CG1 ILE B 22 -21.426 -0.946 49.599 1.00 37.88 B000 C
ATOM 3207 CG2 ILE B 22 -19.708 -2.765 49.315 1.00 33.12 B000 C
ATOM 3208 CD1 ILE B 22 -20.823 -0.118 48.490 1.00 36.24 B000 C
ATOM 3209 N GLY B 23 -19.151 -3.375 52.735 1.00 36.08 B000 N
ATOM 3210 CA GLY B 23 -18.238 -4.377 53.251 1.00 34.14 B000 C
ATOM 3211 C GLY B 23 -18.932 -5.389 54.141 1.00 34.61 B000 C
ATOM 3212 O GLY B 23 -18.703 -6.597 54.023 1.00 34.92 B000 O
TER
HETATM 3213 O HOH B 23 -15.646 -11.492 16.112 1.00 29.95 B000 O
ATOM 3214 N AARG B 24 -19.797 -4.911 55.042 0.58 33.09 B000 N
ATOM 3215 N BARG B 24 -19.804 -4.907 55.035 0.42 33.13 B000 N
ATOM 3216 CA AARG B 24 -20.457 -5.814 55.984 0.58 32.59 B000 C
ATOM 3217 CA BARG B 24 -20.455 -5.795 55.995 0.42 32.62 B000 C
ATOM 3218 C AARG B 24 -21.456 -6.716 55.273 0.58 32.10 B000 C
ATOM 3219 C BARG B 24 -21.482 -6.694 55.310 0.42 32.10 B000 C
ATOM 3220 O AARG B 24 -21.567 -7.906 55.592 0.58 30.23 B000 O
ATOM 3221 O BARG B 24 -21.631 -7.866 55.675 0.42 30.27 B000 O
ATOM 3222 CB AARG B 24 -21.164 -5.024 57.087 0.58 35.62 B000 C
ATOM 3223 CB BARG B 24 -21.115 -4.974 57.111 0.42 35.62 B000 C
ATOM 3224 CG AARG B 24 -20.246 -4.518 58.194 0.58 35.92 B000 C
ATOM 3225 CG BARG B 24 -20.149 -4.123 57.974 0.42 35.62 B000 C
ATOM 3226 CD AARG B 24 -21.042 -4.228 59.462 0.58 36.11 B000 C
ATOM 3227 CD BARG B 24 -20.462 -4.245 59.471 0.42 36.10 B000 C
ATOM 3228 NE AARG B 24 -21.332 -5.450 60.203 0.58 30.68 B000 N
ATOM 3229 NE BARG B 24 -20.090 -3.066 60.254 0.42 36.61 B000 N
ATOM 3230 CZ AARG B 24 -22.540 -5.976 60.382 0.58 32.68 B000 C
ATOM 3231 CZ BARG B 24 -20.949 -2.277 60.892 0.42 36.66 B000 C
ATOM 3232 NH1AARG B 24 -23.637 -5.384 59.924 0.58 17.81 B000 N1+
ATOM 3233 NH1BARG B 24 -22.255 -2.505 60.870 0.42 33.42 B000 N1+
ATOM 3234 NH2AARG B 24 -22.646 -7.131 61.025 0.58 26.50 B000 N
ATOM 3235 NH2BARG B 24 -20.486 -1.241 61.584 0.42 39.17 B000 N
TER
HETATM 3236 O HOH B 24 -3.891 -9.820 44.159 1.00 34.04 B000 O
HETATM 3237 O HOH B 25 -20.981 16.121 2.375 1.00 37.73 B000 O
ATOM 3238 N ILE B 25 -22.192 -6.168 54.307 1.00 35.71 B000 N
ATOM 3239 CA ILE B 25 -23.112 -6.996 53.533 1.00 32.07 B000 C
ATOM 3240 C ILE B 25 -22.334 -7.960 52.644 1.00 35.10 B000 C
ATOM 3241 O ILE B 25 -22.688 -9.141 52.540 1.00 32.92 B000 O
ATOM 3242 CB ILE B 25 -24.092 -6.114 52.734 1.00 42.34 B000 C
ATOM 3243 CG1 ILE B 25 -24.924 -5.253 53.696 1.00 45.36 B000 C
ATOM 3244 CG2 ILE B 25 -25.050 -6.961 51.900 1.00 44.14 B000 C
ATOM 3245 CD1 ILE B 25 -25.750 -4.181 53.001 1.00 45.58 B000 C
TER
HETATM 3246 O HOH B 26 -15.441 -10.930 57.035 1.00 30.85 B000 O
ATOM 3247 N SER B 26 -21.217 -7.498 52.047 1.00 31.49 B000 N
ATOM 3248 CA SER B 26 -20.355 -8.413 51.290 1.00 34.13 B000 C
ATOM 3249 C SER B 26 -19.854 -9.552 52.169 1.00 28.52 B000 C
ATOM 3250 O SER B 26 -19.802 -10.712 51.739 1.00 29.67 B000 O
ATOM 3251 CB SER B 26 -19.167 -7.654 50.684 1.00 35.39 B000 C
ATOM 3252 OG SER B 26 -19.625 -6.659 49.775 1.00 33.91 B000 O
TER
HETATM 3253 O HOH B 27 5.361 -11.249 1.849 1.00 34.23 B000 O
ATOM 3254 N SER B 27 -19.461 -9.240 53.402 1.00 26.48 B000 N
ATOM 3255 CA SER B 27 -19.020 -10.292 54.305 1.00 24.69 B000 C
ATOM 3256 C SER B 27 -20.126 -11.319 54.526 1.00 28.10 B000 C
ATOM 3257 O SER B 27 -19.886 -12.531 54.478 1.00 29.15 B000 O
ATOM 3258 CB SER B 27 -18.580 -9.683 55.631 1.00 28.91 B000 C
ATOM 3259 OG SER B 27 -18.097 -10.698 56.479 1.00 29.07 B000 O
ATOM 3260 N GLN B 28 -21.343 -10.849 54.789 1.00 29.52 B000 N
ATOM 3261 CA AGLN B 28 -22.451 -11.770 55.030 0.55 30.42 B000 C
ATOM 3262 CA BGLN B 28 -22.447 -11.769 55.033 0.45 30.42 B000 C
ATOM 3263 C GLN B 28 -22.656 -12.699 53.841 1.00 30.82 B000 C
ATOM 3264 O GLN B 28 -22.739 -13.923 54.000 1.00 27.11 B000 O
ATOM 3265 CB AGLN B 28 -23.734 -10.995 55.332 0.55 30.60 B000 C
ATOM 3266 CB BGLN B 28 -23.718 -10.980 55.341 0.45 30.59 B000 C
ATOM 3267 CG AGLN B 28 -24.943 -11.914 55.593 0.55 32.04 B000 C
ATOM 3268 CG BGLN B 28 -24.920 -11.860 55.656 0.45 32.05 B000 C
ATOM 3269 CD AGLN B 28 -26.207 -11.150 55.930 0.55 32.04 B000 C
ATOM 3270 CD BGLN B 28 -25.902 -11.918 54.519 0.45 31.67 B000 C
ATOM 3271 NE2AGLN B 28 -26.952 -11.637 56.918 0.55 31.95 B000 N
ATOM 3272 NE2BGLN B 28 -26.212 -13.123 54.069 0.45 36.75 B000 N
ATOM 3273 OE1AGLN B 28 -26.511 -10.133 55.312 0.55 35.89 B000 O
ATOM 3274 OE1BGLN B 28 -26.385 -10.887 54.049 0.45 33.45 B000 O
TER
HETATM 3275 O HOH B 28 -29.083 -9.742 56.639 1.00 32.69 B000 O
HETATM 3276 O HOH B 29 -18.008 -10.793 15.862 1.00 34.36 B000 O
ATOM 3277 N LYS B 29 -22.723 -12.132 52.633 1.00 30.76 B000 N
ATOM 3278 CA LYS B 29 -22.940 -12.943 51.437 1.00 32.11 B000 C
ATOM 3279 C LYS B 29 -21.769 -13.866 51.154 1.00 27.41 B000 C
ATOM 3280 O LYS B 29 -21.962 -15.045 50.834 1.00 28.34 B000 O
ATOM 3281 CB LYS B 29 -23.210 -12.036 50.239 1.00 31.26 B000 C
ATOM 3282 CG LYS B 29 -24.450 -11.198 50.456 1.00 39.55 B000 C
ATOM 3283 CD LYS B 29 -24.788 -10.332 49.258 1.00 50.62 B000 C
ATOM 3284 CE LYS B 29 -26.103 -9.602 49.510 1.00 57.28 B000 C
ATOM 3285 NZ LYS B 29 -26.418 -8.606 48.459 1.00 57.63 B000 N1+
ATOM 3286 N ASN B 30 -20.537 -13.363 51.261 1.00 33.11 B000 N
ATOM 3287 CA ASN B 30 -19.397 -14.217 50.950 1.00 31.16 B000 C
ATOM 3288 C ASN B 30 -19.275 -15.367 51.941 1.00 30.18 B000 C
ATOM 3289 O ASN B 30 -18.831 -16.460 51.568 1.00 28.43 B000 O
ATOM 3290 CB ASN B 30 -18.090 -13.403 50.924 1.00 32.57 B000 C
ATOM 3291 CG ASN B 30 -18.017 -12.469 49.732 1.00 32.97 B000 C
ATOM 3292 ND2 ASN B 30 -17.025 -11.588 49.719 1.00 29.88 B000 N
ATOM 3293 OD1 ASN B 30 -18.837 -12.558 48.820 1.00 34.91 B000 O
TER
HETATM 3294 O HOH B 30 -28.358 5.539 14.317 1.00 34.32 B000 O
ATOM 3295 N GLN B 31 -19.613 -15.129 53.220 1.00 28.65 B000 N
ATOM 3296 CA GLN B 31 -19.597 -16.223 54.191 1.00 36.00 B000 C
ATOM 3297 C GLN B 31 -20.525 -17.347 53.751 1.00 30.51 B000 C
ATOM 3298 O GLN B 31 -20.182 -18.527 53.890 1.00 34.38 B000 O
ATOM 3299 CB GLN B 31 -19.995 -15.729 55.591 1.00 23.84 B000 C
ATOM 3300 CG GLN B 31 -19.780 -16.755 56.699 1.00 30.75 B000 C
ATOM 3301 CD GLN B 31 -20.927 -17.769 56.840 1.00 32.82 B000 C
ATOM 3302 NE2 GLN B 31 -20.606 -18.971 57.308 1.00 32.01 B000 N
ATOM 3303 OE1 GLN B 31 -22.072 -17.467 56.537 1.00 32.81 B000 O
TER
HETATM 3304 O HOH B 31 -2.712 6.316 13.497 1.00 32.21 B000 O
ATOM 3305 N GLN B 32 -21.709 -17.000 53.230 1.00 30.03 B000 N
ATOM 3306 CA GLN B 32 -22.632 -18.039 52.773 1.00 36.61 B000 C
ATOM 3307 C GLN B 32 -22.111 -18.752 51.517 1.00 41.31 B000 C
ATOM 3308 O GLN B 32 -22.514 -19.889 51.250 1.00 36.67 B000 O
ATOM 3309 CB GLN B 32 -24.015 -17.446 52.484 1.00 33.37 B000 C
ATOM 3310 CG GLN B 32 -24.914 -17.142 53.727 1.00 37.05 B000 C
ATOM 3311 CD GLN B 32 -25.226 -18.368 54.588 1.00 46.52 B000 C
ATOM 3312 NE2 GLN B 32 -24.482 -18.522 55.697 1.00 38.00 B000 N
ATOM 3313 OE1 GLN B 32 -26.153 -19.130 54.301 1.00 45.62 B000 O
TER
HETATM 3314 O HOH B 32 -21.707 -8.720 58.024 1.00 27.79 B000 O
ATOM 3315 N ALA B 33 -21.222 -18.116 50.750 1.00 28.93 B000 N
ATOM 3316 CA ALA B 33 -20.639 -18.699 49.542 1.00 38.22 B000 C
ATOM 3317 C ALA B 33 -19.294 -19.351 49.789 1.00 35.79 B000 C
ATOM 3318 O ALA B 33 -18.742 -19.967 48.877 1.00 42.85 B000 O
ATOM 3319 CB ALA B 33 -20.488 -17.629 48.454 1.00 36.17 B000 C
ATOM 3320 N ASN B 34 -18.756 -19.237 51.001 1.00 39.44 B000 N
ATOM 3321 CA ASN B 34 -17.425 -19.736 51.323 1.00 41.34 B000 C
ATOM 3322 C ASN B 34 -16.384 -19.017 50.463 1.00 42.55 B000 C
ATOM 3323 O ASN B 34 -15.452 -19.619 49.924 1.00 40.72 B000 O
ATOM 3324 CB ASN B 34 -17.344 -21.258 51.168 1.00 48.67 B000 C
ATOM 3325 CG ASN B 34 -16.038 -21.825 51.688 1.00 52.36 B000 C
ATOM 3326 ND2 ASN B 34 -15.449 -22.752 50.938 1.00 50.17 B000 N
ATOM 3327 OD1 ASN B 34 -15.560 -21.425 52.752 1.00 57.69 B000 O
TER
HETATM 3328 O HOH B 35 0.391 5.911 63.532 1.00 39.46 B000 O
ATOM 3329 N VAL B 35 -16.570 -17.709 50.334 1.00 37.89 B000 N
ATOM 3330 CA VAL B 35 -15.692 -16.816 49.588 1.00 37.90 B000 C
ATOM 3331 C VAL B 35 -15.010 -15.874 50.577 1.00 34.79 B000 C
ATOM 3332 O VAL B 35 -15.623 -15.473 51.574 1.00 31.50 B000 O
ATOM 3333 CB VAL B 35 -16.522 -16.048 48.541 1.00 32.57 B000 C
ATOM 3334 CG1 VAL B 35 -15.827 -14.777 48.102 1.00 31.89 B000 C
ATOM 3335 CG2 VAL B 35 -16.822 -16.951 47.340 1.00 34.44 B000 C
TER
HETATM 3336 O HOH B 36 -14.197 -15.429 -11.298 1.00 31.54 B000 O
ATOM 3337 N THR B 36 -13.744 -15.533 50.321 1.00 30.32 B000 N
ATOM 3338 CA THR B 36 -12.995 -14.658 51.226 1.00 35.17 B000 C
ATOM 3339 C THR B 36 -12.327 -13.531 50.440 1.00 32.77 B000 C
ATOM 3340 O THR B 36 -12.287 -13.545 49.209 1.00 26.25 B000 O
ATOM 3341 CB THR B 36 -11.956 -15.438 52.060 1.00 31.83 B000 C
ATOM 3342 CG2 THR B 36 -12.637 -16.348 53.074 1.00 31.43 B000 C
ATOM 3343 OG1 THR B 36 -11.116 -16.244 51.228 1.00 31.93 B000 O
ATOM 3344 N GLY B 37 -11.837 -12.518 51.148 1.00 29.32 B000 N
ATOM 3345 CA GLY B 37 -11.098 -11.457 50.466 1.00 24.60 B000 C
ATOM 3346 C GLY B 37 -11.081 -10.160 51.269 1.00 31.06 B000 C
ATOM 3347 O GLY B 37 -11.364 -10.145 52.473 1.00 27.54 B000 O
TER
HETATM 3348 O HOH B 38 -20.609 -14.305 -8.119 1.00 36.16 B000 O
ATOM 3349 N VAL B 38 -10.778 -9.076 50.560 1.00 24.61 B000 N
ATOM 3350 CA VAL B 38 -10.527 -7.781 51.183 1.00 27.46 B000 C
ATOM 3351 C VAL B 38 -10.973 -6.690 50.222 1.00 27.27 B000 C
ATOM 3352 O VAL B 38 -10.771 -6.789 49.006 1.00 29.94 B000 O
ATOM 3353 CB VAL B 38 -9.039 -7.605 51.571 1.00 28.17 B000 C
ATOM 3354 CG1 VAL B 38 -8.109 -7.733 50.349 1.00 27.53 B000 C
ATOM 3355 CG2 VAL B 38 -8.809 -6.235 52.275 1.00 25.58 B000 C
TER
HETATM 3356 O HOH B 39 -20.901 -14.917 9.685 1.00 37.40 B000 O
ATOM 3357 N LEU B 39 -11.576 -5.646 50.776 1.00 27.85 B000 N
ATOM 3358 CA LEU B 39 -12.032 -4.478 50.026 1.00 29.79 B000 C
ATOM 3359 C LEU B 39 -11.401 -3.232 50.630 1.00 35.65 B000 C
ATOM 3360 O LEU B 39 -11.495 -3.010 51.848 1.00 30.30 B000 O
ATOM 3361 CB LEU B 39 -13.573 -4.379 50.051 1.00 30.32 B000 C
ATOM 3362 CG LEU B 39 -14.303 -3.165 49.451 1.00 32.42 B000 C
ATOM 3363 CD1 LEU B 39 -14.130 -3.050 47.949 1.00 31.74 B000 C
ATOM 3364 CD2 LEU B 39 -15.801 -3.197 49.837 1.00 27.91 B000 C
ATOM 3365 N LEU B 40 -10.728 -2.435 49.788 1.00 27.84 B000 N
ATOM 3366 CA LEU B 40 -10.083 -1.210 50.229 1.00 25.56 B000 C
ATOM 3367 C LEU B 40 -10.557 -0.063 49.357 1.00 32.29 B000 C
ATOM 3368 O LEU B 40 -10.823 -0.241 48.168 1.00 30.41 B000 O
ATOM 3369 CB LEU B 40 -8.522 -1.301 50.178 1.00 25.98 B000 C
ATOM 3370 CG LEU B 40 -7.857 -2.513 50.830 1.00 25.55 B000 C
ATOM 3371 CD1 LEU B 40 -7.680 -3.620 49.819 1.00 28.64 B000 C
ATOM 3372 CD2 LEU B 40 -6.497 -2.118 51.435 1.00 27.46 B000 C
ATOM 3373 N CYS B 41 -10.686 1.109 49.956 1.00 28.97 B000 N
ATOM 3374 CA CYS B 41 -11.056 2.282 49.197 1.00 27.99 B000 C
ATOM 3375 C CYS B 41 -10.034 3.364 49.467 1.00 35.87 B000 C
ATOM 3376 O CYS B 41 -9.447 3.422 50.547 1.00 32.80 B000 O
ATOM 3377 CB CYS B 41 -12.461 2.763 49.544 1.00 27.88 B000 C
ATOM 3378 SG CYS B 41 -12.608 3.447 51.182 1.00 37.17 B000 S
TER
HETATM 3379 O HOH B 41 2.308 2.611 61.267 1.00 31.49 B000 O
HETATM 3380 O HOH B 42 -16.266 -4.656 -13.435 1.00 32.25 B000 O
ATOM 3381 N LEU B 42 -9.797 4.200 48.463 1.00 34.97 B000 N
ATOM 3382 CA LEU B 42 -8.866 5.318 48.607 1.00 40.12 B000 C
ATOM 3383 C LEU B 42 -9.255 6.371 47.583 1.00 32.49 B000 C
ATOM 3384 O LEU B 42 -9.099 6.136 46.380 1.00 37.84 B000 O
ATOM 3385 CB LEU B 42 -7.417 4.872 48.408 1.00 35.78 B000 C
ATOM 3386 CG LEU B 42 -6.351 5.979 48.354 1.00 36.71 B000 C
ATOM 3387 CD1 LEU B 42 -6.251 6.706 49.701 1.00 40.10 B000 C
ATOM 3388 CD2 LEU B 42 -4.965 5.422 47.958 1.00 36.10 B000 C
ATOM 3389 N ASP B 43 -9.788 7.502 48.055 1.00 33.80 B000 N
ATOM 3390 CA ASP B 43 -10.034 8.666 47.199 1.00 42.66 B000 C
ATOM 3391 C ASP B 43 -10.881 8.316 45.963 1.00 41.03 B000 C
ATOM 3392 O ASP B 43 -10.552 8.670 44.830 1.00 37.06 B000 O
ATOM 3393 CB ASP B 43 -8.690 9.288 46.802 1.00 45.01 B000 C
ATOM 3394 CG ASP B 43 -8.838 10.622 46.119 1.00 54.36 B000 C
ATOM 3395 OD1 ASP B 43 -9.135 11.619 46.812 1.00 53.63 B000 O
ATOM 3396 OD2 ASP B 43 -8.626 10.666 44.888 1.00 66.53 B000 O1-
TER
HETATM 3397 O HOH B 43 -13.682 -17.604 57.094 1.00 38.72 B000 O
ATOM 3398 N GLY B 44 -11.992 7.614 46.188 1.00 38.31 B000 N
ATOM 3399 CA GLY B 44 -12.896 7.283 45.102 1.00 37.31 B000 C
ATOM 3400 C GLY B 44 -12.442 6.130 44.239 1.00 42.40 B000 C
ATOM 3401 O GLY B 44 -12.928 5.974 43.112 1.00 43.41 B000 O
TER
HETATM 3402 O HOH B 44 -27.960 -6.891 2.211 1.00 30.06 B000 O
HETATM 3403 O HOH B 45 -7.052 13.517 -2.166 1.00 51.44 B000 O
ATOM 3404 N ILE B 45 -11.511 5.325 44.730 1.00 37.14 B000 N
ATOM 3405 CA ILE B 45 -11.058 4.109 44.075 1.00 33.96 B000 C
ATOM 3406 C ILE B 45 -11.424 2.940 44.972 1.00 38.47 B000 C
ATOM 3407 O ILE B 45 -11.174 2.986 46.183 1.00 38.23 B000 O
ATOM 3408 CB ILE B 45 -9.528 4.121 43.874 1.00 39.87 B000 C
ATOM 3409 CG1 ILE B 45 -9.048 5.415 43.217 1.00 42.25 B000 C
ATOM 3410 CG2 ILE B 45 -9.073 2.866 43.115 1.00 32.21 B000 C
ATOM 3411 CD1 ILE B 45 -7.535 5.626 43.421 1.00 39.89 B000 C
TER
HETATM 3412 O HOH B 46 -26.932 -3.223 13.469 1.00 42.90 B000 O
ATOM 3413 N PHE B 46 -11.965 1.879 44.388 1.00 31.54 B000 N
ATOM 3414 CA PHE B 46 -12.103 0.613 45.092 1.00 35.46 B000 C
ATOM 3415 C PHE B 46 -11.002 -0.334 44.632 1.00 36.61 B000 C
ATOM 3416 O PHE B 46 -10.660 -0.370 43.443 1.00 31.54 B000 O
ATOM 3417 CB PHE B 46 -13.453 -0.049 44.822 1.00 31.82 B000 C
ATOM 3418 CG PHE B 46 -14.596 0.530 45.595 1.00 32.71 B000 C
ATOM 3419 CD1 PHE B 46 -14.573 0.570 46.977 1.00 31.14 B000 C
ATOM 3420 CD2 PHE B 46 -15.739 0.957 44.933 1.00 31.71 B000 C
ATOM 3421 CE1 PHE B 46 -15.651 1.092 47.692 1.00 36.01 B000 C
ATOM 3422 CE2 PHE B 46 -16.836 1.450 45.640 1.00 34.07 B000 C
ATOM 3423 CZ PHE B 46 -16.790 1.526 47.021 1.00 37.30 B000 C
TER
HETATM 3424 O HOH B 47 -16.994 -17.046 59.332 1.00 36.67 B000 O
ATOM 3425 N PHE B 47 -10.449 -1.094 45.579 1.00 28.39 B000 N
ATOM 3426 CA PHE B 47 -9.613 -2.252 45.288 1.00 28.99 B000 C
ATOM 3427 C PHE B 47 -10.260 -3.435 45.981 1.00 30.83 B000 C
ATOM 3428 O PHE B 47 -10.636 -3.328 47.154 1.00 31.68 B000 O
ATOM 3429 CB PHE B 47 -8.167 -2.128 45.814 1.00 29.35 B000 C
ATOM 3430 CG PHE B 47 -7.499 -0.801 45.549 1.00 32.50 B000 C
ATOM 3431 CD1 PHE B 47 -7.727 0.283 46.386 1.00 36.21 B000 C
ATOM 3432 CD2 PHE B 47 -6.586 -0.655 44.514 1.00 34.08 B000 C
ATOM 3433 CE1 PHE B 47 -7.090 1.506 46.174 1.00 35.83 B000 C
ATOM 3434 CE2 PHE B 47 -5.943 0.574 44.297 1.00 31.78 B000 C
ATOM 3435 CZ PHE B 47 -6.196 1.645 45.130 1.00 35.29 B000 C
ATOM 3436 N GLN B 48 -10.368 -4.561 45.282 1.00 28.20 B000 N
ATOM 3437 CA GLN B 48 -10.885 -5.762 45.916 1.00 29.37 B000 C
ATOM 3438 C GLN B 48 -10.150 -6.994 45.416 1.00 28.44 B000 C
ATOM 3439 O GLN B 48 -9.817 -7.101 44.228 1.00 30.69 B000 O
ATOM 3440 CB GLN B 48 -12.392 -5.946 45.671 1.00 25.45 B000 C
ATOM 3441 CG GLN B 48 -12.948 -7.108 46.485 1.00 28.16 B000 C
ATOM 3442 CD GLN B 48 -14.453 -7.146 46.506 1.00 41.22 B000 C
ATOM 3443 NE2 GLN B 48 -15.002 -7.813 47.508 1.00 41.92 B000 N
ATOM 3444 OE1 GLN B 48 -15.123 -6.565 45.640 1.00 41.87 B000 O
TER
HETATM 3445 O HOH B 48 -15.647 3.285 55.631 1.00 36.17 B000 O
HETATM 3446 O HOH B 49 -1.291 -0.044 60.539 1.00 37.16 B000 O
ATOM 3447 N ILE B 49 -9.883 -7.907 46.348 1.00 27.44 B000 N
ATOM 3448 CA ILE B 49 -9.436 -9.260 46.059 1.00 26.40 B000 C
ATOM 3449 C ILE B 49 -10.549 -10.209 46.495 1.00 37.75 B000 C
ATOM 3450 O ILE B 49 -11.046 -10.105 47.622 1.00 28.70 B000 O
ATOM 3451 CB ILE B 49 -8.119 -9.574 46.788 1.00 32.74 B000 C
ATOM 3452 CG1 ILE B 49 -7.040 -8.548 46.399 1.00 32.92 B000 C
ATOM 3453 CG2 ILE B 49 -7.653 -10.998 46.496 1.00 29.69 B000 C
ATOM 3454 CD1 ILE B 49 -5.767 -8.614 47.273 1.00 25.64 B000 C
TER
HETATM 3455 O HOH B 50 -10.006 -2.684 58.493 1.00 36.49 B000 O
ATOM 3456 N LEU B 50 -10.940 -11.125 45.610 1.00 32.38 B000 N
ATOM 3457 CA LEU B 50 -11.946 -12.146 45.898 1.00 34.66 B000 C
ATOM 3458 C LEU B 50 -11.368 -13.528 45.636 1.00 38.16 B000 C
ATOM 3459 O LEU B 50 -10.777 -13.754 44.576 1.00 36.43 B000 O
ATOM 3460 CB LEU B 50 -13.181 -11.960 45.018 1.00 40.71 B000 C
ATOM 3461 CG LEU B 50 -14.324 -11.096 45.513 1.00 45.01 B000 C
ATOM 3462 CD1 LEU B 50 -15.468 -11.179 44.518 1.00 39.43 B000 C
ATOM 3463 CD2 LEU B 50 -14.759 -11.587 46.880 1.00 44.90 B000 C
ATOM 3464 N GLU B 51 -11.572 -14.463 46.568 1.00 35.50 B000 N
ATOM 3465 CA GLU B 51 -11.086 -15.825 46.383 1.00 38.25 B000 C
ATOM 3466 C GLU B 51 -12.125 -16.844 46.843 1.00 42.04 B000 C
ATOM 3467 O GLU B 51 -12.841 -16.643 47.829 1.00 36.29 B000 O
ATOM 3468 CB GLU B 51 -9.760 -16.063 47.115 1.00 32.87 B000 C
ATOM 3469 CG GLU B 51 -9.898 -16.043 48.605 1.00 31.88 B000 C
ATOM 3470 CD GLU B 51 -8.591 -15.807 49.340 1.00 40.08 B000 C
ATOM 3471 OE1 GLU B 51 -7.504 -15.879 48.712 1.00 41.97 B000 O
ATOM 3472 OE2 GLU B 51 -8.660 -15.533 50.561 1.00 31.41 B000 O1-
ATOM 3473 N GLY B 52 -12.189 -17.946 46.110 1.00 39.98 B000 N
ATOM 3474 CA GLY B 52 -13.141 -18.994 46.400 1.00 41.55 B000 C
ATOM 3475 C GLY B 52 -13.278 -19.924 45.210 1.00 51.61 B000 C
ATOM 3476 O GLY B 52 -12.496 -19.873 44.261 1.00 46.68 B000 O
TER
HETATM 3477 O HOH B 52 0.676 -13.153 9.882 1.00 44.19 B000 O
ATOM 3478 N GLU B 53 -14.297 -20.774 45.288 1.00 46.33 B000 N
ATOM 3479 CA GLU B 53 -14.585 -21.701 44.204 1.00 51.83 B000 C
ATOM 3480 C GLU B 53 -14.902 -20.929 42.925 1.00 43.74 B000 C
ATOM 3481 O GLU B 53 -15.656 -19.950 42.943 1.00 41.26 B000 O
ATOM 3482 CB GLU B 53 -15.750 -22.613 44.607 1.00 52.15 B000 C
ATOM 3483 CG GLU B 53 -15.955 -23.810 43.699 1.00 57.12 B000 C
ATOM 3484 CD GLU B 53 -16.828 -23.483 42.498 1.00 64.98 B000 C
ATOM 3485 OE1 GLU B 53 -17.956 -22.975 42.705 1.00 67.62 B000 O
ATOM 3486 OE2 GLU B 53 -16.378 -23.719 41.349 1.00 63.63 B000 O1-
TER
HETATM 3487 O HOH B 53 -5.691 -12.415 41.660 1.00 43.32 B000 O
ATOM 3488 N ALA B 54 -14.312 -21.376 41.809 1.00 45.38 B000 N
ATOM 3489 CA ALA B 54 -14.352 -20.597 40.564 1.00 51.68 B000 C
ATOM 3490 C ALA B 54 -15.781 -20.245 40.144 1.00 51.25 B000 C
ATOM 3491 O ALA B 54 -16.071 -19.095 39.783 1.00 46.41 B000 O
ATOM 3492 CB ALA B 54 -13.644 -21.363 39.447 1.00 47.69 B000 C
TER
HETATM 3493 O HOH B 54 -12.479 -17.840 60.073 1.00 46.52 B000 O
ATOM 3494 N GLU B 55 -16.686 -21.229 40.170 1.00 56.97 B000 N
ATOM 3495 CA GLU B 55 -18.075 -20.970 39.798 1.00 55.59 B000 C
ATOM 3496 C GLU B 55 -18.696 -19.905 40.697 1.00 54.71 B000 C
ATOM 3497 O GLU B 55 -19.363 -18.983 40.213 1.00 53.16 B000 O
ATOM 3498 CB GLU B 55 -18.882 -22.272 39.856 1.00 68.97 B000 C
ATOM 3499 CG GLU B 55 -20.393 -22.121 39.667 1.00 71.12 B000 C
ATOM 3500 CD GLU B 55 -20.833 -22.118 38.201 1.00 85.12 B000 C
ATOM 3501 OE1 GLU B 55 -20.177 -21.459 37.358 1.00 77.28 B000 O
ATOM 3502 OE2 GLU B 55 -21.862 -22.764 37.897 1.00 85.36 B000 O1-
TER
HETATM 3503 O HOH B 55 -16.146 -16.864 54.093 1.00 32.98 B000 O
HETATM 3504 O HOH B 56 -19.148 -12.490 -12.706 1.00 40.05 B000 O
ATOM 3505 N LYS B 56 -18.480 -20.005 42.011 1.00 49.74 B000 N
ATOM 3506 CA LYS B 56 -19.029 -18.996 42.914 1.00 53.67 B000 C
ATOM 3507 C LYS B 56 -18.382 -17.632 42.690 1.00 47.20 B000 C
ATOM 3508 O LYS B 56 -19.062 -16.598 42.736 1.00 46.67 B000 O
ATOM 3509 CB LYS B 56 -18.859 -19.450 44.360 1.00 48.72 B000 C
ATOM 3510 CG LYS B 56 -19.903 -20.484 44.786 1.00 52.46 B000 C
ATOM 3511 CD LYS B 56 -19.411 -21.277 45.978 1.00 46.16 B000 C
ATOM 3512 CE LYS B 56 -20.536 -22.009 46.681 1.00 55.97 B000 C
ATOM 3513 NZ LYS B 56 -20.182 -23.426 46.972 1.00 63.17 B000 N1+
TER
HETATM 3514 O HOH B 57 -15.580 -15.529 57.820 1.00 42.62 B000 O
ATOM 3515 N ILE B 57 -17.069 -17.606 42.449 1.00 46.49 B000 N
ATOM 3516 CA ILE B 57 -16.389 -16.334 42.223 1.00 46.28 B000 C
ATOM 3517 C ILE B 57 -17.007 -15.606 41.033 1.00 48.09 B000 C
ATOM 3518 O ILE B 57 -17.309 -14.405 41.107 1.00 44.48 B000 O
ATOM 3519 CB ILE B 57 -14.874 -16.557 42.043 1.00 44.75 B000 C
ATOM 3520 CG1 ILE B 57 -14.221 -16.939 43.373 1.00 42.95 B000 C
ATOM 3521 CG2 ILE B 57 -14.206 -15.294 41.565 1.00 44.59 B000 C
ATOM 3522 CD1 ILE B 57 -14.515 -15.942 44.487 1.00 43.84 B000 C
ATOM 3523 N ASP B 58 -17.255 -16.335 39.931 1.00 49.88 B000 N
ATOM 3524 CA ASP B 58 -17.768 -15.682 38.723 1.00 51.63 B000 C
ATOM 3525 C ASP B 58 -19.178 -15.139 38.937 1.00 52.47 B000 C
ATOM 3526 O ASP B 58 -19.497 -14.036 38.471 1.00 52.37 B000 O
ATOM 3527 CB ASP B 58 -17.721 -16.641 37.525 1.00 54.15 B000 C
ATOM 3528 CG ASP B 58 -16.281 -16.912 37.033 1.00 66.06 B000 C
ATOM 3529 OD1 ASP B 58 -15.920 -18.096 36.826 1.00 66.11 B000 O
ATOM 3530 OD2 ASP B 58 -15.503 -15.946 36.860 1.00 62.18 B000 O1-
ATOM 3531 N ARG B 59 -20.030 -15.884 39.649 1.00 50.11 B000 N
ATOM 3532 CA ARG B 59 -21.365 -15.380 39.967 1.00 48.44 B000 C
ATOM 3533 C ARG B 59 -21.280 -14.045 40.682 1.00 49.35 B000 C
ATOM 3534 O ARG B 59 -21.956 -13.079 40.304 1.00 44.53 B000 O
ATOM 3535 CB ARG B 59 -22.136 -16.388 40.827 1.00 57.33 B000 C
ATOM 3536 CG ARG B 59 -22.249 -17.792 40.239 1.00 65.94 B000 C
ATOM 3537 CD ARG B 59 -23.344 -17.848 39.169 1.00 65.76 B000 C
ATOM 3538 NE ARG B 59 -22.859 -17.583 37.816 1.00 65.37 B000 N
ATOM 3539 CZ ARG B 59 -21.825 -18.177 37.230 1.00 64.09 B000 C
ATOM 3540 NH1 ARG B 59 -21.212 -19.213 37.780 1.00 60.62 B000 N1+
ATOM 3541 NH2 ARG B 59 -21.419 -17.740 36.042 1.00 60.50 B000 N
TER
HETATM 3542 O HOH B 59 -21.866 8.438 15.811 1.00 36.05 B000 O
HETATM 3543 O HOH B 60 -0.707 -12.466 6.524 1.00 38.23 B000 O
ATOM 3544 N ILE B 60 -20.428 -13.969 41.711 1.00 43.34 B000 N
ATOM 3545 CA ILE B 60 -20.289 -12.735 42.476 1.00 43.13 B000 C
ATOM 3546 C ILE B 60 -19.721 -11.633 41.599 1.00 42.88 B000 C
ATOM 3547 O ILE B 60 -20.180 -10.480 41.634 1.00 38.87 B000 O
ATOM 3548 CB ILE B 60 -19.411 -12.979 43.717 1.00 46.83 B000 C
ATOM 3549 CG1 ILE B 60 -20.132 -13.895 44.708 1.00 42.43 B000 C
ATOM 3550 CG2 ILE B 60 -19.063 -11.661 44.384 1.00 33.05 B000 C
ATOM 3551 CD1 ILE B 60 -19.225 -14.465 45.754 1.00 45.97 B000 C
TER
HETATM 3552 O HOH B 61 -17.281 17.388 17.120 1.00 35.94 B000 O
ATOM 3553 N TYR B 61 -18.718 -11.967 40.785 1.00 44.41 B000 N
ATOM 3554 CA TYR B 61 -18.065 -10.921 40.012 1.00 47.25 B000 C
ATOM 3555 C TYR B 61 -18.996 -10.388 38.937 1.00 47.47 B000 C
ATOM 3556 O TYR B 61 -19.002 -9.179 38.662 1.00 45.61 B000 O
ATOM 3557 CB TYR B 61 -16.764 -11.440 39.412 1.00 49.78 B000 C
ATOM 3558 CG TYR B 61 -15.963 -10.358 38.747 1.00 50.46 B000 C
ATOM 3559 CD1 TYR B 61 -15.901 -10.254 37.363 1.00 39.50 B000 C
ATOM 3560 CD2 TYR B 61 -15.286 -9.406 39.513 1.00 48.93 B000 C
ATOM 3561 CE1 TYR B 61 -15.159 -9.256 36.752 1.00 45.32 B000 C
ATOM 3562 CE2 TYR B 61 -14.546 -8.396 38.909 1.00 47.71 B000 C
ATOM 3563 CZ TYR B 61 -14.483 -8.331 37.524 1.00 49.13 B000 C
ATOM 3564 OH TYR B 61 -13.756 -7.331 36.920 1.00 53.26 B000 O
ATOM 3565 N GLU B 62 -19.818 -11.271 38.349 1.00 48.37 B000 N
ATOM 3566 CA GLU B 62 -20.894 -10.828 37.462 1.00 45.93 B000 C
ATOM 3567 C GLU B 62 -21.793 -9.810 38.155 1.00 43.62 B000 C
ATOM 3568 O GLU B 62 -22.141 -8.772 37.579 1.00 49.24 B000 O
ATOM 3569 CB GLU B 62 -21.724 -12.024 36.999 1.00 52.71 B000 C
ATOM 3570 CG GLU B 62 -21.184 -12.738 35.787 1.00 66.58 B000 C
ATOM 3571 CD GLU B 62 -22.252 -13.569 35.110 1.00 72.96 B000 C
ATOM 3572 OE1 GLU B 62 -23.428 -13.454 35.515 1.00 74.79 B000 O
ATOM 3573 OE2 GLU B 62 -21.920 -14.322 34.171 1.00 83.38 B000 O1-
TER
HETATM 3574 O HOH B 62 4.458 -16.567 21.392 1.00 43.48 B000 O
ATOM 3575 N ARG B 63 -22.181 -10.096 39.402 1.00 43.93 B000 N
ATOM 3576 CA ARG B 63 -23.004 -9.153 40.153 1.00 38.89 B000 C
ATOM 3577 C ARG B 63 -22.257 -7.858 40.415 1.00 45.10 B000 C
ATOM 3578 O ARG B 63 -22.826 -6.767 40.282 1.00 42.02 B000 O
ATOM 3579 CB ARG B 63 -23.453 -9.787 41.468 1.00 46.80 B000 C
ATOM 3580 CG ARG B 63 -24.907 -10.156 41.511 1.00 45.20 B000 C
ATOM 3581 CD ARG B 63 -25.346 -10.634 42.881 1.00 54.53 B000 C
ATOM 3582 NE ARG B 63 -24.873 -11.981 43.176 1.00 56.84 B000 N
ATOM 3583 CZ ARG B 63 -24.136 -12.319 44.225 1.00 57.31 B000 C
ATOM 3584 NH1 ARG B 63 -23.773 -11.429 45.136 1.00 50.98 B000 N1+
ATOM 3585 NH2 ARG B 63 -23.774 -13.592 44.376 1.00 50.35 B000 N
TER
HETATM 3586 O HOH B 63 -18.035 6.885 2.209 1.00 37.73 B000 O
HETATM 3587 O HOH B 64 -23.821 -15.916 49.207 1.00 31.94 B000 O
ATOM 3588 N ILE B 64 -20.978 -7.962 40.798 1.00 44.42 B000 N
ATOM 3589 CA ILE B 64 -20.158 -6.777 41.050 1.00 46.57 B000 C
ATOM 3590 C ILE B 64 -20.067 -5.912 39.797 1.00 43.46 B000 C
ATOM 3591 O ILE B 64 -20.248 -4.688 39.853 1.00 47.00 B000 O
ATOM 3592 CB ILE B 64 -18.764 -7.197 41.556 1.00 45.42 B000 C
ATOM 3593 CG1 ILE B 64 -18.872 -7.764 42.979 1.00 44.67 B000 C
ATOM 3594 CG2 ILE B 64 -17.787 -6.028 41.504 1.00 41.33 B000 C
ATOM 3595 CD1 ILE B 64 -17.640 -8.508 43.438 1.00 42.55 B000 C
TER
HETATM 3596 O HOH B 65 -17.925 20.135 14.024 1.00 34.47 B000 O
ATOM 3597 N LEU B 65 -19.796 -6.533 38.647 1.00 35.44 B000 N
ATOM 3598 CA LEU B 65 -19.738 -5.777 37.391 1.00 48.10 B000 C
ATOM 3599 C LEU B 65 -20.990 -4.931 37.174 1.00 49.02 B000 C
ATOM 3600 O LEU B 65 -20.901 -3.787 36.706 1.00 48.59 B000 O
ATOM 3601 CB LEU B 65 -19.540 -6.727 36.212 1.00 46.97 B000 C
ATOM 3602 CG LEU B 65 -18.179 -7.416 36.149 1.00 48.83 B000 C
ATOM 3603 CD1 LEU B 65 -18.186 -8.529 35.109 1.00 52.22 B000 C
ATOM 3604 CD2 LEU B 65 -17.073 -6.406 35.864 1.00 42.12 B000 C
ATOM 3605 N ALA B 66 -22.162 -5.467 37.541 1.00 38.37 B000 N
ATOM 3606 CA ALA B 66 -23.454 -4.814 37.351 1.00 48.38 B000 C
ATOM 3607 C ALA B 66 -23.789 -3.768 38.410 1.00 50.04 B000 C
ATOM 3608 O ALA B 66 -24.761 -3.025 38.227 1.00 51.92 B000 O
ATOM 3609 CB ALA B 66 -24.576 -5.861 37.335 1.00 42.76 B000 C
TER
HETATM 3610 O HOH B 66 -13.688 -4.986 -13.701 1.00 34.57 B000 O
ATOM 3611 N ASP B 67 -23.046 -3.701 39.517 1.00 47.57 B000 N
ATOM 3612 CA ASP B 67 -23.366 -2.748 40.575 1.00 45.93 B000 C
ATOM 3613 C ASP B 67 -23.170 -1.311 40.078 1.00 54.75 B000 C
ATOM 3614 O ASP B 67 -22.076 -0.929 39.643 1.00 50.50 B000 O
ATOM 3615 CB ASP B 67 -22.508 -3.031 41.806 1.00 38.06 B000 C
ATOM 3616 CG ASP B 67 -22.993 -2.317 43.023 1.00 36.97 B000 C
ATOM 3617 OD1 ASP B 67 -23.209 -1.088 42.961 1.00 42.35 B000 O
ATOM 3618 OD2 ASP B 67 -23.158 -2.979 44.073 1.00 47.54 B000 O1-
TER
HETATM 3619 O HOH B 67 -14.037 7.152 52.747 1.00 37.88 B000 O
ATOM 3620 N GLU B 68 -24.234 -0.507 40.166 1.00 53.56 B000 N
ATOM 3621 CA GLU B 68 -24.206 0.857 39.643 1.00 57.67 B000 C
ATOM 3622 C GLU B 68 -23.254 1.763 40.402 1.00 54.12 B000 C
ATOM 3623 O GLU B 68 -22.881 2.822 39.883 1.00 50.68 B000 O
ATOM 3624 CB GLU B 68 -25.608 1.475 39.682 1.00 53.16 B000 C
ATOM 3625 CG GLU B 68 -26.691 0.593 39.073 1.00 74.96 B000 C
ATOM 3626 CD GLU B 68 -27.997 1.343 38.821 1.00 88.10 B000 C
ATOM 3627 OE1 GLU B 68 -28.874 1.349 39.718 1.00 79.26 B000 O
ATOM 3628 OE2 GLU B 68 -28.136 1.934 37.726 1.00 89.44 B000 O1-
TER
HETATM 3629 O HOH B 68 -11.174 -14.072 -1.792 1.00 31.34 B000 O
ATOM 3630 N ARG B 69 -22.859 1.378 41.614 1.00 53.42 B000 N
ATOM 3631 CA ARG B 69 -22.136 2.274 42.503 1.00 47.86 B000 C
ATOM 3632 C ARG B 69 -20.661 2.421 42.139 1.00 47.95 B000 C
ATOM 3633 O ARG B 69 -19.972 3.263 42.735 1.00 41.57 B000 O
ATOM 3634 CB ARG B 69 -22.295 1.783 43.943 1.00 44.96 B000 C
ATOM 3635 CG ARG B 69 -23.740 1.795 44.401 1.00 47.38 B000 C
ATOM 3636 CD ARG B 69 -23.900 1.117 45.731 1.00 45.42 B000 C
ATOM 3637 NE ARG B 69 -23.593 -0.309 45.666 1.00 44.95 B000 N
ATOM 3638 CZ ARG B 69 -23.895 -1.161 46.636 1.00 37.53 B000 C
ATOM 3639 NH1 ARG B 69 -24.498 -0.755 47.742 1.00 34.05 B000 N1+
ATOM 3640 NH2 ARG B 69 -23.586 -2.448 46.494 1.00 38.32 B000 N
TER
HETATM 3641 O HOH B 69 -23.368 -8.921 18.305 1.00 52.07 B000 O
ATOM 3642 N HIS B 70 -20.160 1.650 41.173 1.00 42.12 B000 N
ATOM 3643 CA HIS B 70 -18.821 1.909 40.672 1.00 47.35 B000 C
ATOM 3644 C HIS B 70 -18.755 1.621 39.174 1.00 53.05 B000 C
ATOM 3645 O HIS B 70 -19.630 0.964 38.599 1.00 48.35 B000 O
ATOM 3646 CB HIS B 70 -17.761 1.117 41.464 1.00 41.13 B000 C
ATOM 3647 CG HIS B 70 -17.869 -0.368 41.333 1.00 42.69 B000 C
ATOM 3648 CD2 HIS B 70 -18.808 -1.153 40.755 1.00 36.92 B000 C
ATOM 3649 ND1 HIS B 70 -16.902 -1.223 41.820 1.00 38.73 B000 N
ATOM 3650 CE1 HIS B 70 -17.253 -2.471 41.567 1.00 38.58 B000 C
ATOM 3651 NE2 HIS B 70 -18.404 -2.456 40.919 1.00 41.06 B000 N
TER
HETATM 3652 O HOH B 70 -2.586 8.739 55.551 1.00 40.89 B000 O
HETATM 3653 O HOH B 71 -27.196 -8.125 54.866 1.00 39.01 B000 O
ATOM 3654 N THR B 71 -17.686 2.130 38.553 1.00 48.16 B000 N
ATOM 3655 CA THR B 71 -17.484 2.098 37.112 1.00 48.79 B000 C
ATOM 3656 C THR B 71 -16.020 1.823 36.799 1.00 51.87 B000 C
ATOM 3657 O THR B 71 -15.157 1.803 37.688 1.00 45.36 B000 O
ATOM 3658 CB THR B 71 -17.930 3.418 36.451 1.00 49.81 B000 C
ATOM 3659 CG2 THR B 71 -16.885 4.511 36.625 1.00 53.28 B000 C
ATOM 3660 OG1 THR B 71 -18.185 3.203 35.058 1.00 53.58 B000 O
ATOM 3661 N ASP B 72 -15.759 1.619 35.507 1.00 48.23 B000 N
ATOM 3662 CA ASP B 72 -14.427 1.374 34.969 1.00 44.45 B000 C
ATOM 3663 C ASP B 72 -13.728 0.246 35.719 1.00 50.64 B000 C
ATOM 3664 O ASP B 72 -12.593 0.382 36.182 1.00 47.27 B000 O
ATOM 3665 CB ASP B 72 -13.591 2.652 34.991 1.00 58.48 B000 C
ATOM 3666 CG ASP B 72 -14.286 3.792 34.297 1.00 59.92 B000 C
ATOM 3667 OD1 ASP B 72 -15.227 3.511 33.527 1.00 61.55 B000 O
ATOM 3668 OD2 ASP B 72 -13.883 4.957 34.494 1.00 63.35 B000 O1-
TER
HETATM 3669 O HOH B 72 -24.290 -1.007 -5.072 1.00 42.92 B000 O
ATOM 3670 N ILE B 73 -14.426 -0.880 35.835 1.00 43.10 B000 N
ATOM 3671 CA ILE B 73 -13.923 -2.019 36.591 1.00 50.13 B000 C
ATOM 3672 C ILE B 73 -12.907 -2.776 35.745 1.00 49.15 B000 C
ATOM 3673 O ILE B 73 -13.254 -3.322 34.693 1.00 54.34 B000 O
ATOM 3674 CB ILE B 73 -15.069 -2.939 37.025 1.00 36.70 B000 C
ATOM 3675 CG1 ILE B 73 -16.101 -2.161 37.852 1.00 43.33 B000 C
ATOM 3676 CG2 ILE B 73 -14.526 -4.117 37.813 1.00 39.99 B000 C
ATOM 3677 CD1 ILE B 73 -17.537 -2.677 37.686 1.00 46.34 B000 C
TER
HETATM 3678 O HOH B 74 -1.414 -22.859 14.868 1.00 41.12 B000 O
ATOM 3679 N LEU B 74 -11.657 -2.830 36.220 1.00 41.78 B000 N
ATOM 3680 CA LEU B 74 -10.552 -3.473 35.515 1.00 44.71 B000 C
ATOM 3681 C LEU B 74 -9.954 -4.586 36.369 1.00 41.06 B000 C
ATOM 3682 O LEU B 74 -9.409 -4.322 37.447 1.00 40.59 B000 O
ATOM 3683 CB LEU B 74 -9.471 -2.450 35.161 1.00 42.78 B000 C
ATOM 3684 CG LEU B 74 -8.264 -3.092 34.475 1.00 48.39 B000 C
ATOM 3685 CD1 LEU B 74 -8.631 -3.485 33.043 1.00 50.63 B000 C
ATOM 3686 CD2 LEU B 74 -7.062 -2.157 34.496 1.00 46.25 B000 C
ATOM 3687 N CYS B 75 -10.031 -5.820 35.877 1.00 40.11 B000 N
ATOM 3688 CA CYS B 75 -9.415 -6.968 36.544 1.00 38.93 B000 C
ATOM 3689 C CYS B 75 -7.909 -6.984 36.288 1.00 45.65 B000 C
ATOM 3690 O CYS B 75 -7.465 -7.219 35.158 1.00 39.47 B000 O
ATOM 3691 CB CYS B 75 -10.050 -8.264 36.057 1.00 39.83 B000 C
ATOM 3692 SG CYS B 75 -9.252 -9.750 36.683 1.00 49.48 B000 S
TER
HETATM 3693 O HOH B 75 -15.936 -6.891 20.838 1.00 39.90 B000 O
HETATM 3694 O HOH B 76 -24.929 -9.665 11.112 1.00 41.67 B000 O
ATOM 3695 N LEU B 76 -7.117 -6.779 37.344 1.00 37.41 B000 N
ATOM 3696 CA LEU B 76 -5.662 -6.768 37.211 1.00 38.52 B000 C
ATOM 3697 C LEU B 76 -5.072 -8.169 37.156 1.00 43.01 B000 C
ATOM 3698 O LEU B 76 -4.055 -8.389 36.489 1.00 42.54 B000 O
ATOM 3699 CB LEU B 76 -5.028 -6.010 38.375 1.00 42.51 B000 C
ATOM 3700 CG LEU B 76 -5.483 -4.572 38.555 1.00 41.83 B000 C
ATOM 3701 CD1 LEU B 76 -4.918 -4.019 39.841 1.00 38.48 B000 C
ATOM 3702 CD2 LEU B 76 -5.053 -3.761 37.364 1.00 42.11 B000 C
ATOM 3703 N LYS B 77 -5.674 -9.122 37.852 1.00 43.24 B000 N
ATOM 3704 CA LYS B 77 -5.090 -10.447 37.959 1.00 40.37 B000 C
ATOM 3705 C LYS B 77 -6.206 -11.447 38.150 1.00 38.70 B000 C
ATOM 3706 O LYS B 77 -7.147 -11.191 38.904 1.00 40.67 B000 O
ATOM 3707 CB LYS B 77 -4.116 -10.544 39.134 1.00 39.45 B000 C
ATOM 3708 CG LYS B 77 -3.493 -11.912 39.277 1.00 37.69 B000 C
ATOM 3709 CD LYS B 77 -2.604 -11.982 40.489 1.00 45.65 B000 C
ATOM 3710 CE LYS B 77 -1.241 -11.455 40.187 1.00 50.62 B000 C
ATOM 3711 NZ LYS B 77 -0.268 -11.945 41.201 1.00 59.16 B000 N1+
TER
HETATM 3712 O HOH B 78 -1.435 11.201 23.671 1.00 47.37 B000 O
ATOM 3713 N SER B 78 -6.084 -12.594 37.496 1.00 41.82 B000 N
ATOM 3714 CA SER B 78 -7.051 -13.673 37.651 1.00 41.12 B000 C
ATOM 3715 C SER B 78 -6.283 -14.973 37.819 1.00 45.90 B000 C
ATOM 3716 O SER B 78 -5.699 -15.473 36.854 1.00 53.53 B000 O
ATOM 3717 CB SER B 78 -7.996 -13.748 36.453 1.00 42.69 B000 C
ATOM 3718 OG SER B 78 -8.753 -14.933 36.512 1.00 52.12 B000 O
ATOM 3719 N GLU B 79 -6.281 -15.521 39.032 1.00 41.53 B000 N
ATOM 3720 CA GLU B 79 -5.571 -16.756 39.329 1.00 41.59 B000 C
ATOM 3721 C GLU B 79 -6.541 -17.926 39.318 1.00 51.21 B000 C
ATOM 3722 O GLU B 79 -7.659 -17.825 39.831 1.00 52.78 B000 O
ATOM 3723 CB GLU B 79 -4.869 -16.681 40.688 1.00 44.67 B000 C
ATOM 3724 CG GLU B 79 -3.838 -15.572 40.814 1.00 48.14 B000 C
ATOM 3725 CD GLU B 79 -3.504 -15.246 42.268 1.00 49.02 B000 C
ATOM 3726 OE1 GLU B 79 -2.705 -15.993 42.870 1.00 39.74 B000 O
ATOM 3727 OE2 GLU B 79 -4.066 -14.261 42.812 1.00 42.18 B000 O1-
TER
HETATM 3728 O HOH B 79 -20.277 -11.086 58.184 1.00 38.48 B000 O
HETATM 3729 O HOH B 80 -19.514 18.957 15.571 1.00 39.41 B000 O
ATOM 3730 N VAL B 80 -6.110 -19.031 38.717 1.00 54.84 B000 N
ATOM 3731 CA VAL B 80 -6.878 -20.265 38.692 1.00 51.24 B000 C
ATOM 3732 C VAL B 80 -6.060 -21.339 39.390 1.00 56.55 B000 C
ATOM 3733 O VAL B 80 -4.858 -21.180 39.628 1.00 56.43 B000 O
ATOM 3734 CB VAL B 80 -7.250 -20.696 37.258 1.00 67.19 B000 C
ATOM 3735 CG1 VAL B 80 -8.138 -19.643 36.598 1.00 56.29 B000 C
ATOM 3736 CG2 VAL B 80 -5.984 -20.932 36.432 1.00 50.41 B000 C
ATOM 3737 N GLU B 81 -6.733 -22.440 39.729 1.00 59.34 B000 N
ATOM 3738 CA GLU B 81 -6.106 -23.556 40.437 1.00 62.08 B000 C
ATOM 3739 C GLU B 81 -5.276 -23.054 41.616 1.00 56.87 B000 C
ATOM 3740 O GLU B 81 -4.096 -23.378 41.762 1.00 55.73 B000 O
ATOM 3741 CB GLU B 81 -5.244 -24.395 39.491 1.00 72.84 B000 C
ATOM 3742 CG GLU B 81 -6.016 -25.229 38.473 1.00 77.47 B000 C
ATOM 3743 CD GLU B 81 -5.103 -25.806 37.396 1.00 91.70 B000 C
ATOM 3744 OE1 GLU B 81 -4.374 -25.020 36.745 1.00 86.18 B000 O
ATOM 3745 OE2 GLU B 81 -5.097 -27.046 37.216 1.00 93.74 B000 O1-
TER
HETATM 3746 O HOH B 81 -24.443 -8.757 13.415 1.00 40.37 B000 O
HETATM 3747 O HOH B 82 -21.922 26.605 12.925 1.00 45.14 B000 O
ATOM 3748 N VAL B 82 -5.901 -22.231 42.452 1.00 51.53 B000 N
ATOM 3749 CA VAL B 82 -5.206 -21.628 43.584 1.00 50.20 B000 C
ATOM 3750 C VAL B 82 -5.096 -22.653 44.704 1.00 49.08 B000 C
ATOM 3751 O VAL B 82 -6.081 -23.311 45.060 1.00 52.53 B000 O
ATOM 3752 CB VAL B 82 -5.936 -20.363 44.055 1.00 52.39 B000 C
ATOM 3753 CG1 VAL B 82 -5.564 -20.042 45.490 1.00 52.33 B000 C
ATOM 3754 CG2 VAL B 82 -5.620 -19.201 43.126 1.00 49.28 B000 C
ATOM 3755 N GLN B 83 -3.893 -22.798 45.262 1.00 49.16 B000 N
ATOM 3756 CA GLN B 83 -3.679 -23.844 46.257 1.00 53.78 B000 C
ATOM 3757 C GLN B 83 -4.220 -23.464 47.636 1.00 60.39 B000 C
ATOM 3758 O GLN B 83 -4.802 -24.312 48.324 1.00 57.58 B000 O
ATOM 3759 CB GLN B 83 -2.194 -24.196 46.326 1.00 57.13 B000 C
ATOM 3760 CG GLN B 83 -1.715 -25.036 45.141 1.00 66.24 B000 C
ATOM 3761 CD GLN B 83 -2.850 -25.819 44.493 1.00 65.01 B000 C
ATOM 3762 NE2 GLN B 83 -3.205 -26.954 45.091 1.00 65.79 B000 N
ATOM 3763 OE1 GLN B 83 -3.405 -25.406 43.473 1.00 67.09 B000 O
TER
HETATM 3764 O HOH B 83 -5.521 5.139 61.478 1.00 37.06 B000 O
ATOM 3765 N GLU B 84 -4.041 -22.215 48.071 1.00 60.28 B000 N
ATOM 3766 CA GLU B 84 -4.555 -21.823 49.376 1.00 57.79 B000 C
ATOM 3767 C GLU B 84 -4.978 -20.362 49.359 1.00 50.42 B000 C
ATOM 3768 O GLU B 84 -4.519 -19.564 48.537 1.00 43.63 B000 O
ATOM 3769 CB GLU B 84 -3.539 -22.054 50.505 1.00 62.79 B000 C
ATOM 3770 CG GLU B 84 -2.406 -21.060 50.577 1.00 59.30 B000 C
ATOM 3771 CD GLU B 84 -1.123 -21.579 49.943 1.00 84.68 B000 C
ATOM 3772 OE1 GLU B 84 -1.208 -22.422 49.022 1.00 81.89 B000 O
ATOM 3773 OE2 GLU B 84 -0.026 -21.153 50.381 1.00 94.05 B000 O1-
ATOM 3774 N ARG B 85 -5.859 -20.024 50.301 1.00 39.20 B000 N
ATOM 3775 CA ARG B 85 -6.410 -18.683 50.406 1.00 38.22 B000 C
ATOM 3776 C ARG B 85 -5.388 -17.713 50.985 1.00 35.50 B000 C
ATOM 3777 O ARG B 85 -4.561 -18.077 51.826 1.00 44.05 B000 O
ATOM 3778 CB ARG B 85 -7.666 -18.690 51.283 1.00 39.77 B000 C
ATOM 3779 CG ARG B 85 -8.765 -19.597 50.767 1.00 36.40 B000 C
ATOM 3780 CD ARG B 85 -9.888 -19.779 51.766 1.00 41.91 B000 C
ATOM 3781 NE ARG B 85 -10.959 -20.564 51.161 1.00 42.88 B000 N
ATOM 3782 CZ ARG B 85 -12.023 -20.046 50.562 1.00 39.70 B000 C
ATOM 3783 NH1 ARG B 85 -12.233 -18.739 50.532 1.00 35.89 B000 N1+
ATOM 3784 NH2 ARG B 85 -12.889 -20.859 49.964 1.00 41.03 B000 N
TER
HETATM 3785 O HOH B 86 -27.076 -0.058 8.795 1.00 40.66 B000 O
ATOM 3786 N MET B 86 -5.451 -16.464 50.519 1.00 33.73 B000 N
ATOM 3787 CA MET B 86 -4.669 -15.408 51.150 1.00 34.88 B000 C
ATOM 3788 C MET B 86 -5.354 -14.868 52.397 1.00 41.52 B000 C
ATOM 3789 O MET B 86 -4.674 -14.419 53.324 1.00 35.40 B000 O
ATOM 3790 CB MET B 86 -4.435 -14.253 50.186 1.00 35.12 B000 C
ATOM 3791 CG MET B 86 -3.039 -14.242 49.560 1.00 45.52 B000 C
ATOM 3792 SD MET B 86 -2.983 -13.351 47.986 1.00 56.32 B000 S
ATOM 3793 CE MET B 86 -1.333 -13.818 47.393 1.00 37.30 B000 C
TER
HETATM 3794 O HOH B 87 -25.169 -7.723 17.770 1.00 55.85 B000 O
ATOM 3795 N PHE B 87 -6.685 -14.898 52.439 1.00 30.10 B000 N
ATOM 3796 CA PHE B 87 -7.453 -14.226 53.481 1.00 31.18 B000 C
ATOM 3797 C PHE B 87 -8.465 -15.188 54.099 1.00 28.79 B000 C
ATOM 3798 O PHE B 87 -9.664 -14.906 54.141 1.00 28.21 B000 O
ATOM 3799 CB PHE B 87 -8.121 -12.980 52.896 1.00 27.69 B000 C
ATOM 3800 CG PHE B 87 -7.161 -12.083 52.140 1.00 35.06 B000 C
ATOM 3801 CD1 PHE B 87 -6.181 -11.365 52.827 1.00 28.23 B000 C
ATOM 3802 CD2 PHE B 87 -7.224 -11.960 50.754 1.00 30.99 B000 C
ATOM 3803 CE1 PHE B 87 -5.292 -10.525 52.160 1.00 26.88 B000 C
ATOM 3804 CE2 PHE B 87 -6.332 -11.121 50.066 1.00 28.52 B000 C
ATOM 3805 CZ PHE B 87 -5.377 -10.396 50.770 1.00 30.65 B000 C
TER
HETATM 3806 O HOH B 88 -28.394 -3.742 2.560 1.00 42.51 B000 O
ATOM 3807 N PRO B 88 -8.001 -16.334 54.619 1.00 33.82 B000 N
ATOM 3808 CA PRO B 88 -8.948 -17.405 55.000 1.00 33.05 B000 C
ATOM 3809 C PRO B 88 -9.976 -17.007 56.052 1.00 35.67 B000 C
ATOM 3810 O PRO B 88 -11.085 -17.559 56.057 1.00 34.45 B000 O
ATOM 3811 CB PRO B 88 -8.022 -18.516 55.511 1.00 29.56 B000 C
ATOM 3812 CG PRO B 88 -6.792 -17.800 55.954 1.00 29.76 B000 C
ATOM 3813 CD PRO B 88 -6.613 -16.670 54.992 1.00 32.33 B000 C
ATOM 3814 N ASP B 89 -9.664 -16.064 56.935 1.00 30.15 B000 N
ATOM 3815 CA ASP B 89 -10.607 -15.680 57.977 1.00 34.21 B000 C
ATOM 3816 C ASP B 89 -11.396 -14.428 57.633 1.00 35.16 B000 C
ATOM 3817 O ASP B 89 -12.111 -13.909 58.485 1.00 29.21 B000 O
ATOM 3818 CB ASP B 89 -9.865 -15.508 59.298 1.00 36.12 B000 C
ATOM 3819 CG ASP B 89 -9.168 -16.780 59.714 1.00 38.79 B000 C
ATOM 3820 OD1 ASP B 89 -9.862 -17.822 59.756 1.00 41.22 B000 O
ATOM 3821 OD2 ASP B 89 -7.941 -16.750 59.932 1.00 40.62 B000 O1-
TER
HETATM 3822 O HOH B 89 -3.223 20.971 9.339 1.00 40.84 B000 O
HETATM 3823 O HOH B 90 -23.012 -15.381 46.384 1.00 41.94 B000 O
ATOM 3824 N TRP B 90 -11.282 -13.924 56.410 1.00 24.78 B000 N
ATOM 3825 CA TRP B 90 -11.956 -12.689 56.012 1.00 25.22 B000 C
ATOM 3826 C TRP B 90 -12.997 -13.026 54.952 1.00 29.26 B000 C
ATOM 3827 O TRP B 90 -12.669 -13.077 53.768 1.00 33.24 B000 O
ATOM 3828 CB TRP B 90 -10.949 -11.654 55.460 1.00 24.74 B000 C
ATOM 3829 CG TRP B 90 -9.903 -11.179 56.409 1.00 30.72 B000 C
ATOM 3830 CD1 TRP B 90 -9.798 -11.458 57.748 1.00 26.01 B000 C
ATOM 3831 CD2 TRP B 90 -8.811 -10.303 56.095 1.00 27.91 B000 C
ATOM 3832 CE2 TRP B 90 -8.080 -10.102 57.287 1.00 29.26 B000 C
ATOM 3833 CE3 TRP B 90 -8.383 -9.668 54.919 1.00 26.76 B000 C
ATOM 3834 NE1 TRP B 90 -8.703 -10.823 58.277 1.00 25.47 B000 N
ATOM 3835 CZ2 TRP B 90 -6.934 -9.288 57.340 1.00 27.67 B000 C
ATOM 3836 CZ3 TRP B 90 -7.239 -8.841 54.976 1.00 29.86 B000 C
ATOM 3837 CH2 TRP B 90 -6.529 -8.674 56.176 1.00 28.03 B000 C
TER
HETATM 3838 O HOH B 91 -24.051 7.859 54.321 1.00 44.84 B000 O
ATOM 3839 N SER B 91 -14.249 -13.259 55.353 1.00 32.27 B000 N
ATOM 3840 CA SER B 91 -15.292 -13.368 54.339 1.00 29.02 B000 C
ATOM 3841 C SER B 91 -15.312 -12.113 53.478 1.00 28.80 B000 C
ATOM 3842 O SER B 91 -15.372 -12.194 52.248 1.00 27.08 B000 O
ATOM 3843 CB SER B 91 -16.659 -13.610 54.989 1.00 24.42 B000 C
ATOM 3844 OG SER B 91 -16.674 -14.864 55.659 1.00 28.94 B000 O
TER
HETATM 3845 O HOH B 92 -13.496 -7.111 34.091 1.00 51.52 B000 O
ATOM 3846 N MET B 92 -15.289 -10.940 54.111 1.00 26.82 B000 N
ATOM 3847 CA MET B 92 -14.884 -9.711 53.432 1.00 29.18 B000 C
ATOM 3848 C MET B 92 -14.358 -8.757 54.496 1.00 30.21 B000 C
ATOM 3849 O MET B 92 -15.117 -8.329 55.366 1.00 30.91 B000 O
ATOM 3850 CB MET B 92 -16.025 -9.032 52.657 1.00 30.74 B000 C
ATOM 3851 CG MET B 92 -15.506 -7.815 51.849 1.00 33.56 B000 C
ATOM 3852 SD MET B 92 -14.018 -8.022 50.797 1.00 35.47 B000 S
ATOM 3853 CE MET B 92 -14.095 -9.709 50.188 1.00 32.54 B000 C
ATOM 3854 N GLN B 93 -13.074 -8.413 54.430 1.00 29.28 B000 N
ATOM 3855 CA GLN B 93 -12.497 -7.400 55.317 1.00 27.93 B000 C
ATOM 3856 C GLN B 93 -12.455 -6.066 54.596 1.00 29.32 B000 C
ATOM 3857 O GLN B 93 -11.959 -5.985 53.470 1.00 32.74 B000 O
ATOM 3858 CB GLN B 93 -11.081 -7.772 55.753 1.00 27.06 B000 C
ATOM 3859 CG GLN B 93 -10.350 -6.705 56.567 1.00 25.80 B000 C
ATOM 3860 CD GLN B 93 -10.806 -6.631 58.026 1.00 29.02 B000 C
ATOM 3861 NE2 GLN B 93 -10.219 -5.707 58.772 1.00 26.44 B000 N
ATOM 3862 OE1 GLN B 93 -11.676 -7.386 58.470 1.00 26.20 B000 O
TER
HETATM 3863 O HOH B 93 -22.184 1.650 57.674 1.00 38.93 B000 O
ATOM 3864 N THR B 94 -12.906 -5.016 55.267 1.00 28.09 B000 N
ATOM 3865 CA THR B 94 -13.024 -3.696 54.670 1.00 29.25 B000 C
ATOM 3866 C THR B 94 -12.011 -2.748 55.298 1.00 33.13 B000 C
ATOM 3867 O THR B 94 -11.893 -2.672 56.528 1.00 30.14 B000 O
ATOM 3868 CB THR B 94 -14.451 -3.189 54.844 1.00 33.51 B000 C
ATOM 3869 CG2 THR B 94 -14.621 -1.790 54.238 1.00 29.22 B000 C
ATOM 3870 OG1 THR B 94 -15.326 -4.116 54.184 1.00 35.76 B000 O
TER
HETATM 3871 O HOH B 95 -8.743 18.975 18.918 1.00 31.28 B000 O
ATOM 3872 N ILE B 95 -11.249 -2.061 54.452 1.00 30.16 B000 N
ATOM 3873 CA ILE B 95 -10.150 -1.205 54.890 1.00 28.43 B000 C
ATOM 3874 C ILE B 95 -10.333 0.134 54.194 1.00 31.09 B000 C
ATOM 3875 O ILE B 95 -9.981 0.280 53.020 1.00 28.55 B000 O
ATOM 3876 CB ILE B 95 -8.778 -1.801 54.562 1.00 29.90 B000 C
ATOM 3877 CG1 ILE B 95 -8.624 -3.198 55.181 1.00 27.59 B000 C
ATOM 3878 CG2 ILE B 95 -7.667 -0.877 55.034 1.00 24.50 B000 C
ATOM 3879 CD1 ILE B 95 -7.268 -3.865 54.817 1.00 24.25 B000 C
ATOM 3880 N ASN B 96 -10.865 1.114 54.913 1.00 33.04 B000 N
ATOM 3881 CA ASN B 96 -11.031 2.457 54.374 1.00 38.20 B000 C
ATOM 3882 C ASN B 96 -9.723 3.207 54.575 1.00 37.33 B000 C
ATOM 3883 O ASN B 96 -9.389 3.589 55.701 1.00 33.05 B000 O
ATOM 3884 CB ASN B 96 -12.191 3.183 55.052 1.00 34.64 B000 C
ATOM 3885 CG ASN B 96 -12.502 4.528 54.395 1.00 43.82 B000 C
ATOM 3886 ND2 ASN B 96 -13.780 4.781 54.132 1.00 43.99 B000 N
ATOM 3887 OD1 ASN B 96 -11.600 5.326 54.123 1.00 40.21 B000 O
ATOM 3888 N LEU B 97 -8.981 3.416 53.482 1.00 32.45 B000 N
ATOM 3889 CA LEU B 97 -7.701 4.099 53.592 1.00 29.38 B000 C
ATOM 3890 C LEU B 97 -7.848 5.597 53.786 1.00 32.69 B000 C
ATOM 3891 O LEU B 97 -6.951 6.221 54.359 1.00 30.93 B000 O
ATOM 3892 CB LEU B 97 -6.845 3.814 52.361 1.00 32.03 B000 C
ATOM 3893 CG LEU B 97 -6.463 2.343 52.357 1.00 32.71 B000 C
ATOM 3894 CD1 LEU B 97 -5.890 1.956 51.010 1.00 32.75 B000 C
ATOM 3895 CD2 LEU B 97 -5.484 2.089 53.504 1.00 28.66 B000 C
ATOM 3896 N ASP B 98 -8.944 6.196 53.314 1.00 31.04 B000 N
ATOM 3897 CA ASP B 98 -9.156 7.620 53.559 1.00 34.08 B000 C
ATOM 3898 C ASP B 98 -9.108 7.922 55.042 1.00 34.59 B000 C
ATOM 3899 O ASP B 98 -8.483 8.900 55.468 1.00 45.04 B000 O
ATOM 3900 CB ASP B 98 -10.498 8.073 52.980 1.00 29.11 B000 C
ATOM 3901 CG ASP B 98 -10.545 7.970 51.483 1.00 35.16 B000 C
ATOM 3902 OD1 ASP B 98 -9.619 8.483 50.827 1.00 35.19 B000 O
ATOM 3903 OD2 ASP B 98 -11.494 7.337 50.956 1.00 42.77 B000 O1-
ATOM 3904 N GLU B 99 -9.755 7.086 55.841 1.00 38.26 B000 N
ATOM 3905 CA GLU B 99 -9.809 7.288 57.282 1.00 38.54 B000 C
ATOM 3906 C GLU B 99 -8.567 6.785 58.001 1.00 34.84 B000 C
ATOM 3907 O GLU B 99 -8.397 7.071 59.189 1.00 36.57 B000 O
ATOM 3908 CB GLU B 99 -11.053 6.600 57.841 1.00 37.69 B000 C
ATOM 3909 CG GLU B 99 -12.338 7.141 57.215 1.00 47.42 B000 C
ATOM 3910 CD GLU B 99 -13.589 6.395 57.654 1.00 46.10 B000 C
ATOM 3911 OE1 GLU B 99 -13.548 5.715 58.703 1.00 55.21 B000 O
ATOM 3912 OE2 GLU B 99 -14.614 6.502 56.942 1.00 51.57 B000 O1-
TER
HETATM 3913 O HOH B 99 4.583 2.197 62.691 1.00 38.43 B000 O
ATOM 3914 N ASN B 100 -7.686 6.064 57.330 1.00 32.95 B000 N
ATOM 3915 CA ASN B 100 -6.523 5.550 58.035 1.00 37.26 B000 C
ATOM 3916 C ASN B 100 -5.483 6.654 58.159 1.00 31.04 B000 C
ATOM 3917 O ASN B 100 -5.204 7.358 57.186 1.00 36.53 B000 O
ATOM 3918 CB ASN B 100 -5.943 4.339 57.314 1.00 38.50 B000 C
ATOM 3919 CG ASN B 100 -4.888 3.636 58.142 1.00 37.97 B000 C
ATOM 3920 ND2 ASN B 100 -5.265 2.516 58.761 1.00 28.82 B000 N
ATOM 3921 OD1 ASN B 100 -3.749 4.104 58.239 1.00 32.90 B000 O
ATOM 3922 N THR B 101 -4.923 6.814 59.360 1.00 34.91 B000 N
ATOM 3923 CA THR B 101 -3.900 7.824 59.632 1.00 41.55 B000 C
ATOM 3924 C THR B 101 -2.614 7.208 60.180 1.00 38.20 B000 C
ATOM 3925 O THR B 101 -1.808 7.915 60.780 1.00 37.59 B000 O
ATOM 3926 CB THR B 101 -4.414 8.891 60.611 1.00 43.37 B000 C
ATOM 3927 CG2 THR B 101 -5.738 9.488 60.150 1.00 41.70 B000 C
ATOM 3928 OG1 THR B 101 -4.595 8.320 61.916 1.00 43.45 B000 O
ATOM 3929 N ASP B 102 -2.416 5.906 60.001 1.00 33.90 B000 N
ATOM 3930 CA ASP B 102 -1.240 5.254 60.550 1.00 30.84 B000 C
ATOM 3931 C ASP B 102 0.024 5.780 59.873 1.00 35.08 B000 C
ATOM 3932 O ASP B 102 0.063 6.006 58.658 1.00 31.34 B000 O
ATOM 3933 CB ASP B 102 -1.334 3.739 60.365 1.00 26.29 B000 C
ATOM 3934 CG ASP B 102 -2.486 3.125 61.142 1.00 35.53 B000 C
ATOM 3935 OD1 ASP B 102 -3.081 3.819 61.996 1.00 38.65 B000 O
ATOM 3936 OD2 ASP B 102 -2.854 1.971 60.833 1.00 33.16 B000 O1-
ATOM 3937 N PHE B 103 1.075 5.903 60.678 1.00 30.86 B000 N
ATOM 3938 CA PHE B 103 2.327 6.531 60.267 1.00 33.36 B000 C
ATOM 3939 C PHE B 103 2.899 5.924 58.990 1.00 30.21 B000 C
ATOM 3940 O PHE B 103 3.312 6.647 58.079 1.00 32.70 B000 O
ATOM 3941 CB PHE B 103 3.344 6.392 61.399 1.00 29.07 B000 C
ATOM 3942 CG PHE B 103 4.667 7.015 61.096 1.00 30.91 B000 C
ATOM 3943 CD1 PHE B 103 4.843 8.393 61.224 1.00 32.78 B000 C
ATOM 3944 CD2 PHE B 103 5.728 6.242 60.668 1.00 31.59 B000 C
ATOM 3945 CE1 PHE B 103 6.069 8.970 60.949 1.00 30.04 B000 C
ATOM 3946 CE2 PHE B 103 6.955 6.816 60.407 1.00 33.53 B000 C
ATOM 3947 CZ PHE B 103 7.119 8.180 60.541 1.00 32.11 B000 C
TER
HETATM 3948 O HOH B 104 -3.693 2.451 -1.900 1.00 38.84 B000 O
ATOM 3949 N LEU B 104 3.024 4.596 58.949 1.00 28.88 B000 N
ATOM 3950 CA LEU B 104 3.638 3.954 57.802 1.00 28.79 B000 C
ATOM 3951 C LEU B 104 2.681 3.851 56.620 1.00 29.74 B000 C
ATOM 3952 O LEU B 104 3.136 3.828 55.471 1.00 33.01 B000 O
ATOM 3953 CB LEU B 104 4.150 2.563 58.173 1.00 30.79 B000 C
ATOM 3954 CG LEU B 104 5.349 2.499 59.134 1.00 33.92 B000 C
ATOM 3955 CD1 LEU B 104 5.536 1.088 59.627 1.00 40.98 B000 C
ATOM 3956 CD2 LEU B 104 6.628 3.002 58.460 1.00 31.75 B000 C
TER
HETATM 3957 O HOH B 105 -18.076 13.614 16.619 1.00 39.02 B000 O
ATOM 3958 N ILE B 105 1.368 3.780 56.878 1.00 26.94 B000 N
ATOM 3959 CA ILE B 105 0.409 3.674 55.783 1.00 30.08 B000 C
ATOM 3960 C ILE B 105 0.305 4.965 54.964 1.00 28.37 B000 C
ATOM 3961 O ILE B 105 -0.061 4.910 53.783 1.00 30.78 B000 O
ATOM 3962 CB ILE B 105 -0.964 3.213 56.328 1.00 32.09 B000 C
ATOM 3963 CG1 ILE B 105 -0.906 1.726 56.699 1.00 34.51 B000 C
ATOM 3964 CG2 ILE B 105 -2.060 3.409 55.309 1.00 28.36 B000 C
ATOM 3965 CD1 ILE B 105 -2.215 1.159 57.236 1.00 30.85 B000 C
ATOM 3966 N ARG B 106 0.648 6.124 55.532 1.00 23.73 B000 N
ATOM 3967 CA ARG B 106 0.523 7.370 54.772 1.00 27.65 B000 C
ATOM 3968 C ARG B 106 1.321 7.374 53.468 1.00 30.24 B000 C
ATOM 3969 O ARG B 106 0.724 7.663 52.415 1.00 30.75 B000 O
ATOM 3970 CB ARG B 106 0.876 8.572 55.653 1.00 30.20 B000 C
ATOM 3971 CG ARG B 106 0.556 9.910 54.965 1.00 39.23 B000 C
ATOM 3972 CD ARG B 106 0.891 11.130 55.804 1.00 33.47 B000 C
ATOM 3973 NE ARG B 106 2.320 11.355 55.990 1.00 39.42 B000 N
ATOM 3974 CZ ARG B 106 3.045 12.181 55.248 1.00 40.24 B000 C
ATOM 3975 NH1 ARG B 106 2.547 12.758 54.165 1.00 35.96 B000 N1+
ATOM 3976 NH2 ARG B 106 4.296 12.437 55.604 1.00 37.03 B000 N
TER
HETATM 3977 O HOH B 106 15.335 -4.717 20.593 1.00 39.48 B000 O
ATOM 3978 N PRO B 107 2.633 7.075 53.439 1.00 29.34 B000 N
ATOM 3979 CA PRO B 107 3.328 7.054 52.134 1.00 30.18 B000 C
ATOM 3980 C PRO B 107 2.877 5.911 51.243 1.00 31.14 B000 C
ATOM 3981 O PRO B 107 2.947 6.022 50.015 1.00 28.37 B000 O
ATOM 3982 CB PRO B 107 4.804 6.909 52.521 1.00 29.19 B000 C
ATOM 3983 CG PRO B 107 4.752 6.172 53.821 1.00 28.79 B000 C
ATOM 3984 CD PRO B 107 3.548 6.728 54.541 1.00 29.33 B000 C
TER
HETATM 3985 O HOH B 108 -15.295 18.794 13.685 1.00 38.87 B000 O
ATOM 3986 N ILE B 108 2.411 4.809 51.828 1.00 30.81 B000 N
ATOM 3987 CA ILE B 108 1.872 3.721 51.024 1.00 31.33 B000 C
ATOM 3988 C ILE B 108 0.630 4.189 50.265 1.00 30.28 B000 C
ATOM 3989 O ILE B 108 0.446 3.863 49.082 1.00 29.37 B000 O
ATOM 3990 CB ILE B 108 1.578 2.501 51.914 1.00 35.84 B000 C
ATOM 3991 CG1 ILE B 108 2.865 1.977 52.561 1.00 29.09 B000 C
ATOM 3992 CG2 ILE B 108 0.933 1.424 51.095 1.00 38.25 B000 C
ATOM 3993 CD1 ILE B 108 2.599 0.970 53.690 1.00 32.08 B000 C
TER
HETATM 3994 O HOH B 109 -32.661 -5.423 1.890 1.00 40.78 B000 O
ATOM 3995 N LYS B 109 -0.221 4.993 50.915 1.00 31.84 B000 N
ATOM 3996 CA LYS B 109 -1.403 5.522 50.233 1.00 33.60 B000 C
ATOM 3997 C LYS B 109 -1.016 6.376 49.028 1.00 35.79 B000 C
ATOM 3998 O LYS B 109 -1.617 6.264 47.952 1.00 36.27 B000 O
ATOM 3999 CB LYS B 109 -2.263 6.325 51.212 1.00 30.31 B000 C
ATOM 4000 CG LYS B 109 -3.089 5.468 52.150 1.00 30.20 B000 C
ATOM 4001 CD LYS B 109 -3.597 6.259 53.362 1.00 29.29 B000 C
ATOM 4002 CE LYS B 109 -4.417 7.481 52.968 1.00 34.15 B000 C
ATOM 4003 NZ LYS B 109 -4.867 8.141 54.223 1.00 28.20 B000 N1+
TER
HETATM 4004 O HOH B 110 -20.557 -13.488 -10.924 1.00 39.83 B000 O
ATOM 4005 N VAL B 110 -0.024 7.251 49.190 1.00 35.81 B000 N
ATOM 4006 CA VAL B 110 0.394 8.098 48.073 1.00 31.42 B000 C
ATOM 4007 C VAL B 110 0.867 7.237 46.911 1.00 35.21 B000 C
ATOM 4008 O VAL B 110 0.533 7.502 45.752 1.00 35.64 B000 O
ATOM 4009 CB VAL B 110 1.499 9.077 48.513 1.00 32.13 B000 C
ATOM 4010 CG1 VAL B 110 2.091 9.768 47.283 1.00 34.36 B000 C
ATOM 4011 CG2 VAL B 110 0.972 10.083 49.521 1.00 32.84 B000 C
ATOM 4012 N LEU B 111 1.638 6.182 47.210 1.00 31.70 B000 N
ATOM 4013 CA LEU B 111 2.147 5.264 46.188 1.00 34.87 B000 C
ATOM 4014 C LEU B 111 1.026 4.462 45.532 1.00 32.24 B000 C
ATOM 4015 O LEU B 111 1.002 4.295 44.305 1.00 35.07 B000 O
ATOM 4016 CB LEU B 111 3.169 4.327 46.833 1.00 36.65 B000 C
ATOM 4017 CG LEU B 111 3.984 3.322 46.045 1.00 40.55 B000 C
ATOM 4018 CD1 LEU B 111 5.008 4.041 45.182 1.00 43.42 B000 C
ATOM 4019 CD2 LEU B 111 4.674 2.384 47.028 1.00 37.50 B000 C
TER
HETATM 4020 O HOH B 112 -6.102 10.337 53.523 1.00 44.54 B000 O
ATOM 4021 N LEU B 112 0.118 3.907 46.341 1.00 34.55 B000 N
ATOM 4022 CA LEU B 112 -1.079 3.274 45.799 1.00 34.28 B000 C
ATOM 4023 C LEU B 112 -1.799 4.203 44.833 1.00 31.60 B000 C
ATOM 4024 O LEU B 112 -2.178 3.805 43.729 1.00 34.20 B000 O
ATOM 4025 CB LEU B 112 -2.026 2.874 46.934 1.00 35.97 B000 C
ATOM 4026 CG LEU B 112 -1.849 1.522 47.601 1.00 37.24 B000 C
ATOM 4027 CD1 LEU B 112 -2.959 1.354 48.649 1.00 38.51 B000 C
ATOM 4028 CD2 LEU B 112 -1.866 0.391 46.554 1.00 36.02 B000 C
ATOM 4029 N GLN B 113 -2.020 5.450 45.243 1.00 40.31 B000 N
ATOM 4030 CA GLN B 113 -2.743 6.369 44.373 1.00 37.67 B000 C
ATOM 4031 C GLN B 113 -1.976 6.591 43.074 1.00 39.62 B000 C
ATOM 4032 O GLN B 113 -2.545 6.517 41.981 1.00 38.78 B000 O
ATOM 4033 CB GLN B 113 -2.989 7.692 45.087 1.00 39.04 B000 C
ATOM 4034 CG GLN B 113 -3.723 8.681 44.209 1.00 48.18 B000 C
ATOM 4035 CD GLN B 113 -4.980 9.199 44.849 1.00 51.69 B000 C
ATOM 4036 NE2 GLN B 113 -6.113 8.965 44.200 1.00 54.70 B000 N
ATOM 4037 OE1 GLN B 113 -4.940 9.798 45.923 1.00 59.49 B000 O
TER
HETATM 4038 O HOH B 113 -24.830 11.767 14.785 1.00 33.91 B000 O
HETATM 4039 O HOH B 114 -26.841 -11.234 -4.104 1.00 33.98 B000 O
ATOM 4040 N THR B 114 -0.668 6.822 43.181 1.00 35.87 B000 N
ATOM 4041 CA THR B 114 0.140 7.120 42.004 1.00 36.75 B000 C
ATOM 4042 C THR B 114 0.195 5.932 41.050 1.00 37.36 B000 C
ATOM 4043 O THR B 114 0.081 6.105 39.833 1.00 34.83 B000 O
ATOM 4044 CB THR B 114 1.537 7.538 42.448 1.00 37.48 B000 C
ATOM 4045 CG2 THR B 114 2.486 7.609 41.268 1.00 33.52 B000 C
ATOM 4046 OG1 THR B 114 1.456 8.828 43.058 1.00 39.84 B000 O
ATOM 4047 N LEU B 115 0.356 4.715 41.586 1.00 32.57 B000 N
ATOM 4048 CA LEU B 115 0.404 3.525 40.740 1.00 34.68 B000 C
ATOM 4049 C LEU B 115 -0.912 3.312 40.011 1.00 41.44 B000 C
ATOM 4050 O LEU B 115 -0.931 2.838 38.868 1.00 37.77 B000 O
ATOM 4051 CB LEU B 115 0.716 2.294 41.588 1.00 32.35 B000 C
ATOM 4052 CG LEU B 115 2.139 1.795 41.743 1.00 42.95 B000 C
ATOM 4053 CD1 LEU B 115 2.162 0.756 42.863 1.00 40.45 B000 C
ATOM 4054 CD2 LEU B 115 2.603 1.179 40.435 1.00 45.03 B000 C
TER
HETATM 4055 O HOH B 116 -17.947 -19.685 57.204 1.00 49.12 B000 O
ATOM 4056 N THR B 116 -2.027 3.618 40.682 1.00 36.66 B000 N
ATOM 4057 CA THR B 116 -3.349 3.447 40.096 1.00 30.08 B000 C
ATOM 4058 C THR B 116 -3.596 4.465 38.990 1.00 39.49 B000 C
ATOM 4059 O THR B 116 -4.093 4.116 37.914 1.00 41.83 B000 O
ATOM 4060 CB THR B 116 -4.417 3.577 41.195 1.00 41.62 B000 C
ATOM 4061 CG2 THR B 116 -5.810 3.499 40.613 1.00 32.80 B000 C
ATOM 4062 OG1 THR B 116 -4.260 2.522 42.153 1.00 41.91 B000 O
ATOM 4063 N GLU B 117 -3.285 5.742 39.248 1.00 38.77 B000 N
ATOM 4064 CA GLU B 117 -3.430 6.761 38.209 1.00 41.38 B000 C
ATOM 4065 C GLU B 117 -2.545 6.442 37.009 1.00 42.05 B000 C
ATOM 4066 O GLU B 117 -2.976 6.557 35.857 1.00 37.57 B000 O
ATOM 4067 CB GLU B 117 -3.077 8.143 38.766 1.00 40.42 B000 C
ATOM 4068 CG GLU B 117 -4.032 8.662 39.826 1.00 45.93 B000 C
ATOM 4069 CD GLU B 117 -3.447 9.823 40.625 1.00 52.91 B000 C
ATOM 4070 OE1 GLU B 117 -2.257 10.166 40.412 1.00 59.59 B000 O
ATOM 4071 OE2 GLU B 117 -4.174 10.371 41.481 1.00 54.95 B000 O1-
TER
HETATM 4072 O HOH B 117 -16.288 -11.574 19.802 1.00 48.57 B000 O
HETATM 4073 O HOH B 118 -20.490 -18.692 -4.118 1.00 50.69 B000 O
ATOM 4074 N SER B 118 -1.303 6.032 37.263 1.00 37.42 B000 N
ATOM 4075 CA SER B 118 -0.420 5.639 36.172 1.00 39.96 B000 C
ATOM 4076 C SER B 118 -1.028 4.485 35.388 1.00 44.43 B000 C
ATOM 4077 O SER B 118 -1.121 4.525 34.156 1.00 47.12 B000 O
ATOM 4078 CB SER B 118 0.954 5.258 36.733 1.00 37.91 B000 C
ATOM 4079 OG SER B 118 1.827 4.836 35.697 1.00 48.18 B000 O
ATOM 4080 N HIS B 119 -1.483 3.463 36.102 1.00 44.23 B000 N
ATOM 4081 CA HIS B 119 -2.112 2.313 35.468 1.00 42.90 B000 C
ATOM 4082 C HIS B 119 -3.296 2.718 34.599 1.00 43.37 B000 C
ATOM 4083 O HIS B 119 -3.551 2.101 33.558 1.00 45.21 B000 O
ATOM 4084 CB HIS B 119 -2.568 1.337 36.543 1.00 41.70 B000 C
ATOM 4085 CG HIS B 119 -2.645 -0.065 36.063 1.00 40.16 B000 C
ATOM 4086 CD2 HIS B 119 -1.811 -1.115 36.251 1.00 40.77 B000 C
ATOM 4087 ND1 HIS B 119 -3.646 -0.504 35.228 1.00 35.65 B000 N
ATOM 4088 CE1 HIS B 119 -3.442 -1.778 34.944 1.00 49.25 B000 C
ATOM 4089 NE2 HIS B 119 -2.334 -2.171 35.549 1.00 47.76 B000 N
TER
HETATM 4090 O HOH B 119 -11.194 -16.178 -3.575 1.00 36.04 B000 O
ATOM 4091 N ARG B 120 -4.044 3.741 35.018 1.00 45.56 B000 N
ATOM 4092 CA ARG B 120 -5.191 4.195 34.231 1.00 38.21 B000 C
ATOM 4093 C ARG B 120 -4.749 4.909 32.958 1.00 47.51 B000 C
ATOM 4094 O ARG B 120 -5.408 4.802 31.915 1.00 48.48 B000 O
ATOM 4095 CB ARG B 120 -6.061 5.116 35.076 1.00 43.25 B000 C
ATOM 4096 CG ARG B 120 -6.777 4.434 36.231 1.00 45.89 B000 C
ATOM 4097 CD ARG B 120 -7.596 3.247 35.757 1.00 49.69 B000 C
ATOM 4098 NE ARG B 120 -8.772 3.107 36.602 1.00 58.67 B000 N
ATOM 4099 CZ ARG B 120 -9.733 2.210 36.437 1.00 55.26 B000 C
ATOM 4100 NH1 ARG B 120 -9.691 1.317 35.457 1.00 48.60 B000 N1+
ATOM 4101 NH2 ARG B 120 -10.775 2.227 37.263 1.00 44.19 B000 N
TER
HETATM 4102 O HOH B 120 -18.373 23.054 13.582 1.00 44.10 B000 O
HETATM 4103 O HOH B 121 -21.360 -13.488 58.372 1.00 29.25 B000 O
ATOM 4104 N ILE B 121 -3.650 5.659 33.025 1.00 47.68 B000 N
ATOM 4105 CA ILE B 121 -3.071 6.233 31.815 1.00 47.49 B000 C
ATOM 4106 C ILE B 121 -2.717 5.126 30.832 1.00 48.23 B000 C
ATOM 4107 O ILE B 121 -3.185 5.111 29.687 1.00 44.08 B000 O
ATOM 4108 CB ILE B 121 -1.846 7.097 32.166 1.00 50.47 B000 C
ATOM 4109 CG1 ILE B 121 -2.272 8.254 33.077 1.00 48.66 B000 C
ATOM 4110 CG2 ILE B 121 -1.154 7.593 30.909 1.00 51.86 B000 C
ATOM 4111 CD1 ILE B 121 -1.289 9.410 33.118 1.00 55.32 B000 C
ATOM 4112 N LEU B 122 -1.897 4.171 31.281 1.00 49.89 B000 N
ATOM 4113 CA LEU B 122 -1.454 3.072 30.425 1.00 51.74 B000 C
ATOM 4114 C LEU B 122 -2.613 2.306 29.816 1.00 54.29 B000 C
ATOM 4115 O LEU B 122 -2.483 1.747 28.718 1.00 53.40 B000 O
ATOM 4116 CB LEU B 122 -0.583 2.103 31.226 1.00 52.87 B000 C
ATOM 4117 CG LEU B 122 0.920 2.222 31.026 1.00 55.21 B000 C
ATOM 4118 CD1 LEU B 122 1.369 3.666 31.228 1.00 54.91 B000 C
ATOM 4119 CD2 LEU B 122 1.620 1.292 31.999 1.00 57.84 B000 C
ATOM 4120 N GLU B 123 -3.740 2.248 30.524 1.00 47.85 B000 N
ATOM 4121 CA GLU B 123 -4.895 1.499 30.054 1.00 48.37 B000 C
ATOM 4122 C GLU B 123 -5.491 2.118 28.792 1.00 54.33 B000 C
ATOM 4123 O GLU B 123 -6.025 1.396 27.939 1.00 53.35 B000 O
ATOM 4124 CB GLU B 123 -5.928 1.432 31.183 1.00 43.37 B000 C
ATOM 4125 CG GLU B 123 -7.083 0.497 30.963 1.00 56.93 B000 C
ATOM 4126 CD GLU B 123 -8.235 0.790 31.917 1.00 68.79 B000 C
ATOM 4127 OE1 GLU B 123 -7.972 1.350 33.010 1.00 60.54 B000 O
ATOM 4128 OE2 GLU B 123 -9.397 0.478 31.567 1.00 64.45 B000 O1-
TER
HETATM 4129 O HOH B 124 0.930 3.459 63.146 1.00 49.08 B000 O
ATOM 4130 N LYS B 124 -5.413 3.446 28.659 1.00 46.91 B000 N
ATOM 4131 CA LYS B 124 -5.884 4.117 27.453 1.00 49.72 B000 C
ATOM 4132 C LYS B 124 -4.985 3.855 26.255 1.00 47.56 B000 C
ATOM 4133 O LYS B 124 -5.435 4.001 25.116 1.00 49.25 B000 O
ATOM 4134 CB LYS B 124 -5.978 5.624 27.699 1.00 50.33 B000 C
ATOM 4135 CG LYS B 124 -7.036 6.029 28.710 1.00 46.43 B000 C
ATOM 4136 CD LYS B 124 -8.383 5.456 28.301 1.00 58.59 B000 C
ATOM 4137 CE LYS B 124 -9.473 5.874 29.262 1.00 59.19 B000 C
ATOM 4138 NZ LYS B 124 -9.474 7.349 29.374 1.00 59.85 B000 N1+
TER
HETATM 4139 O HOH B 125 -17.746 -19.333 54.815 1.00 47.96 B000 O
ATOM 4140 N TYR B 125 -3.725 3.488 26.485 1.00 46.10 B000 N
ATOM 4141 CA TYR B 125 -2.733 3.358 25.429 1.00 47.42 B000 C
ATOM 4142 C TYR B 125 -2.387 1.907 25.118 1.00 46.42 B000 C
ATOM 4143 O TYR B 125 -1.402 1.658 24.420 1.00 47.88 B000 O
ATOM 4144 CB TYR B 125 -1.472 4.140 25.803 1.00 43.95 B000 C
ATOM 4145 CG TYR B 125 -1.662 5.637 25.778 1.00 42.60 B000 C
ATOM 4146 CD1 TYR B 125 -2.173 6.313 26.874 1.00 43.87 B000 C
ATOM 4147 CD2 TYR B 125 -1.343 6.376 24.652 1.00 46.20 B000 C
ATOM 4148 CE1 TYR B 125 -2.365 7.678 26.850 1.00 42.66 B000 C
ATOM 4149 CE2 TYR B 125 -1.528 7.744 24.617 1.00 36.09 B000 C
ATOM 4150 CZ TYR B 125 -2.035 8.392 25.717 1.00 51.98 B000 C
ATOM 4151 OH TYR B 125 -2.215 9.760 25.680 1.00 56.24 B000 O
TER
HETATM 4152 O HOH B 126 -21.063 -19.045 -0.228 1.00 53.56 B000 O
ATOM 4153 N THR B 126 -3.166 0.946 25.625 1.00 50.47 B000 N
ATOM 4154 CA THR B 126 -3.042 -0.470 25.284 1.00 61.61 B000 C
ATOM 4155 C THR B 126 -4.365 -1.000 24.748 1.00 63.67 B000 C
ATOM 4156 O THR B 126 -5.438 -0.452 25.025 1.00 66.82 B000 O
ATOM 4157 CB THR B 126 -2.636 -1.347 26.488 1.00 60.43 B000 C
ATOM 4158 CG2 THR B 126 -1.383 -0.860 27.129 1.00 56.98 B000 C
ATOM 4159 OG1 THR B 126 -3.686 -1.353 27.461 1.00 52.39 B000 O
ATOM 4160 N GLN B 127 -4.282 -2.105 23.984 1.00 67.80 B000 N
ATOM 4161 CA GLN B 127 -5.504 -2.710 23.464 1.00 65.27 B000 C
ATOM 4162 C GLN B 127 -6.269 -3.402 24.592 1.00 66.74 B000 C
ATOM 4163 O GLN B 127 -5.661 -4.080 25.429 1.00 63.64 B000 O
ATOM 4164 CB GLN B 127 -5.191 -3.732 22.372 1.00 62.92 B000 C
ATOM 4165 CG GLN B 127 -4.986 -3.227 20.921 1.00 62.87 B000 C
ATOM 4166 CD GLN B 127 -5.710 -1.926 20.554 1.00 66.20 B000 C
ATOM 4167 NE2 GLN B 127 -7.024 -1.868 20.799 1.00 60.48 B000 N
ATOM 4168 OE1 GLN B 127 -5.090 -0.994 20.030 1.00 70.04 B000 O
TER
HETATM 4169 O HOH B 127 1.720 -5.031 16.697 1.00 47.48 B000 O
HETATM 4170 O HOH B 128 -20.470 15.147 16.776 1.00 38.69 B000 O
ATOM 4171 N PRO B 128 -7.603 -3.255 24.632 1.00 64.13 B000 N
ATOM 4172 CA PRO B 128 -8.402 -3.992 25.623 1.00 65.34 B000 C
ATOM 4173 C PRO B 128 -8.374 -5.503 25.446 1.00 61.43 B000 C
ATOM 4174 O PRO B 128 -8.945 -6.219 26.269 1.00 68.20 B000 O
ATOM 4175 CB PRO B 128 -9.817 -3.439 25.409 1.00 68.45 B000 C
ATOM 4176 CG PRO B 128 -9.599 -2.074 24.827 1.00 69.74 B000 C
ATOM 4177 CD PRO B 128 -8.381 -2.198 23.963 1.00 66.24 B000 C
TER
HETATM 4178 O HOH B 129 -12.070 0.564 57.522 1.00 39.47 B000 O
ATOM 4179 N SER B 129 -7.728 -6.014 24.393 1.00 65.88 B000 N
ATOM 4180 CA SER B 129 -7.594 -7.460 24.258 1.00 65.64 B000 C
ATOM 4181 C SER B 129 -6.506 -8.032 25.162 1.00 57.72 B000 C
ATOM 4182 O SER B 129 -6.567 -9.220 25.495 1.00 55.38 B000 O
ATOM 4183 CB SER B 129 -7.318 -7.843 22.799 1.00 59.93 B000 C
ATOM 4184 OG SER B 129 -6.032 -7.409 22.396 1.00 66.43 B000 O
TER
HETATM 4185 O HOH B 130 -0.417 10.760 45.114 1.00 48.48 B000 O
ATOM 4186 N ILE B 130 -5.523 -7.224 25.574 1.00 56.61 B000 N
ATOM 4187 CA ILE B 130 -4.549 -7.701 26.559 1.00 54.49 B000 C
ATOM 4188 C ILE B 130 -5.214 -7.863 27.926 1.00 59.15 B000 C
ATOM 4189 O ILE B 130 -4.930 -8.817 28.663 1.00 56.99 B000 O
ATOM 4190 CB ILE B 130 -3.317 -6.770 26.616 1.00 61.53 B000 C
ATOM 4191 CG1 ILE B 130 -2.265 -7.158 25.558 1.00 64.45 B000 C
ATOM 4192 CG2 ILE B 130 -2.648 -6.799 27.987 1.00 58.69 B000 C
ATOM 4193 CD1 ILE B 130 -2.733 -7.136 24.105 1.00 60.50 B000 C
TER
HETATM 4194 O HOH B 131 -23.665 0.755 51.121 1.00 38.63 B000 O
ATOM 4195 N PHE B 131 -6.129 -6.955 28.275 1.00 55.21 B000 N
ATOM 4196 CA PHE B 131 -6.870 -7.109 29.522 1.00 58.00 B000 C
ATOM 4197 C PHE B 131 -7.822 -8.291 29.465 1.00 58.36 B000 C
ATOM 4198 O PHE B 131 -8.050 -8.948 30.490 1.00 53.44 B000 O
ATOM 4199 CB PHE B 131 -7.638 -5.830 29.852 1.00 59.70 B000 C
ATOM 4200 CG PHE B 131 -6.760 -4.623 29.992 1.00 63.42 B000 C
ATOM 4201 CD1 PHE B 131 -5.770 -4.587 30.965 1.00 56.43 B000 C
ATOM 4202 CD2 PHE B 131 -6.916 -3.530 29.151 1.00 66.97 B000 C
ATOM 4203 CE1 PHE B 131 -4.953 -3.483 31.098 1.00 58.60 B000 C
ATOM 4204 CE2 PHE B 131 -6.100 -2.422 29.275 1.00 63.29 B000 C
ATOM 4205 CZ PHE B 131 -5.115 -2.398 30.254 1.00 58.73 B000 C
TER
HETATM 4206 O HOH B 132 -0.739 -11.072 2.838 1.00 51.63 B000 O
ATOM 4207 N LYS B 132 -8.390 -8.570 28.287 1.00 60.51 B000 N
ATOM 4208 CA LYS B 132 -9.227 -9.754 28.130 1.00 61.24 B000 C
ATOM 4209 C LYS B 132 -8.421 -11.019 28.375 1.00 57.47 B000 C
ATOM 4210 O LYS B 132 -8.878 -11.928 29.077 1.00 59.56 B000 O
ATOM 4211 CB LYS B 132 -9.862 -9.776 26.737 1.00 59.57 B000 C
TER
HETATM 4212 O HOH B 133 -7.710 2.174 59.643 1.00 39.92 B000 O
ATOM 4213 N ILE B 133 -7.210 -11.086 27.818 1.00 53.81 B000 N
ATOM 4214 CA ILE B 133 -6.310 -12.201 28.105 1.00 59.96 B000 C
ATOM 4215 C ILE B 133 -6.030 -12.284 29.602 1.00 54.74 B000 C
ATOM 4216 O ILE B 133 -5.982 -13.376 30.177 1.00 60.97 B000 O
ATOM 4217 CB ILE B 133 -5.005 -12.064 27.290 1.00 56.94 B000 C
ATOM 4218 CG1 ILE B 133 -5.267 -12.258 25.791 1.00 61.29 B000 C
ATOM 4219 CG2 ILE B 133 -3.957 -13.060 27.757 1.00 62.59 B000 C
ATOM 4220 CD1 ILE B 133 -4.259 -11.541 24.896 1.00 55.36 B000 C
ATOM 4221 N ILE B 134 -5.866 -11.133 30.255 1.00 54.48 B000 N
ATOM 4222 CA ILE B 134 -5.518 -11.109 31.675 1.00 59.79 B000 C
ATOM 4223 C ILE B 134 -6.690 -11.587 32.526 1.00 63.73 B000 C
ATOM 4224 O ILE B 134 -6.520 -12.404 33.440 1.00 63.26 B000 O
ATOM 4225 CB ILE B 134 -5.069 -9.697 32.085 1.00 54.41 B000 C
ATOM 4226 CG1 ILE B 134 -3.626 -9.457 31.643 1.00 51.33 B000 C
ATOM 4227 CG2 ILE B 134 -5.221 -9.510 33.589 1.00 52.50 B000 C
ATOM 4228 CD1 ILE B 134 -3.268 -7.993 31.506 1.00 46.83 B000 C
TER
HETATM 4229 O HOH B 135 -29.042 -6.662 53.863 1.00 37.63 B000 O
ATOM 4230 N SER B 135 -7.895 -11.077 32.243 1.00 61.45 B000 N
ATOM 4231 CA SER B 135 -9.095 -11.488 32.967 1.00 64.41 B000 C
ATOM 4232 C SER B 135 -9.365 -12.983 32.851 1.00 68.18 B000 C
ATOM 4233 O SER B 135 -10.048 -13.549 33.713 1.00 73.21 B000 O
ATOM 4234 CB SER B 135 -10.303 -10.714 32.447 1.00 64.99 B000 C
ATOM 4235 OG SER B 135 -10.052 -9.321 32.498 1.00 71.13 B000 O
ATOM 4236 N GLN B 136 -8.860 -13.627 31.800 1.00 68.07 B000 N
ATOM 4237 CA GLN B 136 -9.025 -15.060 31.594 1.00 64.33 B000 C
ATOM 4238 C GLN B 136 -8.014 -15.895 32.370 1.00 66.39 B000 C
ATOM 4239 O GLN B 136 -8.086 -17.128 32.326 1.00 69.21 B000 O
ATOM 4240 CB GLN B 136 -8.940 -15.375 30.096 1.00 68.87 B000 C
ATOM 4241 CG GLN B 136 -10.146 -14.868 29.307 1.00 70.31 B000 C
ATOM 4242 CD GLN B 136 -9.909 -14.838 27.811 1.00 72.65 B000 C
ATOM 4243 NE2 GLN B 136 -10.911 -14.380 27.059 1.00 69.03 B000 N
ATOM 4244 OE1 GLN B 136 -8.838 -15.223 27.334 1.00 74.68 B000 O
TER
HETATM 4245 O HOH B 136 -24.292 -18.496 48.546 1.00 41.99 B000 O
ATOM 4246 N GLY B 137 -7.087 -15.264 33.084 1.00 62.25 B000 N
ATOM 4247 CA GLY B 137 -6.155 -15.994 33.913 1.00 64.34 B000 C
ATOM 4248 C GLY B 137 -4.860 -16.378 33.247 1.00 65.20 B000 C
ATOM 4249 O GLY B 137 -4.213 -17.330 33.696 1.00 66.19 B000 O
TER
HETATM 4250 O HOH B 138 -18.157 5.526 33.541 1.00 61.05 B000 O
ATOM 4251 N THR B 138 -4.454 -15.672 32.191 1.00 66.20 B000 N
ATOM 4252 CA THR B 138 -3.250 -16.015 31.445 1.00 73.70 B000 C
ATOM 4253 C THR B 138 -2.414 -14.762 31.211 1.00 70.68 B000 C
ATOM 4254 O THR B 138 -2.947 -13.715 30.826 1.00 65.94 B000 O
ATOM 4255 CB THR B 138 -3.594 -16.695 30.105 1.00 68.80 B000 C
ATOM 4256 CG2 THR B 138 -4.185 -18.088 30.339 1.00 62.82 B000 C
ATOM 4257 OG1 THR B 138 -4.538 -15.899 29.381 1.00 70.86 B000 O
ATOM 4258 N ASN B 139 -1.115 -14.870 31.460 1.00 67.07 B000 N
ATOM 4259 CA ASN B 139 -0.202 -13.771 31.190 1.00 66.51 B000 C
ATOM 4260 C ASN B 139 -0.057 -13.621 29.682 1.00 63.36 B000 C
ATOM 4261 O ASN B 139 0.374 -14.575 29.018 1.00 62.40 B000 O
ATOM 4262 CB ASN B 139 1.153 -14.036 31.847 1.00 62.66 B000 C
ATOM 4263 CG ASN B 139 2.083 -12.822 31.811 1.00 61.67 B000 C
ATOM 4264 ND2 ASN B 139 2.900 -12.691 32.849 1.00 57.72 B000 N
ATOM 4265 OD1 ASN B 139 2.085 -12.029 30.863 1.00 61.62 B000 O
TER
HETATM 4266 O HOH B 139 -23.132 -20.250 47.041 1.00 53.49 B000 O
HETATM 4267 O HOH B 140 -0.658 21.177 10.005 1.00 41.50 B000 O
ATOM 4268 N PRO B 140 -0.421 -12.469 29.098 1.00 67.76 B000 N
ATOM 4269 CA PRO B 140 -0.238 -12.279 27.645 1.00 62.69 B000 C
ATOM 4270 C PRO B 140 1.189 -12.525 27.158 1.00 65.06 B000 C
ATOM 4271 O PRO B 140 1.375 -12.928 26.000 1.00 56.40 B000 O
ATOM 4272 CB PRO B 140 -0.664 -10.824 27.407 1.00 64.10 B000 C
ATOM 4273 CG PRO B 140 -1.277 -10.331 28.679 1.00 63.33 B000 C
ATOM 4274 CD PRO B 140 -1.141 -11.367 29.751 1.00 66.74 B000 C
TER
HETATM 4275 O HOH B 141 -7.539 -13.859 56.627 1.00 36.15 B000 O
ATOM 4276 N LEU B 141 2.207 -12.301 27.999 1.00 64.58 B000 N
ATOM 4277 CA LEU B 141 3.578 -12.629 27.627 1.00 58.65 B000 C
ATOM 4278 C LEU B 141 3.819 -14.131 27.510 1.00 61.33 B000 C
ATOM 4279 O LEU B 141 4.867 -14.532 26.991 1.00 60.53 B000 O
ATOM 4280 CB LEU B 141 4.553 -12.034 28.645 1.00 65.50 B000 C
ATOM 4281 CG LEU B 141 4.576 -10.509 28.793 1.00 65.90 B000 C
ATOM 4282 CD1 LEU B 141 5.356 -10.115 30.042 1.00 59.68 B000 C
ATOM 4283 CD2 LEU B 141 5.179 -9.850 27.551 1.00 56.38 B000 C
ATOM 4284 N ASN B 142 2.880 -14.965 27.967 1.00 64.65 B000 N
ATOM 4285 CA ASN B 142 3.042 -16.412 27.955 1.00 66.60 B000 C
ATOM 4286 C ASN B 142 2.245 -17.109 26.860 1.00 65.29 B000 C
ATOM 4287 O ASN B 142 2.306 -18.338 26.759 1.00 65.55 B000 O
ATOM 4288 CB ASN B 142 2.652 -17.001 29.316 1.00 69.72 B000 C
ATOM 4289 CG ASN B 142 3.636 -16.632 30.415 1.00 70.62 B000 C
ATOM 4290 ND2 ASN B 142 4.899 -16.447 30.039 1.00 67.58 B000 N
ATOM 4291 OD1 ASN B 142 3.260 -16.496 31.585 1.00 64.80 B000 O
TER
HETATM 4292 O HOH B 142 -15.124 16.669 15.667 1.00 36.43 B000 O
HETATM 4293 O HOH B 143 3.957 2.468 65.589 1.00 44.77 B000 O
ATOM 4294 N ILE B 143 1.494 -16.365 26.045 1.00 61.97 B000 N
ATOM 4295 CA ILE B 143 0.762 -16.973 24.939 1.00 62.84 B000 C
ATOM 4296 C ILE B 143 1.739 -17.630 23.973 1.00 56.99 B000 C
ATOM 4297 O ILE B 143 2.714 -17.009 23.534 1.00 56.16 B000 O
ATOM 4298 CB ILE B 143 -0.100 -15.914 24.234 1.00 61.12 B000 C
ATOM 4299 CG1 ILE B 143 -1.056 -15.261 25.234 1.00 67.65 B000 C
ATOM 4300 CG2 ILE B 143 -0.850 -16.518 23.048 1.00 61.22 B000 C
ATOM 4301 CD1 ILE B 143 -2.338 -16.043 25.471 1.00 64.22 B000 C
ATOM 4302 N ARG B 144 1.481 -18.952 23.639 1.00 59.10 B000 N
ATOM 4303 CA ARG B 144 2.265 -19.709 22.672 1.00 54.81 B000 C
ATOM 4304 C ARG B 144 1.715 -19.497 21.262 1.00 55.40 B000 C
ATOM 4305 O ARG B 144 0.513 -19.270 21.083 1.00 53.82 B000 O
ATOM 4306 CB ARG B 144 2.247 -21.196 23.013 1.00 55.47 B000 C
TER
HETATM 4307 O HOH B 144 -25.524 24.694 12.268 1.00 43.49 B000 O
HETATM 4308 O HOH B 145 -9.343 3.289 58.298 1.00 43.10 B000 O
ATOM 4309 N PRO B 145 2.577 -19.578 20.248 1.00 50.75 B000 N
ATOM 4310 CA PRO B 145 2.173 -19.168 18.894 1.00 46.95 B000 C
ATOM 4311 C PRO B 145 1.061 -20.025 18.298 1.00 42.16 B000 C
ATOM 4312 O PRO B 145 1.059 -21.250 18.422 1.00 45.27 B000 O
ATOM 4313 CB PRO B 145 3.472 -19.291 18.082 1.00 40.46 B000 C
ATOM 4314 CG PRO B 145 4.443 -20.036 18.960 1.00 45.36 B000 C
ATOM 4315 CD PRO B 145 4.032 -19.770 20.363 1.00 45.98 B000 C
ATOM 4316 N LYS B 146 0.125 -19.356 17.618 1.00 36.30 B000 N
ATOM 4317 CA LYS B 146 -1.036 -19.976 16.984 1.00 35.55 B000 C
ATOM 4318 C LYS B 146 -1.375 -19.248 15.686 1.00 32.47 B000 C
ATOM 4319 O LYS B 146 -1.393 -18.016 15.652 1.00 37.06 B000 O
ATOM 4320 CB LYS B 146 -2.250 -19.931 17.937 1.00 39.74 B000 C
ATOM 4321 CG LYS B 146 -3.189 -21.137 17.906 1.00 48.38 B000 C
ATOM 4322 CD LYS B 146 -4.207 -21.068 19.069 1.00 47.51 B000 C
ATOM 4323 CE LYS B 146 -5.285 -19.987 18.880 1.00 61.08 B000 C
ATOM 4324 NZ LYS B 146 -6.366 -20.044 19.934 1.00 57.54 B000 N1+
ATOM 4325 N ALA B 147 -1.645 -20.003 14.623 1.00 29.66 B000 N
ATOM 4326 CA ALA B 147 -2.189 -19.431 13.397 1.00 33.98 B000 C
ATOM 4327 C ALA B 147 -3.709 -19.499 13.470 1.00 37.20 B000 C
ATOM 4328 O ALA B 147 -4.269 -20.558 13.771 1.00 32.76 B000 O
ATOM 4329 CB ALA B 147 -1.696 -20.174 12.158 1.00 34.16 B000 C
TER
HETATM 4330 O HOH B 148 -26.504 -6.260 14.555 1.00 41.21 B000 O
ATOM 4331 N VAL B 148 -4.370 -18.366 13.232 1.00 35.42 B000 N
ATOM 4332 CA AVAL B 148 -5.823 -18.288 13.292 0.52 34.22 B000 C
ATOM 4333 CA BVAL B 148 -5.825 -18.260 13.313 0.48 34.24 B000 C
ATOM 4334 C VAL B 148 -6.310 -17.468 12.108 1.00 37.42 B000 C
ATOM 4335 O VAL B 148 -5.762 -16.404 11.804 1.00 35.66 B000 O
ATOM 4336 CB AVAL B 148 -6.306 -17.673 14.620 0.52 38.13 B000 C
ATOM 4337 CB BVAL B 148 -6.301 -17.570 14.611 0.48 38.09 B000 C
ATOM 4338 CG1AVAL B 148 -5.572 -16.387 14.899 0.52 34.89 B000 C
ATOM 4339 CG1BVAL B 148 -7.776 -17.879 14.867 0.48 34.65 B000 C
ATOM 4340 CG2AVAL B 148 -7.814 -17.450 14.596 0.52 34.81 B000 C
ATOM 4341 CG2BVAL B 148 -5.453 -17.973 15.822 0.48 35.21 B000 C
ATOM 4342 N GLU B 149 -7.332 -17.965 11.432 1.00 40.42 B000 N
ATOM 4343 CA GLU B 149 -7.915 -17.204 10.338 1.00 37.44 B000 C
ATOM 4344 C GLU B 149 -8.881 -16.174 10.915 1.00 34.22 B000 C
ATOM 4345 O GLU B 149 -9.708 -16.502 11.771 1.00 38.55 B000 O
ATOM 4346 CB GLU B 149 -8.642 -18.125 9.368 1.00 44.91 B000 C
ATOM 4347 CG GLU B 149 -8.406 -17.770 7.915 1.00 48.85 B000 C
ATOM 4348 CD GLU B 149 -9.136 -18.707 6.979 1.00 61.17 B000 C
ATOM 4349 OE1 GLU B 149 -8.698 -18.834 5.810 1.00 72.61 B000 O
ATOM 4350 OE2 GLU B 149 -10.159 -19.293 7.408 1.00 60.03 B000 O1-
ATOM 4351 N LYS B 150 -8.747 -14.925 10.482 1.00 30.65 B000 N
ATOM 4352 CA LYS B 150 -9.617 -13.852 10.913 1.00 29.25 B000 C
ATOM 4353 C LYS B 150 -10.193 -13.143 9.703 1.00 33.22 B000 C
ATOM 4354 O LYS B 150 -9.620 -13.160 8.610 1.00 29.99 B000 O
ATOM 4355 CB LYS B 150 -8.887 -12.806 11.765 1.00 30.84 B000 C
ATOM 4356 CG LYS B 150 -8.132 -13.336 12.979 1.00 29.09 B000 C
ATOM 4357 CD LYS B 150 -9.067 -13.628 14.110 1.00 30.26 B000 C
ATOM 4358 CE LYS B 150 -8.296 -13.638 15.439 1.00 43.22 B000 C
ATOM 4359 NZ LYS B 150 -9.090 -14.281 16.516 1.00 39.70 B000 N1+
TER
HETATM 4360 O HOH B 151 0.107 -20.366 25.512 1.00 56.68 B000 O
ATOM 4361 N ILE B 151 -11.322 -12.484 9.924 1.00 25.08 B000 N
ATOM 4362 CA ILE B 151 -11.777 -11.459 8.999 1.00 32.56 B000 C
ATOM 4363 C ILE B 151 -11.046 -10.185 9.366 1.00 29.38 B000 C
ATOM 4364 O ILE B 151 -11.120 -9.737 10.513 1.00 30.85 B000 O
ATOM 4365 CB ILE B 151 -13.299 -11.258 9.096 1.00 32.63 B000 C
ATOM 4366 CG1 ILE B 151 -14.036 -12.589 8.896 1.00 32.36 B000 C
ATOM 4367 CG2 ILE B 151 -13.754 -10.220 8.069 1.00 25.67 B000 C
ATOM 4368 CD1 ILE B 151 -13.949 -13.116 7.502 1.00 35.00 B000 C
TER
HETATM 4369 O HOH B 152 3.381 9.348 58.100 1.00 34.44 B000 O
ATOM 4370 N VAL B 152 -10.352 -9.585 8.409 1.00 23.00 B000 N
ATOM 4371 CA VAL B 152 -9.618 -8.355 8.664 1.00 24.12 B000 C
ATOM 4372 C VAL B 152 -10.373 -7.181 8.057 1.00 22.67 B000 C
ATOM 4373 O VAL B 152 -10.766 -7.219 6.888 1.00 24.56 B000 O
ATOM 4374 CB VAL B 152 -8.178 -8.417 8.132 1.00 29.96 B000 C
ATOM 4375 CG1 VAL B 152 -7.422 -7.236 8.662 1.00 30.32 B000 C
ATOM 4376 CG2 VAL B 152 -7.511 -9.713 8.584 1.00 33.32 B000 C
ATOM 4377 N PHE B 153 -10.526 -6.134 8.855 1.00 23.05 B000 N
ATOM 4378 CA PHE B 153 -11.247 -4.912 8.544 1.00 27.30 B000 C
ATOM 4379 C PHE B 153 -10.220 -3.795 8.399 1.00 23.76 B000 C
ATOM 4380 O PHE B 153 -9.374 -3.616 9.282 1.00 25.67 B000 O
ATOM 4381 CB PHE B 153 -12.241 -4.635 9.689 1.00 24.88 B000 C
ATOM 4382 CG PHE B 153 -12.919 -3.289 9.639 1.00 22.76 B000 C
ATOM 4383 CD1 PHE B 153 -12.230 -2.129 9.969 1.00 19.75 B000 C
ATOM 4384 CD2 PHE B 153 -14.281 -3.197 9.331 1.00 22.81 B000 C
ATOM 4385 CE1 PHE B 153 -12.841 -0.898 9.938 1.00 25.03 B000 C
ATOM 4386 CE2 PHE B 153 -14.919 -1.971 9.318 1.00 21.68 B000 C
ATOM 4387 CZ PHE B 153 -14.209 -0.814 9.626 1.00 26.03 B000 C
TER
HETATM 4388 O HOH B 154 -1.825 10.977 46.929 1.00 52.00 B000 O
ATOM 4389 N PHE B 154 -10.278 -3.066 7.283 1.00 18.92 B000 N
ATOM 4390 CA PHE B 154 -9.500 -1.846 7.072 1.00 21.61 B000 C
ATOM 4391 C PHE B 154 -10.447 -0.758 6.600 1.00 24.86 B000 C
ATOM 4392 O PHE B 154 -11.093 -0.906 5.561 1.00 23.91 B000 O
ATOM 4393 CB PHE B 154 -8.407 -2.028 6.009 1.00 23.19 B000 C
ATOM 4394 CG PHE B 154 -7.310 -2.927 6.415 1.00 28.76 B000 C
ATOM 4395 CD1 PHE B 154 -6.315 -2.487 7.270 1.00 28.14 B000 C
ATOM 4396 CD2 PHE B 154 -7.255 -4.222 5.936 1.00 28.57 B000 C
ATOM 4397 CE1 PHE B 154 -5.280 -3.333 7.633 1.00 34.84 B000 C
ATOM 4398 CE2 PHE B 154 -6.208 -5.062 6.287 1.00 30.68 B000 C
ATOM 4399 CZ PHE B 154 -5.240 -4.622 7.136 1.00 26.89 B000 C
ATOM 4400 N SER B 155 -10.506 0.341 7.326 1.00 24.43 B000 N
ATOM 4401 CA SER B 155 -11.211 1.517 6.846 1.00 26.51 B000 C
ATOM 4402 C SER B 155 -10.250 2.696 6.836 1.00 28.82 B000 C
ATOM 4403 O SER B 155 -9.285 2.726 7.597 1.00 30.48 B000 O
ATOM 4404 CB SER B 155 -12.423 1.838 7.720 1.00 27.53 B000 C
ATOM 4405 OG SER B 155 -12.004 2.258 9.015 1.00 30.71 B000 O
ATOM 4406 N ASP B 156 -10.516 3.689 5.985 1.00 25.55 B000 N
ATOM 4407 CA ASP B 156 -9.711 4.898 6.038 1.00 24.29 B000 C
ATOM 4408 C ASP B 156 -10.584 6.096 5.669 1.00 31.27 B000 C
ATOM 4409 O ASP B 156 -11.776 5.963 5.365 1.00 27.31 B000 O
ATOM 4410 CB ASP B 156 -8.456 4.740 5.164 1.00 27.32 B000 C
ATOM 4411 CG ASP B 156 -8.697 5.034 3.697 1.00 31.51 B000 C
ATOM 4412 OD1 ASP B 156 -9.712 4.598 3.116 1.00 38.52 B000 O
ATOM 4413 OD2 ASP B 156 -7.834 5.712 3.113 1.00 41.46 B000 O1-
TER
HETATM 4414 O HOH B 157 0.239 12.233 52.670 1.00 44.06 B000 O
ATOM 4415 N ILE B 157 -9.996 7.284 5.749 1.00 26.58 B000 N
ATOM 4416 CA ILE B 157 -10.727 8.530 5.574 1.00 25.32 B000 C
ATOM 4417 C ILE B 157 -10.496 9.000 4.150 1.00 26.39 B000 C
ATOM 4418 O ILE B 157 -9.351 9.117 3.723 1.00 27.50 B000 O
ATOM 4419 CB ILE B 157 -10.265 9.598 6.580 1.00 28.83 B000 C
ATOM 4420 CG1 ILE B 157 -10.646 9.195 8.014 1.00 25.00 B000 C
ATOM 4421 CG2 ILE B 157 -10.921 10.946 6.220 1.00 23.39 B000 C
ATOM 4422 CD1 ILE B 157 -10.293 10.248 9.070 1.00 25.90 B000 C
ATOM 4423 N VAL B 158 -11.577 9.264 3.410 1.00 27.42 B000 N
ATOM 4424 CA VAL B 158 -11.425 9.692 2.021 1.00 28.66 B000 C
ATOM 4425 C VAL B 158 -10.753 11.049 1.995 1.00 28.52 B000 C
ATOM 4426 O VAL B 158 -11.145 11.964 2.726 1.00 26.32 B000 O
ATOM 4427 CB VAL B 158 -12.776 9.735 1.308 1.00 28.92 B000 C
ATOM 4428 CG1 VAL B 158 -12.588 10.309 -0.133 1.00 29.22 B000 C
ATOM 4429 CG2 VAL B 158 -13.400 8.341 1.304 1.00 23.24 B000 C
TER
HETATM 4430 O HOH B 159 -9.015 -16.816 -7.823 1.00 43.69 B000 O
ATOM 4431 N SER B 159 -9.675 11.157 1.215 1.00 27.74 B000 N
ATOM 4432 CA SER B 159 -9.028 12.438 0.978 1.00 30.69 B000 C
ATOM 4433 C SER B 159 -8.558 13.063 2.286 1.00 27.83 B000 C
ATOM 4434 O SER B 159 -8.665 14.268 2.497 1.00 30.08 B000 O
ATOM 4435 CB SER B 159 -9.976 13.369 0.221 1.00 33.67 B000 C
ATOM 4436 OG SER B 159 -9.249 14.301 -0.542 1.00 48.29 B000 O
TER
HETATM 4437 O HOH B 160 -7.719 10.066 50.715 1.00 44.46 B000 O
ATOM 4438 N PHE B 160 -8.013 12.230 3.172 1.00 23.10 B000 N
ATOM 4439 CA PHE B 160 -7.592 12.727 4.471 1.00 29.24 B000 C
ATOM 4440 C PHE B 160 -6.563 13.845 4.368 1.00 28.95 B000 C
ATOM 4441 O PHE B 160 -6.554 14.752 5.206 1.00 30.85 B000 O
ATOM 4442 CB PHE B 160 -7.008 11.601 5.295 1.00 30.27 B000 C
ATOM 4443 CG PHE B 160 -6.405 12.072 6.547 1.00 35.93 B000 C
ATOM 4444 CD1 PHE B 160 -7.214 12.425 7.608 1.00 34.59 B000 C
ATOM 4445 CD2 PHE B 160 -5.031 12.203 6.669 1.00 37.06 B000 C
ATOM 4446 CE1 PHE B 160 -6.654 12.884 8.776 1.00 39.26 B000 C
ATOM 4447 CE2 PHE B 160 -4.478 12.673 7.838 1.00 40.63 B000 C
ATOM 4448 CZ PHE B 160 -5.292 12.999 8.889 1.00 30.95 B000 C
TER
HETATM 4449 O HOH B 161 -14.783 -3.608 29.403 1.00 56.36 B000 O
ATOM 4450 N SER B 161 -5.680 13.791 3.365 1.00 29.03 B000 N
ATOM 4451 CA SER B 161 -4.638 14.799 3.244 1.00 37.37 B000 C
ATOM 4452 C SER B 161 -5.221 16.191 3.047 1.00 35.16 B000 C
ATOM 4453 O SER B 161 -4.584 17.177 3.424 1.00 35.48 B000 O
ATOM 4454 CB SER B 161 -3.704 14.444 2.084 1.00 36.26 B000 C
ATOM 4455 OG SER B 161 -4.472 14.112 0.942 1.00 39.65 B000 O
ATOM 4456 N THR B 162 -6.430 16.294 2.469 1.00 30.29 B000 N
ATOM 4457 CA THR B 162 -7.069 17.603 2.307 1.00 31.30 B000 C
ATOM 4458 C THR B 162 -7.398 18.242 3.654 1.00 32.70 B000 C
ATOM 4459 O THR B 162 -7.252 19.456 3.821 1.00 36.81 B000 O
ATOM 4460 CB THR B 162 -8.345 17.483 1.468 1.00 31.83 B000 C
ATOM 4461 CG2 THR B 162 -8.891 18.852 1.111 1.00 35.34 B000 C
ATOM 4462 OG1 THR B 162 -8.081 16.749 0.274 1.00 37.37 B000 O
TER
HETATM 4463 O HOH B 163 -2.352 -7.080 14.228 1.00 42.56 B000 O
ATOM 4464 N PHE B 163 -7.873 17.455 4.620 1.00 31.02 B000 N
ATOM 4465 CA PHE B 163 -8.110 18.014 5.949 1.00 33.61 B000 C
ATOM 4466 C PHE B 163 -6.840 18.645 6.504 1.00 36.36 B000 C
ATOM 4467 O PHE B 163 -6.831 19.821 6.898 1.00 30.07 B000 O
ATOM 4468 CB PHE B 163 -8.611 16.931 6.901 1.00 28.07 B000 C
ATOM 4469 CG PHE B 163 -9.987 16.413 6.573 1.00 28.04 B000 C
ATOM 4470 CD1 PHE B 163 -10.172 15.516 5.548 1.00 20.83 B000 C
ATOM 4471 CD2 PHE B 163 -11.098 16.841 7.297 1.00 25.64 B000 C
ATOM 4472 CE1 PHE B 163 -11.435 15.036 5.254 1.00 31.92 B000 C
ATOM 4473 CE2 PHE B 163 -12.365 16.373 7.008 1.00 24.89 B000 C
ATOM 4474 CZ PHE B 163 -12.540 15.471 5.985 1.00 25.72 B000 C
ATOM 4475 N ALA B 164 -5.751 17.867 6.535 1.00 28.67 B000 N
ATOM 4476 CA ALA B 164 -4.488 18.367 7.066 1.00 40.18 B000 C
ATOM 4477 C ALA B 164 -4.032 19.617 6.327 1.00 34.59 B000 C
ATOM 4478 O ALA B 164 -3.488 20.540 6.936 1.00 41.19 B000 O
ATOM 4479 CB ALA B 164 -3.419 17.276 6.984 1.00 39.18 B000 C
ATOM 4480 N GLU B 165 -4.272 19.678 5.021 1.00 35.14 B000 N
ATOM 4481 CA GLU B 165 -3.815 20.824 4.252 1.00 38.46 B000 C
ATOM 4482 C GLU B 165 -4.685 22.056 4.447 1.00 41.63 B000 C
ATOM 4483 O GLU B 165 -4.188 23.175 4.291 1.00 43.08 B000 O
ATOM 4484 CB GLU B 165 -3.746 20.459 2.769 1.00 36.53 B000 C
ATOM 4485 CG GLU B 165 -2.510 19.636 2.413 1.00 43.24 B000 C
ATOM 4486 CD GLU B 165 -2.700 18.760 1.190 1.00 54.32 B000 C
ATOM 4487 OE1 GLU B 165 -3.794 18.802 0.581 1.00 54.34 B000 O
ATOM 4488 OE2 GLU B 165 -1.745 18.024 0.842 1.00 59.86 B000 O1-
TER
HETATM 4489 O HOH B 165 -4.273 -12.673 35.012 1.00 49.34 B000 O
HETATM 4490 O HOH B 166 -4.951 -11.886 58.597 1.00 38.37 B000 O
ATOM 4491 N LYS B 166 -5.965 21.896 4.778 1.00 35.52 B000 N
ATOM 4492 CA LYS B 166 -6.860 23.044 4.789 1.00 36.13 B000 C
ATOM 4493 C LYS B 166 -7.304 23.492 6.171 1.00 38.54 B000 C
ATOM 4494 O LYS B 166 -7.817 24.608 6.303 1.00 35.38 B000 O
ATOM 4495 CB LYS B 166 -8.100 22.748 3.942 1.00 36.05 B000 C
ATOM 4496 CG LYS B 166 -7.756 22.392 2.533 1.00 38.66 B000 C
ATOM 4497 CD LYS B 166 -8.549 23.207 1.527 1.00 51.94 B000 C
ATOM 4498 CE LYS B 166 -8.037 22.953 0.112 1.00 44.70 B000 C
ATOM 4499 NZ LYS B 166 -7.479 24.197 -0.488 1.00 60.44 B000 N1+
ATOM 4500 N LEU B 167 -7.126 22.672 7.191 1.00 35.38 B000 N
ATOM 4501 CA LEU B 167 -7.667 23.002 8.494 1.00 30.33 B000 C
ATOM 4502 C LEU B 167 -6.543 23.187 9.497 1.00 34.85 B000 C
ATOM 4503 O LEU B 167 -5.500 22.535 9.388 1.00 35.50 B000 O
ATOM 4504 CB LEU B 167 -8.589 21.900 9.028 1.00 36.09 B000 C
ATOM 4505 CG LEU B 167 -9.798 21.436 8.231 1.00 32.51 B000 C
ATOM 4506 CD1 LEU B 167 -10.563 20.383 9.035 1.00 32.44 B000 C
ATOM 4507 CD2 LEU B 167 -10.680 22.642 7.940 1.00 39.43 B000 C
ATOM 4508 N PRO B 168 -6.743 24.024 10.509 1.00 40.11 B000 N
ATOM 4509 CA PRO B 168 -5.811 24.032 11.632 1.00 37.64 B000 C
ATOM 4510 C PRO B 168 -5.729 22.653 12.268 1.00 39.06 B000 C
ATOM 4511 O PRO B 168 -6.681 21.868 12.256 1.00 37.68 B000 O
ATOM 4512 CB PRO B 168 -6.409 25.067 12.589 1.00 42.67 B000 C
ATOM 4513 CG PRO B 168 -7.816 25.220 12.167 1.00 43.44 B000 C
ATOM 4514 CD PRO B 168 -7.866 24.954 10.712 1.00 36.82 B000 C
ATOM 4515 N VAL B 169 -4.556 22.369 12.821 1.00 37.28 B000 N
ATOM 4516 CA VAL B 169 -4.216 21.027 13.269 1.00 30.35 B000 C
ATOM 4517 C VAL B 169 -5.163 20.535 14.358 1.00 33.16 B000 C
ATOM 4518 O VAL B 169 -5.500 19.345 14.404 1.00 31.17 B000 O
ATOM 4519 CB VAL B 169 -2.740 21.034 13.722 1.00 34.04 B000 C
ATOM 4520 CG1 VAL B 169 -2.563 21.938 14.925 1.00 34.81 B000 C
ATOM 4521 CG2 VAL B 169 -2.270 19.643 14.031 1.00 36.71 B000 C
ATOM 4522 N GLU B 170 -5.638 21.431 15.229 1.00 35.75 B000 N
ATOM 4523 CA GLU B 170 -6.546 20.998 16.286 1.00 32.14 B000 C
ATOM 4524 C GLU B 170 -7.857 20.474 15.706 1.00 33.46 B000 C
ATOM 4525 O GLU B 170 -8.479 19.568 16.283 1.00 31.25 B000 O
ATOM 4526 CB GLU B 170 -6.811 22.139 17.276 1.00 39.31 B000 C
ATOM 4527 CG GLU B 170 -7.273 23.454 16.644 1.00 45.65 B000 C
ATOM 4528 CD GLU B 170 -6.137 24.393 16.231 1.00 52.91 B000 C
ATOM 4529 OE1 GLU B 170 -4.940 24.025 16.336 1.00 51.73 B000 O
ATOM 4530 OE2 GLU B 170 -6.457 25.524 15.793 1.00 62.76 B000 O1-
ATOM 4531 N GLU B 171 -8.264 20.999 14.552 1.00 36.31 B000 N
ATOM 4532 CA GLU B 171 -9.510 20.577 13.917 1.00 33.27 B000 C
ATOM 4533 C GLU B 171 -9.356 19.256 13.164 1.00 37.12 B000 C
ATOM 4534 O GLU B 171 -10.315 18.468 13.106 1.00 30.81 B000 O
ATOM 4535 CB GLU B 171 -10.006 21.680 12.979 1.00 36.04 B000 C
ATOM 4536 CG GLU B 171 -10.767 22.793 13.718 1.00 43.66 B000 C
ATOM 4537 CD GLU B 171 -11.226 23.923 12.809 1.00 61.87 B000 C
ATOM 4538 OE1 GLU B 171 -11.105 25.096 13.220 1.00 70.97 B000 O
ATOM 4539 OE2 GLU B 171 -11.759 23.644 11.707 1.00 55.71 B000 O1-
TER
HETATM 4540 O HOH B 172 -25.177 -7.113 56.687 1.00 34.53 B000 O
ATOM 4541 N VAL B 172 -8.177 19.008 12.573 1.00 28.24 B000 N
ATOM 4542 CA VAL B 172 -7.863 17.686 12.026 1.00 30.76 B000 C
ATOM 4543 C VAL B 172 -7.957 16.631 13.114 1.00 27.17 B000 C
ATOM 4544 O VAL B 172 -8.569 15.568 12.934 1.00 31.10 B000 O
ATOM 4545 CB VAL B 172 -6.458 17.675 11.384 1.00 34.91 B000 C
ATOM 4546 CG1 VAL B 172 -6.170 16.317 10.799 1.00 28.02 B000 C
ATOM 4547 CG2 VAL B 172 -6.312 18.746 10.314 1.00 27.82 B000 C
ATOM 4548 N VAL B 173 -7.304 16.884 14.247 1.00 26.57 B000 N
ATOM 4549 CA VAL B 173 -7.391 15.940 15.352 1.00 24.82 B000 C
ATOM 4550 C VAL B 173 -8.849 15.705 15.732 1.00 25.92 B000 C
ATOM 4551 O VAL B 173 -9.265 14.570 15.989 1.00 29.96 B000 O
ATOM 4552 CB VAL B 173 -6.561 16.450 16.542 1.00 27.05 B000 C
ATOM 4553 CG1 VAL B 173 -6.972 15.744 17.842 1.00 27.79 B000 C
ATOM 4554 CG2 VAL B 173 -5.096 16.226 16.255 1.00 31.13 B000 C
ATOM 4555 N SER B 174 -9.646 16.771 15.789 1.00 27.99 B000 N
ATOM 4556 CA SER B 174 -11.042 16.602 16.167 1.00 30.16 B000 C
ATOM 4557 C SER B 174 -11.764 15.684 15.185 1.00 28.57 B000 C
ATOM 4558 O SER B 174 -12.494 14.775 15.600 1.00 29.08 B000 O
ATOM 4559 CB SER B 174 -11.729 17.963 16.250 1.00 35.62 B000 C
ATOM 4560 OG SER B 174 -13.081 17.811 16.639 1.00 36.90 B000 O
ATOM 4561 N VAL B 175 -11.517 15.858 13.879 1.00 26.80 B000 N
ATOM 4562 CA VAL B 175 -12.164 15.005 12.877 1.00 27.02 B000 C
ATOM 4563 C VAL B 175 -11.695 13.558 12.998 1.00 28.37 B000 C
ATOM 4564 O VAL B 175 -12.505 12.629 12.946 1.00 24.74 B000 O
ATOM 4565 CB VAL B 175 -11.922 15.553 11.462 1.00 26.82 B000 C
ATOM 4566 CG1 VAL B 175 -12.373 14.546 10.419 1.00 28.65 B000 C
ATOM 4567 CG2 VAL B 175 -12.687 16.856 11.290 1.00 31.70 B000 C
ATOM 4568 N VAL B 176 -10.384 13.323 13.121 1.00 26.94 B000 N
ATOM 4569 CA VAL B 176 -9.949 11.928 13.145 1.00 25.31 B000 C
ATOM 4570 C VAL B 176 -10.474 11.246 14.396 1.00 25.02 B000 C
ATOM 4571 O VAL B 176 -10.837 10.070 14.369 1.00 28.24 B000 O
ATOM 4572 CB VAL B 176 -8.414 11.805 13.015 1.00 34.97 B000 C
ATOM 4573 CG1 VAL B 176 -7.910 12.594 11.846 1.00 29.07 B000 C
ATOM 4574 CG2 VAL B 176 -7.702 12.211 14.279 1.00 27.50 B000 C
ATOM 4575 N ASN B 177 -10.552 11.985 15.509 1.00 31.08 B000 N
ATOM 4576 CA ASN B 177 -11.085 11.411 16.741 1.00 31.20 B000 C
ATOM 4577 C ASN B 177 -12.553 11.045 16.590 1.00 26.86 B000 C
ATOM 4578 O ASN B 177 -12.984 9.994 17.070 1.00 31.04 B000 O
ATOM 4579 CB ASN B 177 -10.897 12.381 17.909 1.00 33.42 B000 C
ATOM 4580 CG ASN B 177 -9.467 12.414 18.422 1.00 33.50 B000 C
ATOM 4581 ND2 ASN B 177 -9.238 13.220 19.456 1.00 31.72 B000 N
ATOM 4582 OD1 ASN B 177 -8.580 11.721 17.908 1.00 30.95 B000 O
ATOM 4583 N SER B 178 -13.344 11.917 15.959 1.00 27.49 B000 N
ATOM 4584 CA SER B 178 -14.742 11.582 15.706 1.00 29.02 B000 C
ATOM 4585 C SER B 178 -14.839 10.323 14.858 1.00 30.51 B000 C
ATOM 4586 O SER B 178 -15.712 9.477 15.082 1.00 24.98 B000 O
ATOM 4587 CB SER B 178 -15.461 12.734 15.004 1.00 27.99 B000 C
ATOM 4588 OG SER B 178 -15.632 13.852 15.854 1.00 31.45 B000 O
ATOM 4589 N TYR B 179 -13.936 10.187 13.879 1.00 26.33 B000 N
ATOM 4590 CA TYR B 179 -13.920 9.024 13.000 1.00 19.06 B000 C
ATOM 4591 C TYR B 179 -13.519 7.775 13.756 1.00 26.44 B000 C
ATOM 4592 O TYR B 179 -14.214 6.754 13.698 1.00 26.95 B000 O
ATOM 4593 CB TYR B 179 -12.948 9.274 11.844 1.00 22.35 B000 C
ATOM 4594 CG TYR B 179 -12.764 8.095 10.928 1.00 24.30 B000 C
ATOM 4595 CD1 TYR B 179 -13.806 7.665 10.141 1.00 24.61 B000 C
ATOM 4596 CD2 TYR B 179 -11.552 7.425 10.846 1.00 30.72 B000 C
ATOM 4597 CE1 TYR B 179 -13.668 6.606 9.297 1.00 35.22 B000 C
ATOM 4598 CE2 TYR B 179 -11.405 6.339 9.979 1.00 31.09 B000 C
ATOM 4599 CZ TYR B 179 -12.472 5.951 9.218 1.00 22.20 B000 C
ATOM 4600 OH TYR B 179 -12.405 4.881 8.351 1.00 38.06 B000 O
TER
HETATM 4601 O HOH B 180 -18.789 25.536 0.270 1.00 36.68 B000 O
ATOM 4602 N PHE B 180 -12.389 7.831 14.472 1.00 21.94 B000 N
ATOM 4603 CA PHE B 180 -11.962 6.658 15.228 1.00 22.55 B000 C
ATOM 4604 C PHE B 180 -13.008 6.252 16.255 1.00 24.57 B000 C
ATOM 4605 O PHE B 180 -13.179 5.060 16.521 1.00 26.51 B000 O
ATOM 4606 CB PHE B 180 -10.630 6.921 15.938 1.00 27.30 B000 C
ATOM 4607 CG PHE B 180 -9.440 6.935 15.035 1.00 30.92 B000 C
ATOM 4608 CD1 PHE B 180 -9.428 6.227 13.850 1.00 29.99 B000 C
ATOM 4609 CD2 PHE B 180 -8.330 7.682 15.369 1.00 26.31 B000 C
ATOM 4610 CE1 PHE B 180 -8.305 6.243 13.016 1.00 30.81 B000 C
ATOM 4611 CE2 PHE B 180 -7.207 7.700 14.544 1.00 32.56 B000 C
ATOM 4612 CZ PHE B 180 -7.202 6.980 13.367 1.00 28.39 B000 C
TER
HETATM 4613 O HOH B 181 -9.637 0.350 3.199 1.00 33.71 B000 O
ATOM 4614 N SER B 181 -13.729 7.214 16.833 1.00 28.16 B000 N
ATOM 4615 CA SER B 181 -14.719 6.850 17.848 1.00 28.14 B000 C
ATOM 4616 C SER B 181 -15.883 6.081 17.233 1.00 26.63 B000 C
ATOM 4617 O SER B 181 -16.345 5.081 17.800 1.00 25.12 B000 O
ATOM 4618 CB SER B 181 -15.230 8.105 18.550 1.00 33.99 B000 C
ATOM 4619 OG SER B 181 -14.208 8.661 19.359 1.00 38.54 B000 O
TER
HETATM 4620 O HOH B 182 -19.944 3.231 -7.492 1.00 43.19 B000 O
ATOM 4621 N VAL B 182 -16.368 6.539 16.073 1.00 23.67 B000 N
ATOM 4622 CA VAL B 182 -17.497 5.882 15.408 1.00 26.02 B000 C
ATOM 4623 C VAL B 182 -17.121 4.456 15.055 1.00 27.02 B000 C
ATOM 4624 O VAL B 182 -17.849 3.504 15.361 1.00 25.65 B000 O
ATOM 4625 CB VAL B 182 -17.927 6.672 14.152 1.00 25.95 B000 C
ATOM 4626 CG1 VAL B 182 -18.872 5.824 13.251 1.00 27.02 B000 C
ATOM 4627 CG2 VAL B 182 -18.592 7.968 14.528 1.00 28.45 B000 C
ATOM 4628 N CYS B 183 -15.952 4.293 14.428 1.00 24.71 B000 N
ATOM 4629 CA CYS B 183 -15.508 2.971 14.001 1.00 25.23 B000 C
ATOM 4630 C CYS B 183 -15.357 2.048 15.193 1.00 23.35 B000 C
ATOM 4631 O CYS B 183 -15.892 0.933 15.198 1.00 29.23 B000 O
ATOM 4632 CB CYS B 183 -14.184 3.081 13.231 1.00 23.18 B000 C
ATOM 4633 SG CYS B 183 -14.369 4.002 11.650 1.00 24.66 B000 S
TER
HETATM 4634 O HOH B 184 -18.877 30.114 4.293 1.00 51.42 B000 O
ATOM 4635 N THR B 184 -14.645 2.509 16.228 1.00 23.13 B000 N
ATOM 4636 CA THR B 184 -14.307 1.640 17.351 1.00 25.76 B000 C
ATOM 4637 C THR B 184 -15.552 1.160 18.099 1.00 26.37 B000 C
ATOM 4638 O THR B 184 -15.662 -0.032 18.436 1.00 28.72 B000 O
ATOM 4639 CB THR B 184 -13.340 2.374 18.290 1.00 26.24 B000 C
ATOM 4640 CG2 THR B 184 -13.035 1.517 19.506 1.00 35.48 B000 C
ATOM 4641 OG1 THR B 184 -12.118 2.659 17.580 1.00 29.54 B000 O
ATOM 4642 N ALA B 185 -16.509 2.062 18.344 1.00 27.44 B000 N
ATOM 4643 CA ALA B 185 -17.739 1.680 19.049 1.00 31.04 B000 C
ATOM 4644 C ALA B 185 -18.526 0.627 18.278 1.00 24.33 B000 C
ATOM 4645 O ALA B 185 -18.981 -0.365 18.856 1.00 26.84 B000 O
ATOM 4646 CB ALA B 185 -18.617 2.903 19.292 1.00 31.18 B000 C
TER
HETATM 4647 O HOH B 185 -11.989 5.103 -0.064 1.00 33.92 B000 O
ATOM 4648 N ILE B 186 -18.656 0.798 16.960 1.00 25.88 B000 N
ATOM 4649 CA ILE B 186 -19.469 -0.134 16.184 1.00 27.61 B000 C
ATOM 4650 C ILE B 186 -18.771 -1.482 16.034 1.00 27.87 B000 C
ATOM 4651 O ILE B 186 -19.409 -2.538 16.154 1.00 26.74 B000 O
ATOM 4652 CB ILE B 186 -19.835 0.486 14.826 1.00 25.83 B000 C
ATOM 4653 CG1 ILE B 186 -20.782 1.666 15.039 1.00 29.50 B000 C
ATOM 4654 CG2 ILE B 186 -20.530 -0.533 13.927 1.00 25.01 B000 C
ATOM 4655 CD1 ILE B 186 -21.126 2.373 13.757 1.00 27.79 B000 C
ATOM 4656 N ILE B 187 -17.462 -1.478 15.746 1.00 24.48 B000 N
ATOM 4657 CA ILE B 187 -16.714 -2.737 15.643 1.00 24.84 B000 C
ATOM 4658 C ILE B 187 -16.820 -3.532 16.941 1.00 24.93 B000 C
ATOM 4659 O ILE B 187 -17.080 -4.745 16.936 1.00 26.31 B000 O
ATOM 4660 CB ILE B 187 -15.245 -2.460 15.274 1.00 27.13 B000 C
ATOM 4661 CG1 ILE B 187 -15.142 -2.044 13.812 1.00 22.31 B000 C
ATOM 4662 CG2 ILE B 187 -14.360 -3.701 15.518 1.00 27.27 B000 C
ATOM 4663 CD1 ILE B 187 -13.802 -1.433 13.486 1.00 22.72 B000 C
ATOM 4664 N THR B 188 -16.636 -2.851 18.074 1.00 23.59 B000 N
ATOM 4665 CA THR B 188 -16.738 -3.515 19.372 1.00 30.08 B000 C
ATOM 4666 C THR B 188 -18.147 -4.032 19.616 1.00 30.22 B000 C
ATOM 4667 O THR B 188 -18.332 -5.178 20.035 1.00 30.24 B000 O
ATOM 4668 CB THR B 188 -16.329 -2.551 20.481 1.00 31.28 B000 C
ATOM 4669 CG2 THR B 188 -16.376 -3.248 21.828 1.00 41.55 B000 C
ATOM 4670 OG1 THR B 188 -15.003 -2.075 20.224 1.00 30.22 B000 O
ATOM 4671 N ARG B 189 -19.160 -3.202 19.343 1.00 27.31 B000 N
ATOM 4672 CA ARG B 189 -20.542 -3.657 19.468 1.00 32.48 B000 C
ATOM 4673 C ARG B 189 -20.771 -4.938 18.678 1.00 32.90 B000 C
ATOM 4674 O ARG B 189 -21.517 -5.825 19.118 1.00 30.42 B000 O
ATOM 4675 CB ARG B 189 -21.502 -2.555 19.004 1.00 37.57 B000 C
ATOM 4676 CG ARG B 189 -22.939 -2.807 19.386 1.00 42.17 B000 C
ATOM 4677 CD ARG B 189 -23.907 -2.543 18.254 1.00 53.04 B000 C
ATOM 4678 NE ARG B 189 -23.900 -1.159 17.787 1.00 53.88 B000 N
ATOM 4679 CZ ARG B 189 -23.994 -0.802 16.510 1.00 49.20 B000 C
ATOM 4680 NH1 ARG B 189 -23.959 -1.700 15.533 1.00 46.86 B000 N1+
ATOM 4681 NH2 ARG B 189 -24.138 0.485 16.205 1.00 51.19 B000 N
TER
HETATM 4682 O HOH B 189 -22.244 5.622 15.550 1.00 43.71 B000 O
ATOM 4683 N GLN B 190 -20.122 -5.066 17.516 1.00 27.15 B000 N
ATOM 4684 CA GLN B 190 -20.360 -6.198 16.627 1.00 25.59 B000 C
ATOM 4685 C GLN B 190 -19.437 -7.376 16.907 1.00 26.35 B000 C
ATOM 4686 O GLN B 190 -19.445 -8.360 16.152 1.00 30.23 B000 O
ATOM 4687 CB GLN B 190 -20.226 -5.748 15.174 1.00 29.47 B000 C
ATOM 4688 CG GLN B 190 -21.422 -4.894 14.710 1.00 26.43 B000 C
ATOM 4689 CD GLN B 190 -22.726 -5.678 14.646 1.00 38.38 B000 C
ATOM 4690 NE2 GLN B 190 -23.842 -4.968 14.775 1.00 39.36 B000 N
ATOM 4691 OE1 GLN B 190 -22.732 -6.900 14.482 1.00 33.53 B000 O
TER
HETATM 4692 O HOH B 190 -24.521 4.955 16.990 1.00 45.70 B000 O
ATOM 4693 N GLY B 191 -18.673 -7.315 17.990 1.00 29.06 B000 N
ATOM 4694 CA GLY B 191 -17.854 -8.424 18.423 1.00 28.84 B000 C
ATOM 4695 C GLY B 191 -16.477 -8.480 17.813 1.00 32.26 B000 C
ATOM 4696 O GLY B 191 -15.784 -9.489 17.982 1.00 34.06 B000 O
TER
HETATM 4697 O HOH B 191 -17.102 -24.468 48.758 1.00 50.14 B000 O
ATOM 4698 N GLY B 192 -16.070 -7.455 17.073 1.00 31.31 B000 N
ATOM 4699 CA GLY B 192 -14.719 -7.381 16.570 1.00 28.72 B000 C
ATOM 4700 C GLY B 192 -13.842 -6.634 17.538 1.00 33.15 B000 C
ATOM 4701 O GLY B 192 -14.285 -6.129 18.564 1.00 30.80 B000 O
TER
HETATM 4702 O HOH B 192 -24.506 -4.730 57.344 1.00 41.86 B000 O
ATOM 4703 N GLU B 193 -12.565 -6.540 17.198 1.00 29.74 B000 N
ATOM 4704 CA GLU B 193 -11.658 -5.757 18.029 1.00 37.37 B000 C
ATOM 4705 C GLU B 193 -10.731 -4.936 17.145 1.00 33.54 B000 C
ATOM 4706 O GLU B 193 -10.189 -5.446 16.158 1.00 27.09 B000 O
ATOM 4707 CB GLU B 193 -10.848 -6.652 18.982 1.00 34.87 B000 C
ATOM 4708 CG GLU B 193 -9.786 -7.538 18.325 1.00 47.47 B000 C
ATOM 4709 CD GLU B 193 -9.500 -8.836 19.107 1.00 69.79 B000 C
ATOM 4710 OE1 GLU B 193 -8.513 -8.865 19.877 1.00 73.45 B000 O
ATOM 4711 OE2 GLU B 193 -10.256 -9.826 18.947 1.00 70.49 B000 O1-
TER
HETATM 4712 O HOH B 194 -22.542 1.562 18.513 1.00 47.29 B000 O
ATOM 4713 N VAL B 194 -10.560 -3.665 17.494 1.00 25.01 B000 N
ATOM 4714 CA VAL B 194 -9.611 -2.810 16.794 1.00 28.53 B000 C
ATOM 4715 C VAL B 194 -8.210 -3.174 17.274 1.00 36.34 B000 C
ATOM 4716 O VAL B 194 -7.953 -3.229 18.484 1.00 32.29 B000 O
ATOM 4717 CB VAL B 194 -9.934 -1.322 17.045 1.00 31.16 B000 C
ATOM 4718 CG1 VAL B 194 -8.779 -0.424 16.598 1.00 30.52 B000 C
ATOM 4719 CG2 VAL B 194 -11.208 -0.914 16.319 1.00 29.44 B000 C
TER
HETATM 4720 O HOH B 195 -7.049 9.260 2.537 1.00 33.86 B000 O
ATOM 4721 N THR B 195 -7.308 -3.477 16.338 1.00 33.44 B000 N
ATOM 4722 CA THR B 195 -5.944 -3.820 16.714 1.00 29.67 B000 C
ATOM 4723 C THR B 195 -4.984 -2.663 16.599 1.00 35.70 B000 C
ATOM 4724 O THR B 195 -4.047 -2.587 17.392 1.00 33.41 B000 O
ATOM 4725 CB THR B 195 -5.390 -4.974 15.878 1.00 43.62 B000 C
ATOM 4726 CG2 THR B 195 -6.056 -6.216 16.276 1.00 35.62 B000 C
ATOM 4727 OG1 THR B 195 -5.608 -4.721 14.483 1.00 42.98 B000 O
TER
HETATM 4728 O HOH B 196 -4.663 5.341 4.636 1.00 33.66 B000 O
ATOM 4729 N LYS B 196 -5.189 -1.758 15.647 1.00 32.23 B000 N
ATOM 4730 CA LYS B 196 -4.349 -0.574 15.610 1.00 35.81 B000 C
ATOM 4731 C LYS B 196 -4.908 0.433 14.622 1.00 30.73 B000 C
ATOM 4732 O LYS B 196 -5.721 0.110 13.759 1.00 27.75 B000 O
ATOM 4733 CB LYS B 196 -2.905 -0.915 15.238 1.00 39.10 B000 C
ATOM 4734 CG LYS B 196 -2.752 -1.635 13.936 1.00 30.38 B000 C
ATOM 4735 CD LYS B 196 -1.337 -2.239 13.826 1.00 41.15 B000 C
ATOM 4736 CE LYS B 196 -1.047 -3.196 14.978 1.00 36.91 B000 C
ATOM 4737 NZ LYS B 196 0.280 -3.858 14.898 1.00 34.65 B000 N1+
ATOM 4738 N PHE B 197 -4.446 1.659 14.776 1.00 25.29 B000 N
ATOM 4739 CA PHE B 197 -4.596 2.710 13.794 1.00 28.12 B000 C
ATOM 4740 C PHE B 197 -3.290 2.821 13.019 1.00 32.60 B000 C
ATOM 4741 O PHE B 197 -2.212 2.875 13.619 1.00 30.57 B000 O
ATOM 4742 CB PHE B 197 -4.927 4.035 14.481 1.00 26.92 B000 C
ATOM 4743 CG PHE B 197 -6.132 3.964 15.383 1.00 33.09 B000 C
ATOM 4744 CD1 PHE B 197 -7.313 3.355 14.951 1.00 29.29 B000 C
ATOM 4745 CD2 PHE B 197 -6.078 4.477 16.670 1.00 32.59 B000 C
ATOM 4746 CE1 PHE B 197 -8.433 3.280 15.796 1.00 32.35 B000 C
ATOM 4747 CE2 PHE B 197 -7.187 4.401 17.513 1.00 37.08 B000 C
ATOM 4748 CZ PHE B 197 -8.360 3.810 17.073 1.00 34.18 B000 C
TER
HETATM 4749 O HOH B 198 -4.694 6.387 2.730 1.00 34.79 B000 O
ATOM 4750 N ILE B 198 -3.386 2.821 11.699 1.00 30.42 B000 N
ATOM 4751 CA ILE B 198 -2.243 3.062 10.824 1.00 31.06 B000 C
ATOM 4752 C ILE B 198 -2.554 4.367 10.110 1.00 28.71 B000 C
ATOM 4753 O ILE B 198 -3.326 4.375 9.146 1.00 25.64 B000 O
ATOM 4754 CB ILE B 198 -2.028 1.920 9.827 1.00 35.68 B000 C
ATOM 4755 CG1 ILE B 198 -1.998 0.565 10.534 1.00 33.53 B000 C
ATOM 4756 CG2 ILE B 198 -0.754 2.138 9.041 1.00 29.86 B000 C
ATOM 4757 CD1 ILE B 198 -2.481 -0.568 9.621 1.00 30.79 B000 C
ATOM 4758 N GLY B 199 -1.991 5.468 10.590 1.00 27.16 B000 N
ATOM 4759 CA GLY B 199 -2.445 6.764 10.125 1.00 25.92 B000 C
ATOM 4760 C GLY B 199 -3.954 6.894 10.316 1.00 28.41 B000 C
ATOM 4761 O GLY B 199 -4.500 6.591 11.382 1.00 23.19 B000 O
TER
HETATM 4762 O HOH B 199 -21.952 5.652 2.287 1.00 43.21 B000 O
ATOM 4763 N ASP B 200 -4.652 7.336 9.277 1.00 29.11 B000 N
ATOM 4764 CA ASP B 200 -6.110 7.432 9.344 1.00 24.45 B000 C
ATOM 4765 C ASP B 200 -6.794 6.101 9.098 1.00 27.72 B000 C
ATOM 4766 O ASP B 200 -8.024 6.061 8.985 1.00 28.26 B000 O
ATOM 4767 CB ASP B 200 -6.627 8.459 8.331 1.00 26.52 B000 C
ATOM 4768 CG ASP B 200 -6.264 8.097 6.910 1.00 30.72 B000 C
ATOM 4769 OD1 ASP B 200 -5.079 7.889 6.635 1.00 27.74 B000 O
ATOM 4770 OD2 ASP B 200 -7.169 8.013 6.063 1.00 30.06 B000 O1-
ATOM 4771 N CYS B 201 -6.040 5.016 8.995 1.00 26.01 B000 N
ATOM 4772 CA CYS B 201 -6.616 3.701 8.750 1.00 24.53 B000 C
ATOM 4773 C CYS B 201 -6.903 2.959 10.055 1.00 29.67 B000 C
ATOM 4774 O CYS B 201 -6.032 2.836 10.925 1.00 28.41 B000 O
ATOM 4775 CB CYS B 201 -5.685 2.876 7.866 1.00 28.48 B000 C
ATOM 4776 SG CYS B 201 -6.210 1.183 7.753 1.00 35.16 B000 S
TER
HETATM 4777 O HOH B 201 -10.547 -3.217 60.995 1.00 40.80 B000 O
HETATM 4778 O HOH B 202 -3.084 -13.024 4.567 1.00 45.23 B000 O
ATOM 4779 N VAL B 202 -8.135 2.478 10.188 1.00 24.28 B000 N
ATOM 4780 CA VAL B 202 -8.551 1.623 11.293 1.00 27.93 B000 C
ATOM 4781 C VAL B 202 -8.387 0.174 10.861 1.00 25.18 B000 C
ATOM 4782 O VAL B 202 -8.972 -0.241 9.857 1.00 26.50 B000 O
ATOM 4783 CB VAL B 202 -10.012 1.907 11.689 1.00 28.29 B000 C
ATOM 4784 CG1 VAL B 202 -10.493 0.899 12.687 1.00 26.12 B000 C
ATOM 4785 CG2 VAL B 202 -10.151 3.312 12.253 1.00 27.60 B000 C
TER
HETATM 4786 O HOH B 203 -7.744 -12.689 -0.843 1.00 44.18 B000 O
ATOM 4787 N MET B 203 -7.618 -0.604 11.625 1.00 24.12 B000 N
ATOM 4788 CA MET B 203 -7.420 -2.029 11.375 1.00 21.03 B000 C
ATOM 4789 C MET B 203 -8.089 -2.850 12.478 1.00 24.25 B000 C
ATOM 4790 O MET B 203 -7.875 -2.590 13.666 1.00 27.31 B000 O
ATOM 4791 CB MET B 203 -5.923 -2.370 11.316 1.00 25.66 B000 C
ATOM 4792 CG MET B 203 -5.638 -3.849 11.046 1.00 26.00 B000 C
ATOM 4793 SD MET B 203 -3.821 -4.188 11.039 1.00 34.47 B000 S
ATOM 4794 CE MET B 203 -3.856 -5.969 11.043 1.00 34.25 B000 C
ATOM 4795 N ALA B 204 -8.859 -3.869 12.095 1.00 22.08 B000 N
ATOM 4796 CA ALA B 204 -9.617 -4.617 13.089 1.00 24.64 B000 C
ATOM 4797 C ALA B 204 -9.751 -6.066 12.651 1.00 25.61 B000 C
ATOM 4798 O ALA B 204 -9.608 -6.411 11.475 1.00 25.04 B000 O
ATOM 4799 CB ALA B 204 -11.011 -4.011 13.325 1.00 22.57 B000 C
TER
HETATM 4800 O HOH B 204 -32.305 -2.770 0.795 1.00 48.89 B000 O
HETATM 4801 O HOH B 205 -20.953 2.295 61.886 1.00 55.32 B000 O
ATOM 4802 N TYR B 205 -10.014 -6.912 13.624 1.00 20.77 B000 N
ATOM 4803 CA TYR B 205 -10.214 -8.327 13.394 1.00 25.04 B000 C
ATOM 4804 C TYR B 205 -11.614 -8.707 13.811 1.00 26.05 B000 C
ATOM 4805 O TYR B 205 -12.122 -8.207 14.810 1.00 25.23 B000 O
ATOM 4806 CB TYR B 205 -9.246 -9.173 14.210 1.00 28.03 B000 C
ATOM 4807 CG TYR B 205 -7.806 -9.062 13.808 1.00 31.89 B000 C
ATOM 4808 CD1 TYR B 205 -7.438 -8.953 12.476 1.00 28.94 B000 C
ATOM 4809 CD2 TYR B 205 -6.805 -9.041 14.775 1.00 34.59 B000 C
ATOM 4810 CE1 TYR B 205 -6.081 -8.852 12.106 1.00 30.22 B000 C
ATOM 4811 CE2 TYR B 205 -5.459 -8.935 14.424 1.00 35.86 B000 C
ATOM 4812 CZ TYR B 205 -5.111 -8.830 13.090 1.00 38.09 B000 C
ATOM 4813 OH TYR B 205 -3.789 -8.719 12.752 1.00 40.00 B000 O
TER
HETATM 4814 O HOH B 206 -13.704 14.685 18.159 1.00 34.41 B000 O
ATOM 4815 N PHE B 206 -12.208 -9.608 13.056 1.00 28.61 B000 N
ATOM 4816 CA PHE B 206 -13.369 -10.372 13.466 1.00 28.98 B000 C
ATOM 4817 C PHE B 206 -12.965 -11.840 13.423 1.00 31.98 B000 C
ATOM 4818 O PHE B 206 -12.078 -12.207 12.657 1.00 32.17 B000 O
ATOM 4819 CB PHE B 206 -14.565 -10.096 12.533 1.00 25.52 B000 C
ATOM 4820 CG PHE B 206 -15.165 -8.726 12.700 1.00 23.83 B000 C
ATOM 4821 CD1 PHE B 206 -14.600 -7.616 12.079 1.00 23.92 B000 C
ATOM 4822 CD2 PHE B 206 -16.303 -8.547 13.486 1.00 26.42 B000 C
ATOM 4823 CE1 PHE B 206 -15.161 -6.351 12.241 1.00 23.94 B000 C
ATOM 4824 CE2 PHE B 206 -16.867 -7.274 13.653 1.00 28.24 B000 C
ATOM 4825 CZ PHE B 206 -16.298 -6.183 13.027 1.00 25.05 B000 C
ATOM 4826 N ASP B 207 -13.585 -12.675 14.264 1.00 30.83 B000 N
ATOM 4827 CA ASP B 207 -13.369 -14.117 14.181 1.00 34.63 B000 C
ATOM 4828 C ASP B 207 -13.624 -14.608 12.760 1.00 34.25 B000 C
ATOM 4829 O ASP B 207 -14.438 -14.045 12.028 1.00 35.14 B000 O
ATOM 4830 CB ASP B 207 -14.296 -14.866 15.144 1.00 39.73 B000 C
ATOM 4831 CG ASP B 207 -13.910 -14.679 16.604 1.00 44.93 B000 C
ATOM 4832 OD1 ASP B 207 -12.768 -14.245 16.868 1.00 45.90 B000 O
ATOM 4833 OD2 ASP B 207 -14.750 -14.980 17.491 1.00 55.19 B000 O1-
TER
HETATM 4834 O HOH B 207 7.206 -1.180 62.654 1.00 41.69 B000 O
ATOM 4835 N GLY B 208 -12.921 -15.675 12.363 1.00 32.45 B000 N
ATOM 4836 CA GLY B 208 -12.995 -16.126 10.984 1.00 30.35 B000 C
ATOM 4837 C GLY B 208 -14.380 -16.550 10.537 1.00 37.68 B000 C
ATOM 4838 O GLY B 208 -14.665 -16.547 9.335 1.00 41.92 B000 O
ATOM 4839 N ASP B 209 -15.249 -16.915 11.473 1.00 38.93 B000 N
ATOM 4840 CA ASP B 209 -16.613 -17.297 11.149 1.00 39.26 B000 C
ATOM 4841 C ASP B 209 -17.610 -16.157 11.346 1.00 39.60 B000 C
ATOM 4842 O ASP B 209 -18.819 -16.385 11.244 1.00 44.18 B000 O
ATOM 4843 CB ASP B 209 -17.026 -18.524 11.976 1.00 42.37 B000 C
ATOM 4844 CG ASP B 209 -17.161 -18.225 13.468 1.00 52.76 B000 C
ATOM 4845 OD1 ASP B 209 -16.369 -17.421 14.011 1.00 57.51 B000 O
ATOM 4846 OD2 ASP B 209 -18.063 -18.807 14.110 1.00 63.69 B000 O1-
TER
HETATM 4847 O HOH B 209 -22.156 -18.346 2.196 1.00 43.97 B000 O
ATOM 4848 N CYS B 210 -17.146 -14.929 11.572 1.00 36.31 B000 N
ATOM 4849 CA CYS B 210 -18.047 -13.817 11.862 1.00 32.17 B000 C
ATOM 4850 C CYS B 210 -18.099 -12.783 10.742 1.00 29.36 B000 C
ATOM 4851 O CYS B 210 -18.199 -11.584 10.998 1.00 25.96 B000 O
ATOM 4852 CB CYS B 210 -17.678 -13.147 13.177 1.00 33.41 B000 C
ATOM 4853 SG CYS B 210 -18.018 -14.155 14.617 1.00 43.79 B000 S
TER
HETATM 4854 O HOH B 210 -15.720 -0.371 57.037 1.00 44.24 B000 O
ATOM 4855 N ALA B 211 -18.077 -13.243 9.489 1.00 29.04 B000 N
ATOM 4856 CA ALA B 211 -18.148 -12.319 8.360 1.00 34.11 B000 C
ATOM 4857 C ALA B 211 -19.442 -11.520 8.378 1.00 25.00 B000 C
ATOM 4858 O ALA B 211 -19.455 -10.347 7.996 1.00 24.27 B000 O
ATOM 4859 CB ALA B 211 -18.028 -13.075 7.031 1.00 25.41 B000 C
ATOM 4860 N ASP B 212 -20.541 -12.150 8.794 1.00 25.07 B000 N
ATOM 4861 CA ASP B 212 -21.820 -11.445 8.862 1.00 31.52 B000 C
ATOM 4862 C ASP B 212 -21.723 -10.231 9.771 1.00 25.58 B000 C
ATOM 4863 O ASP B 212 -22.269 -9.169 9.460 1.00 27.49 B000 O
ATOM 4864 CB ASP B 212 -22.914 -12.388 9.348 1.00 32.37 B000 C
ATOM 4865 CG ASP B 212 -23.248 -13.453 8.334 1.00 35.11 B000 C
ATOM 4866 OD1 ASP B 212 -23.565 -13.096 7.184 1.00 36.68 B000 O
ATOM 4867 OD2 ASP B 212 -23.186 -14.654 8.683 1.00 40.11 B000 O1-
TER
HETATM 4868 O HOH B 212 -19.908 -26.621 46.940 1.00 59.47 B000 O
ATOM 4869 N GLN B 213 -20.995 -10.366 10.887 1.00 26.68 B000 N
ATOM 4870 CA GLN B 213 -20.836 -9.270 11.833 1.00 23.67 B000 C
ATOM 4871 C GLN B 213 -19.926 -8.190 11.269 1.00 26.08 B000 C
ATOM 4872 O GLN B 213 -20.141 -6.995 11.501 1.00 28.69 B000 O
ATOM 4873 CB GLN B 213 -20.258 -9.802 13.152 1.00 23.69 B000 C
ATOM 4874 CG GLN B 213 -21.275 -10.509 14.067 1.00 31.84 B000 C
ATOM 4875 CD GLN B 213 -21.829 -11.776 13.461 1.00 41.74 B000 C
ATOM 4876 NE2 GLN B 213 -23.159 -11.872 13.418 1.00 37.94 B000 N
ATOM 4877 OE1 GLN B 213 -21.076 -12.664 13.020 1.00 39.85 B000 O
TER
HETATM 4878 O HOH B 213 -15.737 -21.162 47.749 1.00 37.21 B000 O
ATOM 4879 N ALA B 214 -18.871 -8.596 10.568 1.00 25.76 B000 N
ATOM 4880 CA ALA B 214 -17.991 -7.618 9.935 1.00 25.11 B000 C
ATOM 4881 C ALA B 214 -18.731 -6.824 8.862 1.00 22.80 B000 C
ATOM 4882 O ALA B 214 -18.526 -5.614 8.733 1.00 25.05 B000 O
ATOM 4883 CB ALA B 214 -16.763 -8.315 9.342 1.00 20.66 B000 C
ATOM 4884 N ILE B 215 -19.588 -7.483 8.078 1.00 20.55 B000 N
ATOM 4885 CA ILE B 215 -20.373 -6.748 7.088 1.00 21.73 B000 C
ATOM 4886 C ILE B 215 -21.355 -5.806 7.772 1.00 23.88 B000 C
ATOM 4887 O ILE B 215 -21.497 -4.637 7.381 1.00 22.46 B000 O
ATOM 4888 CB ILE B 215 -21.091 -7.714 6.128 1.00 24.35 B000 C
ATOM 4889 CG1 ILE B 215 -20.067 -8.439 5.229 1.00 25.63 B000 C
ATOM 4890 CG2 ILE B 215 -22.073 -6.950 5.230 1.00 21.65 B000 C
ATOM 4891 CD1 ILE B 215 -20.631 -9.724 4.571 1.00 24.22 B000 C
ATOM 4892 N GLN B 216 -22.042 -6.288 8.805 1.00 26.46 B000 N
ATOM 4893 CA GLN B 216 -22.989 -5.426 9.506 1.00 27.82 B000 C
ATOM 4894 C GLN B 216 -22.272 -4.241 10.123 1.00 24.13 B000 C
ATOM 4895 O GLN B 216 -22.746 -3.104 10.040 1.00 24.72 B000 O
ATOM 4896 CB GLN B 216 -23.729 -6.213 10.593 1.00 21.92 B000 C
ATOM 4897 CG GLN B 216 -24.880 -5.450 11.191 1.00 27.00 B000 C
ATOM 4898 CD GLN B 216 -25.976 -5.254 10.167 1.00 31.64 B000 C
ATOM 4899 NE2 GLN B 216 -26.111 -4.034 9.675 1.00 29.36 B000 N
ATOM 4900 OE1 GLN B 216 -26.659 -6.210 9.783 1.00 35.10 B000 O
ATOM 4901 N ALA B 217 -21.122 -4.489 10.752 1.00 22.47 B000 N
ATOM 4902 CA ALA B 217 -20.339 -3.384 11.299 1.00 23.86 B000 C
ATOM 4903 C ALA B 217 -19.997 -2.365 10.226 1.00 20.94 B000 C
ATOM 4904 O ALA B 217 -20.121 -1.158 10.452 1.00 22.07 B000 O
ATOM 4905 CB ALA B 217 -19.069 -3.909 11.972 1.00 20.67 B000 C
ATOM 4906 N SER B 218 -19.589 -2.825 9.042 1.00 18.84 B000 N
ATOM 4907 CA SER B 218 -19.246 -1.897 7.962 1.00 21.05 B000 C
ATOM 4908 C SER B 218 -20.440 -1.052 7.548 1.00 22.42 B000 C
ATOM 4909 O SER B 218 -20.329 0.171 7.381 1.00 20.27 B000 O
ATOM 4910 CB SER B 218 -18.718 -2.685 6.763 1.00 20.16 B000 C
ATOM 4911 OG SER B 218 -17.559 -3.424 7.135 1.00 22.77 B000 O
ATOM 4912 N LEU B 219 -21.590 -1.696 7.346 1.00 20.58 B000 N
ATOM 4913 CA LEU B 219 -22.792 -0.954 6.981 1.00 26.78 B000 C
ATOM 4914 C LEU B 219 -23.173 0.035 8.072 1.00 22.03 B000 C
ATOM 4915 O LEU B 219 -23.524 1.187 7.783 1.00 25.90 B000 O
ATOM 4916 CB LEU B 219 -23.927 -1.937 6.699 1.00 23.98 B000 C
ATOM 4917 CG LEU B 219 -23.650 -2.756 5.431 1.00 27.86 B000 C
ATOM 4918 CD1 LEU B 219 -24.623 -3.921 5.295 1.00 28.05 B000 C
ATOM 4919 CD2 LEU B 219 -23.713 -1.860 4.209 1.00 27.04 B000 C
ATOM 4920 N ASP B 220 -23.116 -0.396 9.339 1.00 24.11 B000 N
ATOM 4921 CA ASP B 220 -23.486 0.491 10.434 1.00 26.51 B000 C
ATOM 4922 C ASP B 220 -22.560 1.699 10.494 1.00 25.16 B000 C
ATOM 4923 O ASP B 220 -23.013 2.827 10.723 1.00 23.51 B000 O
ATOM 4924 CB ASP B 220 -23.473 -0.266 11.765 1.00 29.48 B000 C
ATOM 4925 CG ASP B 220 -24.677 -1.194 11.921 1.00 33.03 B000 C
ATOM 4926 OD1 ASP B 220 -25.569 -1.178 11.037 1.00 35.13 B000 O
ATOM 4927 OD2 ASP B 220 -24.720 -1.955 12.910 1.00 35.24 B000 O1-
TER
HETATM 4928 O HOH B 220 -25.489 2.419 53.445 1.00 54.02 B000 O
HETATM 4929 O HOH B 221 -22.479 4.159 62.252 1.00 66.28 B000 O
ATOM 4930 N ILE B 221 -21.265 1.497 10.240 1.00 24.16 B000 N
ATOM 4931 CA ILE B 221 -20.344 2.630 10.239 1.00 24.32 B000 C
ATOM 4932 C ILE B 221 -20.715 3.611 9.139 1.00 20.36 B000 C
ATOM 4933 O ILE B 221 -20.755 4.828 9.353 1.00 24.65 B000 O
ATOM 4934 CB ILE B 221 -18.887 2.146 10.098 1.00 22.60 B000 C
ATOM 4935 CG1 ILE B 221 -18.451 1.456 11.389 1.00 20.42 B000 C
ATOM 4936 CG2 ILE B 221 -17.979 3.319 9.805 1.00 21.44 B000 C
ATOM 4937 CD1 ILE B 221 -17.015 0.881 11.300 1.00 25.27 B000 C
ATOM 4938 N LEU B 222 -20.975 3.097 7.942 1.00 21.25 B000 N
ATOM 4939 CA LEU B 222 -21.337 3.971 6.840 1.00 25.46 B000 C
ATOM 4940 C LEU B 222 -22.627 4.714 7.153 1.00 24.79 B000 C
ATOM 4941 O LEU B 222 -22.732 5.920 6.903 1.00 27.39 B000 O
ATOM 4942 CB LEU B 222 -21.460 3.168 5.542 1.00 24.45 B000 C
ATOM 4943 CG LEU B 222 -20.147 2.537 5.041 1.00 25.78 B000 C
ATOM 4944 CD1 LEU B 222 -20.366 1.758 3.757 1.00 31.81 B000 C
ATOM 4945 CD2 LEU B 222 -19.048 3.584 4.857 1.00 26.35 B000 C
ATOM 4946 N MET B 223 -23.606 4.011 7.723 1.00 21.75 B000 N
ATOM 4947 CA AMET B 223 -24.860 4.658 8.106 0.49 27.49 B000 C
ATOM 4948 CA BMET B 223 -24.855 4.659 8.098 0.51 27.34 B000 C
ATOM 4949 C MET B 223 -24.619 5.766 9.119 1.00 26.26 B000 C
ATOM 4950 O MET B 223 -25.188 6.857 9.006 1.00 25.59 B000 O
ATOM 4951 CB AMET B 223 -25.850 3.632 8.682 0.49 29.58 B000 C
ATOM 4952 CB BMET B 223 -25.816 3.608 8.655 0.51 29.58 B000 C
ATOM 4953 CG AMET B 223 -26.824 4.232 9.725 0.49 33.21 B000 C
ATOM 4954 CG BMET B 223 -27.177 4.118 9.025 0.51 33.49 B000 C
ATOM 4955 SD AMET B 223 -28.008 3.071 10.470 0.49 37.18 B000 S
ATOM 4956 SD BMET B 223 -28.285 2.710 9.036 0.51 37.20 B000 S
ATOM 4957 CE AMET B 223 -26.952 2.188 11.622 0.49 33.49 B000 C
ATOM 4958 CE BMET B 223 -28.315 2.287 7.303 0.51 34.83 B000 C
ATOM 4959 N GLU B 224 -23.772 5.508 10.121 1.00 22.29 B000 N
ATOM 4960 CA GLU B 224 -23.545 6.512 11.157 1.00 21.50 B000 C
ATOM 4961 C GLU B 224 -22.757 7.697 10.632 1.00 26.44 B000 C
ATOM 4962 O GLU B 224 -22.956 8.827 11.094 1.00 22.80 B000 O
ATOM 4963 CB GLU B 224 -22.814 5.893 12.358 1.00 26.28 B000 C
ATOM 4964 CG GLU B 224 -23.649 4.874 13.074 1.00 36.12 B000 C
ATOM 4965 CD GLU B 224 -24.788 5.509 13.852 1.00 44.00 B000 C
ATOM 4966 OE1 GLU B 224 -24.697 6.719 14.170 1.00 50.53 B000 O
ATOM 4967 OE2 GLU B 224 -25.773 4.802 14.142 1.00 48.90 B000 O1-
ATOM 4968 N LEU B 225 -21.844 7.473 9.684 1.00 24.19 B000 N
ATOM 4969 CA LEU B 225 -21.121 8.613 9.139 1.00 21.62 B000 C
ATOM 4970 C LEU B 225 -22.038 9.475 8.274 1.00 20.85 B000 C
ATOM 4971 O LEU B 225 -21.915 10.701 8.282 1.00 24.92 B000 O
ATOM 4972 CB LEU B 225 -19.889 8.132 8.360 1.00 24.67 B000 C
ATOM 4973 CG LEU B 225 -18.720 7.607 9.225 1.00 22.74 B000 C
ATOM 4974 CD1 LEU B 225 -17.599 7.065 8.315 1.00 20.22 B000 C
ATOM 4975 CD2 LEU B 225 -18.160 8.676 10.144 1.00 23.23 B000 C
ATOM 4976 N GLU B 226 -22.985 8.866 7.551 1.00 25.46 B000 N
ATOM 4977 CA GLU B 226 -23.972 9.667 6.821 1.00 25.83 B000 C
ATOM 4978 C GLU B 226 -24.791 10.522 7.780 1.00 23.65 B000 C
ATOM 4979 O GLU B 226 -25.000 11.721 7.540 1.00 25.51 B000 O
ATOM 4980 CB GLU B 226 -24.907 8.776 5.999 1.00 22.21 B000 C
ATOM 4981 CG GLU B 226 -26.050 9.524 5.277 1.00 25.86 B000 C
ATOM 4982 CD GLU B 226 -25.564 10.319 4.060 1.00 36.16 B000 C
ATOM 4983 OE1 GLU B 226 -26.069 11.443 3.799 1.00 49.22 B000 O
ATOM 4984 OE2 GLU B 226 -24.662 9.822 3.350 1.00 46.45 B000 O1-
TER
HETATM 4985 O HOH B 227 -17.400 -23.042 47.417 1.00 49.57 B000 O
ATOM 4986 N ILE B 227 -25.236 9.934 8.887 1.00 22.97 B000 N
ATOM 4987 CA ILE B 227 -25.979 10.706 9.885 1.00 24.56 B000 C
ATOM 4988 C ILE B 227 -25.107 11.803 10.462 1.00 24.61 B000 C
ATOM 4989 O ILE B 227 -25.557 12.944 10.651 1.00 25.46 B000 O
ATOM 4990 CB ILE B 227 -26.526 9.781 10.990 1.00 20.32 B000 C
ATOM 4991 CG1 ILE B 227 -27.635 8.884 10.438 1.00 29.18 B000 C
ATOM 4992 CG2 ILE B 227 -27.042 10.607 12.164 1.00 30.46 B000 C
ATOM 4993 CD1 ILE B 227 -27.917 7.659 11.271 1.00 29.19 B000 C
ATOM 4994 N LEU B 228 -23.840 11.481 10.746 1.00 27.03 B000 N
ATOM 4995 CA LEU B 228 -22.912 12.487 11.256 1.00 27.33 B000 C
ATOM 4996 C LEU B 228 -22.742 13.648 10.275 1.00 26.49 B000 C
ATOM 4997 O LEU B 228 -22.787 14.821 10.673 1.00 25.43 B000 O
ATOM 4998 CB LEU B 228 -21.565 11.839 11.563 1.00 24.78 B000 C
ATOM 4999 CG LEU B 228 -20.607 12.723 12.334 1.00 31.23 B000 C
ATOM 5000 CD1 LEU B 228 -21.191 13.067 13.734 1.00 26.14 B000 C
ATOM 5001 CD2 LEU B 228 -19.262 11.999 12.485 1.00 29.15 B000 C
ATOM 5002 N ARG B 229 -22.513 13.344 8.990 1.00 23.54 B000 N
ATOM 5003 CA ARG B 229 -22.400 14.413 7.989 1.00 26.37 B000 C
ATOM 5004 C ARG B 229 -23.667 15.267 7.947 1.00 26.34 B000 C
ATOM 5005 O ARG B 229 -23.603 16.501 7.864 1.00 24.99 B000 O
ATOM 5006 CB ARG B 229 -22.149 13.835 6.588 1.00 23.63 B000 C
ATOM 5007 CG ARG B 229 -20.783 13.228 6.352 1.00 22.66 B000 C
ATOM 5008 CD ARG B 229 -20.576 12.930 4.881 1.00 22.94 B000 C
ATOM 5009 NE ARG B 229 -21.389 11.816 4.397 1.00 25.39 B000 N
ATOM 5010 CZ ARG B 229 -21.044 10.542 4.527 1.00 24.61 B000 C
ATOM 5011 NH1 ARG B 229 -19.929 10.188 5.157 1.00 22.23 B000 N1+
ATOM 5012 NH2 ARG B 229 -21.808 9.605 3.983 1.00 23.05 B000 N
ATOM 5013 N ASN B 230 -24.829 14.620 7.936 1.00 22.67 B000 N
ATOM 5014 CA ASN B 230 -26.061 15.372 7.740 1.00 28.24 B000 C
ATOM 5015 C ASN B 230 -26.356 16.272 8.933 1.00 29.39 B000 C
ATOM 5016 O ASN B 230 -26.933 17.347 8.767 1.00 26.46 B000 O
ATOM 5017 CB ASN B 230 -27.241 14.434 7.505 1.00 29.76 B000 C
ATOM 5018 CG ASN B 230 -27.091 13.607 6.268 1.00 32.09 B000 C
ATOM 5019 ND2 ASN B 230 -27.830 12.515 6.208 1.00 33.34 B000 N
ATOM 5020 OD1 ASN B 230 -26.314 13.934 5.370 1.00 34.07 B000 O
ATOM 5021 N SER B 231 -25.949 15.862 10.130 1.00 26.78 B000 N
ATOM 5022 CA SER B 231 -26.429 16.491 11.344 1.00 31.62 B000 C
ATOM 5023 C SER B 231 -25.420 17.453 11.953 1.00 28.06 B000 C
ATOM 5024 O SER B 231 -25.743 18.123 12.934 1.00 28.53 B000 O
ATOM 5025 CB SER B 231 -26.826 15.412 12.349 1.00 27.45 B000 C
ATOM 5026 OG SER B 231 -25.679 14.695 12.765 1.00 32.31 B000 O
ATOM 5027 N ALA B 232 -24.230 17.568 11.368 1.00 27.29 B000 N
ATOM 5028 CA ALA B 232 -23.195 18.439 11.890 1.00 30.37 B000 C
ATOM 5029 C ALA B 232 -23.592 19.909 11.768 1.00 29.93 B000 C
ATOM 5030 O ALA B 232 -24.424 20.274 10.930 1.00 31.68 B000 O
ATOM 5031 CB ALA B 232 -21.878 18.191 11.146 1.00 30.12 B000 C
TER
HETATM 5032 O HOH B 232 -5.535 -14.731 58.366 1.00 45.60 B000 O
HETATM 5033 O HOH B 233 -2.112 -13.671 59.235 1.00 51.42 B000 O
ATOM 5034 N PRO B 233 -23.000 20.774 12.593 1.00 32.67 B000 N
ATOM 5035 CA PRO B 233 -23.268 22.212 12.476 1.00 31.73 B000 C
ATOM 5036 C PRO B 233 -22.908 22.737 11.098 1.00 35.40 B000 C
ATOM 5037 O PRO B 233 -22.092 22.155 10.379 1.00 34.62 B000 O
ATOM 5038 CB PRO B 233 -22.376 22.830 13.564 1.00 32.55 B000 C
ATOM 5039 CG PRO B 233 -22.180 21.738 14.562 1.00 36.21 B000 C
ATOM 5040 CD PRO B 233 -22.174 20.456 13.776 1.00 34.45 B000 C
ATOM 5041 N GLU B 234 -23.547 23.851 10.717 1.00 32.41 B000 N
ATOM 5042 CA GLU B 234 -23.188 24.503 9.466 1.00 30.80 B000 C
ATOM 5043 C GLU B 234 -21.685 24.764 9.438 1.00 28.02 B000 C
ATOM 5044 O GLU B 234 -21.109 25.208 10.430 1.00 33.05 B000 O
ATOM 5045 CB GLU B 234 -23.956 25.823 9.296 1.00 31.73 B000 C
ATOM 5046 CG GLU B 234 -25.442 25.637 9.104 1.00 50.66 B000 C
ATOM 5047 CD GLU B 234 -26.195 26.913 8.713 1.00 51.30 B000 C
ATOM 5048 OE1 GLU B 234 -25.549 27.936 8.385 1.00 57.00 B000 O
ATOM 5049 OE2 GLU B 234 -27.448 26.877 8.755 1.00 59.75 B000 O1-
TER
HETATM 5050 O HOH B 234 -6.739 8.893 41.599 1.00 60.41 B000 O
ATOM 5051 N GLY B 235 -21.045 24.465 8.307 1.00 31.64 B000 N
ATOM 5052 CA GLY B 235 -19.623 24.739 8.163 1.00 30.41 B000 C
ATOM 5053 C GLY B 235 -18.686 23.802 8.903 1.00 32.04 B000 C
ATOM 5054 O GLY B 235 -17.477 24.048 8.920 1.00 34.25 B000 O
TER
HETATM 5055 O HOH B 235 -9.031 8.780 42.063 1.00 60.80 B000 O
ATOM 5056 N SER B 236 -19.206 22.737 9.525 1.00 33.90 B000 N
ATOM 5057 CA SER B 236 -18.385 21.795 10.272 1.00 30.34 B000 C
ATOM 5058 C SER B 236 -17.580 20.911 9.320 1.00 35.26 B000 C
ATOM 5059 O SER B 236 -18.086 20.495 8.276 1.00 26.43 B000 O
ATOM 5060 CB SER B 236 -19.242 20.912 11.163 1.00 31.12 B000 C
ATOM 5061 OG SER B 236 -18.534 19.729 11.492 1.00 29.59 B000 O
ATOM 5062 N PRO B 237 -16.325 20.599 9.661 1.00 32.66 B000 N
ATOM 5063 CA PRO B 237 -15.549 19.684 8.811 1.00 29.49 B000 C
ATOM 5064 C PRO B 237 -16.141 18.298 8.763 1.00 25.49 B000 C
ATOM 5065 O PRO B 237 -15.922 17.588 7.775 1.00 28.85 B000 O
ATOM 5066 CB PRO B 237 -14.154 19.667 9.465 1.00 28.01 B000 C
ATOM 5067 CG PRO B 237 -14.094 20.906 10.300 1.00 33.97 B000 C
ATOM 5068 CD PRO B 237 -15.530 21.138 10.776 1.00 30.01 B000 C
ATOM 5069 N LEU B 238 -16.906 17.895 9.784 1.00 23.65 B000 N
ATOM 5070 CA LEU B 238 -17.503 16.563 9.759 1.00 26.46 B000 C
ATOM 5071 C LEU B 238 -18.440 16.370 8.577 1.00 27.07 B000 C
ATOM 5072 O LEU B 238 -18.690 15.222 8.188 1.00 26.85 B000 O
ATOM 5073 CB LEU B 238 -18.226 16.282 11.073 1.00 22.88 B000 C
ATOM 5074 CG LEU B 238 -17.350 16.396 12.326 1.00 29.39 B000 C
ATOM 5075 CD1 LEU B 238 -18.169 16.167 13.597 1.00 28.61 B000 C
ATOM 5076 CD2 LEU B 238 -16.250 15.357 12.264 1.00 27.98 B000 C
ATOM 5077 N ARG B 239 -18.926 17.451 7.960 1.00 23.75 B000 N
ATOM 5078 CA ARG B 239 -19.825 17.283 6.819 1.00 29.75 B000 C
ATOM 5079 C ARG B 239 -19.142 16.593 5.634 1.00 28.35 B000 C
ATOM 5080 O ARG B 239 -19.835 16.028 4.773 1.00 27.26 B000 O
ATOM 5081 CB ARG B 239 -20.427 18.650 6.422 1.00 27.25 B000 C
ATOM 5082 CG ARG B 239 -21.307 18.647 5.161 1.00 28.87 B000 C
ATOM 5083 CD ARG B 239 -22.464 19.664 5.226 1.00 27.61 B000 C
ATOM 5084 NE ARG B 239 -23.430 19.278 6.245 1.00 24.53 B000 N
ATOM 5085 CZ ARG B 239 -23.522 19.846 7.442 1.00 26.96 B000 C
ATOM 5086 NH1 ARG B 239 -22.851 20.952 7.741 1.00 22.64 B000 N1+
ATOM 5087 NH2 ARG B 239 -24.294 19.286 8.369 1.00 25.91 B000 N
TER
HETATM 5088 O HOH B 240 -8.417 9.210 -0.871 1.00 41.42 B000 O
ATOM 5089 N VAL B 240 -17.806 16.588 5.570 1.00 26.59 B000 N
ATOM 5090 CA VAL B 240 -17.133 15.941 4.447 1.00 25.54 B000 C
ATOM 5091 C VAL B 240 -16.240 14.810 4.934 1.00 34.77 B000 C
ATOM 5092 O VAL B 240 -15.247 14.449 4.274 1.00 27.02 B000 O
ATOM 5093 CB VAL B 240 -16.344 16.955 3.582 1.00 27.82 B000 C
ATOM 5094 CG1 VAL B 240 -17.324 17.807 2.745 1.00 31.53 B000 C
ATOM 5095 CG2 VAL B 240 -15.471 17.856 4.446 1.00 29.42 B000 C
TER
HETATM 5096 O HOH B 241 -0.376 19.117 5.410 1.00 54.12 B000 O
ATOM 5097 N LEU B 241 -16.595 14.239 6.085 1.00 28.80 B000 N
ATOM 5098 CA LEU B 241 -15.928 13.038 6.572 1.00 25.75 B000 C
ATOM 5099 C LEU B 241 -16.582 11.812 5.934 1.00 21.99 B000 C
ATOM 5100 O LEU B 241 -17.748 11.502 6.196 1.00 26.31 B000 O
ATOM 5101 CB LEU B 241 -15.974 12.981 8.094 1.00 22.52 B000 C
ATOM 5102 CG LEU B 241 -15.449 11.727 8.774 1.00 25.52 B000 C
ATOM 5103 CD1 LEU B 241 -13.987 11.465 8.351 1.00 21.64 B000 C
ATOM 5104 CD2 LEU B 241 -15.578 11.828 10.305 1.00 24.41 B000 C
TER
HETATM 5105 O HOH B 242 -2.654 24.535 12.390 1.00 41.55 B000 O
ATOM 5106 N TYR B 242 -15.838 11.137 5.074 1.00 24.93 B000 N
ATOM 5107 CA TYR B 242 -16.287 9.955 4.359 1.00 24.28 B000 C
ATOM 5108 C TYR B 242 -15.315 8.822 4.620 1.00 26.46 B000 C
ATOM 5109 O TYR B 242 -14.112 9.043 4.748 1.00 24.87 B000 O
ATOM 5110 CB TYR B 242 -16.363 10.187 2.837 1.00 23.24 B000 C
ATOM 5111 CG TYR B 242 -17.419 11.178 2.393 1.00 28.45 B000 C
ATOM 5112 CD1 TYR B 242 -17.161 12.531 2.354 1.00 28.21 B000 C
ATOM 5113 CD2 TYR B 242 -18.672 10.741 1.994 1.00 20.30 B000 C
ATOM 5114 CE1 TYR B 242 -18.140 13.437 1.926 1.00 24.78 B000 C
ATOM 5115 CE2 TYR B 242 -19.653 11.627 1.587 1.00 27.06 B000 C
ATOM 5116 CZ TYR B 242 -19.377 12.971 1.547 1.00 25.22 B000 C
ATOM 5117 OH TYR B 242 -20.359 13.855 1.150 1.00 32.32 B000 O
TER
HETATM 5118 O HOH B 243 -14.473 12.518 19.218 1.00 41.43 B000 O
ATOM 5119 N SER B 243 -15.813 7.596 4.625 1.00 25.27 B000 N
ATOM 5120 CA SER B 243 -14.907 6.471 4.798 1.00 29.97 B000 C
ATOM 5121 C SER B 243 -14.968 5.506 3.622 1.00 29.15 B000 C
ATOM 5122 O SER B 243 -16.010 5.363 2.978 1.00 29.86 B000 O
ATOM 5123 CB SER B 243 -15.224 5.728 6.082 1.00 27.01 B000 C
ATOM 5124 OG SER B 243 -14.281 4.715 6.299 1.00 30.46 B000 O
ATOM 5125 N GLY B 244 -13.833 4.848 3.339 1.00 20.85 B000 N
ATOM 5126 CA GLY B 244 -13.819 3.626 2.555 1.00 22.95 B000 C
ATOM 5127 C GLY B 244 -13.591 2.461 3.502 1.00 27.50 B000 C
ATOM 5128 O GLY B 244 -12.907 2.607 4.499 1.00 26.22 B000 O
TER
HETATM 5129 O HOH B 245 -19.482 -0.535 21.470 1.00 38.56 B000 O
ATOM 5130 N ILE B 245 -14.170 1.293 3.201 1.00 20.17 B000 N
ATOM 5131 CA ILE B 245 -13.994 0.129 4.068 1.00 23.58 B000 C
ATOM 5132 C ILE B 245 -13.692 -1.100 3.222 1.00 23.18 B000 C
ATOM 5133 O ILE B 245 -14.394 -1.365 2.242 1.00 25.56 B000 O
ATOM 5134 CB ILE B 245 -15.241 -0.132 4.928 1.00 25.04 B000 C
ATOM 5135 CG1 ILE B 245 -15.609 1.087 5.765 1.00 23.29 B000 C
ATOM 5136 CG2 ILE B 245 -15.052 -1.397 5.788 1.00 22.19 B000 C
ATOM 5137 CD1 ILE B 245 -16.777 0.817 6.734 1.00 26.00 B000 C
ATOM 5138 N GLY B 246 -12.687 -1.868 3.616 1.00 21.19 B000 N
ATOM 5139 CA GLY B 246 -12.355 -3.108 2.922 1.00 19.24 B000 C
ATOM 5140 C GLY B 246 -12.310 -4.260 3.898 1.00 20.48 B000 C
ATOM 5141 O GLY B 246 -11.817 -4.116 5.008 1.00 22.45 B000 O
TER
HETATM 5142 O HOH B 246 -20.046 -2.710 22.610 1.00 40.09 B000 O
HETATM 5143 O HOH B 247 -2.888 2.086 17.137 1.00 37.86 B000 O
ATOM 5144 N LEU B 247 -12.836 -5.412 3.476 1.00 19.45 B000 N
ATOM 5145 CA LEU B 247 -12.766 -6.618 4.304 1.00 22.01 B000 C
ATOM 5146 C LEU B 247 -12.083 -7.729 3.524 1.00 23.66 B000 C
ATOM 5147 O LEU B 247 -12.320 -7.892 2.323 1.00 21.04 B000 O
ATOM 5148 CB LEU B 247 -14.151 -7.132 4.757 1.00 23.10 B000 C
ATOM 5149 CG LEU B 247 -15.146 -6.126 5.317 1.00 25.64 B000 C
ATOM 5150 CD1 LEU B 247 -16.526 -6.799 5.522 1.00 21.18 B000 C
ATOM 5151 CD2 LEU B 247 -14.624 -5.522 6.592 1.00 25.22 B000 C
ATOM 5152 N ALA B 248 -11.216 -8.480 4.207 1.00 23.10 B000 N
ATOM 5153 CA ALA B 248 -10.603 -9.660 3.621 1.00 24.75 B000 C
ATOM 5154 C ALA B 248 -10.459 -10.702 4.716 1.00 29.72 B000 C
ATOM 5155 O ALA B 248 -10.725 -10.426 5.886 1.00 30.37 B000 O
ATOM 5156 CB ALA B 248 -9.240 -9.327 2.979 1.00 26.88 B000 C
TER
HETATM 5157 O HOH B 249 -17.356 -15.849 8.479 1.00 46.89 B000 O
ATOM 5158 N LYS B 249 -10.071 -11.918 4.337 1.00 27.56 B000 N
ATOM 5159 CA LYS B 249 -9.627 -12.898 5.321 1.00 34.22 B000 C
ATOM 5160 C LYS B 249 -8.111 -12.930 5.351 1.00 39.14 B000 C
ATOM 5161 O LYS B 249 -7.450 -12.809 4.311 1.00 34.03 B000 O
ATOM 5162 CB LYS B 249 -10.162 -14.301 5.040 1.00 34.85 B000 C
ATOM 5163 CG LYS B 249 -11.645 -14.410 5.186 1.00 38.75 B000 C
ATOM 5164 CD LYS B 249 -12.171 -15.838 5.133 1.00 37.93 B000 C
ATOM 5165 CE LYS B 249 -12.216 -16.488 6.499 1.00 44.60 B000 C
ATOM 5166 NZ LYS B 249 -13.183 -17.626 6.479 1.00 43.43 B000 N1+
ATOM 5167 N GLY B 250 -7.561 -13.084 6.544 1.00 34.66 B000 N
ATOM 5168 CA GLY B 250 -6.120 -13.124 6.702 1.00 36.05 B000 C
ATOM 5169 C GLY B 250 -5.727 -14.187 7.702 1.00 38.08 B000 C
ATOM 5170 O GLY B 250 -6.464 -14.492 8.641 1.00 36.09 B000 O
TER
HETATM 5171 O HOH B 250 -20.878 -15.423 15.547 1.00 59.98 B000 O
HETATM 5172 O HOH B 251 -28.682 -9.385 6.340 1.00 42.06 B000 O
ATOM 5173 N LYS B 251 -4.560 -14.774 7.477 1.00 44.34 B000 N
ATOM 5174 CA LYS B 251 -3.998 -15.709 8.438 1.00 36.98 B000 C
ATOM 5175 C LYS B 251 -3.171 -14.873 9.397 1.00 33.05 B000 C
ATOM 5176 O LYS B 251 -2.110 -14.359 9.028 1.00 42.22 B000 O
ATOM 5177 CB LYS B 251 -3.150 -16.774 7.754 1.00 40.18 B000 C
ATOM 5178 CG LYS B 251 -2.339 -17.614 8.753 1.00 52.17 B000 C
ATOM 5179 CD LYS B 251 -1.172 -18.352 8.081 1.00 52.16 B000 C
ATOM 5180 CE LYS B 251 0.171 -17.900 8.651 1.00 44.41 B000 C
ATOM 5181 NZ LYS B 251 0.513 -16.460 8.321 1.00 49.64 B000 N1+
TER
HETATM 5182 O HOH B 252 -30.747 -14.274 6.134 1.00 52.55 B000 O
ATOM 5183 N VAL B 252 -3.663 -14.689 10.603 1.00 27.12 B000 N
ATOM 5184 CA VAL B 252 -2.910 -13.939 11.573 1.00 37.23 B000 C
ATOM 5185 C VAL B 252 -2.213 -14.943 12.475 1.00 34.47 B000 C
ATOM 5186 O VAL B 252 -2.572 -16.122 12.539 1.00 31.71 B000 O
ATOM 5187 CB VAL B 252 -3.777 -12.937 12.368 1.00 37.36 B000 C
ATOM 5188 CG1 VAL B 252 -5.041 -12.632 11.601 1.00 38.93 B000 C
ATOM 5189 CG2 VAL B 252 -4.033 -13.408 13.770 1.00 33.42 B000 C
ATOM 5190 N ILE B 253 -1.158 -14.483 13.126 1.00 33.43 B000 N
ATOM 5191 CA ILE B 253 -0.423 -15.292 14.083 1.00 32.92 B000 C
ATOM 5192 C ILE B 253 -0.587 -14.628 15.436 1.00 34.86 B000 C
ATOM 5193 O ILE B 253 -0.303 -13.433 15.580 1.00 36.50 B000 O
ATOM 5194 CB ILE B 253 1.060 -15.433 13.693 1.00 34.30 B000 C
ATOM 5195 CG1 ILE B 253 1.188 -16.188 12.377 1.00 35.14 B000 C
ATOM 5196 CG2 ILE B 253 1.827 -16.168 14.777 1.00 35.62 B000 C
ATOM 5197 CD1 ILE B 253 2.607 -16.237 11.844 1.00 34.52 B000 C
ATOM 5198 N GLU B 254 -1.103 -15.382 16.406 1.00 39.31 B000 N
ATOM 5199 CA GLU B 254 -1.137 -14.961 17.798 1.00 36.81 B000 C
ATOM 5200 C GLU B 254 0.112 -15.489 18.523 1.00 42.11 B000 C
ATOM 5201 O GLU B 254 0.635 -16.557 18.194 1.00 36.19 B000 O
ATOM 5202 CB GLU B 254 -2.433 -15.453 18.459 1.00 44.61 B000 C
ATOM 5203 CG GLU B 254 -3.711 -14.901 17.772 1.00 43.87 B000 C
ATOM 5204 CD GLU B 254 -5.049 -15.336 18.400 1.00 54.79 B000 C
ATOM 5205 OE1 GLU B 254 -5.122 -16.444 18.992 1.00 54.12 B000 O
ATOM 5206 OE2 GLU B 254 -6.032 -14.549 18.300 1.00 48.00 B000 O1-
ATOM 5207 N GLY B 255 0.628 -14.701 19.460 1.00 42.50 B000 N
ATOM 5208 CA GLY B 255 1.829 -15.081 20.180 1.00 40.58 B000 C
ATOM 5209 C GLY B 255 2.411 -13.907 20.946 1.00 41.41 B000 C
ATOM 5210 O GLY B 255 1.805 -12.838 21.035 1.00 43.29 B000 O
ATOM 5211 N ASN B 256 3.600 -14.144 21.514 1.00 34.66 B000 N
ATOM 5212 CA ASN B 256 4.402 -13.098 22.165 1.00 38.35 B000 C
ATOM 5213 C ASN B 256 5.382 -12.572 21.119 1.00 39.11 B000 C
ATOM 5214 O ASN B 256 6.470 -13.117 20.922 1.00 35.48 B000 O
ATOM 5215 CB ASN B 256 5.119 -13.632 23.406 1.00 45.38 B000 C
ATOM 5216 CG ASN B 256 5.874 -12.536 24.181 1.00 50.36 B000 C
ATOM 5217 ND2 ASN B 256 6.791 -12.954 25.041 1.00 58.28 B000 N
ATOM 5218 OD1 ASN B 256 5.627 -11.341 24.014 1.00 46.78 B000 O
TER
HETATM 5219 O HOH B 257 -22.292 2.558 -6.188 1.00 53.80 B000 O
ATOM 5220 N ILE B 257 4.981 -11.495 20.448 1.00 40.18 B000 N
ATOM 5221 CA ILE B 257 5.638 -11.005 19.244 1.00 40.19 B000 C
ATOM 5222 C ILE B 257 6.209 -9.624 19.513 1.00 40.60 B000 C
ATOM 5223 O ILE B 257 5.552 -8.785 20.134 1.00 35.44 B000 O
ATOM 5224 CB ILE B 257 4.655 -10.962 18.053 1.00 41.28 B000 C
ATOM 5225 CG1 ILE B 257 4.129 -12.369 17.729 1.00 36.90 B000 C
ATOM 5226 CG2 ILE B 257 5.301 -10.291 16.852 1.00 37.50 B000 C
ATOM 5227 CD1 ILE B 257 2.642 -12.406 17.388 1.00 33.35 B000 C
ATOM 5228 N GLY B 258 7.424 -9.379 19.036 1.00 32.88 B000 N
ATOM 5229 CA GLY B 258 7.952 -8.039 19.154 1.00 34.72 B000 C
ATOM 5230 C GLY B 258 9.413 -7.997 19.513 1.00 36.56 B000 C
ATOM 5231 O GLY B 258 10.148 -8.956 19.255 1.00 44.72 B000 O
ATOM 5232 N SER B 259 9.843 -6.906 20.141 1.00 44.98 B000 N
ATOM 5233 CA SER B 259 11.259 -6.582 20.249 1.00 44.85 B000 C
ATOM 5234 C SER B 259 11.804 -6.689 21.668 1.00 53.86 B000 C
ATOM 5235 O SER B 259 12.914 -6.207 21.920 1.00 62.65 B000 O
ATOM 5236 CB SER B 259 11.492 -5.168 19.724 1.00 42.92 B000 C
ATOM 5237 OG SER B 259 10.756 -4.231 20.497 1.00 45.04 B000 O
ATOM 5238 N GLU B 260 11.051 -7.276 22.603 1.00 49.29 B000 N
ATOM 5239 CA GLU B 260 11.406 -7.271 24.026 1.00 66.01 B000 C
ATOM 5240 C GLU B 260 11.307 -5.861 24.610 1.00 62.75 B000 C
ATOM 5241 O GLU B 260 10.825 -5.690 25.736 1.00 66.36 B000 O
ATOM 5242 CB GLU B 260 12.803 -7.865 24.269 1.00 69.71 B000 C
TER
HETATM 5243 O HOH B 260 -18.959 0.505 -8.666 1.00 54.97 B000 O
HETATM 5244 O HOH B 261 -15.142 -18.434 2.067 1.00 45.82 B000 O
ATOM 5245 N LEU B 261 11.753 -4.846 23.866 1.00 55.87 B000 N
ATOM 5246 CA LEU B 261 11.326 -3.476 24.131 1.00 60.51 B000 C
ATOM 5247 C LEU B 261 9.803 -3.406 23.998 1.00 62.67 B000 C
ATOM 5248 O LEU B 261 9.094 -3.246 24.997 1.00 60.19 B000 O
ATOM 5249 CB LEU B 261 12.017 -2.491 23.168 1.00 63.40 B000 C
ATOM 5250 CG LEU B 261 11.763 -0.967 23.250 1.00 68.44 B000 C
ATOM 5251 CD1 LEU B 261 13.054 -0.144 23.054 1.00 57.19 B000 C
ATOM 5252 CD2 LEU B 261 10.690 -0.498 22.263 1.00 68.28 B000 C
ATOM 5253 N LYS B 262 9.290 -3.572 22.779 1.00 57.76 B000 N
ATOM 5254 CA LYS B 262 7.866 -3.463 22.481 1.00 47.99 B000 C
ATOM 5255 C LYS B 262 7.288 -4.799 22.037 1.00 50.43 B000 C
ATOM 5256 O LYS B 262 7.887 -5.494 21.208 1.00 44.66 B000 O
ATOM 5257 CB LYS B 262 7.615 -2.408 21.411 1.00 54.81 B000 C
ATOM 5258 CG LYS B 262 6.161 -2.325 20.984 1.00 54.77 B000 C
ATOM 5259 CD LYS B 262 5.405 -1.282 21.753 1.00 61.96 B000 C
ATOM 5260 CE LYS B 262 4.078 -1.846 22.208 1.00 54.77 B000 C
ATOM 5261 NZ LYS B 262 3.498 -2.748 21.173 1.00 48.96 B000 N1+
ATOM 5262 N ARG B 263 6.119 -5.143 22.584 1.00 46.31 B000 N
ATOM 5263 CA ARG B 263 5.479 -6.428 22.359 1.00 41.04 B000 C
ATOM 5264 C ARG B 263 4.080 -6.209 21.812 1.00 49.04 B000 C
ATOM 5265 O ARG B 263 3.507 -5.120 21.923 1.00 45.68 B000 O
ATOM 5266 CB ARG B 263 5.395 -7.265 23.654 1.00 44.59 B000 C
ATOM 5267 CG ARG B 263 6.739 -7.840 24.123 1.00 43.95 B000 C
ATOM 5268 CD ARG B 263 7.240 -8.891 23.145 1.00 50.08 B000 C
ATOM 5269 NE ARG B 263 8.463 -9.557 23.577 1.00 60.02 B000 N
ATOM 5270 CZ ARG B 263 8.985 -10.620 22.974 1.00 61.66 B000 C
ATOM 5271 NH1 ARG B 263 8.401 -11.175 21.920 1.00 55.94 B000 N1+
ATOM 5272 NH2 ARG B 263 10.130 -11.129 23.427 1.00 60.50 B000 N
ATOM 5273 N ASP B 264 3.543 -7.270 21.211 1.00 38.50 B000 N
ATOM 5274 CA ASP B 264 2.141 -7.338 20.830 1.00 43.25 B000 C
ATOM 5275 C ASP B 264 1.741 -8.802 20.810 1.00 40.55 B000 C
ATOM 5276 O ASP B 264 2.577 -9.708 20.906 1.00 40.29 B000 O
ATOM 5277 CB ASP B 264 1.862 -6.673 19.475 1.00 49.57 B000 C
ATOM 5278 CG ASP B 264 0.389 -6.264 19.307 1.00 52.88 B000 C
ATOM 5279 OD1 ASP B 264 -0.522 -6.988 19.782 1.00 54.83 B000 O
ATOM 5280 OD2 ASP B 264 0.144 -5.195 18.709 1.00 64.65 B000 O1-
ATOM 5281 N TYR B 265 0.440 -9.018 20.701 1.00 45.29 B000 N
ATOM 5282 CA TYR B 265 -0.160 -10.335 20.814 1.00 45.99 B000 C
ATOM 5283 C TYR B 265 -0.484 -10.923 19.432 1.00 36.83 B000 C
ATOM 5284 O TYR B 265 -0.744 -12.127 19.308 1.00 38.99 B000 O
ATOM 5285 CB TYR B 265 -1.401 -10.189 21.733 1.00 47.20 B000 C
ATOM 5286 CG TYR B 265 -2.581 -11.103 21.536 1.00 47.89 B000 C
ATOM 5287 CD1 TYR B 265 -2.430 -12.487 21.572 1.00 59.18 B000 C
ATOM 5288 CD2 TYR B 265 -3.853 -10.585 21.286 1.00 54.74 B000 C
ATOM 5289 CE1 TYR B 265 -3.526 -13.336 21.399 1.00 57.27 B000 C
ATOM 5290 CE2 TYR B 265 -4.950 -11.420 21.102 1.00 52.79 B000 C
ATOM 5291 CZ TYR B 265 -4.777 -12.798 21.162 1.00 59.10 B000 C
ATOM 5292 OH TYR B 265 -5.847 -13.651 20.977 1.00 71.92 B000 O
ATOM 5293 N THR B 266 -0.395 -10.121 18.375 1.00 38.83 B000 N
ATOM 5294 CA THR B 266 -0.818 -10.580 17.059 1.00 32.31 B000 C
ATOM 5295 C THR B 266 0.072 -9.981 15.968 1.00 32.42 B000 C
ATOM 5296 O THR B 266 0.676 -8.921 16.142 1.00 31.70 B000 O
ATOM 5297 CB THR B 266 -2.293 -10.222 16.861 1.00 30.28 B000 C
ATOM 5298 CG2 THR B 266 -2.453 -8.728 16.770 1.00 30.70 B000 C
ATOM 5299 OG1 THR B 266 -2.790 -10.860 15.683 1.00 52.05 B000 O
ATOM 5300 N ILE B 267 0.145 -10.677 14.836 1.00 30.32 B000 N
ATOM 5301 CA ILE B 267 0.794 -10.170 13.619 1.00 31.54 B000 C
ATOM 5302 C ILE B 267 0.027 -10.701 12.411 1.00 29.09 B000 C
ATOM 5303 O ILE B 267 -0.296 -11.891 12.341 1.00 34.16 B000 O
ATOM 5304 CB ILE B 267 2.296 -10.549 13.523 1.00 28.44 B000 C
ATOM 5305 CG1 ILE B 267 2.939 -9.937 12.272 1.00 32.41 B000 C
ATOM 5306 CG2 ILE B 267 2.515 -12.054 13.459 1.00 24.74 B000 C
ATOM 5307 CD1 ILE B 267 4.469 -9.916 12.339 1.00 34.51 B000 C
ATOM 5308 N LEU B 268 -0.277 -9.807 11.470 1.00 30.36 B000 N
ATOM 5309 CA LEU B 268 -0.802 -10.157 10.149 1.00 31.27 B000 C
ATOM 5310 C LEU B 268 0.242 -9.758 9.108 1.00 27.11 B000 C
ATOM 5311 O LEU B 268 0.394 -8.571 8.798 1.00 26.02 B000 O
ATOM 5312 CB LEU B 268 -2.131 -9.451 9.881 1.00 28.48 B000 C
ATOM 5313 CG LEU B 268 -2.651 -9.566 8.445 1.00 31.21 B000 C
ATOM 5314 CD1 LEU B 268 -3.155 -10.960 8.187 1.00 33.86 B000 C
ATOM 5315 CD2 LEU B 268 -3.797 -8.553 8.185 1.00 29.81 B000 C
ATOM 5316 N GLY B 269 0.958 -10.742 8.575 1.00 30.75 B000 N
ATOM 5317 CA GLY B 269 1.971 -10.440 7.573 1.00 34.52 B000 C
ATOM 5318 C GLY B 269 1.371 -9.714 6.381 1.00 32.82 B000 C
ATOM 5319 O GLY B 269 0.274 -10.039 5.920 1.00 36.66 B000 O
ATOM 5320 N ASP B 270 2.077 -8.677 5.915 1.00 35.64 B000 N
ATOM 5321 CA ASP B 270 1.671 -7.915 4.715 1.00 43.72 B000 C
ATOM 5322 C ASP B 270 0.317 -7.219 4.898 1.00 38.76 B000 C
ATOM 5323 O ASP B 270 -0.440 -7.024 3.934 1.00 32.59 B000 O
ATOM 5324 CB ASP B 270 1.642 -8.804 3.465 1.00 45.99 B000 C
ATOM 5325 CG ASP B 270 3.009 -9.409 3.145 1.00 46.05 B000 C
ATOM 5326 OD1 ASP B 270 4.047 -8.811 3.523 1.00 41.43 B000 O
ATOM 5327 OD2 ASP B 270 3.036 -10.495 2.529 1.00 43.67 B000 O1-
ATOM 5328 N ALA B 271 0.007 -6.860 6.148 1.00 32.92 B000 N
ATOM 5329 CA ALA B 271 -1.131 -5.995 6.438 1.00 26.37 B000 C
ATOM 5330 C ALA B 271 -1.044 -4.678 5.665 1.00 30.44 B000 C
ATOM 5331 O ALA B 271 -2.062 -4.168 5.170 1.00 29.32 B000 O
ATOM 5332 CB ALA B 271 -1.193 -5.724 7.948 1.00 30.19 B000 C
TER
HETATM 5333 O HOH B 271 -18.637 7.244 -3.554 1.00 62.79 B000 O
ATOM 5334 N VAL B 272 0.168 -4.115 5.565 1.00 28.27 B000 N
ATOM 5335 CA VAL B 272 0.418 -2.895 4.789 1.00 30.01 B000 C
ATOM 5336 C VAL B 272 -0.165 -3.014 3.387 1.00 34.87 B000 C
ATOM 5337 O VAL B 272 -0.850 -2.107 2.893 1.00 27.62 B000 O
ATOM 5338 CB VAL B 272 1.932 -2.606 4.723 1.00 39.55 B000 C
ATOM 5339 CG1 VAL B 272 2.268 -1.675 3.538 1.00 30.89 B000 C
ATOM 5340 CG2 VAL B 272 2.403 -2.006 6.010 1.00 34.50 B000 C
ATOM 5341 N ASN B 273 0.100 -4.136 2.730 1.00 27.97 B000 N
ATOM 5342 CA ASN B 273 -0.252 -4.262 1.321 1.00 35.97 B000 C
ATOM 5343 C ASN B 273 -1.727 -4.592 1.131 1.00 27.58 B000 C
ATOM 5344 O ASN B 273 -2.343 -4.121 0.172 1.00 28.43 B000 O
ATOM 5345 CB ASN B 273 0.644 -5.318 0.679 1.00 34.54 B000 C
ATOM 5346 CG ASN B 273 2.118 -5.101 1.030 1.00 48.50 B000 C
ATOM 5347 ND2 ASN B 273 2.582 -5.807 2.071 1.00 39.85 B000 N
ATOM 5348 OD1 ASN B 273 2.813 -4.267 0.414 1.00 48.33 B000 O
TER
HETATM 5349 O HOH B 274 -5.302 7.094 1.011 1.00 38.13 B000 O
ATOM 5350 N VAL B 274 -2.308 -5.411 2.015 1.00 27.58 B000 N
ATOM 5351 CA VAL B 274 -3.748 -5.647 1.959 1.00 22.78 B000 C
ATOM 5352 C VAL B 274 -4.509 -4.342 2.195 1.00 30.40 B000 C
ATOM 5353 O VAL B 274 -5.474 -4.030 1.479 1.00 30.26 B000 O
ATOM 5354 CB VAL B 274 -4.157 -6.745 2.957 1.00 29.01 B000 C
ATOM 5355 CG1 VAL B 274 -5.672 -6.853 3.052 1.00 29.05 B000 C
ATOM 5356 CG2 VAL B 274 -3.542 -8.088 2.571 1.00 27.26 B000 C
ATOM 5357 N ALA B 275 -4.077 -3.542 3.174 1.00 22.75 B000 N
ATOM 5358 CA ALA B 275 -4.741 -2.252 3.404 1.00 29.42 B000 C
ATOM 5359 C ALA B 275 -4.620 -1.351 2.180 1.00 30.64 B000 C
ATOM 5360 O ALA B 275 -5.613 -0.784 1.707 1.00 25.21 B000 O
ATOM 5361 CB ALA B 275 -4.148 -1.543 4.621 1.00 24.69 B000 C
ATOM 5362 N ALA B 276 -3.398 -1.222 1.643 1.00 25.00 B000 N
ATOM 5363 CA ALA B 276 -3.180 -0.359 0.488 1.00 28.82 B000 C
ATOM 5364 C ALA B 276 -4.023 -0.798 -0.704 1.00 23.97 B000 C
ATOM 5365 O ALA B 276 -4.586 0.040 -1.411 1.00 27.98 B000 O
ATOM 5366 CB ALA B 276 -1.700 -0.348 0.125 1.00 26.51 B000 C
TER
HETATM 5367 O HOH B 276 -25.581 11.031 -2.225 1.00 41.85 B000 O
ATOM 5368 N ARG B 277 -4.147 -2.109 -0.927 1.00 26.14 B000 N
ATOM 5369 CA ARG B 277 -4.924 -2.592 -2.061 1.00 25.42 B000 C
ATOM 5370 C ARG B 277 -6.425 -2.405 -1.857 1.00 32.03 B000 C
ATOM 5371 O ARG B 277 -7.153 -2.150 -2.822 1.00 25.05 B000 O
ATOM 5372 CB ARG B 277 -4.600 -4.056 -2.341 1.00 28.85 B000 C
ATOM 5373 CG ARG B 277 -3.356 -4.209 -3.194 1.00 43.04 B000 C
ATOM 5374 CD ARG B 277 -2.547 -5.426 -2.833 1.00 47.98 B000 C
ATOM 5375 NE ARG B 277 -1.132 -5.217 -3.137 1.00 60.12 B000 N
ATOM 5376 CZ ARG B 277 -0.157 -6.035 -2.763 1.00 58.65 B000 C
ATOM 5377 NH1 ARG B 277 -0.402 -7.113 -2.036 1.00 53.09 B000 N1+
ATOM 5378 NH2 ARG B 277 1.099 -5.754 -3.113 1.00 67.71 B000 N
TER
HETATM 5379 O HOH B 277 -20.363 9.320 -4.410 1.00 67.08 B000 O
HETATM 5380 O HOH B 278 -27.419 -11.903 51.903 1.00 52.32 B000 O
ATOM 5381 N LEU B 278 -6.909 -2.572 -0.627 1.00 23.53 B000 N
ATOM 5382 CA LEU B 278 -8.310 -2.299 -0.344 1.00 26.05 B000 C
ATOM 5383 C LEU B 278 -8.631 -0.818 -0.520 1.00 25.99 B000 C
ATOM 5384 O LEU B 278 -9.696 -0.461 -1.039 1.00 26.23 B000 O
ATOM 5385 CB LEU B 278 -8.659 -2.776 1.075 1.00 24.73 B000 C
ATOM 5386 CG LEU B 278 -8.677 -4.309 1.178 1.00 21.45 B000 C
ATOM 5387 CD1 LEU B 278 -8.696 -4.732 2.631 1.00 22.77 B000 C
ATOM 5388 CD2 LEU B 278 -9.881 -4.879 0.404 1.00 25.56 B000 C
ATOM 5389 N GLU B 279 -7.736 0.059 -0.073 1.00 26.75 B000 N
ATOM 5390 CA GLU B 279 -7.939 1.486 -0.282 1.00 31.52 B000 C
ATOM 5391 C GLU B 279 -7.973 1.828 -1.761 1.00 28.89 B000 C
ATOM 5392 O GLU B 279 -8.762 2.681 -2.180 1.00 30.42 B000 O
ATOM 5393 CB GLU B 279 -6.846 2.285 0.420 1.00 32.54 B000 C
ATOM 5394 CG GLU B 279 -7.014 2.351 1.911 1.00 36.82 B000 C
ATOM 5395 CD GLU B 279 -6.057 3.354 2.550 1.00 43.76 B000 C
ATOM 5396 OE1 GLU B 279 -5.551 4.234 1.810 1.00 42.93 B000 O
ATOM 5397 OE2 GLU B 279 -5.837 3.275 3.794 1.00 35.35 B000 O1-
ATOM 5398 N ALA B 280 -7.124 1.184 -2.572 1.00 27.02 B000 N
ATOM 5399 CA ALA B 280 -7.154 1.465 -4.010 1.00 29.28 B000 C
ATOM 5400 C ALA B 280 -8.495 1.079 -4.594 1.00 29.58 B000 C
ATOM 5401 O ALA B 280 -9.017 1.764 -5.484 1.00 32.31 B000 O
ATOM 5402 CB ALA B 280 -6.028 0.735 -4.753 1.00 28.90 B000 C
TER
HETATM 5403 O HOH B 281 -25.327 2.208 14.857 1.00 52.03 B000 O
ATOM 5404 N LEU B 281 -9.096 0.009 -4.078 1.00 28.48 B000 N
ATOM 5405 CA LEU B 281 -10.363 -0.447 -4.640 1.00 24.69 B000 C
ATOM 5406 C LEU B 281 -11.521 0.467 -4.255 1.00 29.98 B000 C
ATOM 5407 O LEU B 281 -12.403 0.733 -5.079 1.00 26.96 B000 O
ATOM 5408 CB LEU B 281 -10.630 -1.877 -4.199 1.00 24.50 B000 C
ATOM 5409 CG LEU B 281 -9.933 -2.972 -4.995 1.00 33.22 B000 C
ATOM 5410 CD1 LEU B 281 -9.937 -4.241 -4.174 1.00 30.92 B000 C
ATOM 5411 CD2 LEU B 281 -10.677 -3.218 -6.311 1.00 30.70 B000 C
ATOM 5412 N THR B 282 -11.571 0.936 -3.008 1.00 28.40 B000 N
ATOM 5413 CA THR B 282 -12.687 1.803 -2.648 1.00 31.75 B000 C
ATOM 5414 C THR B 282 -12.624 3.105 -3.436 1.00 32.25 B000 C
ATOM 5415 O THR B 282 -13.662 3.629 -3.862 1.00 42.78 B000 O
ATOM 5416 CB THR B 282 -12.730 2.090 -1.140 1.00 28.54 B000 C
ATOM 5417 CG2 THR B 282 -12.922 0.816 -0.309 1.00 24.90 B000 C
ATOM 5418 OG1 THR B 282 -11.532 2.760 -0.731 1.00 27.01 B000 O
ATOM 5419 N ARG B 283 -11.414 3.629 -3.659 1.00 29.35 B000 N
ATOM 5420 CA ARG B 283 -11.250 4.815 -4.506 1.00 30.22 B000 C
ATOM 5421 C ARG B 283 -11.646 4.518 -5.946 1.00 34.87 B000 C
ATOM 5422 O ARG B 283 -12.375 5.287 -6.578 1.00 39.08 B000 O
ATOM 5423 CB ARG B 283 -9.800 5.298 -4.480 1.00 33.26 B000 C
ATOM 5424 CG ARG B 283 -9.248 5.555 -3.100 1.00 44.52 B000 C
ATOM 5425 CD ARG B 283 -9.862 6.792 -2.471 1.00 50.89 B000 C
ATOM 5426 NE ARG B 283 -10.030 6.676 -1.022 1.00 56.37 B000 N
ATOM 5427 CZ ARG B 283 -9.085 6.319 -0.154 1.00 45.93 B000 C
ATOM 5428 NH1 ARG B 283 -7.831 6.105 -0.525 1.00 57.67 B000 N1+
ATOM 5429 NH2 ARG B 283 -9.402 6.206 1.130 1.00 48.62 B000 N
ATOM 5430 N GLN B 284 -11.173 3.395 -6.477 1.00 35.19 B000 N
ATOM 5431 CA GLN B 284 -11.361 3.097 -7.892 1.00 40.07 B000 C
ATOM 5432 C GLN B 284 -12.809 2.759 -8.214 1.00 46.35 B000 C
ATOM 5433 O GLN B 284 -13.289 3.089 -9.304 1.00 44.76 B000 O
ATOM 5434 CB GLN B 284 -10.425 1.956 -8.307 1.00 40.11 B000 C
ATOM 5435 CG GLN B 284 -10.445 1.617 -9.791 1.00 40.84 B000 C
ATOM 5436 CD GLN B 284 -11.224 0.358 -10.094 1.00 42.71 B000 C
ATOM 5437 NE2 GLN B 284 -12.302 0.494 -10.877 1.00 45.71 B000 N
ATOM 5438 OE1 GLN B 284 -10.865 -0.733 -9.631 1.00 40.75 B000 O
TER
HETATM 5439 O HOH B 284 -17.590 -13.152 -11.553 1.00 45.35 B000 O
HETATM 5440 O HOH B 285 1.817 10.687 62.330 1.00 49.39 B000 O
ATOM 5441 N LEU B 285 -13.514 2.114 -7.291 1.00 38.35 B000 N
ATOM 5442 CA LEU B 285 -14.844 1.594 -7.563 1.00 42.95 B000 C
ATOM 5443 C LEU B 285 -15.954 2.553 -7.194 1.00 44.90 B000 C
ATOM 5444 O LEU B 285 -17.123 2.256 -7.478 1.00 47.75 B000 O
ATOM 5445 CB LEU B 285 -15.060 0.280 -6.816 1.00 33.74 B000 C
ATOM 5446 CG LEU B 285 -14.272 -0.875 -7.428 1.00 39.68 B000 C
ATOM 5447 CD1 LEU B 285 -14.302 -2.089 -6.496 1.00 30.69 B000 C
ATOM 5448 CD2 LEU B 285 -14.858 -1.204 -8.798 1.00 41.33 B000 C
TER
HETATM 5449 O HOH B 286 6.255 2.817 66.089 1.00 41.45 B000 O
ATOM 5450 N SER B 286 -15.628 3.685 -6.578 1.00 46.08 B000 N
ATOM 5451 CA SER B 286 -16.651 4.586 -6.061 1.00 55.84 B000 C
ATOM 5452 C SER B 286 -17.628 3.809 -5.187 1.00 50.79 B000 C
ATOM 5453 O SER B 286 -18.839 4.022 -5.220 1.00 49.46 B000 O
ATOM 5454 CB SER B 286 -17.380 5.305 -7.198 1.00 60.35 B000 C
ATOM 5455 OG SER B 286 -16.467 5.719 -8.206 1.00 58.58 B000 O
ATOM 5456 N GLN B 287 -17.091 2.863 -4.423 1.00 48.49 B000 N
ATOM 5457 CA GLN B 287 -17.905 2.013 -3.568 1.00 47.48 B000 C
ATOM 5458 C GLN B 287 -17.335 2.077 -2.169 1.00 35.16 B000 C
ATOM 5459 O GLN B 287 -16.141 1.845 -1.976 1.00 43.61 B000 O
ATOM 5460 CB GLN B 287 -17.933 0.570 -4.061 1.00 43.85 B000 C
ATOM 5461 CG GLN B 287 -19.218 -0.137 -3.685 1.00 48.31 B000 C
ATOM 5462 CD GLN B 287 -20.189 -0.235 -4.827 1.00 46.20 B000 C
ATOM 5463 NE2 GLN B 287 -21.416 -0.638 -4.502 1.00 53.62 B000 N
ATOM 5464 OE1 GLN B 287 -19.853 0.042 -6.000 1.00 39.14 B000 O
ATOM 5465 N ALA B 288 -18.168 2.434 -1.198 1.00 28.93 B000 N
ATOM 5466 CA ALA B 288 -17.629 2.676 0.132 1.00 28.96 B000 C
ATOM 5467 C ALA B 288 -17.238 1.387 0.840 1.00 28.37 B000 C
ATOM 5468 O ALA B 288 -16.488 1.430 1.812 1.00 34.47 B000 O
ATOM 5469 CB ALA B 288 -18.644 3.452 0.976 1.00 26.64 B000 C
ATOM 5470 N LEU B 289 -17.763 0.255 0.407 1.00 24.73 B000 N
ATOM 5471 CA LEU B 289 -17.522 -1.015 1.053 1.00 25.32 B000 C
ATOM 5472 C LEU B 289 -17.177 -2.017 -0.026 1.00 29.06 B000 C
ATOM 5473 O LEU B 289 -17.938 -2.171 -0.989 1.00 24.50 B000 O
ATOM 5474 CB LEU B 289 -18.750 -1.476 1.834 1.00 25.38 B000 C
ATOM 5475 CG LEU B 289 -18.680 -2.891 2.404 1.00 23.28 B000 C
ATOM 5476 CD1 LEU B 289 -17.553 -3.063 3.420 1.00 19.31 B000 C
ATOM 5477 CD2 LEU B 289 -20.035 -3.211 3.039 1.00 23.66 B000 C
ATOM 5478 N VAL B 290 -16.018 -2.664 0.111 1.00 19.68 B000 N
ATOM 5479 CA VAL B 290 -15.611 -3.745 -0.777 1.00 23.42 B000 C
ATOM 5480 C VAL B 290 -15.130 -4.903 0.086 1.00 23.40 B000 C
ATOM 5481 O VAL B 290 -14.623 -4.704 1.191 1.00 25.55 B000 O
ATOM 5482 CB VAL B 290 -14.517 -3.317 -1.796 1.00 21.54 B000 C
ATOM 5483 CG1 VAL B 290 -14.984 -2.098 -2.600 1.00 21.45 B000 C
ATOM 5484 CG2 VAL B 290 -13.151 -3.058 -1.109 1.00 21.09 B000 C
ATOM 5485 N PHE B 291 -15.331 -6.131 -0.398 1.00 19.73 B000 N
ATOM 5486 CA PHE B 291 -14.783 -7.269 0.318 1.00 21.93 B000 C
ATOM 5487 C PHE B 291 -14.539 -8.391 -0.668 1.00 22.63 B000 C
ATOM 5488 O PHE B 291 -15.088 -8.417 -1.774 1.00 22.37 B000 O
ATOM 5489 CB PHE B 291 -15.667 -7.740 1.497 1.00 19.45 B000 C
ATOM 5490 CG PHE B 291 -17.137 -7.814 1.184 1.00 19.95 B000 C
ATOM 5491 CD1 PHE B 291 -17.690 -8.968 0.649 1.00 21.08 B000 C
ATOM 5492 CD2 PHE B 291 -17.975 -6.743 1.476 1.00 19.06 B000 C
ATOM 5493 CE1 PHE B 291 -19.040 -9.034 0.354 1.00 20.79 B000 C
ATOM 5494 CE2 PHE B 291 -19.333 -6.792 1.176 1.00 21.57 B000 C
ATOM 5495 CZ PHE B 291 -19.865 -7.938 0.610 1.00 25.07 B000 C
ATOM 5496 N SER B 292 -13.675 -9.304 -0.256 1.00 24.65 B000 N
ATOM 5497 CA SER B 292 -13.220 -10.387 -1.108 1.00 28.98 B000 C
ATOM 5498 C SER B 292 -14.242 -11.519 -1.161 1.00 27.07 B000 C
ATOM 5499 O SER B 292 -15.121 -11.641 -0.317 1.00 23.79 B000 O
ATOM 5500 CB SER B 292 -11.906 -10.939 -0.585 1.00 27.21 B000 C
ATOM 5501 OG SER B 292 -12.124 -11.477 0.704 1.00 25.77 B000 O
ATOM 5502 N SER B 293 -14.060 -12.374 -2.159 1.00 25.86 B000 N
ATOM 5503 CA SER B 293 -14.837 -13.588 -2.323 1.00 27.57 B000 C
ATOM 5504 C SER B 293 -14.838 -14.439 -1.069 1.00 26.29 B000 C
ATOM 5505 O SER B 293 -15.881 -14.980 -0.683 1.00 30.75 B000 O
ATOM 5506 CB SER B 293 -14.261 -14.393 -3.493 1.00 27.06 B000 C
ATOM 5507 OG SER B 293 -14.974 -15.590 -3.655 1.00 33.46 B000 O
ATOM 5508 N GLU B 294 -13.671 -14.608 -0.442 1.00 24.21 B000 N
ATOM 5509 CA GLU B 294 -13.598 -15.409 0.776 1.00 29.84 B000 C
ATOM 5510 C GLU B 294 -14.523 -14.863 1.860 1.00 29.98 B000 C
ATOM 5511 O GLU B 294 -15.202 -15.632 2.542 1.00 31.41 B000 O
ATOM 5512 CB GLU B 294 -12.159 -15.477 1.284 1.00 31.55 B000 C
ATOM 5513 CG GLU B 294 -11.303 -16.521 0.584 1.00 39.18 B000 C
ATOM 5514 CD GLU B 294 -9.826 -16.397 0.929 1.00 46.36 B000 C
ATOM 5515 OE1 GLU B 294 -9.464 -15.497 1.715 1.00 51.07 B000 O
ATOM 5516 OE2 GLU B 294 -9.020 -17.199 0.408 1.00 56.57 B000 O1-
ATOM 5517 N VAL B 295 -14.558 -13.541 2.035 1.00 29.12 B000 N
ATOM 5518 CA VAL B 295 -15.477 -12.948 3.007 1.00 28.03 B000 C
ATOM 5519 C VAL B 295 -16.914 -13.217 2.582 1.00 30.63 B000 C
ATOM 5520 O VAL B 295 -17.736 -13.723 3.362 1.00 31.14 B000 O
ATOM 5521 CB VAL B 295 -15.207 -11.438 3.159 1.00 20.72 B000 C
ATOM 5522 CG1 VAL B 295 -16.317 -10.767 3.990 1.00 22.47 B000 C
ATOM 5523 CG2 VAL B 295 -13.863 -11.181 3.834 1.00 19.99 B000 C
TER
HETATM 5524 O HOH B 296 -11.971 14.999 20.004 1.00 50.17 B000 O
ATOM 5525 N LYS B 296 -17.221 -12.896 1.325 1.00 24.01 B000 N
ATOM 5526 CA LYS B 296 -18.573 -13.015 0.791 1.00 29.49 B000 C
ATOM 5527 C LYS B 296 -19.112 -14.422 0.980 1.00 32.71 B000 C
ATOM 5528 O LYS B 296 -20.254 -14.609 1.432 1.00 34.56 B000 O
ATOM 5529 CB LYS B 296 -18.564 -12.610 -0.698 1.00 23.35 B000 C
ATOM 5530 CG LYS B 296 -19.911 -12.696 -1.416 1.00 31.87 B000 C
ATOM 5531 CD LYS B 296 -20.004 -13.920 -2.270 1.00 28.28 B000 C
ATOM 5532 CE LYS B 296 -21.273 -13.915 -3.129 1.00 32.71 B000 C
ATOM 5533 NZ LYS B 296 -21.434 -15.265 -3.763 1.00 34.72 B000 N1+
ATOM 5534 N ASN B 297 -18.290 -15.428 0.686 1.00 31.99 B000 N
ATOM 5535 CA ASN B 297 -18.743 -16.802 0.828 1.00 33.46 B000 C
ATOM 5536 C ASN B 297 -18.628 -17.337 2.254 1.00 39.96 B000 C
ATOM 5537 O ASN B 297 -19.236 -18.373 2.559 1.00 39.99 B000 O
ATOM 5538 CB ASN B 297 -18.001 -17.675 -0.190 1.00 37.71 B000 C
ATOM 5539 CG ASN B 297 -18.486 -17.408 -1.615 1.00 41.17 B000 C
ATOM 5540 ND2 ASN B 297 -17.652 -16.760 -2.433 1.00 35.48 B000 N
ATOM 5541 OD1 ASN B 297 -19.615 -17.760 -1.963 1.00 46.21 B000 O
TER
HETATM 5542 O HOH B 297 -12.143 10.999 20.652 1.00 51.33 B000 O
ATOM 5543 N SER B 298 -17.935 -16.641 3.156 1.00 34.14 B000 N
ATOM 5544 CA SER B 298 -18.030 -17.020 4.566 1.00 35.60 B000 C
ATOM 5545 C SER B 298 -19.310 -16.525 5.222 1.00 34.84 B000 C
ATOM 5546 O SER B 298 -19.757 -17.105 6.220 1.00 33.80 B000 O
ATOM 5547 CB SER B 298 -16.850 -16.477 5.357 1.00 32.48 B000 C
ATOM 5548 OG SER B 298 -15.737 -17.328 5.236 1.00 56.80 B000 O
ATOM 5549 N ALA B 299 -19.903 -15.458 4.699 1.00 33.90 B000 N
ATOM 5550 CA ALA B 299 -21.150 -14.948 5.248 1.00 29.84 B000 C
ATOM 5551 C ALA B 299 -22.232 -16.016 5.179 1.00 40.19 B000 C
ATOM 5552 O ALA B 299 -22.267 -16.824 4.250 1.00 46.18 B000 O
ATOM 5553 CB ALA B 299 -21.588 -13.700 4.477 1.00 33.31 B000 C
TER
HETATM 5554 O HOH B 299 -18.002 -2.279 -10.819 1.00 38.26 B000 O
HETATM 5555 O HOH B 300 -18.364 3.218 61.576 1.00 50.90 B000 O
ATOM 5556 N THR B 300 -23.126 -16.026 6.176 1.00 37.48 B000 N
ATOM 5557 CA THR B 300 -24.289 -16.914 6.129 1.00 42.61 B000 C
ATOM 5558 C THR B 300 -25.600 -16.204 5.837 1.00 42.20 B000 C
ATOM 5559 O THR B 300 -26.527 -16.841 5.333 1.00 43.98 B000 O
ATOM 5560 CB THR B 300 -24.462 -17.675 7.448 1.00 39.17 B000 C
ATOM 5561 CG2 THR B 300 -23.267 -18.538 7.708 1.00 35.36 B000 C
ATOM 5562 OG1 THR B 300 -24.607 -16.742 8.527 1.00 40.85 B000 O
TER
HETATM 5563 O HOH B 301 -8.037 -0.886 64.167 1.00 55.34 B000 O
ATOM 5564 N LYS B 301 -25.721 -14.922 6.159 1.00 37.17 B000 N
ATOM 5565 CA LYS B 301 -27.003 -14.269 5.970 1.00 35.21 B000 C
ATOM 5566 C LYS B 301 -27.190 -13.900 4.508 1.00 37.04 B000 C
ATOM 5567 O LYS B 301 -26.243 -13.887 3.716 1.00 35.11 B000 O
ATOM 5568 CB LYS B 301 -27.142 -13.030 6.854 1.00 32.04 B000 C
ATOM 5569 CG LYS B 301 -26.909 -13.265 8.349 1.00 41.74 B000 C
ATOM 5570 CD LYS B 301 -27.246 -12.003 9.153 1.00 37.76 B000 C
ATOM 5571 CE LYS B 301 -26.908 -12.142 10.635 1.00 52.36 B000 C
ATOM 5572 NZ LYS B 301 -27.579 -13.301 11.262 1.00 58.52 B000 N1+
ATOM 5573 N SER B 302 -28.436 -13.599 4.147 1.00 40.56 B000 N
ATOM 5574 CA SER B 302 -28.772 -13.357 2.745 1.00 35.98 B000 C
ATOM 5575 C SER B 302 -28.558 -11.886 2.391 1.00 35.21 B000 C
ATOM 5576 O SER B 302 -29.481 -11.136 2.072 1.00 30.76 B000 O
ATOM 5577 CB SER B 302 -30.195 -13.817 2.463 1.00 43.79 B000 C
ATOM 5578 OG SER B 302 -30.261 -15.220 2.623 1.00 51.61 B000 O
ATOM 5579 N TRP B 303 -27.285 -11.491 2.407 1.00 30.55 B000 N
ATOM 5580 CA TRP B 303 -26.911 -10.137 2.025 1.00 25.58 B000 C
ATOM 5581 C TRP B 303 -27.194 -9.908 0.545 1.00 21.42 B000 C
ATOM 5582 O TRP B 303 -27.112 -10.827 -0.270 1.00 26.80 B000 O
ATOM 5583 CB TRP B 303 -25.427 -9.912 2.297 1.00 23.76 B000 C
ATOM 5584 CG TRP B 303 -25.066 -10.030 3.751 1.00 28.20 B000 C
ATOM 5585 CD1 TRP B 303 -24.468 -11.092 4.372 1.00 29.21 B000 C
ATOM 5586 CD2 TRP B 303 -25.302 -9.049 4.769 1.00 23.38 B000 C
ATOM 5587 CE2 TRP B 303 -24.789 -9.566 5.980 1.00 28.93 B000 C
ATOM 5588 CE3 TRP B 303 -25.887 -7.778 4.771 1.00 25.26 B000 C
ATOM 5589 NE1 TRP B 303 -24.288 -10.815 5.713 1.00 28.32 B000 N
ATOM 5590 CZ2 TRP B 303 -24.850 -8.855 7.182 1.00 29.79 B000 C
ATOM 5591 CZ3 TRP B 303 -25.927 -7.062 5.958 1.00 25.89 B000 C
ATOM 5592 CH2 TRP B 303 -25.419 -7.607 7.149 1.00 27.56 B000 C
ATOM 5593 N ASN B 304 -27.494 -8.657 0.193 1.00 23.18 B000 N
ATOM 5594 CA ASN B 304 -27.735 -8.287 -1.200 1.00 24.29 B000 C
ATOM 5595 C ASN B 304 -26.397 -8.037 -1.903 1.00 27.03 B000 C
ATOM 5596 O ASN B 304 -26.049 -6.913 -2.271 1.00 25.55 B000 O
ATOM 5597 CB ASN B 304 -28.652 -7.075 -1.277 1.00 29.42 B000 C
ATOM 5598 CG ASN B 304 -29.960 -7.281 -0.504 1.00 38.73 B000 C
ATOM 5599 ND2 ASN B 304 -30.478 -6.215 0.084 1.00 30.99 B000 N
ATOM 5600 OD1 ASN B 304 -30.474 -8.393 -0.425 1.00 35.25 B000 O
ATOM 5601 N PHE B 305 -25.653 -9.135 -2.097 1.00 28.63 B000 N
ATOM 5602 CA PHE B 305 -24.308 -9.083 -2.673 1.00 23.34 B000 C
ATOM 5603 C PHE B 305 -24.354 -8.609 -4.118 1.00 26.90 B000 C
ATOM 5604 O PHE B 305 -25.263 -8.963 -4.871 1.00 24.58 B000 O
ATOM 5605 CB PHE B 305 -23.644 -10.463 -2.651 1.00 22.70 B000 C
ATOM 5606 CG PHE B 305 -23.307 -10.988 -1.280 1.00 24.34 B000 C
ATOM 5607 CD1 PHE B 305 -22.474 -10.276 -0.422 1.00 21.63 B000 C
ATOM 5608 CD2 PHE B 305 -23.789 -12.227 -0.868 1.00 24.29 B000 C
ATOM 5609 CE1 PHE B 305 -22.151 -10.778 0.832 1.00 25.84 B000 C
ATOM 5610 CE2 PHE B 305 -23.488 -12.727 0.393 1.00 26.60 B000 C
ATOM 5611 CZ PHE B 305 -22.665 -12.022 1.238 1.00 24.07 B000 C
ATOM 5612 N ILE B 306 -23.345 -7.838 -4.521 1.00 24.68 B000 N
ATOM 5613 CA ILE B 306 -23.153 -7.496 -5.926 1.00 24.94 B000 C
ATOM 5614 C ILE B 306 -21.682 -7.710 -6.286 1.00 24.63 B000 C
ATOM 5615 O ILE B 306 -20.788 -7.304 -5.534 1.00 25.33 B000 O
ATOM 5616 CB ILE B 306 -23.599 -6.049 -6.220 1.00 22.22 B000 C
ATOM 5617 CG1 ILE B 306 -23.422 -5.710 -7.717 1.00 24.23 B000 C
ATOM 5618 CG2 ILE B 306 -22.883 -5.032 -5.296 1.00 22.46 B000 C
ATOM 5619 CD1 ILE B 306 -24.244 -4.520 -8.157 1.00 27.31 B000 C
ATOM 5620 N TRP B 307 -21.430 -8.382 -7.413 1.00 24.42 B000 N
ATOM 5621 CA TRP B 307 -20.072 -8.527 -7.929 1.00 24.60 B000 C
ATOM 5622 C TRP B 307 -19.638 -7.223 -8.596 1.00 27.44 B000 C
ATOM 5623 O TRP B 307 -20.404 -6.639 -9.375 1.00 24.73 B000 O
ATOM 5624 CB TRP B 307 -19.990 -9.693 -8.926 1.00 28.54 B000 C
ATOM 5625 CG TRP B 307 -18.596 -9.872 -9.498 1.00 26.77 B000 C
ATOM 5626 CD1 TRP B 307 -17.584 -10.636 -8.986 1.00 28.08 B000 C
ATOM 5627 CD2 TRP B 307 -18.069 -9.248 -10.681 1.00 25.02 B000 C
ATOM 5628 CE2 TRP B 307 -16.733 -9.679 -10.822 1.00 28.67 B000 C
ATOM 5629 CE3 TRP B 307 -18.596 -8.357 -11.626 1.00 26.24 B000 C
ATOM 5630 NE1 TRP B 307 -16.461 -10.532 -9.781 1.00 25.73 B000 N
ATOM 5631 CZ2 TRP B 307 -15.914 -9.256 -11.882 1.00 27.77 B000 C
ATOM 5632 CZ3 TRP B 307 -17.780 -7.935 -12.674 1.00 31.88 B000 C
ATOM 5633 CH2 TRP B 307 -16.448 -8.382 -12.786 1.00 22.56 B000 C
ATOM 5634 N LEU B 308 -18.412 -6.764 -8.299 1.00 19.98 B000 N
ATOM 5635 CA LEU B 308 -17.903 -5.500 -8.824 1.00 26.19 B000 C
ATOM 5636 C LEU B 308 -16.762 -5.653 -9.824 1.00 28.62 B000 C
ATOM 5637 O LEU B 308 -16.796 -5.029 -10.886 1.00 28.21 B000 O
ATOM 5638 CB LEU B 308 -17.450 -4.593 -7.676 1.00 27.37 B000 C
ATOM 5639 CG LEU B 308 -18.548 -4.229 -6.679 1.00 32.10 B000 C
ATOM 5640 CD1 LEU B 308 -17.972 -3.310 -5.637 1.00 29.92 B000 C
ATOM 5641 CD2 LEU B 308 -19.697 -3.552 -7.414 1.00 25.61 B000 C
ATOM 5642 N THR B 309 -15.743 -6.446 -9.509 1.00 25.34 B000 N
ATOM 5643 CA THR B 309 -14.515 -6.527 -10.296 1.00 25.21 B000 C
ATOM 5644 C THR B 309 -13.666 -7.651 -9.708 1.00 29.92 B000 C
ATOM 5645 O THR B 309 -13.989 -8.207 -8.653 1.00 28.02 B000 O
ATOM 5646 CB THR B 309 -13.744 -5.185 -10.286 1.00 31.13 B000 C
ATOM 5647 CG2 THR B 309 -13.083 -4.960 -8.919 1.00 30.37 B000 C
ATOM 5648 OG1 THR B 309 -12.720 -5.190 -11.299 1.00 30.77 B000 O
ATOM 5649 N ASP B 310 -12.608 -8.026 -10.441 1.00 31.39 B000 N
ATOM 5650 CA ASP B 310 -11.451 -8.740 -9.907 1.00 24.33 B000 C
ATOM 5651 C ASP B 310 -10.352 -7.800 -9.455 1.00 25.77 B000 C
ATOM 5652 O ASP B 310 -10.134 -6.736 -10.037 1.00 30.62 B000 O
ATOM 5653 CB ASP B 310 -10.854 -9.727 -10.915 1.00 28.22 B000 C
ATOM 5654 CG ASP B 310 -11.703 -10.942 -11.129 1.00 29.69 B000 C
ATOM 5655 OD1 ASP B 310 -12.716 -10.893 -11.838 1.00 26.00 B000 O
ATOM 5656 OD2 ASP B 310 -11.208 -12.017 -10.696 1.00 31.13 B000 O1-
ATOM 5657 N SER B 311 -9.627 -8.236 -8.431 1.00 29.08 B000 N
ATOM 5658 CA SER B 311 -8.420 -7.546 -8.016 1.00 30.29 B000 C
ATOM 5659 C SER B 311 -7.461 -8.581 -7.444 1.00 33.79 B000 C
ATOM 5660 O SER B 311 -7.720 -9.790 -7.446 1.00 33.68 B000 O
ATOM 5661 CB SER B 311 -8.746 -6.438 -7.010 1.00 33.38 B000 C
ATOM 5662 OG SER B 311 -7.655 -5.541 -6.865 1.00 42.06 B000 O
ATOM 5663 N GLU B 312 -6.335 -8.102 -6.957 1.00 30.96 B000 N
ATOM 5664 CA GLU B 312 -5.423 -8.957 -6.230 1.00 37.23 B000 C
ATOM 5665 C GLU B 312 -5.167 -8.248 -4.911 1.00 38.96 B000 C
ATOM 5666 O GLU B 312 -4.973 -7.029 -4.896 1.00 43.44 B000 O
ATOM 5667 CB GLU B 312 -4.151 -9.190 -7.043 1.00 35.61 B000 C
ATOM 5668 CG GLU B 312 -3.420 -10.451 -6.630 1.00 51.03 B000 C
ATOM 5669 CD GLU B 312 -2.660 -10.270 -5.331 1.00 55.88 B000 C
ATOM 5670 OE1 GLU B 312 -2.354 -9.100 -4.997 1.00 54.51 B000 O
ATOM 5671 OE2 GLU B 312 -2.412 -11.286 -4.629 1.00 51.10 B000 O1-
ATOM 5672 N LEU B 313 -5.250 -8.981 -3.804 1.00 33.68 B000 N
ATOM 5673 CA LEU B 313 -5.060 -8.357 -2.504 1.00 38.57 B000 C
ATOM 5674 C LEU B 313 -3.802 -8.817 -1.782 1.00 47.25 B000 C
ATOM 5675 O LEU B 313 -3.227 -8.041 -1.011 1.00 45.05 B000 O
ATOM 5676 CB LEU B 313 -6.279 -8.608 -1.606 1.00 41.57 B000 C
ATOM 5677 CG LEU B 313 -7.611 -7.985 -2.046 1.00 40.93 B000 C
ATOM 5678 CD1 LEU B 313 -8.677 -8.244 -0.995 1.00 37.17 B000 C
ATOM 5679 CD2 LEU B 313 -7.464 -6.486 -2.310 1.00 32.47 B000 C
ATOM 5680 N LYS B 314 -3.334 -10.037 -2.040 1.00 43.18 B000 N
ATOM 5681 CA LYS B 314 -2.306 -10.664 -1.217 1.00 48.76 B000 C
ATOM 5682 C LYS B 314 -0.896 -10.523 -1.789 1.00 56.55 B000 C
ATOM 5683 O LYS B 314 0.067 -10.942 -1.137 1.00 54.13 B000 O
ATOM 5684 CB LYS B 314 -2.648 -12.145 -1.021 1.00 46.90 B000 C
ATOM 5685 CG LYS B 314 -4.012 -12.384 -0.339 1.00 44.10 B000 C
ATOM 5686 CD LYS B 314 -4.101 -11.741 1.040 1.00 52.60 B000 C
ATOM 5687 CE LYS B 314 -5.456 -12.041 1.709 1.00 50.86 B000 C
ATOM 5688 NZ LYS B 314 -5.681 -13.506 1.906 1.00 52.97 B000 N1+
ATOM 5689 N GLY B 315 -0.745 -9.928 -2.972 1.00 55.94 B000 N
ATOM 5690 CA GLY B 315 0.530 -9.936 -3.662 1.00 61.47 B000 C
ATOM 5691 C GLY B 315 0.847 -11.237 -4.365 1.00 53.17 B000 C
ATOM 5692 O GLY B 315 1.935 -11.364 -4.938 1.00 65.21 B000 O
TER
HETATM 5693 O HOH B 315 -29.517 -3.997 0.094 1.00 44.81 B000 O
HETATM 5694 O HOH B 316 -20.031 8.196 56.385 1.00 51.10 B000 O
ATOM 5695 N LYS B 316 -0.051 -12.215 -4.305 1.00 55.11 B000 N
ATOM 5696 CA LYS B 316 0.033 -13.420 -5.117 1.00 61.41 B000 C
ATOM 5697 C LYS B 316 -0.330 -13.061 -6.561 1.00 52.99 B000 C
ATOM 5698 O LYS B 316 -0.532 -11.896 -6.920 1.00 59.59 B000 O
ATOM 5699 CB LYS B 316 -0.897 -14.495 -4.556 1.00 65.42 B000 C
ATOM 5700 CG LYS B 316 -0.496 -15.047 -3.191 1.00 63.82 B000 C
ATOM 5701 CD LYS B 316 0.617 -16.079 -3.326 1.00 69.52 B000 C
ATOM 5702 CE LYS B 316 0.863 -16.817 -2.021 1.00 68.84 B000 C
ATOM 5703 NZ LYS B 316 1.167 -15.877 -0.905 1.00 61.58 B000 N1+
TER
HETATM 5704 O HOH B 317 -1.737 10.686 57.931 1.00 57.21 B000 O
ATOM 5705 N SER B 317 -0.446 -14.068 -7.412 1.00 48.10 B000 N
ATOM 5706 CA SER B 317 -0.988 -13.845 -8.743 1.00 55.48 B000 C
ATOM 5707 C SER B 317 -2.463 -14.228 -8.833 1.00 54.43 B000 C
ATOM 5708 O SER B 317 -3.038 -14.190 -9.926 1.00 49.16 B000 O
ATOM 5709 CB SER B 317 -0.170 -14.614 -9.779 1.00 56.00 B000 C
ATOM 5710 OG SER B 317 -0.031 -15.969 -9.388 1.00 66.02 B000 O
ATOM 5711 N GLU B 318 -3.086 -14.589 -7.711 1.00 45.54 B000 N
ATOM 5712 CA GLU B 318 -4.471 -15.044 -7.717 1.00 51.17 B000 C
ATOM 5713 C GLU B 318 -5.411 -13.855 -7.891 1.00 36.10 B000 C
ATOM 5714 O GLU B 318 -5.379 -12.908 -7.103 1.00 41.95 B000 O
ATOM 5715 CB GLU B 318 -4.779 -15.798 -6.427 1.00 53.08 B000 C
ATOM 5716 CG GLU B 318 -3.931 -17.049 -6.242 1.00 60.10 B000 C
ATOM 5717 CD GLU B 318 -4.347 -18.181 -7.167 1.00 71.42 B000 C
ATOM 5718 OE1 GLU B 318 -3.824 -18.250 -8.305 1.00 76.39 B000 O
ATOM 5719 OE2 GLU B 318 -5.195 -19.005 -6.758 1.00 72.42 B000 O1-
TER
HETATM 5720 O HOH B 318 0.746 10.618 59.695 1.00 51.70 B000 O
HETATM 5721 O HOH B 319 -1.333 9.815 51.999 1.00 38.27 B000 O
ATOM 5722 N SER B 319 -6.218 -13.889 -8.940 1.00 31.30 B000 N
ATOM 5723 CA SER B 319 -7.243 -12.879 -9.180 1.00 31.58 B000 C
ATOM 5724 C SER B 319 -8.508 -13.250 -8.420 1.00 32.42 B000 C
ATOM 5725 O SER B 319 -9.110 -14.291 -8.698 1.00 30.22 B000 O
ATOM 5726 CB SER B 319 -7.552 -12.785 -10.669 1.00 28.84 B000 C
ATOM 5727 OG SER B 319 -8.445 -11.721 -10.941 1.00 30.35 B000 O
TER
HETATM 5728 O HOH B 320 -13.021 19.739 13.431 1.00 42.45 B000 O
ATOM 5729 N ILE B 320 -8.932 -12.402 -7.490 1.00 28.75 B000 N
ATOM 5730 CA ILE B 320 -10.079 -12.752 -6.655 1.00 28.57 B000 C
ATOM 5731 C ILE B 320 -11.245 -11.823 -6.971 1.00 34.24 B000 C
ATOM 5732 O ILE B 320 -11.059 -10.662 -7.359 1.00 28.51 B000 O
ATOM 5733 CB ILE B 320 -9.757 -12.686 -5.152 1.00 35.23 B000 C
ATOM 5734 CG1 ILE B 320 -9.428 -11.252 -4.770 1.00 34.60 B000 C
ATOM 5735 CG2 ILE B 320 -8.592 -13.633 -4.814 1.00 38.64 B000 C
ATOM 5736 CD1 ILE B 320 -9.425 -11.022 -3.290 1.00 44.01 B000 C
ATOM 5737 N ASP B 321 -12.461 -12.339 -6.775 1.00 25.68 B000 N
ATOM 5738 CA ASP B 321 -13.669 -11.562 -7.005 1.00 24.56 B000 C
ATOM 5739 C ASP B 321 -13.852 -10.580 -5.865 1.00 25.99 B000 C
ATOM 5740 O ASP B 321 -13.716 -10.955 -4.699 1.00 26.32 B000 O
ATOM 5741 CB ASP B 321 -14.893 -12.474 -7.096 1.00 28.11 B000 C
ATOM 5742 CG ASP B 321 -14.843 -13.410 -8.303 1.00 34.16 B000 C
ATOM 5743 OD1 ASP B 321 -14.590 -12.924 -9.418 1.00 27.85 B000 O
ATOM 5744 OD2 ASP B 321 -15.052 -14.636 -8.139 1.00 29.26 B000 O1-
TER
HETATM 5745 O HOH B 321 -17.838 10.516 16.716 1.00 40.87 B000 O
HETATM 5746 O HOH B 322 -15.983 2.497 21.769 1.00 45.18 B000 O
ATOM 5747 N ILE B 322 -14.144 -9.323 -6.204 1.00 24.62 B000 N
ATOM 5748 CA ILE B 322 -14.440 -8.270 -5.236 1.00 25.67 B000 C
ATOM 5749 C ILE B 322 -15.939 -8.007 -5.276 1.00 29.03 B000 C
ATOM 5750 O ILE B 322 -16.513 -7.814 -6.358 1.00 26.69 B000 O
ATOM 5751 CB ILE B 322 -13.659 -6.971 -5.521 1.00 24.18 B000 C
ATOM 5752 CG1 ILE B 322 -12.148 -7.195 -5.535 1.00 24.59 B000 C
ATOM 5753 CG2 ILE B 322 -13.974 -5.908 -4.436 1.00 24.35 B000 C
ATOM 5754 CD1 ILE B 322 -11.625 -7.894 -4.264 1.00 27.19 B000 C
TER
HETATM 5755 O HOH B 323 -14.245 -18.978 -0.481 1.00 43.72 B000 O
ATOM 5756 N TYR B 323 -16.571 -8.009 -4.104 1.00 22.72 B000 N
ATOM 5757 CA TYR B 323 -18.002 -7.816 -3.966 1.00 23.19 B000 C
ATOM 5758 C TYR B 323 -18.285 -6.596 -3.112 1.00 22.92 B000 C
ATOM 5759 O TYR B 323 -17.419 -6.115 -2.385 1.00 23.98 B000 O
ATOM 5760 CB TYR B 323 -18.678 -9.028 -3.310 1.00 21.98 B000 C
ATOM 5761 CG TYR B 323 -18.589 -10.275 -4.143 1.00 26.87 B000 C
ATOM 5762 CD1 TYR B 323 -17.472 -11.082 -4.077 1.00 28.61 B000 C
ATOM 5763 CD2 TYR B 323 -19.626 -10.648 -4.992 1.00 26.63 B000 C
ATOM 5764 CE1 TYR B 323 -17.374 -12.232 -4.828 1.00 24.14 B000 C
ATOM 5765 CE2 TYR B 323 -19.543 -11.799 -5.754 1.00 29.37 B000 C
ATOM 5766 CZ TYR B 323 -18.405 -12.584 -5.669 1.00 29.73 B000 C
ATOM 5767 OH TYR B 323 -18.296 -13.733 -6.406 1.00 30.25 B000 O
TER
HETATM 5768 O HOH B 324 -22.565 -16.053 0.907 1.00 41.28 B000 O
ATOM 5769 N SER B 324 -19.531 -6.126 -3.172 1.00 25.35 B000 N
ATOM 5770 CA SER B 324 -20.038 -5.198 -2.159 1.00 22.67 B000 C
ATOM 5771 C SER B 324 -21.479 -5.588 -1.819 1.00 26.04 B000 C
ATOM 5772 O SER B 324 -21.944 -6.682 -2.149 1.00 25.77 B000 O
ATOM 5773 CB SER B 324 -19.928 -3.751 -2.659 1.00 26.07 B000 C
ATOM 5774 OG SER B 324 -20.317 -2.827 -1.665 1.00 25.94 B000 O
ATOM 5775 N ILE B 325 -22.174 -4.693 -1.122 1.00 25.79 B000 N
ATOM 5776 CA ILE B 325 -23.610 -4.798 -0.858 1.00 28.55 B000 C
ATOM 5777 C ILE B 325 -24.284 -3.760 -1.727 1.00 29.14 B000 C
ATOM 5778 O ILE B 325 -23.847 -2.606 -1.759 1.00 31.62 B000 O
ATOM 5779 CB ILE B 325 -23.954 -4.542 0.620 1.00 32.05 B000 C
ATOM 5780 CG1 ILE B 325 -23.199 -5.487 1.556 1.00 28.69 B000 C
ATOM 5781 CG2 ILE B 325 -25.459 -4.614 0.853 1.00 30.83 B000 C
ATOM 5782 CD1 ILE B 325 -23.572 -6.915 1.398 1.00 29.95 B000 C
ATOM 5783 N ASP B 326 -25.348 -4.153 -2.418 1.00 21.70 B000 N
ATOM 5784 CA ASP B 326 -26.114 -3.220 -3.243 1.00 29.73 B000 C
ATOM 5785 C ASP B 326 -27.308 -2.774 -2.410 1.00 38.71 B000 C
ATOM 5786 O ASP B 326 -28.244 -3.543 -2.194 1.00 32.07 B000 O
ATOM 5787 CB ASP B 326 -26.536 -3.871 -4.559 1.00 31.12 B000 C
ATOM 5788 CG ASP B 326 -27.298 -2.918 -5.477 1.00 35.57 B000 C
ATOM 5789 OD1 ASP B 326 -27.052 -1.698 -5.429 1.00 34.89 B000 O
ATOM 5790 OD2 ASP B 326 -28.134 -3.397 -6.265 1.00 31.63 B000 O1-
ATOM 5791 N ASN B 327 -27.237 -1.553 -1.882 1.00 38.86 B000 N
ATOM 5792 CA ASN B 327 -28.368 -0.884 -1.251 1.00 38.65 B000 C
ATOM 5793 C ASN B 327 -28.247 0.600 -1.566 1.00 44.06 B000 C
ATOM 5794 O ASN B 327 -27.359 1.020 -2.311 1.00 37.00 B000 O
ATOM 5795 CB ASN B 327 -28.438 -1.142 0.263 1.00 42.71 B000 C
ATOM 5796 CG ASN B 327 -27.153 -0.773 0.999 1.00 45.80 B000 C
ATOM 5797 ND2 ASN B 327 -26.927 -1.414 2.155 1.00 40.05 B000 N
ATOM 5798 OD1 ASN B 327 -26.376 0.066 0.544 1.00 46.21 B000 O
ATOM 5799 N GLU B 328 -29.142 1.404 -0.986 1.00 50.77 B000 N
ATOM 5800 CA GLU B 328 -29.217 2.814 -1.361 1.00 50.20 B000 C
ATOM 5801 C GLU B 328 -27.946 3.549 -0.974 1.00 45.71 B000 C
ATOM 5802 O GLU B 328 -27.495 4.454 -1.686 1.00 52.27 B000 O
ATOM 5803 CB GLU B 328 -30.437 3.456 -0.694 1.00 59.58 B000 C
ATOM 5804 CG GLU B 328 -31.030 4.676 -1.401 1.00 59.43 B000 C
ATOM 5805 CD GLU B 328 -32.366 5.088 -0.782 1.00 62.51 B000 C
ATOM 5806 OE1 GLU B 328 -32.545 4.837 0.436 1.00 59.36 B000 O
ATOM 5807 OE2 GLU B 328 -33.228 5.652 -1.506 1.00 59.91 B000 O1-
ATOM 5808 N MET B 329 -27.337 3.135 0.127 1.00 47.99 B000 N
ATOM 5809 CA MET B 329 -26.179 3.828 0.666 1.00 47.80 B000 C
ATOM 5810 C MET B 329 -24.959 3.641 -0.224 1.00 56.31 B000 C
ATOM 5811 O MET B 329 -24.181 4.581 -0.434 1.00 55.37 B000 O
ATOM 5812 CB MET B 329 -25.919 3.287 2.059 1.00 45.69 B000 C
ATOM 5813 CG MET B 329 -24.631 3.692 2.714 1.00 49.56 B000 C
ATOM 5814 SD MET B 329 -24.964 3.503 4.484 1.00 59.10 B000 S
ATOM 5815 CE MET B 329 -26.467 2.516 4.439 1.00 51.57 B000 C
ATOM 5816 N THR B 330 -24.769 2.429 -0.745 1.00 50.52 B000 N
ATOM 5817 CA THR B 330 -23.615 2.145 -1.585 1.00 51.34 B000 C
ATOM 5818 C THR B 330 -23.842 2.516 -3.047 1.00 53.63 B000 C
ATOM 5819 O THR B 330 -22.900 2.415 -3.839 1.00 44.18 B000 O
ATOM 5820 CB THR B 330 -23.248 0.659 -1.484 1.00 47.60 B000 C
ATOM 5821 CG2 THR B 330 -23.144 0.212 -0.027 1.00 42.37 B000 C
ATOM 5822 OG1 THR B 330 -24.262 -0.122 -2.134 1.00 48.32 B000 O
ATOM 5823 N ARG B 331 -25.059 2.933 -3.426 1.00 48.19 B000 N
ATOM 5824 CA ARG B 331 -25.343 3.331 -4.809 1.00 50.64 B000 C
ATOM 5825 C ARG B 331 -24.945 4.793 -5.004 1.00 55.12 B000 C
ATOM 5826 O ARG B 331 -25.774 5.706 -5.011 1.00 64.78 B000 O
ATOM 5827 CB ARG B 331 -26.810 3.099 -5.156 1.00 47.27 B000 C
ATOM 5828 CG ARG B 331 -27.203 1.625 -5.311 1.00 47.73 B000 C
ATOM 5829 CD ARG B 331 -28.696 1.446 -5.679 1.00 44.37 B000 C
ATOM 5830 NE ARG B 331 -29.159 0.086 -5.413 1.00 40.47 B000 N
ATOM 5831 CZ ARG B 331 -30.185 -0.228 -4.627 1.00 48.70 B000 C
ATOM 5832 NH1 ARG B 331 -30.979 0.700 -4.119 1.00 40.21 B000 N1+
ATOM 5833 NH2 ARG B 331 -30.429 -1.510 -4.357 1.00 39.06 B000 N
ATOM 5834 N LYS B 332 -23.643 5.011 -5.190 1.00 68.61 B000 N
ATOM 5835 CA LYS B 332 -23.061 6.344 -5.273 1.00 62.24 B000 C
ATOM 5836 C LYS B 332 -22.392 6.559 -6.627 1.00 63.75 B000 C
ATOM 5837 O LYS B 332 -22.015 5.609 -7.324 1.00 66.31 B000 O
ATOM 5838 CB LYS B 332 -22.049 6.576 -4.142 1.00 55.51 B000 C
ATOM 5839 CG LYS B 332 -22.694 6.676 -2.762 1.00 58.66 B000 C
ATOM 5840 CD LYS B 332 -23.810 7.713 -2.754 1.00 56.10 B000 C
ATOM 5841 CE LYS B 332 -24.715 7.553 -1.539 1.00 56.71 B000 C
ATOM 5842 NZ LYS B 332 -26.139 7.871 -1.890 1.00 59.02 B000 N1+
ATOM 5843 N SER B 333 -22.253 7.835 -6.994 1.00 69.12 B000 N
ATOM 5844 CA SER B 333 -21.634 8.256 -8.251 1.00 72.31 B000 C
ATOM 5845 C SER B 333 -20.290 8.905 -7.951 1.00 74.90 B000 C
ATOM 5846 O SER B 333 -20.238 9.953 -7.296 1.00 74.70 B000 O
ATOM 5847 CB SER B 333 -22.528 9.235 -9.015 1.00 62.51 B000 C
ATOM 5848 OG SER B 333 -23.613 8.564 -9.625 1.00 63.62 B000 O
ATOM 5849 N SER B 334 -19.215 8.289 -8.438 1.00 84.11 B000 N
ATOM 5850 CA SER B 334 -17.854 8.777 -8.210 1.00 74.82 B000 C
ATOM 5851 C SER B 334 -17.588 9.082 -6.735 1.00 73.89 B000 C
ATOM 5852 O SER B 334 -18.263 8.563 -5.838 1.00 77.34 B000 O
ATOM 5853 CB SER B 334 -17.583 10.024 -9.060 1.00 70.42 B000 C
ATOM 5854 OG SER B 334 -16.254 10.480 -8.871 1.00 84.03 B000 O
ATOM 5855 N GLY B 336 -14.545 9.077 -6.930 1.00 75.90 B000 N
ATOM 5856 CA GLY B 336 -13.410 9.362 -7.790 1.00 64.64 B000 C
ATOM 5857 C GLY B 336 -12.758 10.691 -7.467 1.00 66.26 B000 C
ATOM 5858 O GLY B 336 -12.659 11.088 -6.304 1.00 64.30 B000 O
ATOM 5859 N LEU B 337 -12.297 11.393 -8.500 1.00 63.80 B000 N
ATOM 5860 CA LEU B 337 -11.720 12.709 -8.264 1.00 69.33 B000 C
ATOM 5861 C LEU B 337 -12.783 13.742 -7.907 1.00 69.13 B000 C
ATOM 5862 O LEU B 337 -12.439 14.790 -7.349 1.00 55.92 B000 O
ATOM 5863 CB LEU B 337 -10.906 13.164 -9.486 1.00 71.43 B000 C
ATOM 5864 CG LEU B 337 -11.526 13.148 -10.888 1.00 76.65 B000 C
ATOM 5865 CD1 LEU B 337 -12.400 14.375 -11.141 1.00 83.05 B000 C
ATOM 5866 CD2 LEU B 337 -10.448 13.032 -11.958 1.00 69.62 B000 C
ATOM 5867 N GLU B 338 -14.062 13.469 -8.216 1.00 69.55 B000 N
ATOM 5868 CA GLU B 338 -15.131 14.387 -7.830 1.00 71.34 B000 C
ATOM 5869 C GLU B 338 -15.260 14.467 -6.311 1.00 58.48 B000 C
ATOM 5870 O GLU B 338 -15.459 15.553 -5.756 1.00 56.16 B000 O
ATOM 5871 CB GLU B 338 -16.469 13.962 -8.452 1.00 68.97 B000 C
ATOM 5872 CG GLU B 338 -17.621 14.954 -8.172 1.00 75.14 B000 C
ATOM 5873 CD GLU B 338 -18.969 14.565 -8.812 1.00 77.93 B000 C
ATOM 5874 OE1 GLU B 338 -19.236 14.996 -9.957 1.00 77.80 B000 O
ATOM 5875 OE2 GLU B 338 -19.788 13.882 -8.150 1.00 73.35 B000 O1-
ATOM 5876 N ILE B 339 -15.144 13.332 -5.620 1.00 52.40 B000 N
ATOM 5877 CA ILE B 339 -15.191 13.371 -4.161 1.00 58.33 B000 C
ATOM 5878 C ILE B 339 -14.022 14.182 -3.620 1.00 51.58 B000 C
ATOM 5879 O ILE B 339 -14.184 15.003 -2.710 1.00 43.21 B000 O
ATOM 5880 CB ILE B 339 -15.211 11.947 -3.573 1.00 52.88 B000 C
ATOM 5881 CG1 ILE B 339 -16.086 11.030 -4.423 1.00 61.07 B000 C
ATOM 5882 CG2 ILE B 339 -15.706 11.980 -2.139 1.00 50.00 B000 C
ATOM 5883 CD1 ILE B 339 -17.566 11.254 -4.220 1.00 63.63 B000 C
ATOM 5884 N ALA B 340 -12.830 13.986 -4.186 1.00 56.01 B000 N
ATOM 5885 CA ALA B 340 -11.658 14.703 -3.696 1.00 46.35 B000 C
ATOM 5886 C ALA B 340 -11.843 16.205 -3.835 1.00 47.17 B000 C
ATOM 5887 O ALA B 340 -11.574 16.962 -2.893 1.00 42.72 B000 O
ATOM 5888 CB ALA B 340 -10.409 14.249 -4.447 1.00 46.03 B000 C
ATOM 5889 N ARG B 341 -12.313 16.649 -5.011 1.00 51.84 B000 N
ATOM 5890 CA ARG B 341 -12.474 18.077 -5.287 1.00 51.30 B000 C
ATOM 5891 C ARG B 341 -13.583 18.694 -4.441 1.00 47.31 B000 C
ATOM 5892 O ARG B 341 -13.479 19.858 -4.031 1.00 41.42 B000 O
ATOM 5893 CB ARG B 341 -12.771 18.287 -6.773 1.00 56.79 B000 C
ATOM 5894 CG ARG B 341 -12.980 19.737 -7.177 1.00 58.01 B000 C
ATOM 5895 CD ARG B 341 -13.014 19.894 -8.701 1.00 70.28 B000 C
ATOM 5896 NE ARG B 341 -14.028 19.043 -9.319 1.00 80.46 B000 N
ATOM 5897 CZ ARG B 341 -13.765 17.973 -10.061 1.00 81.60 B000 C
ATOM 5898 NH1 ARG B 341 -12.522 17.605 -10.330 1.00 80.72 B000 N1+
ATOM 5899 NH2 ARG B 341 -14.774 17.254 -10.546 1.00 80.05 B000 N
ATOM 5900 N ASN B 342 -14.665 17.937 -4.203 1.00 35.53 B000 N
ATOM 5901 CA ASN B 342 -15.740 18.398 -3.326 1.00 44.51 B000 C
ATOM 5902 C ASN B 342 -15.226 18.697 -1.922 1.00 38.34 B000 C
ATOM 5903 O ASN B 342 -15.456 19.786 -1.382 1.00 37.34 B000 O
ATOM 5904 CB ASN B 342 -16.858 17.347 -3.275 1.00 40.48 B000 C
ATOM 5905 CG ASN B 342 -17.976 17.712 -2.290 1.00 59.00 B000 C
ATOM 5906 ND2 ASN B 342 -18.466 18.948 -2.385 1.00 61.43 B000 N
ATOM 5907 OD1 ASN B 342 -18.385 16.895 -1.447 1.00 52.73 B000 O
ATOM 5908 N ILE B 343 -14.528 17.735 -1.311 1.00 44.17 B000 N
ATOM 5909 CA ILE B 343 -14.017 17.931 0.047 1.00 38.34 B000 C
ATOM 5910 C ILE B 343 -13.171 19.191 0.124 1.00 36.52 B000 C
ATOM 5911 O ILE B 343 -13.351 20.027 1.018 1.00 34.14 B000 O
ATOM 5912 CB ILE B 343 -13.231 16.694 0.511 1.00 41.18 B000 C
ATOM 5913 CG1 ILE B 343 -14.139 15.468 0.492 1.00 35.91 B000 C
ATOM 5914 CG2 ILE B 343 -12.571 16.934 1.873 1.00 30.88 B000 C
ATOM 5915 CD1 ILE B 343 -13.380 14.155 0.491 1.00 44.77 B000 C
ATOM 5916 N GLY B 344 -12.262 19.368 -0.837 1.00 33.73 B000 N
ATOM 5917 CA GLY B 344 -11.355 20.505 -0.769 1.00 36.43 B000 C
ATOM 5918 C GLY B 344 -12.078 21.828 -0.926 1.00 43.43 B000 C
ATOM 5919 O GLY B 344 -11.817 22.783 -0.184 1.00 37.61 B000 O
ATOM 5920 N HIS B 345 -13.017 21.892 -1.876 1.00 39.45 B000 N
ATOM 5921 CA HIS B 345 -13.812 23.098 -2.054 1.00 38.67 B000 C
ATOM 5922 C HIS B 345 -14.561 23.448 -0.767 1.00 39.88 B000 C
ATOM 5923 O HIS B 345 -14.566 24.606 -0.334 1.00 39.52 B000 O
ATOM 5924 CB HIS B 345 -14.783 22.895 -3.219 1.00 41.29 B000 C
ATOM 5925 CG HIS B 345 -15.495 24.139 -3.642 1.00 52.10 B000 C
ATOM 5926 CD2 HIS B 345 -16.723 24.618 -3.322 1.00 63.58 B000 C
ATOM 5927 ND1 HIS B 345 -14.926 25.074 -4.480 1.00 63.72 B000 N
ATOM 5928 CE1 HIS B 345 -15.780 26.066 -4.673 1.00 67.29 B000 C
ATOM 5929 NE2 HIS B 345 -16.875 25.818 -3.976 1.00 62.83 B000 N
ATOM 5930 N TYR B 346 -15.172 22.452 -0.125 1.00 32.58 B000 N
ATOM 5931 CA TYR B 346 -15.917 22.713 1.104 1.00 33.17 B000 C
ATOM 5932 C TYR B 346 -14.992 23.167 2.224 1.00 32.91 B000 C
ATOM 5933 O TYR B 346 -15.301 24.116 2.951 1.00 37.07 B000 O
ATOM 5934 CB TYR B 346 -16.689 21.457 1.517 1.00 31.68 B000 C
ATOM 5935 CG TYR B 346 -17.455 21.589 2.808 1.00 27.57 B000 C
ATOM 5936 CD1 TYR B 346 -16.860 21.293 4.026 1.00 29.58 B000 C
ATOM 5937 CD2 TYR B 346 -18.796 21.992 2.806 1.00 36.09 B000 C
ATOM 5938 CE1 TYR B 346 -17.563 21.398 5.209 1.00 28.90 B000 C
ATOM 5939 CE2 TYR B 346 -19.512 22.115 3.994 1.00 30.98 B000 C
ATOM 5940 CZ TYR B 346 -18.887 21.823 5.192 1.00 31.94 B000 C
ATOM 5941 OH TYR B 346 -19.585 21.920 6.377 1.00 27.19 B000 O
ATOM 5942 N LEU B 347 -13.866 22.474 2.408 1.00 32.88 B000 N
ATOM 5943 CA LEU B 347 -12.997 22.803 3.535 1.00 38.67 B000 C
ATOM 5944 C LEU B 347 -12.293 24.139 3.321 1.00 38.42 B000 C
ATOM 5945 O LEU B 347 -11.998 24.843 4.291 1.00 39.67 B000 O
ATOM 5946 CB LEU B 347 -11.992 21.672 3.762 1.00 37.69 B000 C
ATOM 5947 CG LEU B 347 -12.571 20.330 4.220 1.00 27.23 B000 C
ATOM 5948 CD1 LEU B 347 -11.465 19.296 4.343 1.00 32.53 B000 C
ATOM 5949 CD2 LEU B 347 -13.254 20.500 5.553 1.00 29.13 B000 C
ATOM 5950 N GLU B 348 -12.057 24.519 2.063 1.00 36.46 B000 N
ATOM 5951 CA GLU B 348 -11.489 25.831 1.775 1.00 46.25 B000 C
ATOM 5952 C GLU B 348 -12.349 26.969 2.324 1.00 49.97 B000 C
ATOM 5953 O GLU B 348 -11.818 28.029 2.678 1.00 56.06 B000 O
ATOM 5954 CB GLU B 348 -11.314 25.986 0.266 1.00 47.61 B000 C
ATOM 5955 CG GLU B 348 -10.637 27.277 -0.169 1.00 58.92 B000 C
ATOM 5956 CD GLU B 348 -9.206 27.384 0.316 1.00 60.75 B000 C
ATOM 5957 OE1 GLU B 348 -8.567 26.328 0.508 1.00 64.08 B000 O
ATOM 5958 OE2 GLU B 348 -8.720 28.523 0.517 1.00 65.98 B000 O1-
ATOM 5959 N ARG B 349 -13.670 26.779 2.411 1.00 46.87 B000 N
ATOM 5960 CA ARG B 349 -14.592 27.862 2.742 1.00 48.57 B000 C
ATOM 5961 C ARG B 349 -15.125 27.803 4.170 1.00 49.51 B000 C
ATOM 5962 O ARG B 349 -16.220 28.313 4.431 1.00 56.29 B000 O
ATOM 5963 CB ARG B 349 -15.757 27.881 1.756 1.00 50.05 B000 C
ATOM 5964 CG ARG B 349 -15.428 28.616 0.483 1.00 61.31 B000 C
ATOM 5965 CD ARG B 349 -15.930 27.887 -0.744 1.00 66.94 B000 C
ATOM 5966 NE ARG B 349 -15.218 28.348 -1.928 1.00 70.35 B000 N
ATOM 5967 CZ ARG B 349 -14.101 27.796 -2.383 1.00 69.22 B000 C
ATOM 5968 NH1 ARG B 349 -13.563 26.740 -1.792 1.00 60.16 B000 N1+
ATOM 5969 NH2 ARG B 349 -13.507 28.316 -3.455 1.00 69.26 B000 N
ATOM 5970 N VAL B 350 -14.385 27.207 5.101 1.00 52.64 B000 N
ATOM 5971 CA VAL B 350 -14.793 27.187 6.514 1.00 56.36 B000 C
ATOM 5972 C VAL B 350 -13.606 27.438 7.451 1.00 65.53 B000 C
ATOM 5973 O VAL B 350 -13.720 28.234 8.392 1.00 76.97 B000 O
ATOM 5974 CB VAL B 350 -15.482 25.857 6.902 1.00 50.95 B000 C
ATOM 5975 CG1 VAL B 350 -16.769 25.644 6.104 1.00 47.74 B000 C
ATOM 5976 CG2 VAL B 350 -14.526 24.663 6.757 1.00 42.89 B000 C
ATOM 5977 OXT VAL B 350 -12.515 26.862 7.312 1.00 63.12 B000 O1-
TER
HETATM 5978 P FMN B 400 -27.906 -10.096 45.675 1.00101.99 B000 P
HETATM 5979 O1P FMN B 400 -27.475 -11.545 45.791 1.00 86.46 B000 O
HETATM 5980 O2P FMN B 400 -29.048 -9.833 46.639 1.00 94.32 B000 O1-
HETATM 5981 O3P FMN B 400 -28.338 -9.810 44.245 1.00 80.22 B000 O
HETATM 5982 C5' FMN B 400 -26.175 -8.145 45.207 1.00 67.94 B000 C
HETATM 5983 O5' FMN B 400 -26.650 -9.153 46.074 1.00 80.03 B000 O
HETATM 5984 C4' FMN B 400 -24.769 -7.730 45.625 1.00 53.32 B000 C
HETATM 5985 O4' FMN B 400 -23.909 -8.847 45.583 1.00 50.07 B000 O
HETATM 5986 C3' FMN B 400 -24.292 -6.654 44.670 1.00 50.93 B000 C
HETATM 5987 O3' FMN B 400 -24.856 -5.428 45.102 1.00 50.83 B000 O
HETATM 5988 C2' FMN B 400 -22.751 -6.611 44.584 1.00 40.39 B000 C
HETATM 5989 O2' FMN B 400 -22.368 -5.853 43.451 1.00 44.38 B000 O
HETATM 5990 C1' FMN B 400 -22.183 -6.025 45.864 1.00 42.67 B000 C
HETATM 5991 N1 FMN B 400 -21.272 -8.619 46.803 1.00 35.67 B000 N
HETATM 5992 C2 FMN B 400 -20.865 -9.855 47.254 1.00 39.03 B000 C
HETATM 5993 O2 FMN B 400 -21.685 -10.759 47.397 1.00 37.49 B000 O
HETATM 5994 N3 FMN B 400 -19.525 -10.094 47.532 1.00 36.26 B000 N
HETATM 5995 C4 FMN B 400 -18.582 -9.097 47.354 1.00 38.24 B000 C
HETATM 5996 C4A FMN B 400 -18.997 -7.857 46.907 1.00 35.99 B000 C
HETATM 5997 O4 FMN B 400 -17.386 -9.289 47.606 1.00 32.55 B000 O
HETATM 5998 C5A FMN B 400 -18.456 -5.635 46.286 1.00 37.72 B000 C
HETATM 5999 N5 FMN B 400 -18.056 -6.876 46.734 1.00 35.35 B000 N
HETATM 6000 C6 FMN B 400 -17.517 -4.641 46.106 1.00 34.12 B000 C
HETATM 6001 C7 FMN B 400 -17.887 -3.389 45.654 1.00 35.58 B000 C
HETATM 6002 C7M FMN B 400 -16.831 -2.334 45.481 1.00 38.53 B000 C
HETATM 6003 C8 FMN B 400 -19.216 -3.121 45.374 1.00 36.44 B000 C
HETATM 6004 C8M FMN B 400 -19.624 -1.764 44.883 1.00 42.42 B000 C
HETATM 6005 C9 FMN B 400 -20.170 -4.119 45.539 1.00 35.49 B000 C
HETATM 6006 C9A FMN B 400 -19.789 -5.379 45.993 1.00 38.39 B000 C
HETATM 6007 C10 FMN B 400 -20.345 -7.613 46.620 1.00 39.87 B000 C
HETATM 6008 N10 FMN B 400 -20.737 -6.366 46.159 1.00 40.32 B000 N
CONECT 2775 2776 2777 2778 2780
CONECT 2776 2775
CONECT 2777 2775
CONECT 2778 2775
CONECT 2779 2780 2781
CONECT 2780 2779 2775
CONECT 2781 2779 2782 2783
CONECT 2782 2781
CONECT 2783 2781 2784 2785
CONECT 2784 2783
CONECT 2785 2783 2786 2787
CONECT 2786 2785
CONECT 2787 2785 2805
CONECT 2788 2789 2804
CONECT 2789 2788 2790 2791
CONECT 2790 2789
CONECT 2791 2789 2792
CONECT 2792 2791 2793 2794
CONECT 2793 2792 2796 2804
CONECT 2794 2792
CONECT 2795 2796 2797 2803
CONECT 2796 2793 2795
CONECT 2797 2795 2798
CONECT 2798 2797 2799 2800
CONECT 2799 2798
CONECT 2800 2798 2801 2802
CONECT 2801 2800
CONECT 2802 2800 2803
CONECT 2803 2795 2802 2805
CONECT 2804 2788 2793 2805
CONECT 2805 2787 2803 2804
CONECT 5978 5979 5980 5981 5983
CONECT 5979 5978
CONECT 5980 5978
CONECT 5981 5978
CONECT 5982 5983 5984
CONECT 5983 5982 5978
CONECT 5984 5982 5985 5986
CONECT 5985 5984
CONECT 5986 5984 5987 5988
CONECT 5987 5986
CONECT 5988 5986 5989 5990
CONECT 5989 5988
CONECT 5990 5988 6008
CONECT 5991 5992 6007
CONECT 5992 5991 5993 5994
CONECT 5993 5992
CONECT 5994 5992 5995
CONECT 5995 5994 5996 5997
CONECT 5996 5995 5999 6007
CONECT 5997 5995
CONECT 5998 5999 6000 6006
CONECT 5999 5996 5998
CONECT 6000 5998 6001
CONECT 6001 6000 6002 6003
CONECT 6002 6001
CONECT 6003 6001 6004 6005
CONECT 6004 6003
CONECT 6005 6003 6006
CONECT 6006 5998 6005 6008
CONECT 6007 5991 5996 6008
CONECT 6008 5990 6006 6007
END
A second structure was input as follows:
CRYST1 54.300 145.800 105.300 90.00 90.00 90.00 C 2 2 21 8
ATOM 1 N MET A 1 16.807 19.807 45.664 1.00 78.68 A N
ANISOU 1 N MET A 1 11789 6426 11679 -920 -3273 -53 A N
ATOM 2 CA MET A 1 16.753 18.367 46.021 1.00 75.46 A C
ANISOU 2 CA MET A 1 11096 6663 10914 -779 -2837 -203 A C
ATOM 3 C MET A 1 16.076 17.580 44.913 1.00 73.85 A C
ANISOU 3 C MET A 1 10797 6798 10464 -700 -2528 42 A C
ATOM 4 O MET A 1 15.232 18.106 44.189 1.00 71.64 A O
ANISOU 4 O MET A 1 10683 6301 10234 -568 -2664 160 A O
ATOM 5 CB MET A 1 16.000 18.157 47.334 1.00 72.49 A C
ANISOU 5 CB MET A 1 10737 6387 10418 -335 -2858 -755 A C
ATOM 6 CG MET A 1 16.458 16.938 48.121 1.00 82.02 A C
ANISOU 6 CG MET A 1 11702 8107 11358 -328 -2560 -901 A C
ATOM 7 SD MET A 1 16.108 16.949 49.901 1.00 95.84 A S
ANISOU 7 SD MET A 1 13515 9940 12961 38 -2666 -1496 A S
ATOM 8 CE MET A 1 15.795 18.677 50.261 1.00 85.33 A C
ANISOU 8 CE MET A 1 12535 7923 11962 198 -3198 -1795 A C
ATOM 9 N LYS A 2 16.445 16.312 44.801 1.00 68.68 A N
ANISOU 9 N LYS A 2 9887 6656 9553 -763 -2153 97 A N
ATOM 10 CA LYS A 2 15.884 15.404 43.813 1.00 61.36 A C
ANISOU 10 CA LYS A 2 8862 6079 8371 -692 -1867 269 A C
ATOM 11 C LYS A 2 15.292 14.200 44.530 1.00 58.49 A C
ANISOU 11 C LYS A 2 8330 6102 7793 -411 -1629 -37 A C
ATOM 12 O LYS A 2 15.796 13.772 45.573 1.00 58.82 A O
ANISOU 12 O LYS A 2 8266 6276 7809 -400 -1574 -241 A O
ATOM 13 CB LYS A 2 16.966 14.972 42.821 1.00 69.53 A C
ANISOU 13 CB LYS A 2 9756 7356 9308 -1061 -1643 658 A C
ATOM 14 CG LYS A 2 16.472 14.197 41.622 1.00 70.47 A C
ANISOU 14 CG LYS A 2 9837 7791 9148 -1010 -1405 843 A C
ATOM 15 CD LYS A 2 17.630 13.891 40.681 1.00 73.65 A C
ANISOU 15 CD LYS A 2 10098 8460 9426 -1353 -1171 1193 A C
ATOM 16 CE LYS A 2 17.149 13.333 39.354 1.00 80.88 A C
ANISOU 16 CE LYS A 2 11050 9654 10028 -1308 -990 1382 A C
ATOM 17 NZ LYS A 2 18.219 13.355 38.321 1.00 69.03 A N
ANISOU 17 NZ LYS A 2 9457 8396 8373 -1644 -782 1763 A N
ATOM 18 N ARG A 3 14.206 13.658 43.982 1.00 57.21 A N
ANISOU 18 N ARG A 3 8143 6111 7481 -200 -1516 -47 A N
ATOM 19 CA ARG A 3 13.617 12.447 44.540 1.00 50.94 A C
ANISOU 19 CA ARG A 3 7174 5679 6503 -0 -1287 -261 A C
ATOM 20 C ARG A 3 13.247 11.494 43.412 1.00 55.44 A C
ANISOU 20 C ARG A 3 7658 6511 6895 -24 -1097 -87 A C
ATOM 21 O ARG A 3 12.552 11.874 42.464 1.00 56.61 A O
ANISOU 21 O ARG A 3 7904 6568 7036 30 -1199 43 A O
ATOM 22 CB ARG A 3 12.390 12.772 45.406 1.00 53.22 A C
ANISOU 22 CB ARG A 3 7481 5916 6825 352 -1385 -583 A C
ATOM 23 CG ARG A 3 11.741 11.548 46.049 1.00 53.93 A C
ANISOU 23 CG ARG A 3 7369 6395 6728 506 -1138 -750 A C
ATOM 24 CD ARG A 3 10.907 11.939 47.260 1.00 61.42 A C
ANISOU 24 CD ARG A 3 8299 7368 7670 810 -1184 -1092 A C
ATOM 25 NE ARG A 3 9.933 12.965 46.909 1.00 66.41 A N
ANISOU 25 NE ARG A 3 9014 7760 8459 1056 -1394 -1189 A N
ATOM 26 CZ ARG A 3 9.777 14.121 47.542 1.00 71.33 A C
ANISOU 26 CZ ARG A 3 9783 8099 9221 1263 -1629 -1441 A C
ATOM 27 NH1 ARG A 3 10.466 14.416 48.634 1.00 74.62 A N
ANISOU 27 NH1 ARG A 3 10284 8464 9606 1256 -1683 -1654 A N
ATOM 28 NH2 ARG A 3 8.900 15.002 47.070 1.00 71.03 A N
ANISOU 28 NH2 ARG A 3 9819 7806 9362 1506 -1851 -1503 A N
ATOM 29 N LEU A 4 13.723 10.255 43.535 1.00 52.11 A N
ANISOU 29 N LEU A 4 7074 6393 6333 -89 -861 -100 A N
ATOM 30 CA LEU A 4 13.534 9.200 42.553 1.00 52.98 A C
ANISOU 30 CA LEU A 4 7110 6747 6272 -109 -692 1 A C
ATOM 31 C LEU A 4 12.698 8.068 43.136 1.00 50.38 A C
ANISOU 31 C LEU A 4 6650 6615 5878 57 -586 -188 A C
ATOM 32 O LEU A 4 12.909 7.644 44.277 1.00 48.44 A O
ANISOU 32 O LEU A 4 6320 6441 5643 90 -523 -322 A O
ATOM 33 CB LEU A 4 14.881 8.631 42.102 1.00 51.89 A C
ANISOU 33 CB LEU A 4 6885 6777 6056 -319 -520 141 A C
ATOM 34 CG LEU A 4 15.322 8.900 40.667 1.00 69.77 A C
ANISOU 34 CG LEU A 4 9213 9099 8197 -479 -471 406 A C
ATOM 35 CD1 LEU A 4 15.349 10.384 40.370 1.00 78.19 A C
ANISOU 35 CD1 LEU A 4 10453 9870 9385 -602 -678 610 A C
ATOM 36 CD2 LEU A 4 16.691 8.266 40.444 1.00 70.16 A C
ANISOU 36 CD2 LEU A 4 9092 9386 8178 -637 -253 477 A C
ATOM 37 N THR A 5 11.765 7.565 42.337 1.00 46.49 A N
ANISOU 37 N THR A 5 6141 6213 5311 134 -584 -172 A N
ATOM 38 CA THR A 5 10.937 6.421 42.702 1.00 45.48 A C
ANISOU 38 CA THR A 5 5870 6259 5151 225 -500 -296 A C
ATOM 39 C THR A 5 11.048 5.397 41.584 1.00 48.66 A C
ANISOU 39 C THR A 5 6270 6786 5432 155 -441 -232 A C
ATOM 40 O THR A 5 10.759 5.718 40.427 1.00 48.05 A O
ANISOU 40 O THR A 5 6291 6693 5272 154 -531 -143 A O
ATOM 41 CB THR A 5 9.470 6.824 42.897 1.00 49.50 A C
ANISOU 41 CB THR A 5 6315 6752 5738 410 -611 -396 A C
ATOM 42 CG2 THR A 5 8.670 5.650 43.421 1.00 51.72 A C
ANISOU 42 CG2 THR A 5 6401 7235 6015 437 -504 -482 A C
ATOM 43 OG1 THR A 5 9.370 7.915 43.818 1.00 48.85 A O
ANISOU 43 OG1 THR A 5 6268 6539 5755 533 -688 -507 A O
ATOM 44 N TYR A 6 11.460 4.172 41.911 1.00 46.53 A N
ANISOU 44 N TYR A 6 5915 6627 5139 113 -320 -287 A N
ATOM 45 CA TYR A 6 11.542 3.131 40.895 1.00 44.48 A C
ANISOU 45 CA TYR A 6 5671 6455 4776 90 -293 -300 A C
ATOM 46 C TYR A 6 11.044 1.805 41.457 1.00 43.90 A C
ANISOU 46 C TYR A 6 5492 6410 4778 98 -280 -394 A C
ATOM 47 O TYR A 6 10.893 1.627 42.667 1.00 43.46 A O
ANISOU 47 O TYR A 6 5348 6354 4811 94 -239 -403 A O
ATOM 48 CB TYR A 6 12.978 2.986 40.339 1.00 46.98 A C
ANISOU 48 CB TYR A 6 6022 6843 4985 21 -171 -250 A C
ATOM 49 CG TYR A 6 13.946 2.287 41.268 1.00 42.38 A C
ANISOU 49 CG TYR A 6 5334 6282 4486 6 -70 -300 A C
ATOM 50 CD1 TYR A 6 14.028 0.902 41.302 1.00 42.66 A C
ANISOU 50 CD1 TYR A 6 5327 6343 4541 57 -49 -405 A C
ATOM 51 CD2 TYR A 6 14.767 3.013 42.127 1.00 49.05 A C
ANISOU 51 CD2 TYR A 6 6135 7091 5410 -53 -47 -247 A C
ATOM 52 CE1 TYR A 6 14.895 0.255 42.164 1.00 52.06 A C
ANISOU 52 CE1 TYR A 6 6433 7525 5823 68 -5 -430 A C
ATOM 53 CE2 TYR A 6 15.646 2.373 42.987 1.00 46.95 A C
ANISOU 53 CE2 TYR A 6 5769 6853 5216 -53 -2 -286 A C
ATOM 54 CZ TYR A 6 15.705 0.996 42.999 1.00 49.06 A C
ANISOU 54 CZ TYR A 6 5996 7150 5496 17 21 -365 A C
ATOM 55 OH TYR A 6 16.562 0.357 43.863 1.00 49.90 A O
ANISOU 55 OH TYR A 6 6015 7258 5687 41 20 -382 A O
ATOM 56 N ILE A 7 10.758 0.884 40.538 1.00 45.02 A N
ANISOU 56 N ILE A 7 5664 6572 4868 100 -335 -456 A N
ATOM 57 CA ILE A 7 10.435 -0.501 40.856 1.00 45.77 A C
ANISOU 57 CA ILE A 7 5697 6627 5065 71 -368 -530 A C
ATOM 58 C ILE A 7 11.364 -1.412 40.065 1.00 49.38 A C
ANISOU 58 C ILE A 7 6244 7078 5441 108 -351 -634 A C
ATOM 59 O ILE A 7 11.847 -1.057 38.985 1.00 46.31 A O
ANISOU 59 O ILE A 7 5950 6781 4865 156 -321 -666 A O
ATOM 60 CB ILE A 7 8.938 -0.812 40.573 1.00 46.92 A C
ANISOU 60 CB ILE A 7 5769 6763 5297 43 -525 -558 A C
ATOM 61 CG1 ILE A 7 8.664 -0.998 39.078 1.00 51.88 A C
ANISOU 61 CG1 ILE A 7 6515 7401 5796 79 -676 -650 A C
ATOM 62 CG2 ILE A 7 8.057 0.270 41.181 1.00 57.75 A C
ANISOU 62 CG2 ILE A 7 7022 8192 6728 78 -526 -494 A C
ATOM 63 CD1 ILE A 7 7.342 -1.707 38.799 1.00 60.84 A C
ANISOU 63 CD1 ILE A 7 7556 8497 7065 19 -885 -712 A C
ATOM 64 N SER A 8 11.632 -2.590 40.619 1.00 43.95 A N
ANISOU 64 N SER A 8 5528 6290 4883 100 -368 -684 A N
ATOM 65 CA SER A 8 12.480 -3.557 39.940 1.00 44.97 A C
ANISOU 65 CA SER A 8 5731 6382 4975 196 -378 -842 A C
ATOM 66 C SER A 8 12.052 -4.959 40.342 1.00 48.24 A C
ANISOU 66 C SER A 8 6154 6576 5599 163 -538 -900 A C
ATOM 67 O SER A 8 11.263 -5.147 41.268 1.00 46.99 A O
ANISOU 67 O SER A 8 5919 6339 5596 28 -590 -759 A O
ATOM 68 CB SER A 8 13.963 -3.334 40.263 1.00 47.36 A C
ANISOU 68 CB SER A 8 5983 6769 5244 268 -214 -826 A C
ATOM 69 OG SER A 8 14.220 -3.605 41.634 1.00 50.17 A O
ANISOU 69 OG SER A 8 6262 7030 5768 226 -218 -722 A O
ATOM 70 N LYS A 9 12.588 -5.946 39.628 1.00 50.26 A N
ANISOU 70 N LYS A 9 6506 6736 5856 288 -618 -1108 A N
ATOM 71 CA LYS A 9 12.295 -7.353 39.857 1.00 50.03 A C
ANISOU 71 CA LYS A 9 6534 6413 6063 268 -831 -1187 A C
ATOM 72 C LYS A 9 13.530 -8.056 40.407 1.00 53.85 A C
ANISOU 72 C LYS A 9 7020 6781 6660 410 -808 -1227 A C
ATOM 73 O LYS A 9 14.652 -7.789 39.961 1.00 54.01 A O
ANISOU 73 O LYS A 9 7014 6965 6541 599 -661 -1354 A O
ATOM 74 CB LYS A 9 11.850 -8.027 38.551 1.00 57.80 A C
ANISOU 74 CB LYS A 9 7663 7307 6992 343 -1030 -1467 A C
ATOM 75 CG LYS A 9 11.288 -9.428 38.734 1.00 69.92 A C
ANISOU 75 CG LYS A 9 9275 8462 8830 262 -1331 -1542 A C
ATOM 76 CD LYS A 9 11.084 -10.178 37.407 1.00 83.29 A C
ANISOU 76 CD LYS A 9 11153 10032 10461 392 -1571 -1912 A C
ATOM 77 CE LYS A 9 12.295 -11.011 36.987 1.00114.69 A C
ANISOU 77 CE LYS A 9 15258 13898 14422 702 -1590 -2228 A C
ATOM 78 NZ LYS A 9 12.007 -12.475 37.027 1.00109.77 A N
ANISOU 78 NZ LYS A 9 14785 12785 14138 699 -1964 -2402 A N
ATOM 79 N PHE A 10 13.325 -8.948 41.379 1.00 54.89 A N
ANISOU 79 N PHE A 10 7161 6644 7049 314 -959 -1091 A N
ATOM 80 CA PHE A 10 14.411 -9.810 41.838 1.00 51.78 A C
ANISOU 80 CA PHE A 10 6798 6065 6811 479 -1032 -1138 A C
ATOM 81 C PHE A 10 14.999 -10.574 40.650 1.00 58.21 A C
ANISOU 81 C PHE A 10 7719 6779 7620 755 -1130 -1523 A C
ATOM 82 O PHE A 10 14.269 -11.227 39.900 1.00 57.02 A O
ANISOU 82 O PHE A 10 7703 6437 7524 739 -1334 -1706 A O
ATOM 83 CB PHE A 10 13.911 -10.824 42.878 1.00 61.98 A C
ANISOU 83 CB PHE A 10 8148 7015 8387 307 -1255 -911 A C
ATOM 84 CG PHE A 10 13.580 -10.246 44.248 1.00 55.27 A C
ANISOU 84 CG PHE A 10 7197 6304 7500 91 -1137 -539 A C
ATOM 85 CD1 PHE A 10 13.358 -8.895 44.441 1.00 52.33 A C
ANISOU 85 CD1 PHE A 10 6704 6281 6900 31 -898 -462 A C
ATOM 86 CD2 PHE A 10 13.464 -11.098 45.342 1.00 63.26 A C
ANISOU 86 CD2 PHE A 10 8260 7080 8696 -45 -1291 -269 A C
ATOM 87 CE1 PHE A 10 13.040 -8.399 45.702 1.00 53.05 A C
ANISOU 87 CE1 PHE A 10 6720 6511 6926 -121 -800 -188 A C
ATOM 88 CE2 PHE A 10 13.148 -10.608 46.602 1.00 63.54 A C
ANISOU 88 CE2 PHE A 10 8220 7298 8625 -228 -1169 58 A C
ATOM 89 CZ PHE A 10 12.933 -9.261 46.781 1.00 61.18 A C
ANISOU 89 CZ PHE A 10 7794 7374 8078 -248 -917 67 A C
ATOM 90 N ASER A 11 16.321 -10.496 40.478 0.70 58.65 A N
ANISOU 90 N ASER A 11 7694 6983 7607 1019 -994 -1671 A N
ATOM 91 N BSER A 11 16.322 -10.492 40.484 0.30 58.72 A N
ANISOU 91 N BSER A 11 7702 6992 7616 1018 -993 -1669 A N
ATOM 92 CA ASER A 11 16.972 -11.324 39.470 0.70 61.15 A C
ANISOU 92 CA ASER A 11 8086 7230 7918 1345 -1069 -2075 A C
ATOM 93 CA BSER A 11 16.994 -11.318 39.488 0.30 61.20 A C
ANISOU 93 CA BSER A 11 8089 7239 7926 1347 -1066 -2072 A C
ATOM 94 C ASER A 11 17.003 -12.787 39.887 0.70 61.19 A C
ANISOU 94 C ASER A 11 8233 6728 8290 1450 -1417 -2165 A C
ATOM 95 C BSER A 11 17.038 -12.781 39.906 0.30 61.39 A C
ANISOU 95 C BSER A 11 8253 6757 8316 1455 -1412 -2163 A C
ATOM 96 O ASER A 11 17.113 -13.669 39.029 0.70 66.98 A O
ANISOU 96 O ASER A 11 9106 7266 9076 1691 -1594 -2544 A O
ATOM 97 O BSER A 11 17.173 -13.659 39.047 0.30 67.01 A O
ANISOU 97 O BSER A 11 9103 7279 9080 1702 -1585 -2545 A O
ATOM 98 CB ASER A 11 18.396 -10.833 39.216 0.70 62.14 A C
ANISOU 98 CB ASER A 11 8012 7709 7890 1600 -797 -2193 A C
ATOM 99 CB BSER A 11 18.418 -10.812 39.249 0.30 62.20 A C
ANISOU 99 CB BSER A 11 8013 7721 7898 1597 -792 -2184 A C
ATOM 100 OG ASER A 11 19.248 -11.193 40.291 0.70 67.01 A O
ANISOU 100 OG ASER A 11 8510 8196 8754 1687 -859 -2067 A O
ATOM 101 OG BSER A 11 18.425 -9.661 38.426 0.30 63.44 A O
ANISOU 101 OG BSER A 11 8098 8308 7699 1538 -510 -2181 A O
ATOM 102 N AARG A 12 16.899 -13.052 41.184 0.70 64.25 A N
ANISOU 102 N AARG A 12 8608 6889 8916 1276 -1537 -1823 A N
ATOM 103 N BARG A 12 16.925 -13.055 41.201 0.30 64.34 A N
ANISOU 103 N BARG A 12 8617 6901 8930 1280 -1536 -1822 A N
ATOM 104 CA AARG A 12 16.951 -14.400 41.728 0.70 71.50 A C
ANISOU 104 CA AARG A 12 9678 7283 10206 1330 -1897 -1802 A C
ATOM 105 CA BARG A 12 16.976 -14.409 41.732 0.30 71.46 A C
ANISOU 105 CA BARG A 12 9671 7277 10204 1337 -1898 -1805 A C
ATOM 106 C AARG A 12 16.277 -14.386 43.091 0.70 68.49 A C
ANISOU 106 C AARG A 12 9302 6767 9953 962 -1972 -1298 A C
ATOM 107 C BARG A 12 16.350 -14.396 43.118 0.30 68.58 A C
ANISOU 107 C BARG A 12 9310 6778 9968 978 -1972 -1299 A C
ATOM 108 O AARG A 12 16.056 -13.314 43.667 0.70 63.38 A O
ANISOU 108 O AARG A 12 8515 6470 9095 768 -1720 -1041 A O
ATOM 109 O BARG A 12 16.224 -13.330 43.733 0.30 64.00 A O
ANISOU 109 O BARG A 12 8586 6550 9181 800 -1719 -1042 A O
ATOM 110 CB AARG A 12 18.403 -14.895 41.848 0.70 72.89 A C
ANISOU 110 CB AARG A 12 9781 7406 10509 1739 -1936 -1995 A C
ATOM 111 CB BARG A 12 18.424 -14.930 41.785 0.30 72.90 A C
ANISOU 111 CB BARG A 12 9787 7401 10511 1758 -1941 -2021 A C
ATOM 112 CG AARG A 12 19.171 -14.305 43.030 0.70 77.27 A C
ANISOU 112 CG AARG A 12 10147 8161 11051 1702 -1806 -1669 A C
ATOM 113 CG BARG A 12 19.061 -14.954 43.172 0.30 79.52 A C
ANISOU 113 CG BARG A 12 10535 8177 11502 1725 -1996 -1667 A C
ATOM 114 CD AARG A 12 20.665 -14.618 42.940 0.70 85.31 A C
ANISOU 114 CD AARG A 12 11002 9240 12170 2138 -1808 -1913 A C
ATOM 115 CD BARG A 12 20.542 -15.331 43.091 0.30 82.81 A C
ANISOU 115 CD BARG A 12 10808 8618 12038 2181 -2024 -1921 A C
ATOM 116 NE AARG A 12 21.475 -13.707 43.742 0.70 88.12 A N
ANISOU 116 NE AARG A 12 11107 9949 12426 2101 -1615 -1685 A N
ATOM 117 NE BARG A 12 21.391 -14.482 43.921 0.30 87.89 A N
ANISOU 117 NE BARG A 12 11200 9610 12584 2168 -1837 -1693 A N
ATOM 118 CZ AARG A 12 21.528 -13.717 45.068 0.70 90.62 A C
ANISOU 118 CZ AARG A 12 11440 10151 12843 1941 -1758 -1310 A C
ATOM 119 CZ BARG A 12 21.884 -13.308 43.548 0.30 87.28 A C
ANISOU 119 CZ BARG A 12 10874 10055 12234 2165 -1477 -1749 A C
ATOM 120 NH1AARG A 12 20.826 -14.582 45.783 0.70 90.10 A N
ANISOU 120 NH1AARG A 12 11616 9646 12970 1780 -2062 -1060 A N
ATOM 121 NH1BARG A 12 21.625 -12.794 42.356 0.30 82.06 A N
ANISOU 121 NH1BARG A 12 10187 9670 11324 2177 -1231 -1990 A N
ATOM 122 NH2AARG A 12 22.306 -12.837 45.693 0.70 88.58 A N
ANISOU 122 NH2AARG A 12 10952 10230 12475 1924 -1608 -1171 A N
ATOM 123 NH2BARG A 12 22.660 -12.634 44.392 0.30 86.22 A N
ANISOU 123 NH2BARG A 12 10525 10159 12075 2131 -1391 -1543 A N
ATOM 124 N PRO A 13 15.920 -15.551 43.623 1.00 74.22 A N
ANISOU 124 N PRO A 13 10199 6993 11010 856 -2318 -1144 A N
ATOM 125 CA PRO A 13 15.408 -15.600 44.997 1.00 72.40 A C
ANISOU 125 CA PRO A 13 9969 6686 10853 513 -2363 -618 A C
ATOM 126 C PRO A 13 16.387 -14.965 45.974 1.00 77.10 A C
ANISOU 126 C PRO A 13 10434 7561 11298 618 -2192 -425 A C
ATOM 127 O PRO A 13 17.581 -15.278 45.981 1.00 79.87 A O
ANISOU 127 O PRO A 13 10764 7840 11741 953 -2276 -587 A O
ATOM 128 CB PRO A 13 15.236 -17.100 45.268 1.00 80.89 A C
ANISOU 128 CB PRO A 13 11276 7115 12342 463 -2812 -518 A C
ATOM 129 CG PRO A 13 15.481 -17.809 43.965 1.00 85.68 A C
ANISOU 129 CG PRO A 13 12016 7430 13109 775 -3025 -1054 A C
ATOM 130 CD PRO A 13 15.663 -16.799 42.885 1.00 86.50 A C
ANISOU 130 CD PRO A 13 11974 8037 12855 962 -2690 -1429 A C
ATOM 131 N LEU A 14 15.871 -14.060 46.799 1.00 74.15 A N
ANISOU 131 N LEU A 14 9957 7520 10695 348 -1969 -106 A N
ATOM 132 CA LEU A 14 16.630 -13.429 47.868 1.00 65.35 A C
ANISOU 132 CA LEU A 14 8749 6664 9415 387 -1852 102 A C
ATOM 133 C LEU A 14 15.977 -13.778 49.197 1.00 72.43 A C
ANISOU 133 C LEU A 14 9736 7480 10303 76 -1945 590 A C
ATOM 134 O LEU A 14 14.755 -13.660 49.341 1.00 69.66 A O
ANISOU 134 O LEU A 14 9375 7200 9892 -239 -1855 780 A O
ATOM 135 CB LEU A 14 16.683 -11.909 47.696 1.00 61.09 A C
ANISOU 135 CB LEU A 14 8025 6629 8557 376 -1501 7 A C
ATOM 136 CG LEU A 14 17.165 -11.361 46.355 1.00 59.93 A C
ANISOU 136 CG LEU A 14 7777 6659 8335 597 -1342 -390 A C
ATOM 137 CD1 LEU A 14 17.112 -9.841 46.366 1.00 63.03 A C
ANISOU 137 CD1 LEU A 14 8025 7479 8447 512 -1046 -376 A C
ATOM 138 CD2 LEU A 14 18.574 -11.841 46.051 1.00 74.85 A C
ANISOU 138 CD2 LEU A 14 9608 8475 10356 952 -1430 -621 A C
ATOM 139 N SER A 15 16.785 -14.203 50.162 1.00 66.14 A N
ANISOU 139 N SER A 15 9010 6571 9550 165 -2121 803 A N
ATOM 140 CA SER A 15 16.252 -14.499 51.481 1.00 73.53 A C
ANISOU 140 CA SER A 15 10050 7495 10393 -128 -2191 1307 A C
ATOM 141 C SER A 15 16.006 -13.204 52.247 1.00 67.72 A C
ANISOU 141 C SER A 15 9184 7307 9240 -252 -1870 1423 A C
ATOM 142 O SER A 15 16.483 -12.128 51.879 1.00 59.65 A O
ANISOU 142 O SER A 15 8014 6593 8059 -89 -1667 1139 A O
ATOM 143 CB SER A 15 17.206 -15.396 52.265 1.00 74.93 A C
ANISOU 143 CB SER A 15 10380 7359 10729 24 -2538 1519 A C
ATOM 144 OG SER A 15 18.550 -14.994 52.077 1.00 81.22 A O
ANISOU 144 OG SER A 15 11055 8278 11527 406 -2553 1223 A O
ATOM 145 N GLY A 16 15.247 -13.315 53.335 1.00 66.09 A N
ANISOU 145 N GLY A 16 9038 7221 8851 -548 -1829 1847 A N
ATOM 146 CA GLY A 16 15.019 -12.150 54.169 1.00 70.84 A C
ANISOU 146 CA GLY A 16 9545 8340 9032 -621 -1549 1923 A C
ATOM 147 C GLY A 16 16.315 -11.551 54.682 1.00 66.85 A C
ANISOU 147 C GLY A 16 9034 7994 8371 -362 -1608 1804 A C
ATOM 148 O GLY A 16 16.452 -10.329 54.775 1.00 60.85 A O
ANISOU 148 O GLY A 16 8160 7593 7368 -296 -1399 1607 A O
ATOM 149 N AASP A 17 17.294 -12.402 54.997 0.53 64.96 A N
ANISOU 149 N AASP A 17 8913 7462 8308 -206 -1932 1908 A N
ATOM 150 N BASP A 17 17.282 -12.404 55.025 0.47 64.99 A N
ANISOU 150 N BASP A 17 8919 7469 8306 -212 -1932 1918 A N
ATOM 151 CA AASP A 17 18.540 -11.891 55.558 0.53 67.95 A C
ANISOU 151 CA AASP A 17 9251 8002 8566 24 -2038 1820 A C
ATOM 152 CA BASP A 17 18.548 -11.900 55.545 0.47 67.96 A C
ANISOU 152 CA BASP A 17 9252 7997 8572 26 -2041 1817 A C
ATOM 153 C AASP A 17 19.352 -11.133 54.514 0.53 64.84 A C
ANISOU 153 C AASP A 17 8639 7694 8302 273 -1931 1352 A C
ATOM 154 C BASP A 17 19.277 -11.073 54.496 0.47 64.83 A C
ANISOU 154 C BASP A 17 8635 7712 8287 259 -1909 1348 A C
ATOM 155 O AASP A 17 20.053 -10.174 54.858 0.53 61.40 A O
ANISOU 155 O AASP A 17 8090 7540 7700 362 -1880 1224 A O
ATOM 156 O BASP A 17 19.841 -10.018 54.807 0.47 61.03 A O
ANISOU 156 O BASP A 17 8039 7535 7613 323 -1819 1214 A O
ATOM 157 CB AASP A 17 19.354 -13.035 56.176 0.53 69.49 A C
ANISOU 157 CB AASP A 17 9607 7856 8942 147 -2453 2073 A C
ATOM 158 CB BASP A 17 19.428 -13.059 56.014 0.47 69.55 A C
ANISOU 158 CB BASP A 17 9597 7832 8997 179 -2458 2022 A C
ATOM 159 CG AASP A 17 19.799 -14.073 55.159 0.53 73.91 A C
ANISOU 159 CG AASP A 17 10174 7922 9985 364 -2685 1884 A C
ATOM 160 CG BASP A 17 18.981 -13.632 57.343 0.47 75.18 A C
ANISOU 160 CG BASP A 17 10545 8540 9482 -55 -2608 2564 A C
ATOM 161 OD1AASP A 17 18.930 -14.735 54.555 0.53 75.99 A O
ANISOU 161 OD1AASP A 17 10524 7907 10443 215 -2684 1917 A O
ATOM 162 OD1BASP A 17 18.142 -12.998 58.019 0.47 79.60 A O
ANISOU 162 OD1BASP A 17 11119 9485 9642 -299 -2350 2739 A O
ATOM 163 OD2AASP A 17 21.026 -14.250 54.992 0.53 77.98 A O
ANISOU 163 OD2AASP A 17 10600 8333 10696 696 -2890 1687 A O
ATOM 164 OD2BASP A 17 19.477 -14.716 57.719 0.47 85.93 A O
ANISOU 164 OD2BASP A 17 12077 9523 11050 20 -2987 2819 A O
ATOM 165 N GLU A 18 19.253 -11.523 53.240 1.00 61.23 A N
ANISOU 165 N GLU A 18 8124 7018 8122 368 -1899 1100 A N
ATOM 166 CA GLU A 18 19.951 -10.792 52.187 1.00 66.45 A C
ANISOU 166 CA GLU A 18 8573 7825 8848 571 -1745 698 A C
ATOM 167 C GLU A 18 19.325 -9.423 51.973 1.00 57.32 A C
ANISOU 167 C GLU A 18 7323 7023 7430 417 -1423 596 A C
ATOM 168 O GLU A 18 20.033 -8.441 51.717 1.00 58.40 A O
ANISOU 168 O GLU A 18 7300 7385 7505 504 -1312 402 A O
ATOM 169 CB GLU A 18 19.939 -11.587 50.882 1.00 65.01 A C
ANISOU 169 CB GLU A 18 8389 7358 8953 726 -1788 443 A C
ATOM 170 CG GLU A 18 20.665 -12.922 50.956 1.00 73.89 A C
ANISOU 170 CG GLU A 18 9601 8076 10399 963 -2141 454 A C
ATOM 171 CD GLU A 18 20.602 -13.683 49.643 1.00 91.17 A C
ANISOU 171 CD GLU A 18 11813 9983 12843 1150 -2193 125 A C
ATOM 172 OE1 GLU A 18 21.493 -13.469 48.792 1.00 87.76 A O
ANISOU 172 OE1 GLU A 18 11193 9684 12468 1445 -2100 -234 A O
ATOM 173 OE2 GLU A 18 19.651 -14.477 49.455 1.00 77.11 A O
ANISOU 173 OE2 GLU A 18 10231 7873 11194 992 -2323 219 A O
ATOM 174 N ILE A 19 17.994 -9.339 52.063 1.00 57.00 A N
ANISOU 174 N ILE A 19 7365 7026 7267 183 -1290 731 A N
ATOM 175 CA ILE A 19 17.321 -8.052 51.915 1.00 56.99 A C
ANISOU 175 CA ILE A 19 7281 7332 7042 77 -1021 630 A C
ATOM 176 C ILE A 19 17.703 -7.125 53.060 1.00 54.44 A C
ANISOU 176 C ILE A 19 6952 7283 6452 65 -996 694 A C
ATOM 177 O ILE A 19 17.939 -5.927 52.856 1.00 52.28 A O
ANISOU 177 O ILE A 19 6585 7199 6079 99 -873 504 A O
ATOM 178 CB ILE A 19 15.796 -8.250 51.828 1.00 65.54 A C
ANISOU 178 CB ILE A 19 8401 8420 8082 -145 -905 761 A C
ATOM 179 CG1 ILE A 19 15.419 -8.888 50.485 1.00 63.02 A C
ANISOU 179 CG1 ILE A 19 8077 7855 8012 -126 -944 597 A C
ATOM 180 CG2 ILE A 19 15.060 -6.918 52.002 1.00 53.92 A C
ANISOU 180 CG2 ILE A 19 6843 7282 6361 -216 -661 690 A C
ATOM 181 CD1 ILE A 19 14.307 -9.919 50.591 1.00 71.68 A C
ANISOU 181 CD1 ILE A 19 9249 8744 9242 -350 -1039 821 A C
ATOM 182 N AGLU A 20 17.755 -7.659 54.284 0.65 56.94 A N
ANISOU 182 N AGLU A 20 7390 7608 6636 8 -1140 969 A N
ATOM 183 N BGLU A 20 17.787 -7.660 54.278 0.35 57.04 A N
ANISOU 183 N BGLU A 20 7401 7618 6652 13 -1144 966 A N
ATOM 184 CA AGLU A 20 18.193 -6.860 55.424 0.65 60.29 A C
ANISOU 184 CA AGLU A 20 7844 8297 6768 23 -1170 1000 A C
ATOM 185 CA BGLU A 20 18.174 -6.831 55.413 0.35 60.26 A C
ANISOU 185 CA BGLU A 20 7838 8298 6760 21 -1163 995 A C
ATOM 186 C AGLU A 20 19.605 -6.338 55.210 0.65 57.29 A C
ANISOU 186 C AGLU A 20 7340 7918 6509 201 -1304 782 A C
ATOM 187 C BGLU A 20 19.628 -6.380 55.307 0.35 57.30 A C
ANISOU 187 C BGLU A 20 7352 7921 6499 200 -1321 801 A C
ATOM 188 O AGLU A 20 19.909 -5.185 55.538 0.65 52.45 A O
ANISOU 188 O AGLU A 20 6678 7510 5739 205 -1267 633 A O
ATOM 189 O BGLU A 20 19.978 -5.304 55.807 0.35 53.32 A O
ANISOU 189 O BGLU A 20 6817 7629 5815 207 -1313 680 A O
ATOM 190 CB AGLU A 20 18.139 -7.688 56.711 0.65 58.83 A C
ANISOU 190 CB AGLU A 20 7836 8117 6398 -54 -1345 1365 A C
ATOM 191 CB BGLU A 20 17.947 -7.591 56.721 0.35 59.65 A C
ANISOU 191 CB BGLU A 20 7940 8258 6468 -78 -1301 1365 A C
ATOM 192 CG AGLU A 20 16.900 -7.457 57.565 0.65 66.38 A C
ANISOU 192 CG AGLU A 20 8875 9361 6987 -251 -1141 1571 A C
ATOM 193 CG BGLU A 20 16.479 -7.735 57.139 0.35 64.78 A C
ANISOU 193 CG BGLU A 20 8645 9071 6899 -307 -1084 1593 A C
ATOM 194 CD AGLU A 20 16.811 -6.041 58.106 0.65 76.12 A C
ANISOU 194 CD AGLU A 20 10079 10963 7882 -200 -990 1347 A C
ATOM 195 CD BGLU A 20 15.705 -6.427 57.100 0.35 69.28 A C
ANISOU 195 CD BGLU A 20 9113 9973 7238 -322 -791 1366 A C
ATOM 196 OE1AGLU A 20 17.713 -5.630 58.869 0.65 67.31 A O
ANISOU 196 OE1AGLU A 20 9028 9952 6594 -97 -1169 1293 A O
ATOM 197 OE1BGLU A 20 16.104 -5.474 57.801 0.35 71.88 A O
ANISOU 197 OE1BGLU A 20 9470 10542 7299 -231 -791 1224 A O
ATOM 198 OE2AGLU A 20 15.835 -5.337 57.765 0.65 71.85 A O
ANISOU 198 OE2AGLU A 20 9449 10584 7265 -247 -728 1206 A O
ATOM 199 OE2BGLU A 20 14.689 -6.355 56.374 0.35 70.46 A O
ANISOU 199 OE2BGLU A 20 9158 10122 7492 -412 -598 1314 A O
ATOM 200 N ALA A 21 20.487 -7.179 54.669 1.00 51.54 A N
ANISOU 200 N ALA A 21 6543 6959 6082 352 -1475 749 A N
ATOM 201 CA ALA A 21 21.876 -6.766 54.491 1.00 52.79 A C
ANISOU 201 CA ALA A 21 6509 7165 6384 517 -1595 565 A C
ATOM 202 C ALA A 21 21.980 -5.648 53.461 1.00 50.17 A C
ANISOU 202 C ALA A 21 5996 6968 6099 496 -1359 298 A C
ATOM 203 O ALA A 21 22.804 -4.738 53.607 1.00 52.06 A O
ANISOU 203 O ALA A 21 6089 7355 6336 500 -1394 184 A O
ATOM 204 CB ALA A 21 22.736 -7.960 54.083 1.00 63.28 A C
ANISOU 204 CB ALA A 21 7764 8240 8038 734 -1807 558 A C
ATOM 205 N ILE A 22 21.143 -5.693 52.420 1.00 51.99 A N
ANISOU 205 N ILE A 22 6241 7138 6373 450 -1147 219 A N
ATOM 206 CA ILE A 22 21.080 -4.587 51.468 1.00 51.34 A C
ANISOU 206 CA ILE A 22 6041 7184 6282 401 -931 30 A C
ATOM 207 C ILE A 22 20.673 -3.306 52.178 1.00 56.50 A C
ANISOU 207 C ILE A 22 6752 8002 6714 269 -882 28 A C
ATOM 208 O ILE A 22 21.249 -2.237 51.943 1.00 51.22 A O
ANISOU 208 O ILE A 22 5972 7422 6067 234 -856 -90 A O
ATOM 209 CB ILE A 22 20.118 -4.923 50.313 1.00 55.19 A C
ANISOU 209 CB ILE A 22 6579 7581 6810 380 -764 -33 A C
ATOM 210 CG1 ILE A 22 20.732 -5.994 49.405 1.00 56.52 A C
ANISOU 210 CG1 ILE A 22 6677 7599 7199 562 -815 -145 A C
ATOM 211 CG2 ILE A 22 19.767 -3.656 49.516 1.00 57.03 A C
ANISOU 211 CG2 ILE A 22 6760 7951 6957 294 -565 -153 A C
ATOM 212 CD1 ILE A 22 19.724 -6.688 48.515 1.00 59.43 A C
ANISOU 212 CD1 ILE A 22 7161 7809 7609 548 -763 -198 A C
ATOM 213 N GLY A 23 19.687 -3.396 53.073 1.00 51.25 A N
ANISOU 213 N GLY A 23 6257 7381 5836 194 -875 155 A N
ATOM 214 CA GLY A 23 19.261 -2.219 53.808 1.00 51.21 A C
ANISOU 214 CA GLY A 23 6319 7544 5595 131 -834 93 A C
ATOM 215 C GLY A 23 20.325 -1.695 54.753 1.00 49.00 A C
ANISOU 215 C GLY A 23 6029 7344 5244 159 -1048 48 A C
ATOM 216 O GLY A 23 20.469 -0.480 54.921 1.00 51.31 A O
ANISOU 216 O GLY A 23 6319 7701 5476 126 -1065 -111 A O
ATOM 217 N ARG A 24 21.064 -2.599 55.405 1.00 51.58 A N
ANISOU 217 N ARG A 24 6366 7643 5591 222 -1258 186 A N
ATOM 218 CA ARG A 24 22.138 -2.178 56.299 1.00 52.74 A C
ANISOU 218 CA ARG A 24 6484 7870 5684 254 -1522 143 A C
ATOM 219 C ARG A 24 23.205 -1.400 55.542 1.00 56.11 A C
ANISOU 219 C ARG A 24 6664 8272 6384 242 -1560 -37 A C
ATOM 220 O ARG A 24 23.612 -0.310 55.959 1.00 52.95 A O
ANISOU 220 O ARG A 24 6246 7936 5938 174 -1676 -170 A O
ATOM 221 CB ARG A 24 22.783 -3.387 56.984 1.00 67.42 A C
ANISOU 221 CB ARG A 24 8376 9673 7567 351 -1779 348 A C
ATOM 222 CG ARG A 24 22.052 -3.893 58.198 1.00 68.00 A C
ANISOU 222 CG ARG A 24 8714 9845 7277 314 -1840 579 A C
ATOM 223 CD ARG A 24 22.977 -4.607 59.177 1.00 63.12 A C
ANISOU 223 CD ARG A 24 8157 9216 6610 404 -2209 761 A C
ATOM 224 NE ARG A 24 23.745 -5.706 58.596 1.00 56.02 A N
ANISOU 224 NE ARG A 24 7125 8066 6093 539 -2369 847 A N
ATOM 225 CZ ARG A 24 23.217 -6.841 58.152 1.00 64.56 A C
ANISOU 225 CZ ARG A 24 8282 8925 7322 551 -2315 1025 A C
ATOM 226 NH1 ARG A 24 21.910 -7.039 58.149 1.00 54.89 A N
ANISOU 226 NH1 ARG A 24 7222 7710 5923 394 -2085 1166 A N
ATOM 227 NH2 ARG A 24 24.022 -7.801 57.707 1.00 62.92 A N
ANISOU 227 NH2 ARG A 24 7967 8471 7469 733 -2517 1046 A N
ATOM 228 N ILE A 25 23.710 -1.973 54.445 1.00 47.01 A N
ANISOU 228 N ILE A 25 5310 7033 5517 304 -1476 -43 A N
ATOM 229 CA ILE A 25 24.767 -1.295 53.702 1.00 53.93 A C
ANISOU 229 CA ILE A 25 5901 7954 6637 268 -1467 -167 A C
ATOM 230 C ILE A 25 24.231 0.000 53.114 1.00 49.20 A C
ANISOU 230 C ILE A 25 5335 7365 5995 105 -1287 -263 A C
ATOM 231 O ILE A 25 24.924 1.026 53.096 1.00 50.38 A O
ANISOU 231 O ILE A 25 5352 7542 6247 -19 -1370 -334 A O
ATOM 232 CB ILE A 25 25.336 -2.218 52.612 1.00 55.42 A C
ANISOU 232 CB ILE A 25 5866 8112 7078 408 -1362 -180 A C
ATOM 233 CG1 ILE A 25 26.221 -3.294 53.236 1.00 62.77 A C
ANISOU 233 CG1 ILE A 25 6700 9005 8143 601 -1631 -118 A C
ATOM 234 CG2 ILE A 25 26.129 -1.417 51.588 1.00 57.80 A C
ANISOU 234 CG2 ILE A 25 5866 8535 7562 325 -1214 -279 A C
ATOM 235 CD1 ILE A 25 26.350 -4.535 52.381 1.00 70.30 A C
ANISOU 235 CD1 ILE A 25 7574 9846 9289 816 -1561 -148 A C
ATOM 236 N SER A 26 22.992 -0.029 52.625 1.00 48.87 A N
ANISOU 236 N SER A 26 5463 7276 5831 95 -1074 -252 A N
ATOM 237 CA ASER A 26 22.375 1.172 52.067 0.82 52.73 A C
ANISOU 237 CA ASER A 26 6011 7739 6286 -23 -941 -329 A C
ATOM 238 CA BSER A 26 22.409 1.179 52.061 0.18 52.71 A C
ANISOU 238 CA BSER A 26 6003 7737 6288 -24 -943 -329 A C
ATOM 239 C SER A 26 22.278 2.273 53.114 1.00 52.06 A C
ANISOU 239 C SER A 26 6059 7652 6071 -85 -1112 -426 A C
ATOM 240 O SER A 26 22.539 3.446 52.826 1.00 50.88 A O
ANISOU 240 O SER A 26 5881 7432 6020 -204 -1156 -505 A O
ATOM 241 CB ASER A 26 20.979 0.854 51.525 0.82 49.32 A C
ANISOU 241 CB ASER A 26 5727 7270 5740 9 -737 -304 A C
ATOM 242 CB BSER A 26 21.052 0.869 51.442 0.18 49.58 A C
ANISOU 242 CB BSER A 26 5745 7302 5790 6 -734 -306 A C
ATOM 243 OG ASER A 26 21.021 -0.039 50.430 0.82 47.02 A O
ANISOU 243 OG ASER A 26 5347 6954 5564 65 -606 -270 A O
ATOM 244 OG BSER A 26 20.402 2.076 51.110 0.18 51.16 A O
ANISOU 244 OG BSER A 26 6027 7462 5949 -70 -669 -378 A O
ATOM 245 N SER A 27 21.879 1.908 54.336 1.00 52.61 A N
ANISOU 245 N SER A 27 6294 7793 5902 -7 -1220 -420 A N
ATOM 246 CA ASER A 27 21.798 2.883 55.418 0.56 58.27 A C
ANISOU 246 CA ASER A 27 7164 8543 6432 -17 -1398 -571 A C
ATOM 247 CA BSER A 27 21.797 2.885 55.415 0.44 58.26 A C
ANISOU 247 CA BSER A 27 7163 8542 6431 -17 -1398 -571 A C
ATOM 248 C SER A 27 23.153 3.529 55.673 1.00 57.19 A C
ANISOU 248 C SER A 27 6892 8362 6477 -112 -1679 -651 A C
ATOM 249 O SER A 27 23.257 4.753 55.812 1.00 60.07 A O
ANISOU 249 O SER A 27 7312 8628 6884 -199 -1810 -813 A O
ATOM 250 CB ASER A 27 21.286 2.208 56.691 0.56 60.82 A C
ANISOU 250 CB ASER A 27 7671 9031 6408 85 -1452 -513 A C
ATOM 251 CB BSER A 27 21.274 2.215 56.686 0.44 60.83 A C
ANISOU 251 CB BSER A 27 7673 9032 6409 85 -1449 -514 A C
ATOM 252 OG ASER A 27 21.077 3.160 57.716 0.56 72.20 A O
ANISOU 252 OG ASER A 27 9287 10550 7594 120 -1593 -713 A O
ATOM 253 OG BSER A 27 20.819 3.179 57.615 0.44 71.88 A O
ANISOU 253 OG BSER A 27 9259 10512 7539 127 -1534 -715 A O
ATOM 254 N GLN A 28 24.207 2.712 55.747 1.00 53.64 A N
ANISOU 254 N GLN A 28 6251 7964 6168 -94 -1806 -544 A N
ATOM 255 CA GLN A 28 25.528 3.229 56.072 1.00 53.39 A C
ANISOU 255 CA GLN A 28 6026 7929 6330 -190 -2103 -607 A C
ATOM 256 C GLN A 28 26.020 4.214 55.024 1.00 58.07 A C
ANISOU 256 C GLN A 28 6412 8421 7233 -391 -2033 -635 A C
ATOM 257 O GLN A 28 26.582 5.261 55.361 1.00 59.65 A O
ANISOU 257 O GLN A 28 6579 8537 7549 -550 -2275 -742 A O
ATOM 258 CB GLN A 28 26.517 2.072 56.206 1.00 54.06 A C
ANISOU 258 CB GLN A 28 5888 8102 6552 -88 -2231 -479 A C
ATOM 259 CG GLN A 28 26.278 1.206 57.432 1.00 61.92 A C
ANISOU 259 CG GLN A 28 7102 9173 7250 66 -2416 -399 A C
ATOM 260 CD GLN A 28 27.017 -0.120 57.367 1.00 67.68 A C
ANISOU 260 CD GLN A 28 7653 9914 8147 217 -2517 -238 A C
ATOM 261 NE2 GLN A 28 26.487 -1.127 58.055 1.00 65.12 A N
ANISOU 261 NE2 GLN A 28 7561 9593 7589 340 -2568 -73 A N
ATOM 262 OE1 GLN A 28 28.055 -0.234 56.713 1.00 64.22 A O
ANISOU 262 OE1 GLN A 28 6864 9483 8052 228 -2552 -256 A O
ATOM 263 N ALYS A 29 25.829 3.890 53.743 0.45 51.27 A N
ANISOU 263 N ALYS A 29 5418 7562 6500 -402 -1723 -528 A N
ATOM 264 N BLYS A 29 25.830 3.889 53.744 0.55 51.20 A N
ANISOU 264 N BLYS A 29 5410 7554 6491 -402 -1724 -528 A N
ATOM 265 CA ALYS A 29 26.327 4.758 52.681 0.45 57.81 A C
ANISOU 265 CA ALYS A 29 6045 8342 7579 -616 -1625 -485 A C
ATOM 266 CA BLYS A 29 26.326 4.759 52.682 0.55 57.81 A C
ANISOU 266 CA BLYS A 29 6044 8342 7578 -616 -1626 -485 A C
ATOM 267 C ALYS A 29 25.463 6.006 52.535 0.45 57.72 A C
ANISOU 267 C ALYS A 29 6287 8132 7511 -731 -1621 -553 A C
ATOM 268 C BLYS A 29 25.463 6.007 52.541 0.55 57.74 A C
ANISOU 268 C BLYS A 29 6290 8134 7513 -731 -1623 -554 A C
ATOM 269 O ALYS A 29 25.986 7.116 52.376 0.45 56.34 A O
ANISOU 269 O ALYS A 29 6049 7824 7535 -959 -1767 -556 A O
ATOM 270 O BLYS A 29 25.985 7.120 52.399 0.55 56.30 A O
ANISOU 270 O BLYS A 29 6046 7817 7528 -958 -1773 -559 A O
ATOM 271 CB ALYS A 29 26.385 3.977 51.367 0.45 59.49 A C
ANISOU 271 CB ALYS A 29 6065 8671 7868 -559 -1296 -366 A C
ATOM 272 CB BLYS A 29 26.383 3.978 51.368 0.55 59.49 A C
ANISOU 272 CB BLYS A 29 6066 8670 7867 -559 -1296 -366 A C
ATOM 273 CG ALYS A 29 27.409 2.842 51.389 0.45 60.61 A C
ANISOU 273 CG ALYS A 29 5903 8983 8144 -415 -1323 -338 A C
ATOM 274 CG BLYS A 29 27.426 2.858 51.392 0.55 60.61 A C
ANISOU 274 CG BLYS A 29 5898 8983 8146 -418 -1326 -337 A C
ATOM 275 CD ALYS A 29 27.499 2.113 50.056 0.45 63.06 A C
ANISOU 275 CD ALYS A 29 6032 9420 8508 -317 -999 -292 A C
ATOM 276 CD BLYS A 29 27.403 2.005 50.130 0.55 63.00 A C
ANISOU 276 CD BLYS A 29 6056 9401 8481 -291 -1006 -297 A C
ATOM 277 CE ALYS A 29 28.373 2.864 49.066 0.45 66.17 A C
ANISOU 277 CE ALYS A 29 6089 9965 9087 -531 -844 -215 A C
ATOM 278 CE BLYS A 29 28.177 2.654 48.993 0.55 66.28 A C
ANISOU 278 CE BLYS A 29 6151 9973 9060 -478 -809 -225 A C
ATOM 279 NZ ALYS A 29 28.065 2.486 47.658 0.45 65.05 A N
ANISOU 279 NZ ALYS A 29 5907 9950 8857 -466 -482 -183 A N
ATOM 280 NZ BLYS A 29 29.598 2.927 49.352 0.55 69.04 A N
ANISOU 280 NZ BLYS A 29 6090 10465 9676 -592 -980 -205 A N
ATOM 281 N ASN A 30 24.142 5.848 52.607 1.00 54.11 A N
ANISOU 281 N ASN A 30 6106 7637 6815 -578 -1482 -604 A N
ATOM 282 CA ASN A 30 23.251 6.991 52.432 1.00 56.01 A C
ANISOU 282 CA ASN A 30 6574 7685 7024 -620 -1487 -691 A C
ATOM 283 C ASN A 30 23.469 8.036 53.520 1.00 56.19 A C
ANISOU 283 C ASN A 30 6748 7557 7045 -665 -1830 -897 A C
ATOM 284 O ASN A 30 23.466 9.242 53.245 1.00 57.46 A O
ANISOU 284 O ASN A 30 6989 7471 7372 -807 -1964 -949 A O
ATOM 285 CB ASN A 30 21.797 6.521 52.426 1.00 50.98 A C
ANISOU 285 CB ASN A 30 6137 7094 6139 -416 -1285 -726 A C
ATOM 286 CG ASN A 30 21.420 5.768 51.159 1.00 53.48 A C
ANISOU 286 CG ASN A 30 6358 7477 6485 -398 -997 -565 A C
ATOM 287 ND2 ASN A 30 20.164 5.343 51.086 1.00 50.07 A N
ANISOU 287 ND2 ASN A 30 6056 7080 5886 -258 -848 -582 A N
ATOM 288 OD1 ASN A 30 22.241 5.568 50.260 1.00 50.02 A O
ANISOU 288 OD1 ASN A 30 5716 7084 6207 -506 -912 -441 A O
ATOM 289 N GLN A 31 23.663 7.593 54.766 1.00 55.83 A N
ANISOU 289 N GLN A 31 6769 7639 6806 -545 -2007 -1017 A N
ATOM 290 CA GLN A 31 23.916 8.533 55.852 1.00 56.36 A C
ANISOU 290 CA GLN A 31 7002 7589 6823 -563 -2369 -1265 A C
ATOM 291 C GLN A 31 25.079 9.458 55.522 1.00 63.51 A C
ANISOU 291 C GLN A 31 7731 8286 8112 -858 -2634 -1246 A C
ATOM 292 O GLN A 31 25.017 10.666 55.779 1.00 67.39 A O
ANISOU 292 O GLN A 31 8394 8505 8707 -947 -2891 -1430 A O
ATOM 293 CB GLN A 31 24.201 7.764 57.143 1.00 63.07 A C
ANISOU 293 CB GLN A 31 7908 8667 7388 -419 -2536 -1334 A C
ATOM 294 CG GLN A 31 24.338 8.640 58.377 1.00 83.28 A C
ANISOU 294 CG GLN A 31 10697 11164 9783 -381 -2918 -1645 A C
ATOM 295 CD GLN A 31 23.767 7.981 59.616 1.00 98.37 A C
ANISOU 295 CD GLN A 31 12832 13357 11188 -137 -2923 -1736 A C
ATOM 296 NE2 GLN A 31 22.763 8.614 60.215 1.00113.30 A N
ANISOU 296 NE2 GLN A 31 15007 15269 12774 41 -2898 -2005 A N
ATOM 297 OE1 GLN A 31 24.212 6.906 60.022 1.00 93.25 A O
ANISOU 297 OE1 GLN A 31 12097 12917 10417 -99 -2944 -1555 A O
ATOM 298 N GLN A 32 26.156 8.906 54.959 1.00 61.37 A N
ANISOU 298 N GLN A 32 7102 8139 8077 -1014 -2585 -1031 A N
ATOM 299 CA GLN A 32 27.314 9.725 54.630 1.00 65.29 A C
ANISOU 299 CA GLN A 32 7348 8498 8960 -1343 -2807 -962 A C
ATOM 300 C GLN A 32 26.999 10.728 53.530 1.00 69.31 A C
ANISOU 300 C GLN A 32 7899 8754 9680 -1560 -2691 -837 A C
ATOM 301 O GLN A 32 27.581 11.822 53.507 1.00 70.48 A O
ANISOU 301 O GLN A 32 8014 8646 10121 -1851 -2969 -835 A O
ATOM 302 CB GLN A 32 28.481 8.841 54.193 1.00 75.69 A C
ANISOU 302 CB GLN A 32 8206 10080 10471 -1421 -2712 -758 A C
ATOM 303 CG GLN A 32 28.979 7.895 55.251 1.00 73.10 A C
ANISOU 303 CG GLN A 32 7810 9957 10006 -1228 -2911 -838 A C
ATOM 304 CD GLN A 32 30.173 7.100 54.776 1.00 61.84 A C
ANISOU 304 CD GLN A 32 5891 8769 8837 -1266 -2849 -668 A C
ATOM 305 NE2 GLN A 32 29.935 5.855 54.386 1.00 76.69 A N
ANISOU 305 NE2 GLN A 32 7710 10829 10598 -1018 -2567 -575 A N
ATOM 306 OE1 GLN A 32 31.291 7.609 54.727 1.00 70.58 A O
ANISOU 306 OE1 GLN A 32 6655 9891 10270 -1514 -3055 -629 A O
ATOM 307 N ALA A 33 26.101 10.371 52.612 1.00 67.61 A N
ANISOU 307 N ALA A 33 7762 8590 9335 -1442 -2321 -712 A N
ATOM 308 CA ALA A 33 25.768 11.200 51.464 1.00 67.89 A C
ANISOU 308 CA ALA A 33 7848 8421 9525 -1627 -2198 -536 A C
ATOM 309 C ALA A 33 24.571 12.105 51.718 1.00 72.57 A C
ANISOU 309 C ALA A 33 8849 8695 10030 -1493 -2326 -724 A C
ATOM 310 O ALA A 33 24.117 12.786 50.791 1.00 72.20 A O
ANISOU 310 O ALA A 33 8902 8441 10089 -1594 -2258 -575 A O
ATOM 311 CB ALA A 33 25.493 10.317 50.244 1.00 65.18 A C
ANISOU 311 CB ALA A 33 7359 8328 9077 -1561 -1761 -308 A C
ATOM 312 N AASN A 34 24.058 12.138 52.946 0.46 67.36 A N
ANISOU 312 N AASN A 34 8420 8008 9164 -1248 -2515 -1047 A N
ATOM 313 N BASN A 34 24.055 12.130 52.945 0.54 67.34 A N
ANISOU 313 N BASN A 34 8418 8009 9161 -1247 -2513 -1047 A N
ATOM 314 CA AASN A 34 22.869 12.924 53.268 0.46 66.95 A C
ANISOU 314 CA AASN A 34 8721 7714 9002 -1035 -2610 -1293 A C
ATOM 315 CA BASN A 34 22.869 12.918 53.270 0.54 66.93 A C
ANISOU 315 CA BASN A 34 8718 7714 8999 -1034 -2609 -1293 A C
ATOM 316 C AASN A 34 21.722 12.560 52.330 0.46 66.42 A C
ANISOU 316 C AASN A 34 8704 7722 8811 -873 -2259 -1159 A C
ATOM 317 C BASN A 34 21.724 12.560 52.330 0.54 66.41 A C
ANISOU 317 C BASN A 34 8703 7721 8810 -874 -2259 -1159 A C
ATOM 318 O AASN A 34 21.020 13.425 51.802 0.46 67.82 A O
ANISOU 318 O AASN A 34 9058 7620 9092 -847 -2310 -1167 A O
ATOM 319 O BASN A 34 21.029 13.428 51.796 0.54 67.84 A O
ANISOU 319 O BASN A 34 9058 7620 9096 -850 -2311 -1165 A O
ATOM 320 CB AASN A 34 23.165 14.424 53.213 0.46 70.34 A C
ANISOU 320 CB AASN A 34 9306 7661 9760 -1247 -2991 -1367 A C
ATOM 321 CB BASN A 34 23.174 14.415 53.224 0.54 70.34 A C
ANISOU 321 CB BASN A 34 9303 7663 9758 -1247 -2992 -1368 A C
ATOM 322 CG AASN A 34 24.074 14.882 54.339 0.46 73.75 A C
ANISOU 322 CG AASN A 34 9758 7975 10288 -1357 -3424 -1609 A C
ATOM 323 CG BASN A 34 22.184 15.237 54.031 0.54 74.53 A C
ANISOU 323 CG BASN A 34 10205 7942 10172 -949 -3220 -1777 A C
ATOM 324 ND2AASN A 34 24.956 15.827 54.039 0.46 77.59 A N
ANISOU 324 ND2AASN A 34 10178 8119 11182 -1734 -3733 -1498 A N
ATOM 325 ND2BASN A 34 21.993 16.491 53.635 0.54 75.61 A N
ANISOU 325 ND2BASN A 34 10538 7591 10601 -1044 -3481 -1809 A N
ATOM 326 OD1AASN A 34 23.980 14.396 55.466 0.46 76.11 A O
ANISOU 326 OD1AASN A 34 10136 8493 10290 -1124 -3499 -1876 A O
ATOM 327 OD1BASN A 34 21.602 14.751 55.000 0.54 76.65 A O
ANISOU 327 OD1BASN A 34 10581 8456 10086 -628 -3164 -2056 A O
ATOM 328 N VAL A 35 21.547 11.260 52.110 1.00 59.58 A N
ANISOU 328 N VAL A 35 7683 7209 7745 -765 -1942 -1035 A N
ATOM 329 CA VAL A 35 20.461 10.717 51.306 1.00 60.27 A C
ANISOU 329 CA VAL A 35 7794 7408 7696 -611 -1633 -932 A C
ATOM 330 C VAL A 35 19.506 9.999 52.248 1.00 54.33 A C
ANISOU 330 C VAL A 35 7135 6877 6630 -315 -1530 -1124 A C
ATOM 331 O VAL A 35 19.937 9.386 53.229 1.00 54.38 A O
ANISOU 331 O VAL A 35 7109 7068 6485 -267 -1582 -1199 A O
ATOM 332 CB VAL A 35 21.006 9.765 50.224 1.00 52.84 A C
ANISOU 332 CB VAL A 35 6606 6677 6792 -739 -1368 -645 A C
ATOM 333 CG1 VAL A 35 19.896 8.917 49.638 1.00 52.76 A C
ANISOU 333 CG1 VAL A 35 6625 6825 6598 -552 -1094 -598 A C
ATOM 334 CG2 VAL A 35 21.739 10.561 49.141 1.00 61.29 A C
ANISOU 334 CG2 VAL A 35 7583 7591 8113 -1038 -1395 -410 A C
ATOM 335 N THR A 36 18.209 10.098 51.972 1.00 52.87 A N
ANISOU 335 N THR A 36 7052 6689 6345 -125 -1395 -1183 A N
ATOM 336 CA THR A 36 17.203 9.411 52.767 1.00 48.23 A C
ANISOU 336 CA THR A 36 6497 6361 5465 119 -1242 -1315 A C
ATOM 337 C THR A 36 16.260 8.682 51.824 1.00 53.65 A C
ANISOU 337 C THR A 36 7092 7165 6126 170 -975 -1150 A C
ATOM 338 O THR A 36 16.219 8.959 50.622 1.00 53.38 A O
ANISOU 338 O THR A 36 7036 6986 6261 78 -947 -1004 A O
ATOM 339 CB THR A 36 16.404 10.372 53.655 1.00 55.17 A C
ANISOU 339 CB THR A 36 7563 7170 6229 357 -1375 -1651 A C
ATOM 340 CG2 THR A 36 17.279 10.958 54.733 1.00 60.67 A C
ANISOU 340 CG2 THR A 36 8380 7782 6891 332 -1671 -1870 A C
ATOM 341 OG1 THR A 36 15.856 11.431 52.857 1.00 57.02 A O
ANISOU 341 OG1 THR A 36 7886 7096 6682 402 -1469 -1694 A O
ATOM 342 N GLY A 37 15.492 7.748 52.368 1.00 49.64 A N
ANISOU 342 N GLY A 37 6537 6927 5397 298 -796 -1158 A N
ATOM 343 CA GLY A 37 14.556 7.027 51.532 1.00 53.89 A C
ANISOU 343 CA GLY A 37 6976 7562 5937 324 -589 -1021 A C
ATOM 344 C GLY A 37 14.021 5.781 52.211 1.00 53.93 A C
ANISOU 344 C GLY A 37 6901 7852 5737 363 -417 -950 A C
ATOM 345 O GLY A 37 14.241 5.541 53.400 1.00 50.73 A O
ANISOU 345 O GLY A 37 6539 7606 5132 402 -437 -1004 A O
ATOM 346 N VAL A 38 13.316 4.990 51.407 1.00 51.03 A N
ANISOU 346 N VAL A 38 6431 7538 5420 333 -273 -809 A N
ATOM 347 CA AVAL A 38 12.656 3.783 51.879 0.77 49.05 A C
ANISOU 347 CA AVAL A 38 6093 7506 5039 318 -123 -689 A C
ATOM 348 CA BVAL A 38 12.627 3.791 51.865 0.23 49.36 A C
ANISOU 348 CA BVAL A 38 6131 7546 5079 319 -121 -690 A C
ATOM 349 C VAL A 38 12.776 2.713 50.802 1.00 53.16 A C
ANISOU 349 C VAL A 38 6545 7945 5708 196 -86 -511 A C
ATOM 350 O VAL A 38 12.788 3.005 49.603 1.00 48.75 A O
ANISOU 350 O VAL A 38 5982 7251 5291 178 -110 -513 A O
ATOM 351 CB AVAL A 38 11.182 4.084 52.242 0.77 55.67 A C
ANISOU 351 CB AVAL A 38 6845 8534 5774 453 5 -785 A C
ATOM 352 CB BVAL A 38 11.135 4.063 52.151 0.23 55.79 A C
ANISOU 352 CB BVAL A 38 6852 8542 5802 450 8 -779 A C
ATOM 353 CG1AVAL A 38 10.370 4.354 50.988 0.77 53.89 A C
ANISOU 353 CG1AVAL A 38 6538 8199 5741 481 8 -787 A C
ATOM 354 CG1BVAL A 38 10.451 2.808 52.674 0.23 59.30 A C
ANISOU 354 CG1BVAL A 38 7176 9230 6126 364 172 -596 A C
ATOM 355 CG2AVAL A 38 10.590 2.955 53.057 0.77 59.00 A C
ANISOU 355 CG2AVAL A 38 7169 9231 6017 391 166 -629 A C
ATOM 356 CG2BVAL A 38 10.987 5.208 53.131 0.23 58.44 A C
ANISOU 356 CG2BVAL A 38 7268 8952 5984 640 -35 -1036 A C
ATOM 357 N LEU A 39 12.896 1.465 51.248 1.00 48.06 A N
ANISOU 357 N LEU A 39 5873 7374 5014 119 -49 -359 A N
ATOM 358 CA LEU A 39 13.030 0.308 50.371 1.00 44.52 A C
ANISOU 358 CA LEU A 39 5387 6816 4712 33 -53 -233 A C
ATOM 359 C LEU A 39 11.989 -0.715 50.793 1.00 49.73 A C
ANISOU 359 C LEU A 39 5982 7575 5336 -46 21 -84 A C
ATOM 360 O LEU A 39 11.999 -1.174 51.937 1.00 49.28 A O
ANISOU 360 O LEU A 39 5947 7643 5134 -85 42 37 A O
ATOM 361 CB LEU A 39 14.437 -0.286 50.453 1.00 45.46 A C
ANISOU 361 CB LEU A 39 5541 6840 4890 14 -153 -181 A C
ATOM 362 CG LEU A 39 14.700 -1.573 49.671 1.00 53.41 A C
ANISOU 362 CG LEU A 39 6530 7714 6049 -14 -185 -105 A C
ATOM 363 CD1 LEU A 39 14.432 -1.351 48.194 1.00 49.44 A C
ANISOU 363 CD1 LEU A 39 6004 7143 5637 -1 -145 -200 A C
ATOM 364 CD2 LEU A 39 16.130 -2.076 49.898 1.00 60.54 A C
ANISOU 364 CD2 LEU A 39 7428 8551 7024 31 -293 -86 A C
ATOM 365 N LEU A 40 11.083 -1.059 49.886 1.00 49.40 A N
ANISOU 365 N LEU A 40 5860 7491 5419 -91 45 -73 A N
ATOM 366 CA LEU A 40 10.057 -2.052 50.159 1.00 47.44 A C
ANISOU 366 CA LEU A 40 5511 7311 5202 -224 92 92 A C
ATOM 367 C LEU A 40 10.244 -3.230 49.222 1.00 50.67 A C
ANISOU 367 C LEU A 40 5957 7476 5817 -316 -35 148 A C
ATOM 368 O LEU A 40 10.702 -3.073 48.089 1.00 49.93 A O
ANISOU 368 O LEU A 40 5917 7244 5808 -244 -105 8 A O
ATOM 369 CB LEU A 40 8.656 -1.474 49.975 1.00 54.15 A C
ANISOU 369 CB LEU A 40 6184 8333 6056 -204 188 33 A C
ATOM 370 CG LEU A 40 8.335 -0.322 50.915 1.00 66.96 A C
ANISOU 370 CG LEU A 40 7761 10202 7479 -55 310 -84 A C
ATOM 371 CD1 LEU A 40 8.173 0.926 50.119 1.00 69.45 A C
ANISOU 371 CD1 LEU A 40 8084 10439 7865 116 252 -301 A C
ATOM 372 CD2 LEU A 40 7.060 -0.622 51.670 1.00 69.91 A C
ANISOU 372 CD2 LEU A 40 7911 10886 7766 -118 485 23 A C
ATOM 373 N CYS A 41 9.895 -4.417 49.693 1.00 47.90 A N
ANISOU 373 N CYS A 41 5594 7073 5535 -477 -72 354 A N
ATOM 374 CA CYS A 41 9.824 -5.554 48.796 1.00 51.88 A C
ANISOU 374 CA CYS A 41 6137 7303 6271 -563 -234 370 A C
ATOM 375 C CYS A 41 8.524 -6.307 49.029 1.00 52.46 A C
ANISOU 375 C CYS A 41 6073 7400 6458 -801 -239 568 A C
ATOM 376 O CYS A 41 7.967 -6.329 50.129 1.00 54.55 A O
ANISOU 376 O CYS A 41 6237 7886 6606 -926 -107 784 A O
ATOM 377 CB CYS A 41 11.026 -6.485 48.942 1.00 55.46 A C
ANISOU 377 CB CYS A 41 6752 7513 6809 -522 -382 417 A C
ATOM 378 SG CYS A 41 11.138 -7.352 50.481 1.00 61.43 A S
ANISOU 378 SG CYS A 41 7567 8264 7511 -670 -420 769 A S
ATOM 379 N LEU A 42 8.036 -6.897 47.950 1.00 51.08 A N
ANISOU 379 N LEU A 42 5884 7025 6498 -871 -394 487 A N
ATOM 380 CA LEU A 42 6.783 -7.638 47.991 1.00 54.40 A C
ANISOU 380 CA LEU A 42 6140 7429 7099 -1139 -452 664 A C
ATOM 381 C LEU A 42 6.823 -8.643 46.859 1.00 55.81 A C
ANISOU 381 C LEU A 42 6438 7227 7540 -1190 -740 542 A C
ATOM 382 O LEU A 42 6.890 -8.246 45.688 1.00 53.82 A O
ANISOU 382 O LEU A 42 6232 6935 7282 -1034 -818 264 A O
ATOM 383 CB LEU A 42 5.588 -6.695 47.850 1.00 53.44 A C
ANISOU 383 CB LEU A 42 5748 7629 6927 -1139 -310 605 A C
ATOM 384 CG LEU A 42 4.202 -7.337 47.942 1.00 61.06 A C
ANISOU 384 CG LEU A 42 6438 8668 8093 -1436 -340 798 A C
ATOM 385 CD1 LEU A 42 3.985 -8.028 49.284 1.00 68.57 A C
ANISOU 385 CD1 LEU A 42 7311 9738 9005 -1693 -210 1181 A C
ATOM 386 CD2 LEU A 42 3.141 -6.277 47.697 1.00 64.91 A C
ANISOU 386 CD2 LEU A 42 6631 9488 8544 -1342 -219 673 A C
ATOM 387 N ASP A 43 6.801 -9.924 47.199 1.00 59.33 A N
ANISOU 387 N ASP A 43 6961 7385 8198 -1398 -916 746 A N
ATOM 388 CA ASP A 43 6.683 -11.009 46.234 1.00 67.45 A C
ANISOU 388 CA ASP A 43 8110 7997 9520 -1474 -1243 622 A C
ATOM 389 C ASP A 43 7.581 -10.782 45.018 1.00 67.24 A C
ANISOU 389 C ASP A 43 8273 7850 9424 -1146 -1335 211 A C
ATOM 390 O ASP A 43 7.136 -10.755 43.873 1.00 63.38 A O
ANISOU 390 O ASP A 43 7790 7310 8980 -1108 -1474 -34 A O
ATOM 391 CB ASP A 43 5.233 -11.185 45.786 1.00 76.09 A C
ANISOU 391 CB ASP A 43 8976 9129 10806 -1740 -1343 665 A C
ATOM 392 CG ASP A 43 5.011 -12.492 45.054 1.00 86.87 A C
ANISOU 392 CG ASP A 43 10477 10008 12523 -1904 -1741 595 A C
ATOM 393 OD1 ASP A 43 5.620 -13.506 45.458 1.00 79.90 A O
ANISOU 393 OD1 ASP A 43 9800 8755 11805 -1963 -1913 723 A O
ATOM 394 OD2 ASP A 43 4.254 -12.505 44.060 1.00 78.51 A O
ANISOU 394 OD2 ASP A 43 9338 8910 11581 -1955 -1923 392 A O
ATOM 395 N GLY A 44 8.869 -10.605 45.297 1.00 58.21 A N
ANISOU 395 N GLY A 44 7268 6702 8148 -911 -1253 150 A N
ATOM 396 CA GLY A 44 9.863 -10.554 44.241 1.00 59.44 A C
ANISOU 396 CA GLY A 44 7575 6770 8240 -610 -1308 -202 A C
ATOM 397 C GLY A 44 9.984 -9.231 43.530 1.00 54.20 A C
ANISOU 397 C GLY A 44 6849 6435 7308 -444 -1110 -389 A C
ATOM 398 O GLY A 44 10.657 -9.166 42.491 1.00 52.83 A O
ANISOU 398 O GLY A 44 6780 6252 7042 -230 -1133 -665 A O
ATOM 399 N ILE A 45 9.335 -8.180 44.042 1.00 53.61 A N
ANISOU 399 N ILE A 45 6613 6654 7104 -530 -922 -245 A N
ATOM 400 CA ILE A 45 9.427 -6.829 43.508 1.00 49.56 A C
ANISOU 400 CA ILE A 45 6059 6403 6369 -389 -766 -366 A C
ATOM 401 C ILE A 45 10.049 -5.928 44.562 1.00 49.56 A C
ANISOU 401 C ILE A 45 6013 6594 6226 -334 -559 -244 A C
ATOM 402 O ILE A 45 9.688 -5.998 45.740 1.00 48.04 A O
ANISOU 402 O ILE A 45 5739 6473 6043 -451 -492 -43 A O
ATOM 403 CB ILE A 45 8.041 -6.273 43.093 1.00 50.58 A C
ANISOU 403 CB ILE A 45 6042 6672 6505 -485 -793 -361 A C
ATOM 404 CG1 ILE A 45 7.342 -7.235 42.137 1.00 54.02 A C
ANISOU 404 CG1 ILE A 45 6513 6907 7106 -578 -1060 -481 A C
ATOM 405 CG2 ILE A 45 8.188 -4.885 42.493 1.00 52.81 A C
ANISOU 405 CG2 ILE A 45 6333 7155 6579 -323 -687 -462 A C
ATOM 406 CD1 ILE A 45 8.071 -7.392 40.810 1.00 64.82 A C
ANISOU 406 CD1 ILE A 45 8092 8187 8350 -382 -1167 -769 A C
ATOM 407 N PHE A 46 10.992 -5.089 44.135 1.00 45.25 A N
ANISOU 407 N PHE A 46 5520 6142 5532 -172 -465 -362 A N
ATOM 408 CA PHE A 46 11.512 -3.998 44.947 1.00 45.48 A C
ANISOU 408 CA PHE A 46 5510 6336 5435 -128 -317 -296 A C
ATOM 409 C PHE A 46 10.802 -2.703 44.565 1.00 44.27 A C
ANISOU 409 C PHE A 46 5306 6328 5185 -104 -258 -333 A C
ATOM 410 O PHE A 46 10.549 -2.454 43.384 1.00 46.97 A O
ANISOU 410 O PHE A 46 5688 6664 5495 -64 -311 -429 A O
ATOM 411 CB PHE A 46 13.014 -3.792 44.727 1.00 43.76 A C
ANISOU 411 CB PHE A 46 5344 6119 5166 -3 -275 -374 A C
ATOM 412 CG PHE A 46 13.905 -4.781 45.432 1.00 49.28 A C
ANISOU 412 CG PHE A 46 6063 6699 5962 31 -340 -326 A C
ATOM 413 CD1 PHE A 46 13.917 -4.883 46.812 1.00 51.49 A C
ANISOU 413 CD1 PHE A 46 6330 6999 6235 -36 -348 -153 A C
ATOM 414 CD2 PHE A 46 14.776 -5.569 44.699 1.00 46.87 A C
ANISOU 414 CD2 PHE A 46 5795 6282 5732 163 -402 -467 A C
ATOM 415 CE1 PHE A 46 14.768 -5.774 47.446 1.00 50.51 A C
ANISOU 415 CE1 PHE A 46 6244 6750 6199 9 -455 -80 A C
ATOM 416 CE2 PHE A 46 15.631 -6.459 45.325 1.00 54.15 A C
ANISOU 416 CE2 PHE A 46 6727 7068 6780 242 -502 -434 A C
ATOM 417 CZ PHE A 46 15.625 -6.563 46.700 1.00 52.24 A C
ANISOU 417 CZ PHE A 46 6486 6812 6550 156 -547 -221 A C
ATOM 418 N PHE A 47 10.511 -1.871 45.562 1.00 44.20 A N
ANISOU 418 N PHE A 47 5231 6447 5118 -103 -170 -270 A N
ATOM 419 CA PHE A 47 10.096 -0.488 45.359 1.00 46.18 A C
ANISOU 419 CA PHE A 47 5462 6782 5301 -23 -142 -329 A C
ATOM 420 C PHE A 47 11.033 0.384 46.188 1.00 46.96 A C
ANISOU 420 C PHE A 47 5613 6909 5321 29 -86 -338 A C
ATOM 421 O PHE A 47 11.244 0.090 47.368 1.00 47.59 A O
ANISOU 421 O PHE A 47 5674 7052 5357 8 -44 -288 A O
ATOM 422 CB PHE A 47 8.652 -0.208 45.814 1.00 46.77 A C
ANISOU 422 CB PHE A 47 5378 6987 5404 -23 -118 -315 A C
ATOM 423 CG PHE A 47 7.639 -1.255 45.414 1.00 54.32 A C
ANISOU 423 CG PHE A 47 6216 7938 6485 -142 -186 -265 A C
ATOM 424 CD1 PHE A 47 7.637 -2.510 46.006 1.00 50.05 A C
ANISOU 424 CD1 PHE A 47 5645 7357 6015 -296 -183 -138 A C
ATOM 425 CD2 PHE A 47 6.636 -0.950 44.506 1.00 57.54 A C
ANISOU 425 CD2 PHE A 47 6536 8366 6960 -114 -291 -326 A C
ATOM 426 CE1 PHE A 47 6.703 -3.458 45.656 1.00 51.42 A C
ANISOU 426 CE1 PHE A 47 5707 7481 6350 -452 -284 -77 A C
ATOM 427 CE2 PHE A 47 5.691 -1.896 44.150 1.00 56.10 A C
ANISOU 427 CE2 PHE A 47 6220 8171 6924 -252 -397 -290 A C
ATOM 428 CZ PHE A 47 5.719 -3.151 44.729 1.00 50.71 A C
ANISOU 428 CZ PHE A 47 5506 7424 6338 -438 -391 -166 A C
ATOM 429 N GLN A 48 11.580 1.452 45.604 1.00 46.21 A N
ANISOU 429 N GLN A 48 5592 6764 5203 76 -111 -384 A N
ATOM 430 CA GLN A 48 12.456 2.327 46.374 1.00 47.15 A C
ANISOU 430 CA GLN A 48 5755 6869 5291 92 -111 -405 A C
ATOM 431 C GLN A 48 12.202 3.793 46.056 1.00 48.93 A C
ANISOU 431 C GLN A 48 6044 7015 5533 147 -180 -453 A C
ATOM 432 O GLN A 48 11.911 4.157 44.910 1.00 45.89 A O
ANISOU 432 O GLN A 48 5701 6569 5165 148 -225 -418 A O
ATOM 433 CB GLN A 48 13.931 2.007 46.121 1.00 50.55 A C
ANISOU 433 CB GLN A 48 6201 7265 5741 35 -106 -370 A C
ATOM 434 CG GLN A 48 14.888 2.818 46.999 1.00 48.80 A C
ANISOU 434 CG GLN A 48 5992 7025 5524 15 -154 -389 A C
ATOM 435 CD GLN A 48 16.301 2.264 46.977 1.00 46.97 A C
ANISOU 435 CD GLN A 48 5691 6812 5342 -31 -153 -352 A C
ATOM 436 NE2 GLN A 48 16.908 2.121 48.151 1.00 48.17 A N
ANISOU 436 NE2 GLN A 48 5824 6991 5488 -28 -223 -360 A N
ATOM 437 OE1 GLN A 48 16.845 1.986 45.909 1.00 49.69 A O
ANISOU 437 OE1 GLN A 48 5990 7175 5715 -51 -94 -326 A O
ATOM 438 N ILE A 49 12.299 4.623 47.094 1.00 48.98 A N
ANISOU 438 N ILE A 49 6081 7005 5524 205 -217 -538 A N
ATOM 439 CA ILE A 49 12.310 6.078 46.980 1.00 47.57 A C
ANISOU 439 CA ILE A 49 6003 6664 5408 259 -342 -603 A C
ATOM 440 C ILE A 49 13.626 6.575 47.562 1.00 49.41 A C
ANISOU 440 C ILE A 49 6298 6808 5669 168 -416 -616 A C
ATOM 441 O ILE A 49 13.992 6.194 48.680 1.00 48.22 A O
ANISOU 441 O ILE A 49 6124 6757 5440 181 -402 -682 A O
ATOM 442 CB ILE A 49 11.125 6.728 47.713 1.00 52.25 A C
ANISOU 442 CB ILE A 49 6575 7291 5985 458 -370 -772 A C
ATOM 443 CG1 ILE A 49 9.797 6.242 47.132 1.00 46.29 A C
ANISOU 443 CG1 ILE A 49 5690 6651 5247 532 -316 -751 A C
ATOM 444 CG2 ILE A 49 11.188 8.238 47.583 1.00 53.24 A C
ANISOU 444 CG2 ILE A 49 6843 7162 6224 543 -561 -864 A C
ATOM 445 CD1 ILE A 49 8.608 6.447 48.066 1.00 54.81 A C
ANISOU 445 CD1 ILE A 49 6631 7910 6283 726 -251 -911 A C
ATOM 446 N LEU A 50 14.326 7.427 46.810 1.00 45.59 A N
ANISOU 446 N LEU A 50 5885 6145 5291 56 -512 -529 A N
ATOM 447 CA LEU A 50 15.581 8.032 47.249 1.00 46.84 A C
ANISOU 447 CA LEU A 50 6067 6193 5536 -81 -621 -521 A C
ATOM 448 C LEU A 50 15.508 9.544 47.093 1.00 56.73 A C
ANISOU 448 C LEU A 50 7472 7149 6935 -102 -831 -542 A C
ATOM 449 O LEU A 50 15.031 10.039 46.067 1.00 52.01 A O
ANISOU 449 O LEU A 50 6946 6429 6385 -112 -866 -420 A O
ATOM 450 CB LEU A 50 16.765 7.518 46.434 1.00 52.91 A C
ANISOU 450 CB LEU A 50 6722 7043 6338 -271 -527 -336 A C
ATOM 451 CG LEU A 50 17.117 6.033 46.458 1.00 60.00 A C
ANISOU 451 CG LEU A 50 7479 8164 7152 -244 -369 -321 A C
ATOM 452 CD1 LEU A 50 17.906 5.691 45.198 1.00 61.05 A C
ANISOU 452 CD1 LEU A 50 7514 8392 7291 -354 -244 -175 A C
ATOM 453 CD2 LEU A 50 17.912 5.681 47.693 1.00 60.75 A C
ANISOU 453 CD2 LEU A 50 7507 8315 7260 -245 -436 -393 A C
ATOM 454 N GLU A 51 16.013 10.280 48.087 1.00 54.10 A N
ANISOU 454 N GLU A 51 7208 6671 6676 -113 -1013 -691 A N
ATOM 455 CA GLU A 51 15.949 11.737 48.044 1.00 52.19 A C
ANISOU 455 CA GLU A 51 7144 6064 6620 -125 -1278 -746 A C
ATOM 456 C GLU A 51 17.222 12.343 48.619 1.00 59.72 A C
ANISOU 456 C GLU A 51 8117 6849 7726 -337 -1483 -765 A C
ATOM 457 O GLU A 51 17.791 11.836 49.590 1.00 55.14 A O
ANISOU 457 O GLU A 51 7460 6432 7059 -334 -1484 -893 A O
ATOM 458 CB GLU A 51 14.707 12.268 48.789 1.00 65.22 A C
ANISOU 458 CB GLU A 51 8913 7642 8227 205 -1373 -1050 A C
ATOM 459 CG GLU A 51 14.654 11.922 50.261 1.00 61.17 A C
ANISOU 459 CG GLU A 51 8383 7329 7531 368 -1350 -1336 A C
ATOM 460 CD GLU A 51 13.288 12.155 50.894 1.00 68.58 A C
ANISOU 460 CD GLU A 51 9349 8363 8344 726 -1315 -1622 A C
ATOM 461 OE1 GLU A 51 12.390 12.729 50.235 1.00 65.22 A O
ANISOU 461 OE1 GLU A 51 8957 7784 8039 876 -1370 -1637 A O
ATOM 462 OE2 GLU A 51 13.117 11.759 52.065 1.00 61.49 A O
ANISOU 462 OE2 GLU A 51 8425 7726 7214 866 -1232 -1826 A O
ATOM 463 N GLY A 52 17.670 13.416 47.982 1.00 60.07 A N
ANISOU 463 N GLY A 52 8258 6560 8006 -545 -1681 -606 A N
ATOM 464 CA GLY A 52 18.866 14.120 48.392 1.00 63.23 A C
ANISOU 464 CA GLY A 52 8657 6745 8623 -813 -1923 -586 A C
ATOM 465 C GLY A 52 19.310 15.041 47.272 1.00 65.76 A C
ANISOU 465 C GLY A 52 9031 6769 9185 -1127 -2039 -244 A C
ATOM 466 O GLY A 52 18.587 15.257 46.301 1.00 62.48 A O
ANISOU 466 O GLY A 52 8718 6277 8743 -1080 -1982 -66 A O
ATOM 467 N AGLU A 53 20.522 15.569 47.433 0.44 68.04 A N
ANISOU 467 N AGLU A 53 9240 6907 9706 -1468 -2219 -128 A N
ATOM 468 N BGLU A 53 20.512 15.587 47.433 0.56 68.01 A N
ANISOU 468 N BGLU A 53 9240 6896 9705 -1467 -2224 -129 A N
ATOM 469 CA AGLU A 53 21.112 16.414 46.404 0.44 70.70 A C
ANISOU 469 CA AGLU A 53 9586 6998 10279 -1858 -2312 275 A C
ATOM 470 CA BGLU A 53 21.051 16.458 46.397 0.56 70.67 A C
ANISOU 470 CA BGLU A 53 9600 6973 10277 -1847 -2322 271 A C
ATOM 471 C AGLU A 53 21.196 15.656 45.084 0.44 73.08 A C
ANISOU 471 C AGLU A 53 9712 7678 10378 -1961 -1917 638 A C
ATOM 472 C BGLU A 53 21.200 15.682 45.093 0.56 73.07 A C
ANISOU 472 C BGLU A 53 9715 7666 10383 -1964 -1925 638 A C
ATOM 473 O AGLU A 53 21.594 14.488 45.045 0.44 69.73 A O
ANISOU 473 O AGLU A 53 9029 7703 9762 -1912 -1611 622 A O
ATOM 474 O BGLU A 53 21.644 14.530 45.078 0.56 69.70 A O
ANISOU 474 O BGLU A 53 9022 7686 9773 -1926 -1625 622 A O
ATOM 475 CB AGLU A 53 22.503 16.880 46.843 0.44 75.62 A C
ANISOU 475 CB AGLU A 53 10044 7503 11185 -2250 -2521 355 A C
ATOM 476 CB BGLU A 53 22.392 17.052 46.824 0.56 75.63 A C
ANISOU 476 CB BGLU A 53 10097 7429 11211 -2244 -2566 352 A C
ATOM 477 CG AGLU A 53 22.576 17.359 48.294 0.44 77.45 A C
ANISOU 477 CG AGLU A 53 10416 7469 11542 -2122 -2906 -84 A C
ATOM 478 CG BGLU A 53 22.271 18.256 47.761 0.56 70.98 A C
ANISOU 478 CG BGLU A 53 9794 6276 10901 -2224 -3079 63 A C
ATOM 479 CD AGLU A 53 22.987 16.258 49.261 0.44 75.90 A C
ANISOU 479 CD AGLU A 53 10007 7700 11133 -1959 -2773 -336 A C
ATOM 480 CD BGLU A 53 21.486 19.410 47.159 0.56 73.94 A C
ANISOU 480 CD BGLU A 53 10513 6117 11463 -2208 -3335 178 A C
ATOM 481 OE1AGLU A 53 22.184 15.317 49.469 0.44 64.68 A O
ANISOU 481 OE1AGLU A 53 8597 6590 9389 -1605 -2513 -495 A O
ATOM 482 OE1BGLU A 53 20.238 19.361 47.187 0.56 83.62 A O
ANISOU 482 OE1BGLU A 53 11939 7308 12525 -1785 -3303 -38 A O
ATOM 483 OE2AGLU A 53 24.105 16.340 49.814 0.44 77.98 A O
ANISOU 483 OE2AGLU A 53 10088 7973 11568 -2200 -2958 -356 A O
ATOM 484 OE2BGLU A 53 22.114 20.369 46.663 0.56 83.84 A O
ANISOU 484 OE2BGLU A 53 11825 6980 13051 -2625 -3587 501 A O
ATOM 485 N ALA A 54 20.810 16.328 43.992 1.00 77.04 A N
ANISOU 485 N ALA A 54 10379 7982 10910 -2084 -1951 956 A N
ATOM 486 CA ALA A 54 20.761 15.660 42.694 1.00 81.27 A C
ANISOU 486 CA ALA A 54 10808 8892 11178 -2141 -1597 1267 A C
ATOM 487 C ALA A 54 22.077 14.975 42.347 1.00 79.82 A C
ANISOU 487 C ALA A 54 10249 9142 10938 -2417 -1297 1463 A C
ATOM 488 O ALA A 54 22.083 13.854 41.827 1.00 71.82 A O
ANISOU 488 O ALA A 54 9065 8579 9643 -2282 -951 1454 A O
ATOM 489 CB ALA A 54 20.393 16.674 41.607 1.00 87.24 A C
ANISOU 489 CB ALA A 54 11812 9346 11988 -2320 -1743 1656 A C
ATOM 490 N GLU A 55 23.202 15.639 42.619 1.00 86.87 A N
ANISOU 490 N GLU A 55 10990 9900 12118 -2796 -1443 1622 A N
ATOM 491 CA GLU A 55 24.503 15.047 42.321 1.00 91.82 A C
ANISOU 491 CA GLU A 55 11185 10969 12733 -3053 -1162 1801 A C
ATOM 492 C GLU A 55 24.676 13.707 43.025 1.00 81.37 A C
ANISOU 492 C GLU A 55 9632 10022 11264 -2737 -976 1445 A C
ATOM 493 O GLU A 55 25.175 12.744 42.431 1.00 79.27 A O
ANISOU 493 O GLU A 55 9083 10226 10809 -2700 -621 1510 A O
ATOM 494 CB GLU A 55 25.621 16.007 42.735 1.00104.25 A C
ANISOU 494 CB GLU A 55 12603 12296 14712 -3510 -1428 1976 A C
ATOM 495 CG GLU A 55 25.764 17.241 41.853 1.00133.22 A C
ANISOU 495 CG GLU A 55 16416 15647 18553 -3950 -1565 2470 A C
ATOM 496 CD GLU A 55 24.643 18.248 42.051 1.00147.86 A C
ANISOU 496 CD GLU A 55 18783 16859 20537 -3812 -1977 2390 A C
ATOM 497 OE1 GLU A 55 24.025 18.252 43.138 1.00105.88 A O
ANISOU 497 OE1 GLU A 55 13654 11289 15287 -3466 -2229 1918 A O
ATOM 498 OE2 GLU A 55 24.383 19.037 41.118 1.00165.70 A O
ANISOU 498 OE2 GLU A 55 21257 18883 22821 -4035 -2051 2803 A O
ATOM 499 N LYS A 56 24.268 13.629 44.294 1.00 77.78 A N
ANISOU 499 N LYS A 56 9308 9365 10879 -2493 -1221 1065 A N
ATOM 500 CA ALYS A 56 24.438 12.396 45.054 0.66 77.45 A C
ANISOU 500 CA ALYS A 56 9085 9634 10708 -2220 -1097 777 A C
ATOM 501 CA BLYS A 56 24.441 12.394 45.050 0.34 77.46 A C
ANISOU 501 CA BLYS A 56 9086 9637 10709 -2221 -1096 778 A C
ATOM 502 C LYS A 56 23.461 11.321 44.589 1.00 75.06 A C
ANISOU 502 C LYS A 56 8873 9567 10081 -1874 -824 678 A C
ATOM 503 O LYS A 56 23.830 10.149 44.469 1.00 64.98 A O
ANISOU 503 O LYS A 56 7375 8642 8674 -1743 -589 622 A O
ATOM 504 CB ALYS A 56 24.259 12.677 46.547 0.66 75.91 A C
ANISOU 504 CB ALYS A 56 9037 9185 10618 -2081 -1441 435 A C
ATOM 505 CB BLYS A 56 24.273 12.671 46.544 0.34 75.97 A C
ANISOU 505 CB BLYS A 56 9041 9197 10627 -2083 -1440 436 A C
ATOM 506 CG ALYS A 56 25.165 13.778 47.105 0.66 78.44 A C
ANISOU 506 CG ALYS A 56 9313 9206 11286 -2416 -1805 465 A C
ATOM 507 CG BLYS A 56 25.575 12.964 47.284 0.34 80.00 A C
ANISOU 507 CG BLYS A 56 9303 9688 11404 -2339 -1667 418 A C
ATOM 508 CD ALYS A 56 26.625 13.339 47.164 0.66 82.02 A C
ANISOU 508 CD ALYS A 56 9310 9961 11894 -2660 -1742 587 A C
ATOM 509 CD BLYS A 56 26.391 14.051 46.593 0.34 81.90 A C
ANISOU 509 CD BLYS A 56 9423 9747 11949 -2818 -1772 761 A C
ATOM 510 CE ALYS A 56 27.419 14.134 48.202 0.66 86.99 A C
ANISOU 510 CE ALYS A 56 9894 10320 12840 -2889 -2189 460 A C
ATOM 511 CE BLYS A 56 27.545 14.542 47.464 0.34 86.81 A C
ANISOU 511 CE BLYS A 56 9832 10250 12902 -3098 -2112 702 A C
ATOM 512 NZ ALYS A 56 28.461 13.306 48.879 0.66 81.06 A N
ANISOU 512 NZ ALYS A 56 8764 9900 12134 -2870 -2206 355 A N
ATOM 513 NZ BLYS A 56 27.119 14.920 48.843 0.34 83.72 A N
ANISOU 513 NZ BLYS A 56 9737 9539 12534 -2895 -2525 288 A N
ATOM 514 N ILE A 57 22.210 11.705 44.321 1.00 69.37 A N
ANISOU 514 N ILE A 57 8465 8635 9258 -1718 -886 645 A N
ATOM 515 CA ILE A 57 21.198 10.740 43.892 1.00 70.53 A C
ANISOU 515 CA ILE A 57 8690 8975 9135 -1420 -680 548 A C
ATOM 516 C ILE A 57 21.600 10.094 42.571 1.00 64.80 A C
ANISOU 516 C ILE A 57 7806 8587 8227 -1494 -368 763 A C
ATOM 517 O ILE A 57 21.500 8.873 42.399 1.00 62.29 A O
ANISOU 517 O ILE A 57 7386 8545 7738 -1296 -166 639 A O
ATOM 518 CB ILE A 57 19.822 11.425 43.781 1.00 67.88 A C
ANISOU 518 CB ILE A 57 8668 8352 8769 -1261 -840 494 A C
ATOM 519 CG1 ILE A 57 19.394 11.998 45.135 1.00 67.46 A C
ANISOU 519 CG1 ILE A 57 8759 8026 8849 -1115 -1114 205 A C
ATOM 520 CG2 ILE A 57 18.767 10.461 43.256 1.00 70.83 A C
ANISOU 520 CG2 ILE A 57 9083 8929 8898 -1002 -657 419 A C
ATOM 521 CD1 ILE A 57 19.278 10.955 46.236 1.00 66.73 A C
ANISOU 521 CD1 ILE A 57 8570 8155 8631 -895 -1038 -68 A C
ATOM 522 N ASP A 58 22.039 10.906 41.610 1.00 67.26 A N
ANISOU 522 N ASP A 58 8116 8880 8559 -1778 -334 1090 A N
ATOM 523 CA ASP A 58 22.398 10.362 40.304 1.00 77.50 A C
ANISOU 523 CA ASP A 58 9282 10559 9605 -1836 -12 1290 A C
ATOM 524 C ASP A 58 23.486 9.299 40.434 1.00 75.93 A C
ANISOU 524 C ASP A 58 8707 10754 9389 -1793 230 1182 A C
ATOM 525 O ASP A 58 23.392 8.231 39.815 1.00 70.47 A O
ANISOU 525 O ASP A 58 7947 10372 8457 -1585 470 1076 A O
ATOM 526 CB ASP A 58 22.827 11.499 39.374 1.00 79.22 A C
ANISOU 526 CB ASP A 58 9541 10718 9843 -2208 -14 1721 A C
ATOM 527 CG ASP A 58 21.640 12.288 38.822 1.00 72.70 A C
ANISOU 527 CG ASP A 58 9107 9577 8938 -2170 -210 1861 A C
ATOM 528 OD1 ASP A 58 20.516 12.141 39.350 1.00 73.15 A O
ANISOU 528 OD1 ASP A 58 9368 9421 9005 -1869 -382 1591 A O
ATOM 529 OD2 ASP A 58 21.834 13.069 37.871 1.00 79.85 A O
ANISOU 529 OD2 ASP A 58 10102 10460 9777 -2444 -200 2260 A O
ATOM 530 N AARG A 59 24.522 9.562 41.235 0.57 73.16 A N
ANISOU 530 N AARG A 59 8110 10379 9308 -1965 135 1180 A N
ATOM 531 N BARG A 59 24.507 9.562 41.256 0.43 73.16 A N
ANISOU 531 N BARG A 59 8114 10374 9310 -1962 130 1175 A N
ATOM 532 CA AARG A 59 25.589 8.578 41.401 0.57 70.74 A C
ANISOU 532 CA AARG A 59 7410 10439 9030 -1892 324 1071 A C
ATOM 533 CA BARG A 59 25.600 8.609 41.428 0.43 70.79 A C
ANISOU 533 CA BARG A 59 7417 10436 9046 -1899 315 1073 A C
ATOM 534 C AARG A 59 25.058 7.304 42.046 0.57 70.08 A C
ANISOU 534 C AARG A 59 7385 10382 8859 -1495 312 728 A C
ATOM 535 C BARG A 59 25.111 7.319 42.081 0.43 70.09 A C
ANISOU 535 C BARG A 59 7374 10384 8873 -1503 307 730 A C
ATOM 536 O AARG A 59 25.307 6.198 41.557 0.57 71.06 A O
ANISOU 536 O AARG A 59 7354 10804 8841 -1290 537 620 A O
ATOM 537 O BARG A 59 25.473 6.218 41.651 0.43 70.77 A O
ANISOU 537 O BARG A 59 7273 10778 8840 -1308 529 623 A O
ATOM 538 CB AARG A 59 26.736 9.161 42.229 0.57 78.40 A C
ANISOU 538 CB AARG A 59 8099 11346 10342 -2156 145 1129 A C
ATOM 539 CB BARG A 59 26.717 9.229 42.270 0.43 78.38 A C
ANISOU 539 CB BARG A 59 8111 11318 10352 -2168 125 1131 A C
ATOM 540 CG AARG A 59 27.842 8.158 42.621 0.57 83.15 A C
ANISOU 540 CG AARG A 59 8265 12289 11039 -2034 255 981 A C
ATOM 541 CG BARG A 59 27.404 10.457 41.676 0.43 78.14 A C
ANISOU 541 CG BARG A 59 7961 11248 10480 -2640 116 1518 A C
ATOM 542 CD AARG A 59 28.123 7.100 41.547 0.57 85.21 A C
ANISOU 542 CD AARG A 59 8311 13010 11054 -1832 657 957 A C
ATOM 543 CD BARG A 59 28.106 10.195 40.346 0.43 81.01 A C
ANISOU 543 CD BARG A 59 8020 12110 10651 -2780 539 1787 A C
ATOM 544 NE AARG A 59 29.405 6.428 41.744 0.57 97.54 A N
ANISOU 544 NE AARG A 59 9369 14917 12773 -1771 768 878 A N
ATOM 545 NE BARG A 59 27.818 11.253 39.382 0.43 83.92 A N
ANISOU 545 NE BARG A 59 8589 12369 10926 -3105 570 2191 A N
ATOM 546 CZ AARG A 59 29.978 5.634 40.848 0.57101.17 A C
ANISOU 546 CZ AARG A 59 9528 15832 13080 -1610 1121 840 A C
ATOM 547 CZ BARG A 59 26.720 11.321 38.640 0.43 74.15 A C
ANISOU 547 CZ BARG A 59 7740 11043 9393 -2968 607 2249 A C
ATOM 548 NH1AARG A 59 29.402 5.374 39.685 0.57 93.27 A N
ANISOU 548 NH1AARG A 59 8704 15010 11724 -1504 1397 866 A N
ATOM 549 NH1BARG A 59 25.829 10.344 38.628 0.43 77.60 A N
ANISOU 549 NH1BARG A 59 8363 11535 9587 -2538 666 1931 A N
ATOM 550 NH2AARG A 59 31.155 5.082 41.129 0.57107.05 A N
ANISOU 550 NH2AARG A 59 9778 16872 14024 -1525 1181 746 A N
ATOM 551 NH2BARG A 59 26.516 12.395 37.882 0.43 77.47 A N
ANISOU 551 NH2BARG A 59 8362 11298 9775 -3289 553 2658 A N
ATOM 552 N ILE A 60 24.317 7.438 43.148 1.00 67.45 A N
ANISOU 552 N ILE A 60 7283 9740 8604 -1380 47 555 A N
ATOM 553 CA ILE A 60 23.808 6.248 43.829 1.00 67.11 A C
ANISOU 553 CA ILE A 60 7298 9719 8481 -1061 30 300 A C
ATOM 554 C ILE A 60 22.916 5.440 42.893 1.00 61.59 A C
ANISOU 554 C ILE A 60 6738 9126 7539 -862 215 251 A C
ATOM 555 O ILE A 60 23.006 4.209 42.835 1.00 61.14 A O
ANISOU 555 O ILE A 60 6595 9216 7419 -648 315 107 A O
ATOM 556 CB ILE A 60 23.074 6.640 45.125 1.00 64.48 A C
ANISOU 556 CB ILE A 60 7195 9097 8205 -993 -246 154 A C
ATOM 557 CG1 ILE A 60 24.084 7.025 46.215 1.00 69.61 A C
ANISOU 557 CG1 ILE A 60 7690 9695 9064 -1115 -466 111 A C
ATOM 558 CG2 ILE A 60 22.207 5.499 45.639 1.00 60.89 A C
ANISOU 558 CG2 ILE A 60 6860 8664 7611 -710 -228 -24 A C
ATOM 559 CD1 ILE A 60 23.719 8.271 46.984 1.00 69.28 A C
ANISOU 559 CD1 ILE A 60 7868 9335 9121 -1226 -753 57 A C
ATOM 560 N TYR A 61 22.043 6.115 42.143 1.00 66.87 A N
ANISOU 560 N TYR A 61 7633 9690 8085 -922 220 363 A N
ATOM 561 CA TYR A 61 21.161 5.399 41.225 1.00 59.77 A C
ANISOU 561 CA TYR A 61 6871 8886 6951 -747 343 306 A C
ATOM 562 C TYR A 61 21.964 4.599 40.203 1.00 63.12 A C
ANISOU 562 C TYR A 61 7099 9662 7222 -695 607 303 A C
ATOM 563 O TYR A 61 21.649 3.434 39.935 1.00 56.11 A O
ANISOU 563 O TYR A 61 6230 8865 6223 -463 673 110 A O
ATOM 564 CB TYR A 61 20.219 6.389 40.535 1.00 66.27 A C
ANISOU 564 CB TYR A 61 7947 9554 7678 -833 264 462 A C
ATOM 565 CG TYR A 61 19.123 5.751 39.709 1.00 67.58 A C
ANISOU 565 CG TYR A 61 8279 9779 7620 -654 302 384 A C
ATOM 566 CD1 TYR A 61 18.168 4.938 40.299 1.00 59.34 A C
ANISOU 566 CD1 TYR A 61 7303 8644 6599 -452 216 170 A C
ATOM 567 CD2 TYR A 61 19.031 5.982 38.345 1.00 63.90 A C
ANISOU 567 CD2 TYR A 61 7901 9469 6911 -712 404 544 A C
ATOM 568 CE1 TYR A 61 17.153 4.357 39.552 1.00 62.49 A C
ANISOU 568 CE1 TYR A 61 7827 9078 6837 -321 205 95 A C
ATOM 569 CE2 TYR A 61 18.017 5.406 37.584 1.00 71.54 A C
ANISOU 569 CE2 TYR A 61 9029 10486 7669 -548 382 448 A C
ATOM 570 CZ TYR A 61 17.083 4.594 38.198 1.00 71.13 A C
ANISOU 570 CZ TYR A 61 9017 10312 7699 -359 268 213 A C
ATOM 571 OH TYR A 61 16.072 4.014 37.461 1.00 68.94 A O
ANISOU 571 OH TYR A 61 8869 10067 7258 -229 204 113 A O
ATOM 572 N GLU A 62 23.022 5.192 39.644 1.00 64.99 A N
ANISOU 572 N GLU A 62 7130 10103 7458 -907 756 503 A N
ATOM 573 CA GLU A 62 23.826 4.476 38.656 1.00 63.21 A C
ANISOU 573 CA GLU A 62 6677 10292 7048 -827 1055 476 A C
ATOM 574 C GLU A 62 24.423 3.206 39.252 1.00 64.71 A C
ANISOU 574 C GLU A 62 6644 10580 7362 -563 1079 196 A C
ATOM 575 O GLU A 62 24.474 2.164 38.588 1.00 64.72 A O
ANISOU 575 O GLU A 62 6608 10786 7198 -312 1231 -0 A O
ATOM 576 CB GLU A 62 24.928 5.386 38.109 1.00 72.79 A C
ANISOU 576 CB GLU A 62 7635 11750 8270 -1145 1232 780 A C
ATOM 577 N AARG A 63 24.859 3.269 40.510 0.50 65.40 A N
ANISOU 577 N AARG A 63 6609 10501 7739 -595 891 161 A N
ATOM 578 N BARG A 63 24.896 3.280 40.502 0.50 65.42 A N
ANISOU 578 N BARG A 63 6602 10512 7744 -599 896 165 A N
ATOM 579 CA AARG A 63 25.415 2.090 41.168 0.50 66.90 A C
ANISOU 579 CA AARG A 63 6613 10735 8069 -338 848 -64 A C
ATOM 580 CA BARG A 63 25.411 2.090 41.174 0.50 66.89 A C
ANISOU 580 CA BARG A 63 6614 10733 8070 -338 847 -65 A C
ATOM 581 C AARG A 63 24.337 1.044 41.425 0.50 62.20 A C
ANISOU 581 C AARG A 63 6297 9927 7408 -79 728 -266 A C
ATOM 582 C BARG A 63 24.312 1.047 41.342 0.50 62.20 A C
ANISOU 582 C BARG A 63 6304 9937 7394 -79 740 -265 A C
ATOM 583 O AARG A 63 24.589 -0.161 41.300 0.50 60.03 A O
ANISOU 583 O AARG A 63 5947 9715 7147 186 758 -465 A O
ATOM 584 O BARG A 63 24.523 -0.145 41.093 0.50 60.08 A O
ANISOU 584 O BARG A 63 5969 9746 7113 187 789 -467 A O
ATOM 585 CB AARG A 63 26.096 2.517 42.470 0.50 68.25 A C
ANISOU 585 CB AARG A 63 6623 10780 8528 -462 626 -19 A C
ATOM 586 CB BARG A 63 25.992 2.448 42.547 0.50 68.23 A C
ANISOU 586 CB BARG A 63 6651 10749 8523 -441 606 -35 A C
ATOM 587 CG AARG A 63 26.333 1.413 43.487 0.50 68.89 A C
ANISOU 587 CG AARG A 63 6645 10774 8755 -207 450 -207 A C
ATOM 588 CG BARG A 63 27.098 3.502 42.576 0.50 74.23 A C
ANISOU 588 CG BARG A 63 7107 11643 9453 -750 625 163 A C
ATOM 589 CD AARG A 63 27.268 0.344 42.963 0.50 69.79 A C
ANISOU 589 CD AARG A 63 6444 11159 8913 49 607 -357 A C
ATOM 590 CD BARG A 63 28.077 3.220 43.729 0.50 78.07 A C
ANISOU 590 CD BARG A 63 7314 12130 10219 -713 419 83 A C
ATOM 591 NE AARG A 63 26.561 -0.917 42.774 0.50 70.69 A N
ANISOU 591 NE AARG A 63 6773 11149 8936 358 585 -559 A N
ATOM 592 NE BARG A 63 27.376 2.878 44.964 0.50 75.37 A N
ANISOU 592 NE BARG A 63 7252 11485 9902 -575 127 -43 A N
ATOM 593 CZ AARG A 63 26.980 -1.907 42.002 0.50 71.65 A C
ANISOU 593 CZ AARG A 63 6757 11448 9021 641 732 -758 A C
ATOM 594 CZ BARG A 63 26.702 3.740 45.716 0.50 67.53 A C
ANISOU 594 CZ BARG A 63 6532 10219 8907 -723 -87 -6 A C
ATOM 595 NH1AARG A 63 28.108 -1.819 41.315 0.50 78.94 A N
ANISOU 595 NH1AARG A 63 7288 12754 9951 685 970 -789 A N
ATOM 596 NH1BARG A 63 26.730 5.039 45.472 0.50 76.33 A N
ANISOU 596 NH1BARG A 63 7683 11244 10076 -1020 -119 147 A N
ATOM 597 NH2AARG A 63 26.252 -3.016 41.920 0.50 73.35 A N
ANISOU 597 NH2AARG A 63 7218 11453 9197 888 635 -941 A N
ATOM 598 NH2BARG A 63 25.984 3.285 46.738 0.50 70.22 A N
ANISOU 598 NH2BARG A 63 7119 10374 9188 -564 -277 -123 A N
ATOM 599 N ILE A 64 23.130 1.481 41.787 1.00 55.85 A N
ANISOU 599 N ILE A 64 5800 8862 6559 -152 578 -218 A N
ATOM 600 CA ILE A 64 22.030 0.544 41.986 1.00 53.28 A C
ANISOU 600 CA ILE A 64 5702 8357 6185 30 476 -362 A C
ATOM 601 C ILE A 64 21.664 -0.139 40.673 1.00 59.24 A C
ANISOU 601 C ILE A 64 6536 9238 6736 172 613 -481 A C
ATOM 602 O ILE A 64 21.274 -1.313 40.665 1.00 54.24 A O
ANISOU 602 O ILE A 64 5983 8508 6119 369 544 -661 A O
ATOM 603 CB ILE A 64 20.815 1.268 42.602 1.00 55.50 A C
ANISOU 603 CB ILE A 64 6224 8406 6458 -79 323 -285 A C
ATOM 604 CG1 ILE A 64 21.063 1.603 44.079 1.00 61.99 A C
ANISOU 604 CG1 ILE A 64 7017 9102 7435 -134 153 -262 A C
ATOM 605 CG2 ILE A 64 19.560 0.418 42.467 1.00 57.99 A C
ANISOU 605 CG2 ILE A 64 6730 8603 6701 48 264 -387 A C
ATOM 606 CD1 ILE A 64 20.166 2.733 44.615 1.00 57.21 A C
ANISOU 606 CD1 ILE A 64 6594 8331 6813 -244 37 -206 A C
ATOM 607 N LEU A 65 21.773 0.577 39.546 1.00 55.05 A N
ANISOU 607 N LEU A 65 6007 8910 6000 66 782 -377 A N
ATOM 608 CA LEU A 65 21.457 -0.028 38.254 1.00 59.41 A C
ANISOU 608 CA LEU A 65 6658 9630 6286 214 903 -512 A C
ATOM 609 C LEU A 65 22.401 -1.168 37.917 1.00 66.14 A C
ANISOU 609 C LEU A 65 7310 10684 7134 473 1033 -757 A C
ATOM 610 O LEU A 65 22.044 -2.055 37.134 1.00 62.83 A O
ANISOU 610 O LEU A 65 7013 10307 6552 686 1046 -991 A O
ATOM 611 CB LEU A 65 21.516 1.006 37.127 1.00 65.79 A C
ANISOU 611 CB LEU A 65 7507 10670 6819 37 1069 -302 A C
ATOM 612 CG LEU A 65 20.536 2.173 37.215 1.00 71.72 A C
ANISOU 612 CG LEU A 65 8488 11202 7562 -172 911 -70 A C
ATOM 613 CD1 LEU A 65 20.853 3.213 36.161 1.00 72.92 A C
ANISOU 613 CD1 LEU A 65 8662 11570 7475 -377 1060 210 A C
ATOM 614 CD2 LEU A 65 19.116 1.671 37.065 1.00 73.22 A C
ANISOU 614 CD2 LEU A 65 8935 11199 7685 -42 727 -209 A C
ATOM 615 N ALA A 66 23.612 -1.149 38.470 1.00 59.61 A N
ANISOU 615 N ALA A 66 6170 9984 6496 478 1105 -734 A N
ATOM 616 CA ALA A 66 24.599 -2.176 38.190 1.00 58.37 A C
ANISOU 616 CA ALA A 66 5765 10035 6378 770 1223 -983 A C
ATOM 617 C ALA A 66 24.488 -3.389 39.107 1.00 59.72 A C
ANISOU 617 C ALA A 66 5985 9887 6817 1013 968 -1185 A C
ATOM 618 O ALA A 66 25.191 -4.381 38.872 1.00 61.36 A O
ANISOU 618 O ALA A 66 6035 10186 7094 1323 1002 -1440 A O
ATOM 619 CB ALA A 66 26.008 -1.583 38.303 1.00 66.77 A C
ANISOU 619 CB ALA A 66 6398 11424 7548 664 1413 -851 A C
ATOM 620 N ASP A 67 23.627 -3.341 40.126 1.00 54.82 A N
ANISOU 620 N ASP A 67 5581 8908 6342 891 715 -1072 A N
ATOM 621 CA ASP A 67 23.517 -4.428 41.095 1.00 57.61 A C
ANISOU 621 CA ASP A 67 5998 8955 6937 1057 462 -1168 A C
ATOM 622 C ASP A 67 22.899 -5.651 40.432 1.00 61.72 A C
ANISOU 622 C ASP A 67 6722 9308 7420 1291 378 -1425 A C
ATOM 623 O ASP A 67 21.784 -5.587 39.910 1.00 57.96 A O
ANISOU 623 O ASP A 67 6491 8740 6790 1201 348 -1431 A O
ATOM 624 CB ASP A 67 22.680 -3.990 42.295 1.00 52.75 A C
ANISOU 624 CB ASP A 67 5559 8078 6406 840 266 -956 A C
ATOM 625 CG ASP A 67 22.927 -4.849 43.534 1.00 55.99 A C
ANISOU 625 CG ASP A 67 5967 8259 7048 945 24 -941 A C
ATOM 626 OD1 ASP A 67 22.707 -6.073 43.464 1.00 55.96 A O
ANISOU 626 OD1 ASP A 67 6070 8049 7141 1138 -109 -1074 A O
ATOM 627 OD2 ASP A 67 23.318 -4.299 44.587 1.00 56.19 A O
ANISOU 627 OD2 ASP A 67 5911 8286 7152 828 -66 -789 A O
ATOM 628 N AGLU A 68 23.618 -6.772 40.457 0.65 63.42 A N
ANISOU 628 N AGLU A 68 6834 9458 7803 1602 298 -1652 A N
ATOM 629 N BGLU A 68 23.622 -6.772 40.465 0.35 63.55 A N
ANISOU 629 N BGLU A 68 6850 9475 7821 1602 297 -1651 A N
ATOM 630 CA AGLU A 68 23.139 -7.968 39.778 0.65 68.54 A C
ANISOU 630 CA AGLU A 68 7687 9904 8449 1850 175 -1949 A C
ATOM 631 CA BGLU A 68 23.166 -7.992 39.813 0.35 68.59 A C
ANISOU 631 CA BGLU A 68 7689 9905 8468 1856 169 -1950 A C
ATOM 632 C AGLU A 68 21.933 -8.605 40.461 0.65 64.63 A C
ANISOU 632 C AGLU A 68 7499 8945 8112 1730 -135 -1856 A C
ATOM 633 C BGLU A 68 21.912 -8.579 40.446 0.35 64.72 A C
ANISOU 633 C BGLU A 68 7512 8961 8117 1723 -131 -1853 A C
ATOM 634 O AGLU A 68 21.355 -9.541 39.897 0.65 67.23 A O
ANISOU 634 O AGLU A 68 8033 9044 8467 1862 -290 -2079 A O
ATOM 635 O BGLU A 68 21.287 -9.454 39.836 0.35 66.99 A O
ANISOU 635 O BGLU A 68 8009 9034 8410 1842 -274 -2071 A O
ATOM 636 CB AGLU A 68 24.279 -8.989 39.667 0.65 73.66 A C
ANISOU 636 CB AGLU A 68 8138 10566 9281 2261 138 -2244 A C
ATOM 637 CB BGLU A 68 24.281 -9.043 39.838 0.35 73.97 A C
ANISOU 637 CB BGLU A 68 8182 10561 9364 2256 102 -2222 A C
ATOM 638 CG AGLU A 68 24.694 -9.617 40.993 0.65 80.72 A C
ANISOU 638 CG AGLU A 68 8984 11142 10545 2336 -152 -2131 A C
ATOM 639 CG BGLU A 68 24.723 -9.451 41.241 0.35 80.55 A C
ANISOU 639 CG BGLU A 68 8941 11123 10541 2278 -160 -2055 A C
ATOM 640 CD AGLU A 68 26.160 -10.018 41.029 0.65 88.16 A C
ANISOU 640 CD AGLU A 68 9559 12270 11667 2686 -114 -2317 A C
ATOM 641 CD BGLU A 68 24.412 -10.903 41.562 0.35 82.40 A C
ANISOU 641 CD BGLU A 68 9404 10861 11045 2506 -518 -2201 A C
ATOM 642 OE1AGLU A 68 26.954 -9.482 40.225 0.65 86.89 A O
ANISOU 642 OE1AGLU A 68 9093 12585 11338 2771 213 -2438 A O
ATOM 643 OE1BGLU A 68 23.326 -11.384 41.176 0.35 80.61 A O
ANISOU 643 OE1BGLU A 68 9487 10363 10778 2436 -644 -2267 A O
ATOM 644 OE2AGLU A 68 26.520 -10.870 41.869 0.65 96.07 A O
ANISOU 644 OE2AGLU A 68 10563 12957 12984 2875 -416 -2321 A O
ATOM 645 OE2BGLU A 68 25.256 -11.563 42.205 0.35 85.29 A O
ANISOU 645 OE2BGLU A 68 9637 11083 11687 2747 -706 -2236 A O
ATOM 646 N ARG A 69 21.515 -8.118 41.631 1.00 60.13 A N
ANISOU 646 N ARG A 69 6961 8251 7635 1472 -229 -1541 A N
ATOM 647 CA ARG A 69 20.421 -8.763 42.350 1.00 57.58 A C
ANISOU 647 CA ARG A 69 6874 7550 7452 1338 -483 -1410 A C
ATOM 648 C ARG A 69 19.038 -8.328 41.891 1.00 60.72 A C
ANISOU 648 C ARG A 69 7443 7935 7692 1110 -460 -1349 A C
ATOM 649 O ARG A 69 18.046 -8.889 42.367 1.00 55.62 A O
ANISOU 649 O ARG A 69 6950 7016 7167 973 -649 -1241 A O
ATOM 650 CB ARG A 69 20.555 -8.515 43.851 1.00 59.39 A C
ANISOU 650 CB ARG A 69 7064 7706 7797 1189 -584 -1110 A C
ATOM 651 CG ARG A 69 21.809 -9.163 44.421 1.00 73.09 A C
ANISOU 651 CG ARG A 69 8654 9377 9741 1427 -715 -1152 A C
ATOM 652 CD ARG A 69 22.063 -8.750 45.843 1.00 65.92 A C
ANISOU 652 CD ARG A 69 7702 8475 8868 1285 -814 -867 A C
ATOM 653 NE ARG A 69 22.716 -7.448 45.888 1.00 63.31 A N
ANISOU 653 NE ARG A 69 7153 8490 8411 1190 -620 -830 A N
ATOM 654 CZ ARG A 69 23.257 -6.916 46.972 1.00 63.96 A C
ANISOU 654 CZ ARG A 69 7140 8650 8511 1106 -704 -666 A C
ATOM 655 NH1 ARG A 69 23.324 -7.588 48.111 1.00 62.98 A N
ANISOU 655 NH1 ARG A 69 7112 8333 8486 1138 -962 -513 A N
ATOM 656 NH2 ARG A 69 23.751 -5.683 46.909 1.00 59.08 A N
ANISOU 656 NH2 ARG A 69 6345 8299 7806 977 -554 -644 A N
ATOM 657 N HIS A 70 18.928 -7.360 40.992 1.00 57.34 A N
ANISOU 657 N HIS A 70 6980 7796 7012 1055 -252 -1387 A N
ATOM 658 CA HIS A 70 17.618 -7.020 40.453 1.00 53.36 A C
ANISOU 658 CA HIS A 70 6630 7269 6374 889 -281 -1356 A C
ATOM 659 C HIS A 70 17.776 -6.636 38.992 1.00 57.63 A C
ANISOU 659 C HIS A 70 7194 8073 6630 988 -130 -1542 A C
ATOM 660 O HIS A 70 18.888 -6.471 38.481 1.00 52.30 A O
ANISOU 660 O HIS A 70 6383 7650 5837 1142 59 -1649 A O
ATOM 661 CB HIS A 70 16.915 -5.940 41.297 1.00 46.69 A C
ANISOU 661 CB HIS A 70 5764 6470 5507 634 -242 -1069 A C
ATOM 662 CG HIS A 70 17.594 -4.605 41.335 1.00 47.88 A C
ANISOU 662 CG HIS A 70 5788 6880 5523 572 -46 -953 A C
ATOM 663 CD2 HIS A 70 18.833 -4.205 40.959 1.00 50.31 A C
ANISOU 663 CD2 HIS A 70 5943 7407 5765 651 116 -991 A C
ATOM 664 ND1 HIS A 70 16.963 -3.482 41.834 1.00 47.19 A N
ANISOU 664 ND1 HIS A 70 5711 6831 5388 392 -21 -770 A N
ATOM 665 CE1 HIS A 70 17.783 -2.448 41.759 1.00 53.10 A C
ANISOU 665 CE1 HIS A 70 6358 7751 6065 347 111 -696 A C
ATOM 666 NE2 HIS A 70 18.922 -2.859 41.227 1.00 51.46 A N
ANISOU 666 NE2 HIS A 70 6032 7676 5845 475 208 -804 A N
ATOM 667 N THR A 71 16.641 -6.571 38.304 1.00 50.70 A N
ANISOU 667 N THR A 71 6476 7156 5632 902 -223 -1581 A N
ATOM 668 CA THR A 71 16.603 -6.366 36.865 1.00 52.07 A C
ANISOU 668 CA THR A 71 6740 7561 5484 1000 -144 -1764 A C
ATOM 669 C THR A 71 15.262 -5.730 36.524 1.00 50.94 A C
ANISOU 669 C THR A 71 6717 7402 5236 810 -254 -1640 A C
ATOM 670 O THR A 71 14.440 -5.466 37.406 1.00 49.85 A O
ANISOU 670 O THR A 71 6550 7101 5289 630 -354 -1441 A O
ATOM 671 CB THR A 71 16.831 -7.685 36.118 1.00 61.62 A C
ANISOU 671 CB THR A 71 8061 8662 6688 1268 -271 -2154 A C
ATOM 672 CG2 THR A 71 15.644 -8.623 36.283 1.00 59.06 A C
ANISOU 672 CG2 THR A 71 7913 7938 6591 1189 -621 -2236 A C
ATOM 673 OG1 THR A 71 17.040 -7.424 34.726 1.00 64.53 A O
ANISOU 673 OG1 THR A 71 8504 9363 6651 1403 -134 -2351 A O
ATOM 674 N ASP A 72 15.048 -5.472 35.236 1.00 54.37 A N
ANISOU 674 N ASP A 72 7274 8039 5343 870 -235 -1759 A N
ATOM 675 CA ASP A 72 13.847 -4.785 34.769 1.00 58.23 A C
ANISOU 675 CA ASP A 72 7869 8547 5708 726 -368 -1641 A C
ATOM 676 C ASP A 72 13.539 -3.566 35.639 1.00 53.85 A C
ANISOU 676 C ASP A 72 7204 7988 5268 533 -298 -1300 A C
ATOM 677 O ASP A 72 12.450 -3.423 36.197 1.00 49.82 A O
ANISOU 677 O ASP A 72 6672 7318 4941 414 -456 -1199 A O
ATOM 678 CB ASP A 72 12.648 -5.737 34.736 1.00 61.80 A C
ANISOU 678 CB ASP A 72 8418 8716 6346 690 -699 -1795 A C
ATOM 679 CG ASP A 72 12.868 -6.929 33.831 1.00 75.08 A C
ANISOU 679 CG ASP A 72 10259 10339 7929 895 -841 -2187 A C
ATOM 680 OD1 ASP A 72 13.823 -6.903 33.027 1.00 93.62 A O
ANISOU 680 OD1 ASP A 72 12651 12954 9965 1095 -653 -2358 A O
ATOM 681 OD2 ASP A 72 12.069 -7.886 33.908 1.00 86.93 A O
ANISOU 681 OD2 ASP A 72 11834 11534 9661 852 -1145 -2333 A O
ATOM 682 N AILE A 73 14.544 -2.699 35.775 0.43 52.74 A N
ANISOU 682 N AILE A 73 6973 8031 5036 509 -62 -1142 A N
ATOM 683 N BILE A 73 14.517 -2.671 35.744 0.57 52.73 A N
ANISOU 683 N BILE A 73 6977 8034 5026 506 -64 -1139 A N
ATOM 684 CA AILE A 73 14.378 -1.471 36.535 0.43 49.14 A C
ANISOU 684 CA AILE A 73 6447 7545 4680 350 -23 -865 A C
ATOM 685 CA BILE A 73 14.377 -1.486 36.591 0.57 49.06 A C
ANISOU 685 CA BILE A 73 6432 7526 4683 348 -24 -865 A C
ATOM 686 C AILE A 73 13.534 -0.500 35.728 0.43 51.59 A C
ANISOU 686 C AILE A 73 6885 7916 4801 286 -114 -734 A C
ATOM 687 C BILE A 73 13.650 -0.396 35.812 0.57 51.53 A C
ANISOU 687 C BILE A 73 6863 7912 4801 276 -91 -711 A C
ATOM 688 O AILE A 73 13.739 -0.326 34.519 0.43 50.56 A O
ANISOU 688 O AILE A 73 6872 7985 4352 324 -72 -745 A O
ATOM 689 O BILE A 73 14.064 -0.029 34.708 0.57 50.30 A O
ANISOU 689 O BILE A 73 6800 7972 4339 291 -4 -673 A O
ATOM 690 CB AILE A 73 15.750 -0.856 36.870 0.43 53.08 A C
ANISOU 690 CB AILE A 73 6809 8187 5174 311 204 -740 A C
ATOM 691 CB BILE A 73 15.756 -0.998 37.069 0.57 53.28 A C
ANISOU 691 CB BILE A 73 6818 8179 5247 318 193 -756 A C
ATOM 692 CG1AILE A 73 16.427 -1.645 37.991 0.43 52.61 A C
ANISOU 692 CG1AILE A 73 6604 8015 5370 367 221 -819 A C
ATOM 693 CG1BILE A 73 16.508 -2.129 37.780 0.57 53.27 A C
ANISOU 693 CG1BILE A 73 6698 8104 5440 434 214 -913 A C
ATOM 694 CG2AILE A 73 15.594 0.608 37.269 0.43 50.47 A C
ANISOU 694 CG2AILE A 73 6475 7820 4881 145 205 -475 A C
ATOM 695 CG2BILE A 73 15.602 0.206 37.988 0.57 51.28 A C
ANISOU 695 CG2BILE A 73 6518 7828 5137 164 177 -526 A C
ATOM 696 CD1AILE A 73 16.898 -3.018 37.568 0.43 55.22 A C
ANISOU 696 CD1AILE A 73 6931 8353 5697 568 217 -1086 A C
ATOM 697 CD1BILE A 73 17.986 -1.840 38.030 0.57 54.79 A C
ANISOU 697 CD1BILE A 73 6694 8469 5654 445 411 -861 A C
ATOM 698 N LEU A 74 12.569 0.136 36.387 1.00 52.40 A N
ANISOU 698 N LEU A 74 6966 7865 5079 211 -247 -612 A N
ATOM 699 CA LEU A 74 11.775 1.187 35.750 1.00 48.86 A C
ANISOU 699 CA LEU A 74 6623 7430 4512 180 -375 -466 A C
ATOM 700 C LEU A 74 11.604 2.350 36.715 1.00 47.13 A C
ANISOU 700 C LEU A 74 6338 7078 4489 117 -383 -291 A C
ATOM 701 O LEU A 74 11.037 2.190 37.799 1.00 45.41 A O
ANISOU 701 O LEU A 74 6002 6744 4507 127 -425 -342 A O
ATOM 702 CB LEU A 74 10.405 0.669 35.301 1.00 49.85 A C
ANISOU 702 CB LEU A 74 6787 7497 4656 227 -630 -585 A C
ATOM 703 CG LEU A 74 9.531 1.739 34.645 1.00 52.27 A C
ANISOU 703 CG LEU A 74 7189 7808 4864 234 -819 -436 A C
ATOM 704 CD1 LEU A 74 10.161 2.217 33.337 1.00 59.10 A C
ANISOU 704 CD1 LEU A 74 8262 8862 5332 233 -774 -324 A C
ATOM 705 CD2 LEU A 74 8.118 1.196 34.400 1.00 57.60 A C
ANISOU 705 CD2 LEU A 74 7817 8427 5641 273 -1100 -564 A C
ATOM 706 N CYS A 75 12.083 3.522 36.312 1.00 49.77 A N
ANISOU 706 N CYS A 75 6761 7433 4718 49 -351 -86 A N
ATOM 707 CA CYS A 75 11.890 4.734 37.097 1.00 48.80 A C
ANISOU 707 CA CYS A 75 6629 7126 4788 12 -424 47 A C
ATOM 708 C CYS A 75 10.474 5.250 36.859 1.00 49.18 A C
ANISOU 708 C CYS A 75 6731 7064 4892 110 -672 57 A C
ATOM 709 O CYS A 75 10.107 5.565 35.723 1.00 50.07 A O
ANISOU 709 O CYS A 75 6989 7219 4814 123 -804 162 A O
ATOM 710 CB CYS A 75 12.925 5.789 36.713 1.00 54.70 A C
ANISOU 710 CB CYS A 75 7458 7875 5450 -134 -347 289 A C
ATOM 711 SG CYS A 75 12.722 7.375 37.601 1.00 58.60 A S
ANISOU 711 SG CYS A 75 8001 8046 6216 -174 -520 422 A S
ATOM 712 N LEU A 76 9.676 5.330 37.929 1.00 50.87 A N
ANISOU 712 N LEU A 76 6811 7170 5347 194 -738 -51 A N
ATOM 713 CA LEU A 76 8.288 5.766 37.815 1.00 45.85 A C
ANISOU 713 CA LEU A 76 6141 6468 4815 327 -962 -78 A C
ATOM 714 C LEU A 76 8.130 7.268 37.982 1.00 52.31 A C
ANISOU 714 C LEU A 76 7052 7079 5743 398 -1108 35 A C
ATOM 715 O LEU A 76 7.176 7.848 37.448 1.00 53.91 A O
ANISOU 715 O LEU A 76 7294 7207 5983 523 -1346 76 A O
ATOM 716 CB LEU A 76 7.422 5.072 38.875 1.00 52.38 A C
ANISOU 716 CB LEU A 76 6723 7342 5836 393 -930 -255 A C
ATOM 717 CG LEU A 76 7.292 3.547 38.843 1.00 60.49 A C
ANISOU 717 CG LEU A 76 7647 8488 6849 316 -864 -360 A C
ATOM 718 CD1 LEU A 76 6.578 3.049 40.095 1.00 62.40 A C
ANISOU 718 CD1 LEU A 76 7646 8777 7287 322 -794 -443 A C
ATOM 719 CD2 LEU A 76 6.554 3.082 37.604 1.00 61.20 A C
ANISOU 719 CD2 LEU A 76 7781 8629 6844 328 -1068 -391 A C
ATOM 720 N LYS A 77 9.035 7.910 38.719 1.00 45.57 A N
ANISOU 720 N LYS A 77 6240 6105 4970 331 -1015 76 A N
ATOM 721 CA LYS A 77 8.878 9.326 39.021 1.00 46.56 A C
ANISOU 721 CA LYS A 77 6472 5960 5260 408 -1199 136 A C
ATOM 722 C LYS A 77 10.243 9.917 39.332 1.00 55.37 A C
ANISOU 722 C LYS A 77 7690 6950 6397 218 -1118 259 A C
ATOM 723 O LYS A 77 11.014 9.341 40.105 1.00 51.69 A O
ANISOU 723 O LYS A 77 7114 6588 5936 134 -927 164 A O
ATOM 724 CB LYS A 77 7.909 9.514 40.194 1.00 53.38 A C
ANISOU 724 CB LYS A 77 7166 6785 6331 636 -1245 -111 A C
ATOM 725 CG LYS A 77 7.091 10.794 40.142 1.00 64.30 A C
ANISOU 725 CG LYS A 77 8628 7910 7893 856 -1531 -126 A C
ATOM 726 CD LYS A 77 6.333 11.035 41.445 1.00 65.67 A C
ANISOU 726 CD LYS A 77 8613 8098 8241 1111 -1514 -424 A C
ATOM 727 CE LYS A 77 6.048 12.513 41.660 1.00106.07 A C
ANISOU 727 CE LYS A 77 13875 12858 13568 1334 -1792 -490 A C
ATOM 728 NZ LYS A 77 4.837 12.762 42.493 1.00107.57 A N
ANISOU 728 NZ LYS A 77 13836 13129 13908 1699 -1828 -802 A N
ATOM 729 N SER A 78 10.537 11.059 38.715 1.00 53.57 A N
ANISOU 729 N SER A 78 7665 6489 6198 132 -1293 496 A N
ATOM 730 CA SER A 78 11.778 11.789 38.947 1.00 64.01 A C
ANISOU 730 CA SER A 78 9073 7647 7601 -98 -1272 658 A C
ATOM 731 C SER A 78 11.398 13.226 39.272 1.00 66.80 A C
ANISOU 731 C SER A 78 9601 7564 8215 -13 -1595 686 A C
ATOM 732 O SER A 78 11.001 13.979 38.380 1.00 63.21 A O
ANISOU 732 O SER A 78 9338 6915 7763 -11 -1822 920 A O
ATOM 733 CB SER A 78 12.698 11.723 37.728 1.00 63.48 A C
ANISOU 733 CB SER A 78 9086 7733 7299 -369 -1151 994 A C
ATOM 734 OG SER A 78 13.926 12.389 37.973 1.00 77.83 A O
ANISOU 734 OG SER A 78 10917 9427 9229 -638 -1116 1175 A O
ATOM 735 N GLU A 79 11.505 13.601 40.541 1.00 53.51 A N
ANISOU 735 N GLU A 79 7874 5715 6742 78 -1646 437 A N
ATOM 736 CA GLU A 79 11.158 14.941 40.992 1.00 57.87 A C
ANISOU 736 CA GLU A 79 8601 5815 7570 213 -1978 366 A C
ATOM 737 C GLU A 79 12.425 15.759 41.184 1.00 65.17 A C
ANISOU 737 C GLU A 79 9657 6455 8651 -97 -2079 539 A C
ATOM 738 O GLU A 79 13.351 15.330 41.880 1.00 57.55 A O
ANISOU 738 O GLU A 79 8561 5634 7671 -255 -1909 450 A O
ATOM 739 CB GLU A 79 10.371 14.892 42.302 1.00 66.04 A C
ANISOU 739 CB GLU A 79 9515 6868 8710 556 -1991 -80 A C
ATOM 740 CG GLU A 79 9.206 13.926 42.282 1.00 58.87 A C
ANISOU 740 CG GLU A 79 8386 6313 7668 797 -1836 -243 A C
ATOM 741 CD GLU A 79 8.599 13.707 43.657 1.00 66.19 A C
ANISOU 741 CD GLU A 79 9136 7387 8625 1069 -1741 -640 A C
ATOM 742 OE1 GLU A 79 7.925 14.625 44.169 1.00 69.93 A O
ANISOU 742 OE1 GLU A 79 9657 7642 9271 1365 -1946 -869 A O
ATOM 743 OE2 GLU A 79 8.779 12.604 44.212 1.00 61.49 A O
ANISOU 743 OE2 GLU A 79 8357 7136 7868 1000 -1463 -718 A O
ATOM 744 N VAL A 80 12.461 16.932 40.569 1.00 65.15 A N
ANISOU 744 N VAL A 80 9903 6032 8819 -199 -2386 806 A N
ATOM 745 CA VAL A 80 13.555 17.874 40.741 1.00 69.96 A C
ANISOU 745 CA VAL A 80 10648 6278 9654 -526 -2562 999 A C
ATOM 746 C VAL A 80 12.969 19.145 41.339 1.00 77.22 A C
ANISOU 746 C VAL A 80 11805 6607 10928 -292 -3010 799 A C
ATOM 747 O VAL A 80 11.764 19.399 41.263 1.00 84.68 A O
ANISOU 747 O VAL A 80 12822 7431 11923 91 -3185 634 A O
ATOM 748 CB VAL A 80 14.292 18.147 39.415 1.00 79.82 A C
ANISOU 748 CB VAL A 80 11996 7534 10798 -942 -2529 1576 A C
ATOM 749 CG1 VAL A 80 14.620 16.828 38.718 1.00 72.21 A C
ANISOU 749 CG1 VAL A 80 10809 7191 9435 -1041 -2090 1684 A C
ATOM 750 CG2 VAL A 80 13.450 19.008 38.492 1.00 74.58 A C
ANISOU 750 CG2 VAL A 80 11621 6528 10189 -847 -2860 1848 A C
ATOM 751 N GLU A 81 13.832 19.938 41.963 1.00 84.94 A N
ANISOU 751 N GLU A 81 12888 7212 12174 -505 -3221 779 A N
ATOM 752 CA GLU A 81 13.382 21.140 42.658 1.00 90.58 A C
ANISOU 752 CA GLU A 81 13849 7321 13247 -262 -3680 502 A C
ATOM 753 C GLU A 81 12.507 20.775 43.858 1.00 93.60 A C
ANISOU 753 C GLU A 81 14110 7882 13570 254 -3616 -126 A C
ATOM 754 O GLU A 81 11.530 21.460 44.163 1.00 99.14 A O
ANISOU 754 O GLU A 81 14946 8279 14446 673 -3894 -418 A O
ATOM 755 CB GLU A 81 12.633 22.070 41.698 1.00102.34 A C
ANISOU 755 CB GLU A 81 15619 8358 14907 -161 -4043 783 A C
ATOM 756 CG GLU A 81 12.644 23.537 42.086 1.00112.11 A C
ANISOU 756 CG GLU A 81 17192 8797 16608 -108 -4609 701 A C
ATOM 757 CD GLU A 81 12.111 24.431 40.980 1.00132.15 A C
ANISOU 757 CD GLU A 81 20034 10858 19320 -105 -4991 1126 A C
ATOM 758 OE1 GLU A 81 10.994 24.166 40.485 1.00142.39 A O
ANISOU 758 OE1 GLU A 81 21299 12322 20481 267 -4980 1087 A O
ATOM 759 OE2 GLU A 81 12.807 25.402 40.611 1.00120.05 A O
ANISOU 759 OE2 GLU A 81 18747 8809 18056 -489 -5311 1510 A O
ATOM 760 N VAL A 82 12.848 19.678 44.536 1.00 76.63 A N
ANISOU 760 N VAL A 82 11698 6253 11166 236 -3242 -323 A N
ATOM 761 CA VAL A 82 12.158 19.295 45.764 1.00 87.78 A C
ANISOU 761 CA VAL A 82 12988 7897 12467 654 -3140 -865 A C
ATOM 762 C VAL A 82 12.695 20.146 46.907 1.00 93.89 A C
ANISOU 762 C VAL A 82 13928 8304 13441 690 -3436 -1212 A C
ATOM 763 O VAL A 82 13.903 20.400 46.999 1.00 89.34 A O
ANISOU 763 O VAL A 82 13406 7553 12986 293 -3542 -1048 A O
ATOM 764 CB VAL A 82 12.337 17.792 46.045 1.00 82.79 A C
ANISOU 764 CB VAL A 82 12050 7918 11486 591 -2671 -886 A C
ATOM 765 CG1 VAL A 82 11.750 17.422 47.402 1.00 84.85 A C
ANISOU 765 CG1 VAL A 82 12198 8442 11599 953 -2555 -1382 A C
ATOM 766 CG2 VAL A 82 11.690 16.961 44.946 1.00 76.55 A C
ANISOU 766 CG2 VAL A 82 11121 7450 10514 599 -2435 -624 A C
ATOM 767 N GLN A 83 11.796 20.588 47.789 1.00 94.46 A N
ANISOU 767 N GLN A 83 14063 8280 13547 1177 -3579 -1718 A N
ATOM 768 CA GLN A 83 12.143 21.530 48.847 1.00 99.20 A C
ANISOU 768 CA GLN A 83 14883 8474 14335 1301 -3934 -2134 A C
ATOM 769 C GLN A 83 11.884 20.978 50.243 1.00101.21 A C
ANISOU 769 C GLN A 83 15005 9168 14280 1619 -3725 -2661 A C
ATOM 770 O GLN A 83 12.021 21.719 51.226 1.00 99.34 A O
ANISOU 770 O GLN A 83 14959 8663 14121 1817 -4012 -3111 A O
ATOM 771 CB GLN A 83 11.372 22.847 48.656 1.00 98.64 A C
ANISOU 771 CB GLN A 83 15092 7767 14619 1643 -4402 -2319 A C
ATOM 772 CG GLN A 83 9.885 22.816 49.043 1.00120.04 A C
ANISOU 772 CG GLN A 83 17691 10691 17227 2300 -4320 -2762 A C
ATOM 773 CD GLN A 83 9.061 21.817 48.243 1.00127.84 A C
ANISOU 773 CD GLN A 83 18375 12204 17992 2354 -3933 -2488 A C
ATOM 774 NE2 GLN A 83 7.837 22.204 47.896 1.00130.80 A N
ANISOU 774 NE2 GLN A 83 18715 12488 18493 2795 -4058 -2619 A N
ATOM 775 OE1 GLN A 83 9.515 20.712 47.946 1.00107.85 A O
ANISOU 775 OE1 GLN A 83 15639 10139 15200 2020 -3557 -2184 A O
ATOM 776 N GLU A 84 11.525 19.702 50.365 1.00101.70 A N
ANISOU 776 N GLU A 84 14770 9891 13980 1664 -3254 -2612 A N
ATOM 777 CA GLU A 84 11.167 19.135 51.661 1.00 93.51 A C
ANISOU 777 CA GLU A 84 13605 9323 12601 1958 -3025 -3042 A C
ATOM 778 C GLU A 84 11.274 17.620 51.576 1.00 92.60 A C
ANISOU 778 C GLU A 84 13194 9831 12160 1758 -2553 -2771 A C
ATOM 779 O GLU A 84 10.704 17.006 50.669 1.00 86.66 A O
ANISOU 779 O GLU A 84 12270 9269 11387 1722 -2340 -2486 A O
ATOM 780 CB GLU A 84 9.751 19.581 52.058 1.00113.51 A C
ANISOU 780 CB GLU A 84 16108 11914 15108 2548 -3035 -3475 A C
ATOM 781 CG GLU A 84 9.165 18.925 53.303 1.00129.11 A C
ANISOU 781 CG GLU A 84 17894 14499 16661 2872 -2706 -3870 A C
ATOM 782 CD GLU A 84 7.643 18.978 53.328 1.00149.05 A C
ANISOU 782 CD GLU A 84 20208 17283 19143 3378 -2547 -4121 A C
ATOM 783 OE1 GLU A 84 7.060 18.771 54.413 1.00152.49 A O
ANISOU 783 OE1 GLU A 84 20512 18166 19259 3721 -2326 -4521 A O
ATOM 784 OE2 GLU A 84 7.030 19.233 52.268 1.00134.34 A O
ANISOU 784 OE2 GLU A 84 18291 15205 17547 3434 -2644 -3912 A O
ATOM 785 N ARG A 85 12.008 17.026 52.516 1.00 82.12 A N
ANISOU 785 N ARG A 85 11827 8786 10591 1635 -2438 -2865 A N
ATOM 786 CA ARG A 85 12.199 15.583 52.518 1.00 73.38 A C
ANISOU 786 CA ARG A 85 10475 8199 9207 1448 -2049 -2609 A C
ATOM 787 C ARG A 85 10.937 14.871 52.982 1.00 69.10 A C
ANISOU 787 C ARG A 85 9730 8145 8381 1768 -1722 -2764 A C
ATOM 788 O ARG A 85 10.226 15.345 53.872 1.00 71.49 A O
ANISOU 788 O ARG A 85 10064 8549 8550 2140 -1740 -3173 A O
ATOM 789 CB ARG A 85 13.360 15.190 53.432 1.00 72.38 A C
ANISOU 789 CB ARG A 85 10374 8205 8919 1245 -2079 -2652 A C
ATOM 790 CG ARG A 85 14.724 15.239 52.778 1.00 76.23 A C
ANISOU 790 CG ARG A 85 10873 8446 9644 800 -2226 -2321 A C
ATOM 791 CD ARG A 85 15.824 14.917 53.776 1.00 71.76 A C
ANISOU 791 CD ARG A 85 10306 8013 8947 648 -2316 -2411 A C
ATOM 792 NE ARG A 85 17.078 15.556 53.401 1.00 73.35 A N
ANISOU 792 NE ARG A 85 10554 7846 9472 285 -2610 -2251 A N
ATOM 793 CZ ARG A 85 18.007 14.997 52.638 1.00 70.75 A C
ANISOU 793 CZ ARG A 85 10033 7591 9260 -68 -2499 -1860 A C
ATOM 794 NH1 ARG A 85 17.871 13.767 52.169 1.00 65.80 A N
ANISOU 794 NH1 ARG A 85 9196 7346 8458 -87 -2137 -1623 A N
ATOM 795 NH2 ARG A 85 19.100 15.692 52.334 1.00 71.56 A N
ANISOU 795 NH2 ARG A 85 10138 7376 9674 -411 -2765 -1715 A N
ATOM 796 N AMET A 86 10.665 13.728 52.354 0.61 67.77 A N
ANISOU 796 N AMET A 86 9339 8284 8125 1615 -1425 -2440 A N
ATOM 797 N BMET A 86 10.663 13.712 52.384 0.39 67.78 A N
ANISOU 797 N BMET A 86 9339 8296 8119 1617 -1420 -2444 A N
ATOM 798 CA AMET A 86 9.551 12.877 52.745 0.61 66.87 A C
ANISOU 798 CA AMET A 86 8982 8655 7769 1807 -1099 -2492 A C
ATOM 799 CA BMET A 86 9.514 12.912 52.789 0.39 66.88 A C
ANISOU 799 CA BMET A 86 8985 8660 7766 1825 -1101 -2512 A C
ATOM 800 C AMET A 86 9.897 12.042 53.970 0.61 67.53 A C
ANISOU 800 C AMET A 86 9018 9146 7493 1765 -903 -2551 A C
ATOM 801 C BMET A 86 9.848 11.898 53.875 0.39 67.53 A C
ANISOU 801 C BMET A 86 8991 9174 7494 1743 -871 -2506 A C
ATOM 802 O AMET A 86 9.077 11.903 54.885 0.61 68.48 A O
ANISOU 802 O AMET A 86 9036 9634 7348 2020 -720 -2776 A O
ATOM 803 O BMET A 86 8.943 11.482 54.608 0.39 70.92 A O
ANISOU 803 O BMET A 86 9261 10018 7668 1943 -631 -2636 A O
ATOM 804 CB AMET A 86 9.185 11.961 51.579 0.61 65.95 A C
ANISOU 804 CB AMET A 86 8678 8648 7731 1620 -925 -2123 A C
ATOM 805 CB BMET A 86 8.924 12.178 51.578 0.39 65.70 A C
ANISOU 805 CB BMET A 86 8643 8596 7723 1703 -948 -2184 A C
ATOM 806 CG AMET A 86 7.722 11.884 51.247 0.61 70.37 A C
ANISOU 806 CG AMET A 86 9021 9395 8322 1866 -807 -2181 A C
ATOM 807 CG BMET A 86 8.052 13.057 50.693 0.39 67.98 A C
ANISOU 807 CG BMET A 86 8940 8619 8269 1912 -1125 -2229 A C
ATOM 808 SD AMET A 86 7.505 10.949 49.720 0.61 66.71 A S
ANISOU 808 SD AMET A 86 8419 8945 7981 1605 -731 -1768 A S
ATOM 809 SD BMET A 86 6.784 12.150 49.779 0.39 70.01 A S
ANISOU 809 SD BMET A 86 8882 9174 8546 1938 -920 -2025 A S
ATOM 810 CE AMET A 86 6.842 12.219 48.648 0.61 72.87 A C
ANISOU 810 CE AMET A 86 9295 9332 9059 1815 -1041 -1803 A C
ATOM 811 CE BMET A 86 5.893 11.354 51.112 0.39 74.12 A C
ANISOU 811 CE BMET A 86 9102 10290 8771 2119 -566 -2227 A C
ATOM 812 N PHE A 87 11.112 11.496 54.004 1.00 68.16 A N
ANISOU 812 N PHE A 87 9162 9187 7550 1455 -943 -2339 A N
ATOM 813 CA PHE A 87 11.543 10.552 55.036 1.00 68.60 A C
ANISOU 813 CA PHE A 87 9183 9601 7281 1374 -796 -2298 A C
ATOM 814 C PHE A 87 12.824 11.048 55.699 1.00 69.89 A C
ANISOU 814 C PHE A 87 9548 9577 7429 1274 -1076 -2425 A C
ATOM 815 O PHE A 87 13.874 10.403 55.624 1.00 59.72 A O
ANISOU 815 O PHE A 87 8240 8286 6167 1013 -1113 -2194 A O
ATOM 816 CB PHE A 87 11.748 9.167 54.424 1.00 69.16 A C
ANISOU 816 CB PHE A 87 9088 9829 7360 1111 -594 -1897 A C
ATOM 817 CG PHE A 87 10.623 8.724 53.523 1.00 63.12 A C
ANISOU 817 CG PHE A 87 8133 9152 6697 1142 -407 -1753 A C
ATOM 818 CD1 PHE A 87 9.405 8.335 54.055 1.00 69.96 A C
ANISOU 818 CD1 PHE A 87 8825 10382 7375 1308 -175 -1818 A C
ATOM 819 CD2 PHE A 87 10.789 8.699 52.148 1.00 61.91 A C
ANISOU 819 CD2 PHE A 87 7961 8752 6810 994 -467 -1550 A C
ATOM 820 CE1 PHE A 87 8.372 7.924 53.230 1.00 68.95 A C
ANISOU 820 CE1 PHE A 87 8487 10334 7378 1312 -44 -1690 A C
ATOM 821 CE2 PHE A 87 9.761 8.291 51.317 1.00 63.58 A C
ANISOU 821 CE2 PHE A 87 8012 9042 7102 1022 -349 -1439 A C
ATOM 822 CZ PHE A 87 8.550 7.906 51.861 1.00 65.10 A C
ANISOU 822 CZ PHE A 87 8012 9563 7161 1177 -157 -1514 A C
ATOM 823 N PRO A 88 12.769 12.198 56.374 1.00 65.42 A N
ANISOU 823 N PRO A 88 9171 8848 6839 1496 -1307 -2819 A N
ATOM 824 CA PRO A 88 14.007 12.794 56.905 1.00 73.49 A C
ANISOU 824 CA PRO A 88 10389 9616 7918 1368 -1657 -2958 A C
ATOM 825 C PRO A 88 14.729 11.951 57.948 1.00 75.71 A C
ANISOU 825 C PRO A 88 10674 10231 7860 1274 -1632 -2917 A C
ATOM 826 O PRO A 88 15.941 12.131 58.124 1.00 74.74 A O
ANISOU 826 O PRO A 88 10623 9919 7854 1066 -1911 -2895 A O
ATOM 827 CB PRO A 88 13.518 14.121 57.508 1.00 74.29 A C
ANISOU 827 CB PRO A 88 10706 9503 8017 1703 -1902 -3463 A C
ATOM 828 CG PRO A 88 12.083 13.874 57.824 1.00 79.56 A C
ANISOU 828 CG PRO A 88 11247 10566 8417 2060 -1577 -3625 A C
ATOM 829 CD PRO A 88 11.592 13.033 56.677 1.00 74.25 A C
ANISOU 829 CD PRO A 88 10323 9984 7905 1892 -1297 -3192 A C
ATOM 830 N ASP A 89 14.044 11.048 58.647 1.00 72.00 A N
ANISOU 830 N ASP A 89 10119 10250 6987 1402 -1331 -2880 A N
ATOM 831 CA ASP A 89 14.671 10.273 59.713 1.00 88.83 A C
ANISOU 831 CA ASP A 89 12299 12700 8753 1334 -1342 -2817 A C
ATOM 832 C ASP A 89 15.253 8.944 59.238 1.00 77.07 A C
ANISOU 832 C ASP A 89 10643 11297 7343 1048 -1215 -2344 A C
ATOM 833 O ASP A 89 15.769 8.183 60.062 1.00 72.13 A O
ANISOU 833 O ASP A 89 10051 10912 6442 989 -1242 -2226 A O
ATOM 834 CB ASP A 89 13.660 9.995 60.835 1.00 99.11 A C
ANISOU 834 CB ASP A 89 13620 14520 9517 1608 -1087 -2992 A C
ATOM 835 CG ASP A 89 13.199 11.256 61.542 1.00107.46 A C
ANISOU 835 CG ASP A 89 14864 15557 10408 1964 -1232 -3552 A C
ATOM 836 OD1 ASP A 89 14.000 12.208 61.658 1.00105.59 A O
ANISOU 836 OD1 ASP A 89 14834 14935 10352 1961 -1639 -3824 A O
ATOM 837 OD2 ASP A 89 12.033 11.289 61.992 1.00100.51 A O
ANISOU 837 OD2 ASP A 89 13896 15026 9269 2227 -936 -3690 A O
ATOM 838 N TRP A 90 15.186 8.645 57.943 1.00 62.32 A N
ANISOU 838 N TRP A 90 8615 9233 5830 895 -1104 -2084 A N
ATOM 839 CA TRP A 90 15.487 7.307 57.437 1.00 60.69 A C
ANISOU 839 CA TRP A 90 8250 9125 5686 697 -945 -1691 A C
ATOM 840 C TRP A 90 16.562 7.385 56.361 1.00 62.00 A C
ANISOU 840 C TRP A 90 8335 8971 6249 477 -1088 -1532 A C
ATOM 841 O TRP A 90 16.273 7.738 55.217 1.00 53.90 A O
ANISOU 841 O TRP A 90 7248 7749 5482 431 -1027 -1472 A O
ATOM 842 CB TRP A 90 14.234 6.645 56.862 1.00 61.75 A C
ANISOU 842 CB TRP A 90 8236 9419 5807 737 -622 -1530 A C
ATOM 843 CG TRP A 90 13.170 6.315 57.851 1.00 66.63 A C
ANISOU 843 CG TRP A 90 8839 10442 6037 895 -402 -1587 A C
ATOM 844 CD1 TRP A 90 13.276 6.301 59.203 1.00 71.71 A C
ANISOU 844 CD1 TRP A 90 9607 11374 6267 995 -426 -1706 A C
ATOM 845 CD2 TRP A 90 11.831 5.922 57.546 1.00 72.12 A C
ANISOU 845 CD2 TRP A 90 9357 11345 6700 954 -112 -1504 A C
ATOM 846 CE2 TRP A 90 11.174 5.693 58.767 1.00 82.33 A C
ANISOU 846 CE2 TRP A 90 10645 13080 7556 1076 71 -1560 A C
ATOM 847 CE3 TRP A 90 11.123 5.743 56.352 1.00 68.91 A C
ANISOU 847 CE3 TRP A 90 8782 10817 6582 907 0 -1384 A C
ATOM 848 NE1 TRP A 90 12.077 5.935 59.769 1.00 75.48 A N
ANISOU 848 NE1 TRP A 90 9988 12262 6428 1110 -123 -1687 A N
ATOM 849 CZ2 TRP A 90 9.839 5.298 58.832 1.00 85.41 A C
ANISOU 849 CZ2 TRP A 90 10819 13806 7828 1131 386 -1483 A C
ATOM 850 CZ3 TRP A 90 9.804 5.349 56.418 1.00 68.22 A C
ANISOU 850 CZ3 TRP A 90 8497 11024 6399 970 260 -1331 A C
ATOM 851 CH2 TRP A 90 9.174 5.132 57.650 1.00 80.88 A C
ANISOU 851 CH2 TRP A 90 10050 13076 7602 1071 463 -1372 A C
ATOM 852 N SER A 91 17.798 7.027 56.710 1.00 53.92 A N
ANISOU 852 N SER A 91 7292 7936 5259 345 -1272 -1447 A N
ATOM 853 CA ASER A 91 18.839 6.931 55.691 0.72 51.99 A C
ANISOU 853 CA ASER A 91 6894 7490 5370 140 -1340 -1269 A C
ATOM 854 CA BSER A 91 18.841 6.931 55.692 0.28 52.21 A C
ANISOU 854 CA BSER A 91 6922 7518 5398 140 -1341 -1269 A C
ATOM 855 C SER A 91 18.469 5.901 54.631 1.00 56.41 A C
ANISOU 855 C SER A 91 7306 8100 6028 98 -1073 -1015 A C
ATOM 856 O SER A 91 18.699 6.116 53.436 1.00 52.96 A O
ANISOU 856 O SER A 91 6773 7511 5837 -7 -1019 -921 A O
ATOM 857 CB ASER A 91 20.176 6.584 56.346 0.72 54.87 A C
ANISOU 857 CB ASER A 91 7202 7897 5750 45 -1579 -1229 A C
ATOM 858 CB BSER A 91 20.178 6.583 56.345 0.28 55.04 A C
ANISOU 858 CB BSER A 91 7222 7918 5771 45 -1579 -1229 A C
ATOM 859 OG ASER A 91 20.694 7.707 57.028 0.72 60.86 A O
ANISOU 859 OG ASER A 91 8078 8524 6522 24 -1894 -1479 A O
ATOM 860 OG BSER A 91 20.042 5.485 57.230 0.28 61.04 A O
ANISOU 860 OG BSER A 91 8020 8936 6238 135 -1535 -1129 A O
ATOM 861 N MET A 92 17.899 4.774 55.052 1.00 53.97 A N
ANISOU 861 N MET A 92 6991 8000 5514 166 -920 -894 A N
ATOM 862 CA MET A 92 17.277 3.801 54.161 1.00 55.60 A C
ANISOU 862 CA MET A 92 7100 8230 5795 145 -699 -705 A C
ATOM 863 C MET A 92 16.471 2.834 55.014 1.00 62.82 A C
ANISOU 863 C MET A 92 8054 9370 6447 199 -581 -596 A C
ATOM 864 O MET A 92 17.019 1.862 55.548 1.00 61.41 A O
ANISOU 864 O MET A 92 7878 9251 6202 165 -648 -435 A O
ATOM 865 CB MET A 92 18.284 3.022 53.320 1.00 48.56 A C
ANISOU 865 CB MET A 92 6068 7251 5131 50 -714 -548 A C
ATOM 866 CG MET A 92 17.655 2.232 52.153 1.00 53.98 A C
ANISOU 866 CG MET A 92 6684 7904 5921 40 -526 -432 A C
ATOM 867 SD MET A 92 16.174 2.928 51.397 1.00 52.97 A S
ANISOU 867 SD MET A 92 6597 7750 5782 76 -378 -502 A S
ATOM 868 CE MET A 92 16.852 4.489 50.832 1.00 51.38 A C
ANISOU 868 CE MET A 92 6421 7369 5731 20 -498 -608 A C
ATOM 869 N GLN A 93 15.183 3.100 55.165 1.00 51.80 A N
ANISOU 869 N GLN A 93 6670 8103 4910 278 -416 -661 A N
ATOM 870 CA GLN A 93 14.317 2.222 55.934 1.00 57.17 A C
ANISOU 870 CA GLN A 93 7342 9042 5339 281 -258 -512 A C
ATOM 871 C GLN A 93 13.881 1.071 55.040 1.00 59.71 A C
ANISOU 871 C GLN A 93 7550 9285 5851 164 -147 -277 A C
ATOM 872 O GLN A 93 13.435 1.286 53.910 1.00 57.33 A O
ANISOU 872 O GLN A 93 7167 8854 5760 158 -89 -322 A O
ATOM 873 CB GLN A 93 13.108 2.991 56.460 1.00 58.30 A C
ANISOU 873 CB GLN A 93 7478 9412 5263 427 -104 -698 A C
ATOM 874 CG GLN A 93 12.167 2.168 57.318 1.00 63.78 A C
ANISOU 874 CG GLN A 93 8115 10460 5657 403 110 -520 A C
ATOM 875 CD GLN A 93 12.612 2.102 58.763 1.00 70.32 A C
ANISOU 875 CD GLN A 93 9098 11543 6076 445 51 -517 A C
ATOM 876 NE2 GLN A 93 11.665 1.876 59.663 1.00 85.18 A N
ANISOU 876 NE2 GLN A 93 10942 13832 7590 481 278 -454 A N
ATOM 877 OE1 GLN A 93 13.797 2.256 59.067 1.00 82.16 A O
ANISOU 877 OE1 GLN A 93 10736 12907 7575 442 -199 -566 A O
ATOM 878 N THR A 94 14.015 -0.147 55.542 1.00 55.45 A N
ANISOU 878 N THR A 94 7030 8799 5240 72 -157 -26 A N
ATOM 879 CA THR A 94 13.721 -1.349 54.771 1.00 56.76 A C
ANISOU 879 CA THR A 94 7127 8821 5620 -45 -124 183 A C
ATOM 880 C THR A 94 12.461 -1.980 55.338 1.00 55.76 A C
ANISOU 880 C THR A 94 6944 8905 5335 -149 46 384 A C
ATOM 881 O THR A 94 12.382 -2.232 56.539 1.00 55.45 A O
ANISOU 881 O THR A 94 6973 9093 5004 -179 76 531 A O
ATOM 882 CB THR A 94 14.905 -2.310 54.814 1.00 61.30 A C
ANISOU 882 CB THR A 94 7763 9212 6317 -72 -318 327 A C
ATOM 883 CG2 THR A 94 14.601 -3.588 54.057 1.00 61.87 A C
ANISOU 883 CG2 THR A 94 7802 9080 6624 -163 -330 498 A C
ATOM 884 OG1 THR A 94 16.035 -1.668 54.210 1.00 59.77 A O
ANISOU 884 OG1 THR A 94 7540 8882 6286 7 -432 141 A O
ATOM 885 N ILE A 95 11.467 -2.196 54.482 1.00 53.48 A N
ANISOU 885 N ILE A 95 6519 8578 5223 -215 154 400 A N
ATOM 886 CA ILE A 95 10.187 -2.755 54.891 1.00 54.87 A C
ANISOU 886 CA ILE A 95 6562 8972 5314 -355 327 600 A C
ATOM 887 C ILE A 95 9.948 -3.988 54.032 1.00 55.33 A C
ANISOU 887 C ILE A 95 6581 8759 5682 -538 236 791 A C
ATOM 888 O ILE A 95 9.678 -3.871 52.830 1.00 55.99 A O
ANISOU 888 O ILE A 95 6596 8673 6006 -517 196 645 A O
ATOM 889 CB ILE A 95 9.041 -1.747 54.743 1.00 61.24 A C
ANISOU 889 CB ILE A 95 7186 10019 6062 -249 514 400 A C
ATOM 890 CG1 ILE A 95 9.243 -0.550 55.674 1.00 67.89 A C
ANISOU 890 CG1 ILE A 95 8100 11100 6596 -35 573 163 A C
ATOM 891 CG2 ILE A 95 7.717 -2.401 55.089 1.00 63.98 A C
ANISOU 891 CG2 ILE A 95 7312 10631 6367 -421 709 628 A C
ATOM 892 CD1 ILE A 95 8.581 0.726 55.182 1.00 68.89 A C
ANISOU 892 CD1 ILE A 95 8122 11268 6786 174 629 -157 A C
ATOM 893 N ASN A 96 10.052 -5.168 54.641 1.00 54.62 A N
ANISOU 893 N ASN A 96 6562 8608 5582 -715 169 1114 A N
ATOM 894 CA ASN A 96 9.751 -6.426 53.961 1.00 63.54 A C
ANISOU 894 CA ASN A 96 7680 9434 7026 -908 37 1303 A C
ATOM 895 C ASN A 96 8.268 -6.723 54.153 1.00 52.12 A C
ANISOU 895 C ASN A 96 6014 8206 5583 -1142 209 1505 A C
ATOM 896 O ASN A 96 7.841 -7.193 55.210 1.00 58.28 A O
ANISOU 896 O ASN A 96 6765 9206 6172 -1328 316 1834 A O
ATOM 897 CB ASN A 96 10.620 -7.557 54.495 1.00 67.72 A C
ANISOU 897 CB ASN A 96 8410 9716 7605 -981 -178 1568 A C
ATOM 898 CG ASN A 96 10.506 -8.815 53.660 1.00 75.89 A C
ANISOU 898 CG ASN A 96 9486 10321 9027 -1119 -391 1672 A C
ATOM 899 ND2 ASN A 96 11.601 -9.554 53.549 1.00 69.01 A N
ANISOU 899 ND2 ASN A 96 8796 9108 8318 -1019 -647 1687 A N
ATOM 900 OD1 ASN A 96 9.444 -9.114 53.110 1.00 70.14 A O
ANISOU 900 OD1 ASN A 96 8619 9563 8468 -1296 -353 1711 A O
ATOM 901 N LEU A 97 7.473 -6.455 53.123 1.00 58.68 A N
ANISOU 901 N LEU A 97 6670 9003 6623 -1146 231 1330 A N
ATOM 902 CA LEU A 97 6.037 -6.640 53.252 1.00 71.54 A C
ANISOU 902 CA LEU A 97 8011 10878 8294 -1359 389 1493 A C
ATOM 903 C LEU A 97 5.639 -8.109 53.210 1.00 65.40 A C
ANISOU 903 C LEU A 97 7223 9852 7775 -1715 240 1853 A C
ATOM 904 O LEU A 97 4.558 -8.456 53.698 1.00 65.36 A O
ANISOU 904 O LEU A 97 6971 10096 7766 -1983 389 2128 A O
ATOM 905 CB LEU A 97 5.315 -5.859 52.157 1.00 71.12 A C
ANISOU 905 CB LEU A 97 7765 10858 8399 -1233 402 1190 A C
ATOM 906 CG LEU A 97 4.837 -4.471 52.598 1.00 77.35 A C
ANISOU 906 CG LEU A 97 8391 12059 8941 -998 640 976 A C
ATOM 907 CD1 LEU A 97 4.758 -3.558 51.371 1.00 76.47 A C
ANISOU 907 CD1 LEU A 97 8263 11809 8985 -776 533 636 A C
ATOM 908 CD2 LEU A 97 3.526 -4.511 53.340 1.00 92.61 A C
ANISOU 908 CD2 LEU A 97 9973 14439 10776 -1137 898 1151 A C
ATOM 909 N ASP A 98 6.483 -8.982 52.648 1.00 62.29 A N
ANISOU 909 N ASP A 98 7076 8970 7621 -1726 -58 1855 A N
ATOM 910 CA ASP A 98 6.200 -10.413 52.723 1.00 69.23 A C
ANISOU 910 CA ASP A 98 8007 9527 8771 -2059 -261 2206 A C
ATOM 911 C ASP A 98 6.067 -10.871 54.168 1.00 69.41 A C
ANISOU 911 C ASP A 98 8044 9771 8557 -2293 -135 2686 A C
ATOM 912 O ASP A 98 5.254 -11.752 54.473 1.00 76.22 A O
ANISOU 912 O ASP A 98 8795 10597 9567 -2677 -157 3080 A O
ATOM 913 CB ASP A 98 7.297 -11.228 52.027 1.00 65.97 A C
ANISOU 913 CB ASP A 98 7896 8551 8620 -1938 -613 2081 A C
ATOM 914 CG ASP A 98 7.372 -10.969 50.527 1.00 69.47 A C
ANISOU 914 CG ASP A 98 8340 8790 9266 -1747 -742 1641 A C
ATOM 915 OD1 ASP A 98 6.310 -10.892 49.870 1.00 67.66 A O
ANISOU 915 OD1 ASP A 98 7913 8616 9178 -1883 -739 1572 A O
ATOM 916 OD2 ASP A 98 8.500 -10.875 50.000 1.00 76.46 A O
ANISOU 916 OD2 ASP A 98 9413 9480 10159 -1465 -855 1377 A O
ATOM 917 N GLU A 99 6.842 -10.272 55.071 1.00 80.23 A N
ANISOU 917 N GLU A 99 9551 11386 9547 -2088 -15 2676 A N
ATOM 918 CA GLU A 99 6.899 -10.690 56.465 1.00 89.99 A C
ANISOU 918 CA GLU A 99 10874 12848 10471 -2265 72 3125 A C
ATOM 919 C GLU A 99 5.906 -9.958 57.356 1.00 78.75 A C
ANISOU 919 C GLU A 99 9179 12100 8641 -2341 487 3232 A C
ATOM 920 O GLU A 99 5.762 -10.326 58.527 1.00 81.02 A O
ANISOU 920 O GLU A 99 9506 12673 8605 -2531 615 3647 A O
ATOM 921 CB GLU A 99 8.316 -10.470 57.005 1.00 94.25 A C
ANISOU 921 CB GLU A 99 11716 13306 10790 -1988 -71 3040 A C
ATOM 922 CG GLU A 99 9.358 -11.376 56.378 1.00 96.42 A C
ANISOU 922 CG GLU A 99 12239 12960 11436 -1907 -473 3010 A C
ATOM 923 CD GLU A 99 10.728 -11.207 57.002 1.00112.01 A C
ANISOU 923 CD GLU A 99 14447 14897 13214 -1650 -628 2967 A C
ATOM 924 OE1 GLU A 99 11.587 -12.093 56.799 1.00106.13 A O
ANISOU 924 OE1 GLU A 99 13898 13692 12735 -1585 -964 3036 A O
ATOM 925 OE2 GLU A 99 10.947 -10.185 57.686 1.00111.72 A O
ANISOU 925 OE2 GLU A 99 14390 15281 12778 -1494 -443 2837 A O
ATOM 926 N ASN A 100 5.219 -8.945 56.840 1.00 83.69 A N
ANISOU 926 N ASN A 100 10915 14604 6278 1618 -1195 1798 A N
ATOM 927 CA ASN A 100 4.296 -8.150 57.638 1.00 80.72 A C
ANISOU 927 CA ASN A 100 10677 14374 5619 1494 -1015 1677 A C
ATOM 928 C ASN A 100 2.925 -8.815 57.667 1.00 78.41 A C
ANISOU 928 C ASN A 100 10571 13860 5360 1406 -631 1925 A C
ATOM 929 O ASN A 100 2.429 -9.289 56.640 1.00 89.17 A O
ANISOU 929 O ASN A 100 11851 14913 7115 1310 -464 1996 A O
ATOM 930 CB ASN A 100 4.196 -6.735 57.062 1.00 81.46 A C
ANISOU 930 CB ASN A 100 10565 14483 5903 1292 -1012 1252 A C
ATOM 931 CG ASN A 100 3.258 -5.845 57.850 1.00 82.24 A C
ANISOU 931 CG ASN A 100 10791 14720 5735 1191 -830 1081 A C
ATOM 932 ND2 ASN A 100 3.825 -4.941 58.638 1.00 79.61 A N
ANISOU 932 ND2 ASN A 100 10464 14683 5102 1206 -1026 824 A N
ATOM 933 OD1 ASN A 100 2.037 -5.963 57.745 1.00 87.44 A O
ANISOU 933 OD1 ASN A 100 11527 15232 6466 1099 -516 1155 A O
ATOM 934 N THR A 101 2.316 -8.847 58.855 1.00 84.90 A N
ANISOU 934 N THR A 101 11640 14858 5759 1426 -484 2040 A N
ATOM 935 CA THR A 101 0.995 -9.437 59.049 1.00 89.62 A C
ANISOU 935 CA THR A 101 12409 15297 6345 1313 -84 2259 A C
ATOM 936 C THR A 101 0.099 -8.521 59.874 1.00 84.27 A C
ANISOU 936 C THR A 101 11803 14841 5374 1206 129 2063 A C
ATOM 937 O THR A 101 -0.757 -8.991 60.629 1.00 91.45 A O
ANISOU 937 O THR A 101 12929 15784 6035 1167 423 2268 A O
ATOM 938 CB THR A 101 1.092 -10.810 59.721 1.00 80.92 A C
ANISOU 938 CB THR A 101 11616 14129 5003 1461 -34 2722 A C
ATOM 939 CG2 THR A 101 1.392 -11.895 58.691 1.00 93.99 A C
ANISOU 939 CG2 THR A 101 13214 15420 7075 1501 -61 2935 A C
ATOM 940 OG1 THR A 101 2.122 -10.790 60.718 1.00 92.37 A O
ANISOU 940 OG1 THR A 101 13193 15755 6148 1639 -348 2711 A O
ATOM 941 N AASP A 102 0.275 -7.211 59.749 0.81 83.90 A N
ANISOU 941 N AASP A 102 11587 14938 5352 1152 7 1661 A N
ATOM 942 N BASP A 102 0.304 -7.213 59.759 0.19 83.96 A N
ANISOU 942 N BASP A 102 11596 14949 5355 1155 -1 1662 A N
ATOM 943 CA AASP A 102 -0.636 -6.286 60.410 0.81 86.93 A C
ANISOU 943 CA AASP A 102 12018 15493 5517 1061 226 1429 A C
ATOM 944 CA BASP A 102 -0.515 -6.241 60.469 0.19 86.52 A C
ANISOU 944 CA BASP A 102 11971 15467 5436 1074 190 1417 A C
ATOM 945 C AASP A 102 -1.983 -6.285 59.693 0.81 87.50 A C
ANISOU 945 C AASP A 102 11968 15336 5943 895 585 1393 A C
ATOM 946 C BASP A 102 -1.925 -6.233 59.889 0.19 87.31 A C
ANISOU 946 C BASP A 102 11973 15361 5839 910 572 1388 A C
ATOM 947 O AASP A 102 -2.050 -6.267 58.459 0.81 79.00 A O
ANISOU 947 O AASP A 102 10682 14004 5329 824 558 1323 A O
ATOM 948 O BASP A 102 -2.100 -6.254 58.670 0.19 80.54 A O
ANISOU 948 O BASP A 102 10910 14241 5450 830 578 1330 A O
ATOM 949 CB AASP A 102 -0.041 -4.881 60.438 0.81 84.95 A C
ANISOU 949 CB AASP A 102 11643 15410 5225 1052 -13 995 A C
ATOM 950 CB BASP A 102 0.100 -4.845 60.380 0.19 84.54 A C
ANISOU 950 CB BASP A 102 11575 15358 5189 1057 -54 980 A C
ATOM 951 CG AASP A 102 -0.966 -3.872 61.094 0.81 87.63 A C
ANISOU 951 CG AASP A 102 12037 15902 5355 985 208 718 A C
ATOM 952 CG BASP A 102 1.346 -4.698 61.231 0.19 80.85 A C
ANISOU 952 CG BASP A 102 11188 15114 4417 1177 -407 922 A C
ATOM 953 OD1AASP A 102 -1.866 -3.349 60.402 0.81 90.91 A O
ANISOU 953 OD1AASP A 102 12309 16142 6091 878 413 544 A O
ATOM 954 OD1BASP A 102 1.582 -5.558 62.104 0.19 80.78 A O
ANISOU 954 OD1BASP A 102 11390 15135 4170 1282 -440 1191 A O
ATOM 955 OD2AASP A 102 -0.798 -3.608 62.298 0.81 99.99 A O
ANISOU 955 OD2AASP A 102 13785 17654 6553 1028 166 650 A O
ATOM 956 OD2BASP A 102 2.091 -3.716 61.027 0.19 81.89 A O
ANISOU 956 OD2BASP A 102 11173 15322 4620 1141 -649 587 A O
ATOM 957 N APHE A 103 -3.064 -6.303 60.482 0.48 87.24 A N
ANISOU 957 N APHE A 103 12054 15418 5674 835 923 1428 A N
ATOM 958 N CPHE A 103 -2.887 -6.737 59.641 0.52 89.12 A N
ANISOU 958 N CPHE A 103 12187 15444 6229 813 862 1513 A N
ATOM 959 CA APHE A 103 -4.400 -6.479 59.919 0.48 89.99 A C
ANISOU 959 CA APHE A 103 12265 15589 6338 681 1282 1421 A C
ATOM 960 CA CPHE A 103 -4.311 -6.504 59.871 0.52 89.95 A C
ANISOU 960 CA CPHE A 103 12258 15573 6345 687 1256 1428 A C
ATOM 961 C APHE A 103 -4.726 -5.404 58.891 0.48 86.62 A C
ANISOU 961 C APHE A 103 11560 15043 6307 630 1228 1048 A C
ATOM 962 C CPHE A 103 -4.796 -5.389 58.944 0.52 86.62 A C
ANISOU 962 C CPHE A 103 11564 15054 6293 627 1249 1044 A C
ATOM 963 O APHE A 103 -5.384 -5.677 57.880 0.48 80.97 A O
ANISOU 963 O APHE A 103 10661 14095 6008 538 1345 1052 A O
ATOM 964 O CPHE A 103 -5.619 -5.629 58.059 0.52 80.93 A O
ANISOU 964 O CPHE A 103 10664 14128 5959 528 1415 1039 A O
ATOM 965 CB APHE A 103 -5.446 -6.464 61.036 0.48 96.16 A C
ANISOU 965 CB APHE A 103 13187 16581 6767 626 1660 1445 A C
ATOM 966 CB CPHE A 103 -4.559 -6.170 61.345 0.52 95.89 A C
ANISOU 966 CB CPHE A 103 13237 16660 6535 733 1398 1402 A C
ATOM 967 CG APHE A 103 -5.905 -5.080 61.420 0.48100.19 A C
ANISOU 967 CG APHE A 103 13614 17298 7154 640 1717 1026 A C
ATOM 968 CG CPHE A 103 -5.982 -5.787 61.663 0.52102.11 A C
ANISOU 968 CG CPHE A 103 13958 17528 7310 619 1815 1251 A C
ATOM 969 CD1APHE A 103 -5.183 -4.320 62.329 0.48101.95 A C
ANISOU 969 CD1APHE A 103 13996 17785 6955 752 1515 850 A C
ATOM 970 CD1CPHE A 103 -6.991 -6.738 61.674 0.52100.78 A C
ANISOU 970 CD1CPHE A 103 13797 17258 7238 481 2197 1498 A C
ATOM 971 CD2APHE A 103 -7.055 -4.537 60.866 0.48 97.16 A C
ANISOU 971 CD2APHE A 103 12993 16836 7088 555 1957 786 A C
ATOM 972 CD2CPHE A 103 -6.301 -4.478 61.991 0.52105.42 A C
ANISOU 972 CD2CPHE A 103 14305 18129 7620 650 1834 847 A C
ATOM 973 CE1APHE A 103 -5.605 -3.049 62.682 0.48100.53 A C
ANISOU 973 CE1APHE A 103 13765 17726 6706 760 1568 441 A C
ATOM 974 CE1CPHE A 103 -8.296 -6.385 61.978 0.52 93.21 A C
ANISOU 974 CE1CPHE A 103 12725 16409 6280 373 2593 1333 A C
ATOM 975 CE2APHE A 103 -7.478 -3.266 61.214 0.48 98.96 A C
ANISOU 975 CE2APHE A 103 13160 17224 7216 603 2008 395 A C
ATOM 976 CE2CPHE A 103 -7.604 -4.121 62.300 0.52102.09 A C
ANISOU 976 CE2CPHE A 103 13795 17801 7193 579 2220 686 A C
ATOM 977 CZ APHE A 103 -6.752 -2.521 62.123 0.48101.16 A C
ANISOU 977 CZ APHE A 103 13625 17739 7073 704 1829 223 A C
ATOM 978 CZ CPHE A 103 -8.601 -5.076 62.294 0.52 92.49 A C
ANISOU 978 CZ CPHE A 103 12542 16518 6082 440 2601 925 A C
ATOM 979 N LEU A 104 -4.275 -4.175 59.130 1.00 85.09 A N
ANISOU 979 N LEU A 104 11351 14996 5982 689 1043 720 A N
ATOM 980 CA LEU A 104 -4.597 -3.080 58.225 1.00 84.42 A C
ANISOU 980 CA LEU A 104 11065 14775 6238 657 1000 377 A C
ATOM 981 C LEU A 104 -3.669 -3.065 57.018 1.00 77.05 A C
ANISOU 981 C LEU A 104 10011 13614 5650 649 710 368 A C
ATOM 982 O LEU A 104 -4.076 -2.621 55.938 1.00 78.87 A O
ANISOU 982 O LEU A 104 10081 13635 6250 606 717 221 A O
ATOM 983 CB LEU A 104 -4.525 -1.739 58.959 1.00 91.59 A C
ANISOU 983 CB LEU A 104 12038 15882 6881 708 947 16 A C
ATOM 984 CG LEU A 104 -4.717 -0.492 58.092 1.00 87.52 A C
ANISOU 984 CG LEU A 104 11379 15192 6682 701 870 -342 A C
ATOM 985 CD1 LEU A 104 -5.473 0.576 58.871 1.00 96.34 A C
ANISOU 985 CD1 LEU A 104 12546 16464 7593 751 1038 -665 A C
ATOM 986 CD2 LEU A 104 -3.388 0.064 57.604 1.00100.23 A C
ANISOU 986 CD2 LEU A 104 12989 16723 8373 689 515 -467 A C
ATOM 987 N ILE A 105 -2.433 -3.545 57.179 1.00 79.58 A N
ANISOU 987 N ILE A 105 10405 13987 5845 702 456 518 A N
ATOM 988 CA ILE A 105 -1.524 -3.665 56.043 1.00 71.70 A C
ANISOU 988 CA ILE A 105 9277 12793 5173 690 219 525 A C
ATOM 989 C ILE A 105 -2.034 -4.704 55.053 1.00 62.39 A C
ANISOU 989 C ILE A 105 8011 11349 4346 643 350 756 A C
ATOM 990 O ILE A 105 -1.795 -4.589 53.851 1.00 60.18 A O
ANISOU 990 O ILE A 105 7593 10859 4413 602 256 686 A O
ATOM 991 CB ILE A 105 -0.105 -4.032 56.513 1.00 74.42 A C
ANISOU 991 CB ILE A 105 9681 13293 5302 783 -76 627 A C
ATOM 992 CG1 ILE A 105 0.542 -2.931 57.353 1.00 84.58 A C
ANISOU 992 CG1 ILE A 105 11016 14842 6278 802 -262 337 A C
ATOM 993 CG2 ILE A 105 0.820 -4.261 55.320 1.00 71.14 A C
ANISOU 993 CG2 ILE A 105 9103 12688 5237 769 -278 638 A C
ATOM 994 CD1 ILE A 105 0.288 -1.560 56.865 1.00 84.68 A C
ANISOU 994 CD1 ILE A 105 10946 14764 6464 702 -253 -38 A C
ATOM 995 N ARG A 106 -2.713 -5.742 55.536 1.00 63.11 A N
ANISOU 995 N ARG A 106 8196 11438 4344 634 574 1029 A N
ATOM 996 CA ARG A 106 -3.086 -6.867 54.675 1.00 65.08 A C
ANISOU 996 CA ARG A 106 8386 11426 4915 574 684 1256 A C
ATOM 997 C ARG A 106 -3.816 -6.430 53.412 1.00 59.66 A C
ANISOU 997 C ARG A 106 7490 10536 4641 482 745 1061 A C
ATOM 998 O ARG A 106 -3.364 -6.785 52.311 1.00 57.46 A O
ANISOU 998 O ARG A 106 7125 10052 4657 470 617 1091 A O
ATOM 999 CB ARG A 106 -3.900 -7.853 55.531 1.00 70.70 A C
ANISOU 999 CB ARG A 106 9252 12173 5440 531 979 1534 A C
ATOM 1000 CG ARG A 106 -5.013 -8.614 54.814 1.00 94.02 A C
ANISOU 1000 CG ARG A 106 12097 14895 8731 382 1245 1629 A C
ATOM 1001 CD ARG A 106 -4.475 -9.817 54.052 1.00 96.59 A C
ANISOU 1001 CD ARG A 106 12452 14948 9301 382 1159 1876 A C
ATOM 1002 NE ARG A 106 -4.294 -10.970 54.928 1.00103.01 A N
ANISOU 1002 NE ARG A 106 13527 15740 9873 414 1265 2243 A N
ATOM 1003 CZ ARG A 106 -5.286 -11.659 55.475 1.00 99.33 A C
ANISOU 1003 CZ ARG A 106 13166 15237 9338 278 1608 2427 A C
ATOM 1004 NH1 ARG A 106 -6.551 -11.343 55.254 1.00 96.56 A N
ANISOU 1004 NH1 ARG A 106 12632 14899 9158 102 1877 2256 A N
ATOM 1005 NH2 ARG A 106 -5.001 -12.688 56.269 1.00104.54 A N
ANISOU 1005 NH2 ARG A 106 14123 15848 9751 323 1686 2791 A N
ATOM 1006 N PRO A 107 -4.911 -5.668 53.475 1.00 59.19 A N
ANISOU 1006 N PRO A 107 7343 10530 4616 436 921 851 A N
ATOM 1007 CA PRO A 107 -5.587 -5.285 52.221 1.00 60.30 A C
ANISOU 1007 CA PRO A 107 7289 10480 5141 389 934 676 A C
ATOM 1008 C PRO A 107 -4.743 -4.389 51.328 1.00 58.57 A C
ANISOU 1008 C PRO A 107 7032 10157 5065 430 665 484 A C
ATOM 1009 O PRO A 107 -4.820 -4.501 50.095 1.00 54.64 A O
ANISOU 1009 O PRO A 107 6432 9453 4877 401 602 458 A O
ATOM 1010 CB PRO A 107 -6.861 -4.576 52.713 1.00 57.55 A C
ANISOU 1010 CB PRO A 107 6861 10266 4739 384 1162 477 A C
ATOM 1011 CG PRO A 107 -6.521 -4.109 54.104 1.00 67.24 A C
ANISOU 1011 CG PRO A 107 8260 11753 5536 443 1187 443 A C
ATOM 1012 CD PRO A 107 -5.628 -5.178 54.666 1.00 69.16 A C
ANISOU 1012 CD PRO A 107 8676 12033 5568 446 1123 762 A C
ATOM 1013 N ILE A 108 -3.924 -3.509 51.905 1.00 53.93 A N
ANISOU 1013 N ILE A 108 6534 9705 4252 482 512 342 A N
ATOM 1014 CA ILE A 108 -3.062 -2.676 51.072 1.00 54.23 A C
ANISOU 1014 CA ILE A 108 6548 9629 4429 478 287 166 A C
ATOM 1015 C ILE A 108 -2.039 -3.542 50.340 1.00 52.60 A C
ANISOU 1015 C ILE A 108 6310 9307 4370 461 138 345 A C
ATOM 1016 O ILE A 108 -1.753 -3.321 49.155 1.00 52.09 A O
ANISOU 1016 O ILE A 108 6178 9057 4556 425 51 276 A O
ATOM 1017 CB ILE A 108 -2.388 -1.585 51.927 1.00 63.48 A C
ANISOU 1017 CB ILE A 108 7815 10974 5329 500 166 -46 A C
ATOM 1018 CG1 ILE A 108 -3.435 -0.841 52.762 1.00 63.60 A C
ANISOU 1018 CG1 ILE A 108 7877 11115 5174 540 342 -224 A C
ATOM 1019 CG2 ILE A 108 -1.634 -0.596 51.027 1.00 61.28 A C
ANISOU 1019 CG2 ILE A 108 7519 10542 5224 450 -14 -255 A C
ATOM 1020 CD1 ILE A 108 -2.857 0.071 53.829 1.00 68.80 A C
ANISOU 1020 CD1 ILE A 108 8659 11976 5505 561 250 -430 A C
ATOM 1021 N LYS A 109 -1.489 -4.552 51.020 1.00 58.11 A N
ANISOU 1021 N LYS A 109 7068 10107 4904 503 115 581 A N
ATOM 1022 CA LYS A 109 -0.559 -5.475 50.374 1.00 54.73 A C
ANISOU 1022 CA LYS A 109 6603 9567 4624 526 -13 752 A C
ATOM 1023 C LYS A 109 -1.177 -6.125 49.148 1.00 53.08 A C
ANISOU 1023 C LYS A 109 6314 9098 4758 470 85 822 A C
ATOM 1024 O LYS A 109 -0.537 -6.235 48.097 1.00 52.04 A O
ANISOU 1024 O LYS A 109 6114 8823 4837 458 -26 794 A O
ATOM 1025 CB LYS A 109 -0.121 -6.565 51.348 1.00 58.99 A C
ANISOU 1025 CB LYS A 109 7255 10225 4935 622 -27 1028 A C
ATOM 1026 CG LYS A 109 1.346 -6.622 51.590 1.00 73.98 A C
ANISOU 1026 CG LYS A 109 9139 12251 6717 719 -289 1039 A C
ATOM 1027 CD LYS A 109 1.660 -7.487 52.811 1.00 72.23 A C
ANISOU 1027 CD LYS A 109 9077 12196 6172 859 -323 1297 A C
ATOM 1028 CE LYS A 109 1.587 -8.978 52.502 1.00 68.06 A C
ANISOU 1028 CE LYS A 109 8618 11457 5785 924 -246 1623 A C
ATOM 1029 NZ LYS A 109 1.983 -9.805 53.689 1.00 73.36 A N
ANISOU 1029 NZ LYS A 109 9492 12264 6117 1092 -302 1904 A N
ATOM 1030 N VAL A 110 -2.418 -6.599 49.279 1.00 55.25 A N
ANISOU 1030 N VAL A 110 6588 9322 5083 426 302 902 A N
ATOM 1031 CA VAL A 110 -3.075 -7.296 48.175 1.00 52.42 A C
ANISOU 1031 CA VAL A 110 6141 8734 5041 358 389 951 A C
ATOM 1032 C VAL A 110 -3.264 -6.370 46.986 1.00 48.50 A C
ANISOU 1032 C VAL A 110 5545 8126 4755 334 305 713 A C
ATOM 1033 O VAL A 110 -3.012 -6.752 45.834 1.00 52.23 A O
ANISOU 1033 O VAL A 110 5971 8421 5452 311 238 718 A O
ATOM 1034 CB VAL A 110 -4.417 -7.881 48.644 1.00 55.65 A C
ANISOU 1034 CB VAL A 110 6535 9148 5461 282 651 1041 A C
ATOM 1035 CG1 VAL A 110 -5.045 -8.709 47.536 1.00 58.43 A C
ANISOU 1035 CG1 VAL A 110 6785 9271 6145 191 723 1076 A C
ATOM 1036 CG2 VAL A 110 -4.211 -8.732 49.872 1.00 61.67 A C
ANISOU 1036 CG2 VAL A 110 7459 10009 5966 303 753 1302 A C
ATOM 1037 N ALEU A 111 -3.722 -5.143 47.242 0.73 54.00 A N
ANISOU 1037 N ALEU A 111 6234 8915 5368 351 312 502 A N
ATOM 1038 N BLEU A 111 -3.708 -5.140 47.228 0.27 53.90 A N
ANISOU 1038 N BLEU A 111 6222 8901 5357 351 309 501 A N
ATOM 1039 CA ALEU A 111 -3.926 -4.187 46.160 0.73 51.55 A C
ANISOU 1039 CA ALEU A 111 5882 8477 5228 355 227 295 A C
ATOM 1040 CA BLEU A 111 -3.918 -4.235 46.106 0.27 51.66 A C
ANISOU 1040 CA BLEU A 111 5893 8481 5253 353 225 301 A C
ATOM 1041 C ALEU A 111 -2.606 -3.853 45.481 0.73 52.39 A C
ANISOU 1041 C ALEU A 111 6035 8503 5367 341 45 259 A C
ATOM 1042 C BLEU A 111 -2.596 -3.838 45.464 0.27 52.33 A C
ANISOU 1042 C BLEU A 111 6028 8493 5361 341 43 256 A C
ATOM 1043 O ALEU A 111 -2.509 -3.857 44.250 0.73 50.53 A O
ANISOU 1043 O ALEU A 111 5778 8097 5324 318 -12 226 A O
ATOM 1044 O BLEU A 111 -2.493 -3.781 44.234 0.27 50.66 A O
ANISOU 1044 O BLEU A 111 5798 8111 5338 319 -17 215 A O
ATOM 1045 CB ALEU A 111 -4.579 -2.912 46.697 0.73 54.14 A C
ANISOU 1045 CB ALEU A 111 6229 8898 5442 406 266 78 A C
ATOM 1046 CB BLEU A 111 -4.677 -2.998 46.557 0.27 54.10 A C
ANISOU 1046 CB BLEU A 111 6210 8872 5472 403 272 86 A C
ATOM 1047 CG ALEU A 111 -6.097 -2.776 46.608 0.73 58.23 A C
ANISOU 1047 CG ALEU A 111 6632 9423 6069 440 413 -15 A C
ATOM 1048 CG BLEU A 111 -6.119 -3.253 46.972 0.27 56.32 A C
ANISOU 1048 CG BLEU A 111 6384 9232 5784 415 472 70 A C
ATOM 1049 CD1ALEU A 111 -6.607 -3.033 45.193 0.73 59.51 A C
ANISOU 1049 CD1ALEU A 111 6696 9398 6517 435 359 -38 A C
ATOM 1050 CD1BLEU A 111 -6.643 -1.957 47.489 0.27 60.71 A C
ANISOU 1050 CD1BLEU A 111 6960 9878 6229 502 499 -165 A C
ATOM 1051 CD2ALEU A 111 -6.778 -3.698 47.616 0.73 59.40 A C
ANISOU 1051 CD2ALEU A 111 6726 9725 6120 395 630 127 A C
ATOM 1052 CD2BLEU A 111 -6.984 -3.759 45.836 0.27 55.59 A C
ANISOU 1052 CD2BLEU A 111 6148 8995 5980 391 496 66 A C
ATOM 1053 N LEU A 112 -1.576 -3.552 46.276 1.00 49.85 A N
ANISOU 1053 N LEU A 112 5769 8323 4849 348 -44 250 A N
ATOM 1054 CA LEU A 112 -0.292 -3.167 45.704 1.00 49.76 A C
ANISOU 1054 CA LEU A 112 5760 8271 4876 308 -197 182 A C
ATOM 1055 C LEU A 112 0.266 -4.285 44.834 1.00 50.48 A C
ANISOU 1055 C LEU A 112 5789 8249 5143 305 -225 334 A C
ATOM 1056 O LEU A 112 0.796 -4.032 43.741 1.00 50.24 A O
ANISOU 1056 O LEU A 112 5742 8091 5256 256 -280 262 A O
ATOM 1057 CB LEU A 112 0.686 -2.788 46.812 1.00 47.50 A C
ANISOU 1057 CB LEU A 112 5498 8201 4349 314 -300 132 A C
ATOM 1058 CG LEU A 112 2.065 -2.316 46.357 1.00 55.55 A C
ANISOU 1058 CG LEU A 112 6472 9225 5408 242 -448 21 A C
ATOM 1059 CD1 LEU A 112 1.901 -1.063 45.537 1.00 59.32 A C
ANISOU 1059 CD1 LEU A 112 7015 9532 5992 147 -437 -187 A C
ATOM 1060 CD2 LEU A 112 2.947 -2.045 47.559 1.00 58.02 A C
ANISOU 1060 CD2 LEU A 112 6774 9796 5475 253 -573 -44 A C
ATOM 1061 N GLN A 113 0.130 -5.533 45.285 1.00 48.50 A N
ANISOU 1061 N GLN A 113 5525 8023 4878 357 -170 545 A N
ATOM 1062 CA GLN A 113 0.623 -6.650 44.490 1.00 48.97 A C
ANISOU 1062 CA GLN A 113 5543 7946 5115 374 -189 678 A C
ATOM 1063 C GLN A 113 -0.177 -6.800 43.204 1.00 51.99 A C
ANISOU 1063 C GLN A 113 5903 8119 5734 319 -123 629 A C
ATOM 1064 O GLN A 113 0.402 -7.036 42.137 1.00 52.12 A O
ANISOU 1064 O GLN A 113 5893 8014 5895 304 -172 602 A O
ATOM 1065 CB GLN A 113 0.569 -7.943 45.298 1.00 57.07 A C
ANISOU 1065 CB GLN A 113 6612 8998 6075 448 -133 926 A C
ATOM 1066 CG GLN A 113 0.799 -9.192 44.465 1.00 67.69 A C
ANISOU 1066 CG GLN A 113 7941 10142 7635 472 -116 1058 A C
ATOM 1067 CD GLN A 113 1.577 -10.251 45.210 1.00 86.32 A C
ANISOU 1067 CD GLN A 113 10357 12536 9905 604 -165 1280 A C
ATOM 1068 NE2 GLN A 113 1.174 -10.524 46.445 1.00 84.88 A N
ANISOU 1068 NE2 GLN A 113 10283 12458 9507 642 -101 1437 A N
ATOM 1069 OE1 GLN A 113 2.534 -10.816 44.684 1.00103.11 A O
ANISOU 1069 OE1 GLN A 113 12439 14596 12141 687 -256 1311 A O
ATOM 1070 N THR A 114 -1.505 -6.655 43.288 1.00 49.00 A N
ANISOU 1070 N THR A 114 5519 7716 5384 293 -15 597 A N
ATOM 1071 CA THR A 114 -2.356 -6.792 42.109 1.00 50.72 A C
ANISOU 1071 CA THR A 114 5693 7768 5811 255 16 529 A C
ATOM 1072 C THR A 114 -2.064 -5.692 41.093 1.00 48.57 A C
ANISOU 1072 C THR A 114 5456 7423 5574 250 -87 353 A C
ATOM 1073 O THR A 114 -1.955 -5.957 39.889 1.00 46.72 A O
ANISOU 1073 O THR A 114 5226 7048 5479 230 -124 327 A O
ATOM 1074 CB THR A 114 -3.829 -6.759 42.534 1.00 50.94 A C
ANISOU 1074 CB THR A 114 5660 7837 5856 238 143 498 A C
ATOM 1075 CG2 THR A 114 -4.762 -6.774 41.334 1.00 50.17 A C
ANISOU 1075 CG2 THR A 114 5485 7612 5965 216 132 385 A C
ATOM 1076 OG1 THR A 114 -4.128 -7.899 43.353 1.00 52.71 A O
ANISOU 1076 OG1 THR A 114 5878 8089 6061 204 279 685 A O
ATOM 1077 N ALEU A 115 -1.926 -4.450 41.562 0.60 47.80 A N
ANISOU 1077 N ALEU A 115 5414 7406 5342 262 -125 231 A N
ATOM 1078 N BLEU A 115 -1.924 -4.453 41.568 0.41 47.89 A N
ANISOU 1078 N BLEU A 115 5425 7418 5352 262 -125 232 A N
ATOM 1079 CA ALEU A 115 -1.626 -3.344 40.658 0.60 48.43 A C
ANISOU 1079 CA ALEU A 115 5581 7380 5442 244 -202 85 A C
ATOM 1080 CA BLEU A 115 -1.628 -3.333 40.680 0.41 48.45 A C
ANISOU 1080 CA BLEU A 115 5583 7384 5440 245 -202 84 A C
ATOM 1081 C ALEU A 115 -0.238 -3.482 40.045 0.60 49.08 A C
ANISOU 1081 C ALEU A 115 5680 7421 5546 180 -258 102 A C
ATOM 1082 C BLEU A 115 -0.242 -3.464 40.059 0.41 49.05 A C
ANISOU 1082 C BLEU A 115 5678 7418 5540 180 -258 100 A C
ATOM 1083 O ALEU A 115 -0.035 -3.159 38.867 0.60 45.45 A O
ANISOU 1083 O ALEU A 115 5288 6823 5159 145 -282 45 A O
ATOM 1084 O BLEU A 115 -0.048 -3.130 38.882 0.41 45.50 A O
ANISOU 1084 O BLEU A 115 5295 6829 5163 145 -282 43 A O
ATOM 1085 CB ALEU A 115 -1.735 -2.018 41.405 0.60 48.76 A C
ANISOU 1085 CB ALEU A 115 5700 7486 5339 261 -216 -55 A C
ATOM 1086 CB BLEU A 115 -1.739 -2.026 41.462 0.41 48.82 A C
ANISOU 1086 CB BLEU A 115 5706 7502 5342 262 -214 -53 A C
ATOM 1087 CG ALEU A 115 -3.100 -1.341 41.363 0.60 55.52 A C
ANISOU 1087 CG ALEU A 115 6572 8302 6220 351 -186 -164 A C
ATOM 1088 CG BLEU A 115 -2.002 -0.736 40.691 0.41 48.95 A C
ANISOU 1088 CG BLEU A 115 5857 7362 5379 278 -261 -208 A C
ATOM 1089 CD1ALEU A 115 -3.226 -0.321 42.477 0.60 58.56 A C
ANISOU 1089 CD1ALEU A 115 7016 8789 6444 386 -165 -289 A C
ATOM 1090 CD1BLEU A 115 -3.387 -0.732 40.075 0.41 54.41 A C
ANISOU 1090 CD1BLEU A 115 6525 7972 6178 384 -255 -241 A C
ATOM 1091 CD2ALEU A 115 -3.315 -0.681 40.012 0.60 54.44 A C
ANISOU 1091 CD2ALEU A 115 6539 7964 6180 379 -260 -244 A C
ATOM 1092 CD2BLEU A 115 -1.827 0.449 41.627 0.41 52.19 A C
ANISOU 1092 CD2BLEU A 115 6359 7828 5642 277 -267 -348 A C
ATOM 1093 N THR A 116 0.737 -3.931 40.835 1.00 45.11 A N
ANISOU 1093 N THR A 116 5117 7054 4968 173 -279 172 A N
ATOM 1094 CA THR A 116 2.095 -4.048 40.314 1.00 44.42 A C
ANISOU 1094 CA THR A 116 4992 6968 4917 120 -326 157 A C
ATOM 1095 C THR A 116 2.166 -5.120 39.234 1.00 44.87 A C
ANISOU 1095 C THR A 116 5015 6896 5138 139 -296 237 A C
ATOM 1096 O THR A 116 2.804 -4.921 38.190 1.00 45.87 A O
ANISOU 1096 O THR A 116 5159 6942 5329 80 -293 170 A O
ATOM 1097 CB THR A 116 3.071 -4.349 41.444 1.00 51.47 A C
ANISOU 1097 CB THR A 116 5795 8066 5695 150 -389 203 A C
ATOM 1098 CG2 THR A 116 4.500 -4.430 40.905 1.00 51.32 A C
ANISOU 1098 CG2 THR A 116 5677 8085 5738 101 -439 151 A C
ATOM 1099 OG1 THR A 116 3.018 -3.300 42.418 1.00 49.04 A O
ANISOU 1099 OG1 THR A 116 5532 7884 5217 120 -424 91 A O
ATOM 1100 N GLU A 117 1.523 -6.263 39.475 1.00 45.17 A N
ANISOU 1100 N GLU A 117 5017 6905 5238 206 -256 370 A N
ATOM 1101 CA GLU A 117 1.532 -7.338 38.488 1.00 50.79 A C
ANISOU 1101 CA GLU A 117 5711 7473 6114 220 -225 423 A C
ATOM 1102 C GLU A 117 0.944 -6.852 37.171 1.00 48.55 A C
ANISOU 1102 C GLU A 117 5499 7048 5899 170 -221 307 A C
ATOM 1103 O GLU A 117 1.493 -7.115 36.098 1.00 46.44 A O
ANISOU 1103 O GLU A 117 5250 6693 5701 150 -217 267 A O
ATOM 1104 CB GLU A 117 0.738 -8.541 38.999 1.00 53.68 A C
ANISOU 1104 CB GLU A 117 6059 7791 6545 263 -162 571 A C
ATOM 1105 CG GLU A 117 1.290 -9.172 40.273 1.00 89.20 A C
ANISOU 1105 CG GLU A 117 10542 12403 10948 341 -168 731 A C
ATOM 1106 CD GLU A 117 1.579 -10.656 40.122 1.00125.16 A C
ANISOU 1106 CD GLU A 117 15101 16825 15629 410 -136 881 A C
ATOM 1107 OE1 GLU A 117 0.906 -11.313 39.302 1.00130.15 A O
ANISOU 1107 OE1 GLU A 117 15750 17274 16426 364 -71 871 A O
ATOM 1108 OE2 GLU A 117 2.486 -11.164 40.819 1.00120.02 A O
ANISOU 1108 OE2 GLU A 117 14440 16247 14913 521 -188 998 A O
ATOM 1109 N SER A 118 -0.170 -6.128 37.246 1.00 41.89 A N
ANISOU 1109 N SER A 118 4700 6193 5022 170 -227 246 A N
ATOM 1110 CA SER A 118 -0.810 -5.605 36.043 1.00 41.87 A C
ANISOU 1110 CA SER A 118 4783 6070 5057 165 -261 143 A C
ATOM 1111 C SER A 118 0.072 -4.570 35.358 1.00 43.91 A C
ANISOU 1111 C SER A 118 5166 6283 5234 114 -284 62 A C
ATOM 1112 O SER A 118 0.277 -4.618 34.138 1.00 42.88 A O
ANISOU 1112 O SER A 118 5119 6048 5127 91 -287 26 A O
ATOM 1113 CB SER A 118 -2.162 -5.006 36.427 1.00 43.60 A C
ANISOU 1113 CB SER A 118 4994 6314 5258 217 -276 87 A C
ATOM 1114 OG SER A 118 -2.848 -4.528 35.284 1.00 45.79 A O
ANISOU 1114 OG SER A 118 5349 6486 5561 255 -346 -9 A O
ATOM 1115 N HIS A 119 0.619 -3.636 36.139 1.00 45.53 A N
ANISOU 1115 N HIS A 119 5398 6565 5336 78 -287 27 A N
ATOM 1116 CA HIS A 119 1.506 -2.615 35.596 1.00 42.09 A C
ANISOU 1116 CA HIS A 119 5083 6073 4835 -19 -279 -54 A C
ATOM 1117 C HIS A 119 2.662 -3.240 34.829 1.00 43.77 A C
ANISOU 1117 C HIS A 119 5246 6284 5100 -89 -229 -42 A C
ATOM 1118 O HIS A 119 3.002 -2.798 33.724 1.00 43.76 A O
ANISOU 1118 O HIS A 119 5375 6174 5079 -159 -188 -89 A O
ATOM 1119 CB HIS A 119 2.034 -1.739 36.735 1.00 43.23 A C
ANISOU 1119 CB HIS A 119 5217 6324 4882 -74 -289 -113 A C
ATOM 1120 CG HIS A 119 2.670 -0.461 36.277 1.00 42.08 A C
ANISOU 1120 CG HIS A 119 5232 6078 4679 -202 -266 -220 A C
ATOM 1121 CD2 HIS A 119 2.212 0.812 36.294 1.00 45.76 A C
ANISOU 1121 CD2 HIS A 119 5893 6418 5078 -213 -276 -303 A C
ATOM 1122 ND1 HIS A 119 3.937 -0.405 35.737 1.00 42.49 A N
ANISOU 1122 ND1 HIS A 119 5260 6136 4747 -347 -207 -254 A N
ATOM 1123 CE1 HIS A 119 4.233 0.849 35.445 1.00 47.27 A C
ANISOU 1123 CE1 HIS A 119 6048 6617 5296 -476 -168 -346 A C
ATOM 1124 NE2 HIS A 119 3.204 1.608 35.775 1.00 46.65 A N
ANISOU 1124 NE2 HIS A 119 6123 6438 5165 -388 -217 -371 A N
ATOM 1125 N ARG A 120 3.283 -4.275 35.401 1.00 40.75 A N
ANISOU 1125 N ARG A 120 4688 6020 4776 -57 -223 23 A N
ATOM 1126 CA ARG A 120 4.486 -4.838 34.797 1.00 43.59 A C
ANISOU 1126 CA ARG A 120 4960 6405 5197 -96 -173 9 A C
ATOM 1127 C ARG A 120 4.176 -5.554 33.488 1.00 43.53 A C
ANISOU 1127 C ARG A 120 5018 6258 5263 -70 -129 11 A C
ATOM 1128 O ARG A 120 5.045 -5.633 32.613 1.00 47.94 A O
ANISOU 1128 O ARG A 120 5577 6801 5837 -128 -54 -46 A O
ATOM 1129 CB ARG A 120 5.176 -5.781 35.787 1.00 45.69 A C
ANISOU 1129 CB ARG A 120 5031 6824 5504 -11 -208 83 A C
ATOM 1130 CG ARG A 120 5.587 -5.081 37.074 1.00 49.87 A C
ANISOU 1130 CG ARG A 120 5495 7529 5925 -35 -274 58 A C
ATOM 1131 CD ARG A 120 7.099 -5.030 37.267 1.00 48.75 A C
ANISOU 1131 CD ARG A 120 5176 7554 5794 -81 -292 -19 A C
ATOM 1132 NE ARG A 120 7.753 -4.011 36.450 1.00 48.31 A N
ANISOU 1132 NE ARG A 120 5157 7463 5738 -270 -214 -168 A N
ATOM 1133 CZ ARG A 120 9.063 -3.796 36.423 1.00 49.98 A C
ANISOU 1133 CZ ARG A 120 5193 7818 5980 -368 -194 -281 A C
ATOM 1134 NH1 ARG A 120 9.902 -4.479 37.199 1.00 49.95 A N
ANISOU 1134 NH1 ARG A 120 4947 8027 6005 -262 -286 -275 A N
ATOM 1135 NH2 ARG A 120 9.548 -2.861 35.610 1.00 51.89 A N
ANISOU 1135 NH2 ARG A 120 5503 7992 6222 -578 -78 -405 A N
ATOM 1136 N ILE A 121 2.950 -6.053 33.330 1.00 40.96 A N
ANISOU 1136 N ILE A 121 4740 5845 4978 6 -167 53 A N
ATOM 1137 CA ILE A 121 2.515 -6.625 32.059 1.00 41.62 A C
ANISOU 1137 CA ILE A 121 4903 5801 5110 22 -153 19 A C
ATOM 1138 C ILE A 121 2.270 -5.521 31.036 1.00 44.03 A C
ANISOU 1138 C ILE A 121 5415 6019 5295 -30 -161 -55 A C
ATOM 1139 O ILE A 121 2.728 -5.600 29.891 1.00 45.89 A O
ANISOU 1139 O ILE A 121 5747 6195 5493 -70 -105 -104 A O
ATOM 1140 CB ILE A 121 1.255 -7.482 32.263 1.00 45.09 A C
ANISOU 1140 CB ILE A 121 5299 6188 5643 91 -200 60 A C
ATOM 1141 CG1 ILE A 121 1.626 -8.806 32.934 1.00 44.69 A C
ANISOU 1141 CG1 ILE A 121 5114 6151 5716 138 -162 154 A C
ATOM 1142 CG2 ILE A 121 0.537 -7.732 30.934 1.00 46.28 A C
ANISOU 1142 CG2 ILE A 121 5551 6223 5809 97 -234 -22 A C
ATOM 1143 CD1 ILE A 121 0.446 -9.448 33.659 1.00 51.14 A C
ANISOU 1143 CD1 ILE A 121 5879 6943 6610 161 -170 227 A C
ATOM 1144 N LEU A 122 1.552 -4.470 31.438 1.00 40.12 A N
ANISOU 1144 N LEU A 122 5011 5509 4722 -17 -222 -62 A N
ATOM 1145 CA LEU A 122 1.255 -3.375 30.519 1.00 43.24 A C
ANISOU 1145 CA LEU A 122 5649 5788 4993 -31 -246 -108 A C
ATOM 1146 C LEU A 122 2.528 -2.696 30.016 1.00 42.21 A C
ANISOU 1146 C LEU A 122 5634 5627 4776 -176 -129 -132 A C
ATOM 1147 O LEU A 122 2.551 -2.185 28.891 1.00 43.06 A O
ANISOU 1147 O LEU A 122 5970 5618 4771 -208 -100 -147 A O
ATOM 1148 CB LEU A 122 0.342 -2.349 31.196 1.00 43.94 A C
ANISOU 1148 CB LEU A 122 5807 5855 5034 38 -329 -119 A C
ATOM 1149 CG LEU A 122 -1.084 -2.783 31.547 1.00 50.35 A C
ANISOU 1149 CG LEU A 122 6510 6701 5920 174 -428 -125 A C
ATOM 1150 CD1 LEU A 122 -1.801 -1.617 32.240 1.00 54.49 A C
ANISOU 1150 CD1 LEU A 122 7100 7214 6390 253 -482 -162 A C
ATOM 1151 CD2 LEU A 122 -1.836 -3.254 30.324 1.00 49.23 A C
ANISOU 1151 CD2 LEU A 122 6428 6492 5786 244 -510 -161 A C
ATOM 1152 N GLU A 123 3.594 -2.676 30.823 1.00 40.16 A N
ANISOU 1152 N GLU A 123 5219 5481 4558 -270 -59 -141 A N
ATOM 1153 CA GLU A 123 4.828 -2.051 30.360 1.00 42.05 A C
ANISOU 1153 CA GLU A 123 5517 5715 4744 -445 74 -193 A C
ATOM 1154 C GLU A 123 5.319 -2.676 29.063 1.00 41.87 A C
ANISOU 1154 C GLU A 123 5540 5660 4707 -475 180 -211 A C
ATOM 1155 O GLU A 123 5.920 -1.987 28.232 1.00 43.43 A O
ANISOU 1155 O GLU A 123 5910 5788 4804 -616 308 -242 A O
ATOM 1156 CB GLU A 123 5.930 -2.176 31.411 1.00 44.13 A C
ANISOU 1156 CB GLU A 123 5526 6159 5081 -523 106 -230 A C
ATOM 1157 CG GLU A 123 5.713 -1.399 32.691 1.00 45.02 A C
ANISOU 1157 CG GLU A 123 5613 6326 5166 -535 25 -248 A C
ATOM 1158 CD GLU A 123 6.611 -1.912 33.793 1.00 47.49 A C
ANISOU 1158 CD GLU A 123 5640 6864 5541 -539 -5 -270 A C
ATOM 1159 OE1 GLU A 123 7.759 -2.291 33.473 1.00 47.64 A O
ANISOU 1159 OE1 GLU A 123 5501 6981 5618 -613 71 -319 A O
ATOM 1160 OE2 GLU A 123 6.179 -1.955 34.971 1.00 43.36 A O
ANISOU 1160 OE2 GLU A 123 5045 6433 4997 -454 -106 -243 A O
ATOM 1161 N LYS A 124 5.110 -3.983 28.893 1.00 41.07 A N
ANISOU 1161 N LYS A 124 5301 5601 4702 -358 149 -199 A N
ATOM 1162 CA ALYS A 124 5.628 -4.672 27.719 0.60 47.44 A C
ANISOU 1162 CA ALYS A 124 6136 6391 5500 -374 258 -247 A C
ATOM 1163 CA BLYS A 124 5.624 -4.675 27.720 0.40 47.43 A C
ANISOU 1163 CA BLYS A 124 6134 6389 5499 -373 258 -247 A C
ATOM 1164 C LYS A 124 4.819 -4.355 26.466 1.00 40.80 A C
ANISOU 1164 C LYS A 124 5592 5406 4503 -350 232 -252 A C
ATOM 1165 O LYS A 124 5.302 -4.600 25.352 1.00 42.88 A O
ANISOU 1165 O LYS A 124 5959 5648 4684 -396 349 -303 A O
ATOM 1166 CB ALYS A 124 5.635 -6.186 27.950 0.60 49.12 A C
ANISOU 1166 CB ALYS A 124 6134 6654 5874 -246 229 -247 A C
ATOM 1167 CB BLYS A 124 5.618 -6.190 27.947 0.40 49.15 A C
ANISOU 1167 CB BLYS A 124 6140 6656 5878 -244 227 -246 A C
ATOM 1168 CG ALYS A 124 6.579 -6.677 29.042 0.60 54.33 A C
ANISOU 1168 CG ALYS A 124 6514 7461 6668 -222 245 -233 A C
ATOM 1169 CG BLYS A 124 6.405 -6.681 29.159 0.40 54.54 A C
ANISOU 1169 CG BLYS A 124 6546 7482 6697 -209 222 -220 A C
ATOM 1170 CD ALYS A 124 8.022 -6.327 28.740 0.60 58.69 A C
ANISOU 1170 CD ALYS A 124 6964 8124 7213 -344 398 -322 A C
ATOM 1171 CD BLYS A 124 7.793 -6.070 29.232 0.40 57.56 A C
ANISOU 1171 CD BLYS A 124 6816 7990 7064 -343 343 -291 A C
ATOM 1172 CE ALYS A 124 8.980 -7.224 29.509 0.60 71.57 A C
ANISOU 1172 CE ALYS A 124 8285 9910 8998 -247 392 -335 A C
ATOM 1173 CE BLYS A 124 8.717 -6.835 30.185 0.40 69.69 A C
ANISOU 1173 CE BLYS A 124 8043 9695 8739 -256 318 -292 A C
ATOM 1174 NZ ALYS A 124 10.314 -6.585 29.657 0.60 69.50 A N
ANISOU 1174 NZ ALYS A 124 7847 9819 8742 -386 495 -436 A N
ATOM 1175 NZ BLYS A 124 8.035 -7.908 30.966 0.40 65.71 A N
ANISOU 1175 NZ BLYS A 124 7473 9163 8329 -67 190 -182 A N
ATOM 1176 N TYR A 125 3.602 -3.835 26.623 1.00 40.69 A N
ANISOU 1176 N TYR A 125 5710 5313 4437 -262 77 -211 A N
ATOM 1177 CA TYR A 125 2.759 -3.465 25.495 1.00 42.99 A C
ANISOU 1177 CA TYR A 125 6283 5487 4565 -197 -1 -215 A C
ATOM 1178 C TYR A 125 2.769 -1.970 25.225 1.00 44.38 A C
ANISOU 1178 C TYR A 125 6759 5540 4562 -255 19 -169 A C
ATOM 1179 O TYR A 125 2.065 -1.518 24.317 1.00 47.43 A O
ANISOU 1179 O TYR A 125 7423 5818 4781 -170 -69 -150 A O
ATOM 1180 CB TYR A 125 1.317 -3.923 25.735 1.00 42.47 A C
ANISOU 1180 CB TYR A 125 6147 5419 4570 -31 -206 -223 A C
ATOM 1181 CG TYR A 125 1.148 -5.413 25.689 1.00 39.41 A C
ANISOU 1181 CG TYR A 125 5553 5085 4337 11 -221 -273 A C
ATOM 1182 CD1 TYR A 125 1.106 -6.091 24.487 1.00 38.62 A C
ANISOU 1182 CD1 TYR A 125 5548 4952 4173 27 -219 -351 A C
ATOM 1183 CD2 TYR A 125 1.079 -6.157 26.865 1.00 45.67 A C
ANISOU 1183 CD2 TYR A 125 6082 5946 5327 27 -225 -241 A C
ATOM 1184 CE1 TYR A 125 0.967 -7.452 24.443 1.00 39.88 A C
ANISOU 1184 CE1 TYR A 125 5542 5122 4489 54 -223 -416 A C
ATOM 1185 CE2 TYR A 125 0.938 -7.519 26.829 1.00 48.74 A C
ANISOU 1185 CE2 TYR A 125 6324 6332 5864 57 -222 -273 A C
ATOM 1186 CZ TYR A 125 0.882 -8.163 25.617 1.00 47.28 A C
ANISOU 1186 CZ TYR A 125 6232 6090 5641 66 -221 -369 A C
ATOM 1187 OH TYR A 125 0.741 -9.521 25.577 1.00 45.21 A O
ANISOU 1187 OH TYR A 125 5845 5788 5543 86 -212 -420 A O
ATOM 1188 N THR A 126 3.568 -1.208 25.962 1.00 44.55 A N
ANISOU 1188 N THR A 126 6747 5568 4612 -395 125 -158 A N
ATOM 1189 CA ATHR A 126 3.638 0.243 25.880 0.87 46.75 A C
ANISOU 1189 CA ATHR A 126 7316 5689 4756 -479 165 -120 A C
ATOM 1190 CA BTHR A 126 3.616 0.236 25.806 0.13 46.98 A C
ANISOU 1190 CA BTHR A 126 7360 5714 4777 -476 164 -118 A C
ATOM 1191 C THR A 126 5.007 0.677 25.371 1.00 49.36 A C
ANISOU 1191 C THR A 126 7737 5999 5017 -733 416 -137 A C
ATOM 1192 O THR A 126 6.020 0.075 25.730 1.00 51.11 A O
ANISOU 1192 O THR A 126 7674 6382 5364 -848 538 -201 A O
ATOM 1193 CB ATHR A 126 3.417 0.862 27.265 0.87 49.56 A C
ANISOU 1193 CB ATHR A 126 7555 6061 5214 -471 92 -130 A C
ATOM 1194 CB BTHR A 126 3.224 0.940 27.108 0.13 50.24 A C
ANISOU 1194 CB BTHR A 126 7696 6118 5275 -444 72 -122 A C
ATOM 1195 CG2ATHR A 126 3.319 2.369 27.161 0.87 52.24 A C
ANISOU 1195 CG2ATHR A 126 8236 6185 5429 -528 114 -104 A C
ATOM 1196 CG2BTHR A 126 1.737 0.750 27.381 0.13 52.22 A C
ANISOU 1196 CG2BTHR A 126 7921 6364 5556 -196 -148 -110 A C
ATOM 1197 OG1ATHR A 126 2.227 0.324 27.850 0.87 52.01 A O
ANISOU 1197 OG1ATHR A 126 7714 6435 5612 -261 -95 -128 A O
ATOM 1198 OG1BTHR A 126 3.979 0.390 28.193 0.13 51.20 A O
ANISOU 1198 OG1BTHR A 126 7474 6423 5556 -528 123 -168 A O
ATOM 1199 N GLN A 127 5.049 1.745 24.577 1.00 58.62 A N
ANISOU 1199 N GLN A 127 9303 6974 5998 -818 500 -80 A N
ATOM 1200 CA GLN A 127 6.343 2.257 24.133 1.00 59.10 A C
ANISOU 1200 CA GLN A 127 9455 7003 5997 -1109 781 -99 A C
ATOM 1201 C GLN A 127 7.088 2.903 25.300 1.00 59.18 A C
ANISOU 1201 C GLN A 127 9279 7050 6155 -1303 852 -168 A C
ATOM 1202 O GLN A 127 6.490 3.636 26.091 1.00 54.76 A O
ANISOU 1202 O GLN A 127 8795 6388 5624 -1241 719 -156 A O
ATOM 1203 CB GLN A 127 6.194 3.276 23.004 1.00 67.87 A C
ANISOU 1203 CB GLN A 127 11090 7857 6842 -1171 876 5 A C
ATOM 1204 CG GLN A 127 5.120 2.955 21.997 1.00 78.11 A C
ANISOU 1204 CG GLN A 127 12645 9087 7947 -916 705 79 A C
ATOM 1205 CD GLN A 127 4.324 4.161 21.599 1.00102.95 A C
ANISOU 1205 CD GLN A 127 16273 11952 10891 -807 598 203 A C
ATOM 1206 NE2 GLN A 127 3.166 3.914 21.003 1.00102.37 A N
ANISOU 1206 NE2 GLN A 127 16353 11855 10689 -517 352 246 A N
ATOM 1207 OE1 GLN A 127 4.743 5.304 21.786 1.00106.03 A O
ANISOU 1207 OE1 GLN A 127 16906 12139 11241 -976 730 254 A O
ATOM 1208 N PRO A 128 8.402 2.675 25.419 1.00 60.31 A N
ANISOU 1208 N PRO A 128 9172 7350 6393 -1536 1058 -263 A N
ATOM 1209 CA PRO A 128 9.134 3.230 26.569 1.00 63.92 A C
ANISOU 1209 CA PRO A 128 9407 7886 6995 -1722 1092 -364 A C
ATOM 1210 C PRO A 128 9.119 4.744 26.616 1.00 63.23 A C
ANISOU 1210 C PRO A 128 9673 7530 6821 -1912 1168 -347 A C
ATOM 1211 O PRO A 128 9.246 5.324 27.702 1.00 62.64 A O
ANISOU 1211 O PRO A 128 9491 7464 6844 -1989 1105 -429 A O
ATOM 1212 CB PRO A 128 10.562 2.692 26.370 1.00 77.22 A C
ANISOU 1212 CB PRO A 128 10770 9794 8777 -1932 1314 -482 A C
ATOM 1213 CG PRO A 128 10.422 1.571 25.391 1.00 62.78 A C
ANISOU 1213 CG PRO A 128 8922 8036 6897 -1773 1345 -447 A C
ATOM 1214 CD PRO A 128 9.314 1.983 24.491 1.00 73.92 A C
ANISOU 1214 CD PRO A 128 10801 9196 8090 -1648 1278 -310 A C
ATOM 1215 N SER A 129 8.979 5.402 25.462 1.00 49.00 A N
ANISOU 1215 N SER A 129 5956 5976 6686 618 427 339 A N
ATOM 1216 CA SER A 129 8.929 6.860 25.440 1.00 64.56 A C
ANISOU 1216 CA SER A 129 7835 7955 8741 437 328 377 A C
ATOM 1217 C SER A 129 7.768 7.400 26.267 1.00 60.01 A C
ANISOU 1217 C SER A 129 7394 7330 8079 265 85 141 A C
ATOM 1218 O SER A 129 7.854 8.506 26.816 1.00 56.43 A O
ANISOU 1218 O SER A 129 6900 6854 7688 117 -109 154 A O
ATOM 1219 CB SER A 129 8.825 7.345 23.994 1.00 66.51 A C
ANISOU 1219 CB SER A 129 8188 8191 8892 586 526 423 A C
ATOM 1220 OG SER A 129 7.563 7.026 23.448 1.00 63.54 A O
ANISOU 1220 OG SER A 129 8143 7709 8290 648 498 151 A O
ATOM 1221 N ILE A 130 6.667 6.654 26.355 1.00 53.90 A N
ANISOU 1221 N ILE A 130 6795 6523 7162 313 69 -27 A N
ATOM 1222 CA ILE A 130 5.562 7.076 27.208 1.00 55.51 A C
ANISOU 1222 CA ILE A 130 7074 6738 7280 237 -89 -137 A C
ATOM 1223 C ILE A 130 6.025 7.172 28.658 1.00 52.68 A C
ANISOU 1223 C ILE A 130 6626 6431 6958 208 -238 -97 A C
ATOM 1224 O ILE A 130 5.687 8.127 29.370 1.00 50.99 A O
ANISOU 1224 O ILE A 130 6512 6212 6651 200 -397 -148 A O
ATOM 1225 CB ILE A 130 4.372 6.111 27.063 1.00 55.37 A C
ANISOU 1225 CB ILE A 130 7155 6683 7200 284 -96 -179 A C
ATOM 1226 CG1 ILE A 130 3.762 6.152 25.658 1.00 66.12 A C
ANISOU 1226 CG1 ILE A 130 8700 7924 8500 312 -62 -245 A C
ATOM 1227 CG2 ILE A 130 3.275 6.447 28.069 1.00 58.58 A C
ANISOU 1227 CG2 ILE A 130 7552 7169 7536 282 -187 -154 A C
ATOM 1228 CD1 ILE A 130 3.441 7.538 25.140 1.00 67.44 A C
ANISOU 1228 CD1 ILE A 130 8923 8102 8597 260 -41 -304 A C
ATOM 1229 N PHE A 131 6.808 6.187 29.120 1.00 54.07 A N
ANISOU 1229 N PHE A 131 6672 6637 7237 234 -211 -11 A N
ATOM 1230 CA PHE A 131 7.207 6.163 30.526 1.00 55.37 A C
ANISOU 1230 CA PHE A 131 6790 6832 7417 230 -377 19 A C
ATOM 1231 C PHE A 131 8.102 7.342 30.877 1.00 56.07 A C
ANISOU 1231 C PHE A 131 6867 6837 7600 122 -611 76 A C
ATOM 1232 O PHE A 131 8.012 7.882 31.986 1.00 57.21 A O
ANISOU 1232 O PHE A 131 7165 6928 7644 155 -867 20 A O
ATOM 1233 CB PHE A 131 7.921 4.854 30.862 1.00 55.29 A C
ANISOU 1233 CB PHE A 131 6627 6861 7518 267 -301 112 A C
ATOM 1234 CG PHE A 131 7.030 3.661 30.830 1.00 51.78 A C
ANISOU 1234 CG PHE A 131 6219 6438 7016 348 -211 84 A C
ATOM 1235 CD1 PHE A 131 7.205 2.682 29.872 1.00 63.01 A C
ANISOU 1235 CD1 PHE A 131 7663 7797 8479 405 -93 99 A C
ATOM 1236 CD2 PHE A 131 6.025 3.510 31.770 1.00 66.86 A C
ANISOU 1236 CD2 PHE A 131 8159 8413 8833 406 -274 93 A C
ATOM 1237 CE1 PHE A 131 6.383 1.578 29.838 1.00 63.89 A C
ANISOU 1237 CE1 PHE A 131 7841 7848 8587 441 -136 99 A C
ATOM 1238 CE2 PHE A 131 5.206 2.407 31.745 1.00 68.46 A C
ANISOU 1238 CE2 PHE A 131 8322 8616 9075 436 -249 173 A C
ATOM 1239 CZ PHE A 131 5.387 1.439 30.778 1.00 69.24 A C
ANISOU 1239 CZ PHE A 131 8456 8589 9264 415 -229 164 A C
ATOM 1240 N LYS A 132 8.989 7.750 29.970 1.00 52.56 A N
ANISOU 1240 N LYS A 132 6262 6359 7351 23 -566 231 A N
ATOM 1241 CA LYS A 132 9.844 8.873 30.320 1.00 62.05 A C
ANISOU 1241 CA LYS A 132 7407 7434 8737 -137 -890 372 A C
ATOM 1242 C LYS A 132 9.021 10.141 30.483 1.00 61.57 A C
ANISOU 1242 C LYS A 132 7639 7256 8499 -155 -1125 195 A C
ATOM 1243 O LYS A 132 9.321 10.963 31.351 1.00 56.31 A O
ANISOU 1243 O LYS A 132 7138 6415 7841 -212 -1545 186 A O
ATOM 1244 CB LYS A 132 10.971 9.091 29.300 1.00 72.62 A C
ANISOU 1244 CB LYS A 132 8420 8789 10383 -225 -774 712 A C
ATOM 1245 CG LYS A 132 10.676 8.806 27.835 1.00 86.29 A C
ANISOU 1245 CG LYS A 132 10121 10630 12034 -79 -362 737 A C
ATOM 1246 CD LYS A 132 10.266 10.076 27.092 1.00 94.10 A C
ANISOU 1246 CD LYS A 132 11188 11553 13013 -160 -422 722 A C
ATOM 1247 CE LYS A 132 10.585 9.989 25.607 1.00 99.68 A C
ANISOU 1247 CE LYS A 132 11764 12360 13750 -5 -50 930 A C
ATOM 1248 NZ LYS A 132 10.026 11.128 24.826 1.00 99.87 A N
ANISOU 1248 NZ LYS A 132 11890 12333 13724 -62 -71 879 A N
ATOM 1249 N ILE A 133 7.957 10.302 29.693 1.00 50.50 A N
ANISOU 1249 N ILE A 133 6356 5917 6914 -79 -903 50 A N
ATOM 1250 CA ILE A 133 7.097 11.470 29.854 1.00 51.58 A C
ANISOU 1250 CA ILE A 133 6785 5967 6848 -46 -1085 -110 A C
ATOM 1251 C ILE A 133 6.417 11.431 31.219 1.00 50.02 A C
ANISOU 1251 C ILE A 133 6872 5768 6365 161 -1240 -251 A C
ATOM 1252 O ILE A 133 6.413 12.420 31.963 1.00 50.51 A O
ANISOU 1252 O ILE A 133 7242 5668 6283 232 -1594 -327 A O
ATOM 1253 CB ILE A 133 6.071 11.545 28.708 1.00 56.87 A C
ANISOU 1253 CB ILE A 133 7490 6718 7398 -3 -799 -199 A C
ATOM 1254 CG1 ILE A 133 6.788 11.697 27.363 1.00 54.46 A C
ANISOU 1254 CG1 ILE A 133 6974 6410 7307 -114 -640 -43 A C
ATOM 1255 CG2 ILE A 133 5.121 12.708 28.921 1.00 51.33 A C
ANISOU 1255 CG2 ILE A 133 7085 5953 6465 69 -949 -345 A C
ATOM 1256 CD1 ILE A 133 5.874 11.561 26.166 1.00 63.91 A C
ANISOU 1256 CD1 ILE A 133 8248 7659 8374 -40 -373 -139 A C
ATOM 1257 N ILE A 134 5.832 10.286 31.568 1.00 49.46 A N
ANISOU 1257 N ILE A 134 6734 5862 6196 304 -997 -256 A N
ATOM 1258 CA ILE A 134 5.159 10.162 32.859 1.00 53.37 A C
ANISOU 1258 CA ILE A 134 7452 6414 6410 580 -1059 -298 A C
ATOM 1259 C ILE A 134 6.131 10.467 33.990 1.00 54.35 A C
ANISOU 1259 C ILE A 134 7749 6380 6522 614 -1439 -310 A C
ATOM 1260 O ILE A 134 5.835 11.248 34.905 1.00 52.98 A O
ANISOU 1260 O ILE A 134 7982 6098 6051 860 -1704 -404 A O
ATOM 1261 CB ILE A 134 4.557 8.753 33.014 1.00 50.91 A C
ANISOU 1261 CB ILE A 134 6934 6298 6113 672 -764 -197 A C
ATOM 1262 CG1 ILE A 134 3.473 8.513 31.959 1.00 55.70 A C
ANISOU 1262 CG1 ILE A 134 7437 6985 6741 635 -523 -161 A C
ATOM 1263 CG2 ILE A 134 4.020 8.557 34.448 1.00 55.39 A C
ANISOU 1263 CG2 ILE A 134 7670 6965 6411 1008 -789 -143 A C
ATOM 1264 CD1 ILE A 134 2.999 7.073 31.898 1.00 51.20 A C
ANISOU 1264 CD1 ILE A 134 6647 6512 6295 634 -356 -17 A C
ATOM 1265 N SER A 135 7.314 9.860 33.937 1.00 51.70 A N
ANISOU 1265 N SER A 135 7146 6004 6492 403 -1499 -198 A N
ATOM 1266 CA SER A 135 8.256 9.981 35.043 1.00 58.04 A C
ANISOU 1266 CA SER A 135 8078 6640 7336 404 -1899 -169 A C
ATOM 1267 C SER A 135 8.685 11.423 35.275 1.00 58.18 A C
ANISOU 1267 C SER A 135 8418 6339 7348 334 -2444 -210 A C
ATOM 1268 O SER A 135 9.069 11.772 36.396 1.00 63.85 A O
ANISOU 1268 O SER A 135 9479 6840 7940 452 -2902 -261 A O
ATOM 1269 CB SER A 135 9.474 9.093 34.778 1.00 58.88 A C
ANISOU 1269 CB SER A 135 7764 6777 7829 169 -1835 33 A C
ATOM 1270 OG SER A 135 10.331 9.680 33.813 1.00 64.72 A O
ANISOU 1270 OG SER A 135 8261 7420 8910 -104 -1922 219 A O
ATOM 1271 N GLN A 136 8.603 12.270 34.250 1.00 58.97 A N
ANISOU 1271 N GLN A 136 8462 6374 7569 161 -2452 -189 A N
ATOM 1272 CA GLN A 136 8.990 13.671 34.357 1.00 65.88 A C
ANISOU 1272 CA GLN A 136 9630 6908 8492 51 -3021 -195 A C
ATOM 1273 C GLN A 136 7.876 14.549 34.907 1.00 68.07 A C
ANISOU 1273 C GLN A 136 10514 7089 8260 409 -3177 -459 A C
ATOM 1274 O GLN A 136 8.091 15.754 35.085 1.00 72.59 A O
ANISOU 1274 O GLN A 136 11462 7322 8796 378 -3723 -513 A O
ATOM 1275 CB GLN A 136 9.420 14.193 32.983 1.00 75.82 A C
ANISOU 1275 CB GLN A 136 10525 8158 10124 -274 -2937 4 A C
ATOM 1276 CG GLN A 136 10.759 13.652 32.508 1.00 82.20 A C
ANISOU 1276 CG GLN A 136 10780 8999 11451 -567 -2900 381 A C
ATOM 1277 CD GLN A 136 11.116 14.127 31.112 1.00103.39 A C
ANISOU 1277 CD GLN A 136 13094 11736 14452 -774 -2712 647 A C
ATOM 1278 NE2 GLN A 136 12.390 14.015 30.757 1.00133.09 A N
ANISOU 1278 NE2 GLN A 136 16385 15482 18701 -999 -2783 1102 A N
ATOM 1279 OE1 GLN A 136 10.254 14.581 30.357 1.00 93.15 A O
ANISOU 1279 OE1 GLN A 136 11915 10511 12966 -703 -2485 491 A O
ATOM 1280 N GLY A 137 6.699 13.984 35.165 1.00 66.85 A N
ANISOU 1280 N GLY A 137 10458 7213 7730 763 -2729 -573 A N
ATOM 1281 CA GLY A 137 5.594 14.721 35.739 1.00 63.49 A C
ANISOU 1281 CA GLY A 137 10578 6766 6779 1215 -2775 -738 A C
ATOM 1282 C GLY A 137 4.564 15.224 34.757 1.00 61.84 A C
ANISOU 1282 C GLY A 137 10320 6699 6476 1237 -2450 -770 A C
ATOM 1283 O GLY A 137 3.692 16.006 35.152 1.00 70.22 A O
ANISOU 1283 O GLY A 137 11846 7728 7107 1625 -2505 -875 A O
ATOM 1284 N THR A 138 4.631 14.804 33.496 1.00 56.64 A N
ANISOU 1284 N THR A 138 9159 6191 6172 885 -2120 -676 A N
ATOM 1285 CA THR A 138 3.692 15.222 32.467 1.00 61.90 A C
ANISOU 1285 CA THR A 138 9759 6973 6786 868 -1833 -700 A C
ATOM 1286 C THR A 138 2.754 14.065 32.162 1.00 57.42 A C
ANISOU 1286 C THR A 138 8887 6727 6203 958 -1314 -600 A C
ATOM 1287 O THR A 138 3.184 12.912 32.094 1.00 57.35 A O
ANISOU 1287 O THR A 138 8556 6817 6416 823 -1154 -507 A O
ATOM 1288 CB THR A 138 4.435 15.649 31.199 1.00 62.62 A C
ANISOU 1288 CB THR A 138 9568 6957 7266 450 -1888 -641 A C
ATOM 1289 CG2 THR A 138 3.466 15.910 30.056 1.00 62.63 A C
ANISOU 1289 CG2 THR A 138 9484 7093 7220 432 -1557 -671 A C
ATOM 1290 OG1 THR A 138 5.182 16.842 31.465 1.00 70.80 A O
ANISOU 1290 OG1 THR A 138 10870 7659 8372 338 -2446 -659 A O
ATOM 1291 N ASN A 139 1.468 14.360 32.005 1.00 54.72 A N
ANISOU 1291 N ASN A 139 8648 6524 5618 1190 -1093 -581 A N
ATOM 1292 CA ASN A 139 0.524 13.329 31.604 1.00 51.81 A C
ANISOU 1292 CA ASN A 139 7954 6403 5328 1208 -701 -407 A C
ATOM 1293 C ASN A 139 0.489 13.342 30.084 1.00 45.98 A C
ANISOU 1293 C ASN A 139 6993 5628 4849 872 -593 -439 A C
ATOM 1294 O ASN A 139 0.031 14.333 29.497 1.00 46.22 A O
ANISOU 1294 O ASN A 139 7167 5607 4787 869 -614 -510 A O
ATOM 1295 CB ASN A 139 -0.856 13.575 32.187 1.00 59.41 A C
ANISOU 1295 CB ASN A 139 9061 7552 5958 1636 -512 -248 A C
ATOM 1296 CG ASN A 139 -1.852 12.511 31.767 1.00 55.41 A C
ANISOU 1296 CG ASN A 139 8152 7262 5639 1593 -199 39 A C
ATOM 1297 ND2 ASN A 139 -3.005 12.486 32.422 1.00 70.82 A N
ANISOU 1297 ND2 ASN A 139 10095 9433 7379 1988 7 336 A N
ATOM 1298 OD1 ASN A 139 -1.579 11.709 30.872 1.00 55.42 A O
ANISOU 1298 OD1 ASN A 139 7869 7214 5974 1238 -172 36 A O
ATOM 1299 N PRO A 140 0.993 12.309 29.405 1.00 44.97 A N
ANISOU 1299 N PRO A 140 6576 5505 5006 632 -490 -398 A N
ATOM 1300 CA PRO A 140 1.062 12.371 27.935 1.00 42.88 A C
ANISOU 1300 CA PRO A 140 6204 5175 4912 408 -404 -441 A C
ATOM 1301 C PRO A 140 -0.297 12.518 27.283 1.00 45.44 A C
ANISOU 1301 C PRO A 140 6544 5556 5165 451 -277 -394 A C
ATOM 1302 O PRO A 140 -0.377 12.990 26.144 1.00 45.83 A O
ANISOU 1302 O PRO A 140 6621 5530 5263 326 -250 -468 A O
ATOM 1303 CB PRO A 140 1.736 11.046 27.547 1.00 48.76 A C
ANISOU 1303 CB PRO A 140 6738 5916 5874 293 -316 -385 A C
ATOM 1304 CG PRO A 140 1.612 10.163 28.747 1.00 51.81 A C
ANISOU 1304 CG PRO A 140 7056 6397 6232 419 -320 -287 A C
ATOM 1305 CD PRO A 140 1.558 11.058 29.945 1.00 48.56 A C
ANISOU 1305 CD PRO A 140 6846 6008 5595 612 -456 -315 A C
ATOM 1306 N LEU A 141 -1.373 12.159 27.982 1.00 47.66 A N
ANISOU 1306 N LEU A 141 6786 5976 5346 642 -197 -219 A N
ATOM 1307 CA LEU A 141 -2.702 12.303 27.404 1.00 51.36 A C
ANISOU 1307 CA LEU A 141 7206 6501 5808 670 -104 -74 A C
ATOM 1308 C LEU A 141 -3.087 13.759 27.191 1.00 51.18 A C
ANISOU 1308 C LEU A 141 7409 6467 5569 769 -112 -181 A C
ATOM 1309 O LEU A 141 -3.973 14.033 26.370 1.00 51.48 A O
ANISOU 1309 O LEU A 141 7414 6508 5638 716 -54 -117 A O
ATOM 1310 CB LEU A 141 -3.735 11.618 28.299 1.00 51.08 A C
ANISOU 1310 CB LEU A 141 6992 6654 5763 886 1 279 A C
ATOM 1311 CG LEU A 141 -3.545 10.105 28.431 1.00 52.94 A C
ANISOU 1311 CG LEU A 141 6981 6874 6260 758 -34 435 A C
ATOM 1312 CD1 LEU A 141 -4.385 9.560 29.574 1.00 61.58 A C
ANISOU 1312 CD1 LEU A 141 7868 8189 7343 1019 79 850 A C
ATOM 1313 CD2 LEU A 141 -3.901 9.403 27.139 1.00 54.21 A C
ANISOU 1313 CD2 LEU A 141 7049 6857 6690 479 -149 463 A C
ATOM 1314 N ASN A 142 -2.442 14.693 27.894 1.00 48.58 A N
ANISOU 1314 N ASN A 142 7338 6086 5033 904 -239 -338 A N
ATOM 1315 CA ASN A 142 -2.771 16.108 27.807 1.00 54.51 A C
ANISOU 1315 CA ASN A 142 8381 6781 5551 1033 -317 -450 A C
ATOM 1316 C ASN A 142 -1.866 16.886 26.859 1.00 50.78 A C
ANISOU 1316 C ASN A 142 7971 6107 5218 741 -483 -657 A C
ATOM 1317 O ASN A 142 -1.995 18.112 26.771 1.00 54.21 A O
ANISOU 1317 O ASN A 142 8662 6444 5492 805 -617 -762 A O
ATOM 1318 CB ASN A 142 -2.699 16.753 29.194 1.00 60.59 A C
ANISOU 1318 CB ASN A 142 9514 7543 5963 1425 -457 -480 A C
ATOM 1319 CG ASN A 142 -3.756 16.227 30.136 1.00 66.95 A C
ANISOU 1319 CG ASN A 142 10282 8604 6553 1851 -217 -188 A C
ATOM 1320 ND2 ASN A 142 -3.429 16.183 31.421 1.00 72.78 A N
ANISOU 1320 ND2 ASN A 142 11268 9356 7029 2198 -303 -181 A N
ATOM 1321 OD1 ASN A 142 -4.854 15.856 29.715 1.00 67.97 A O
ANISOU 1321 OD1 ASN A 142 10148 8910 6765 1880 28 78 A O
ATOM 1322 N ILE A 143 -0.935 16.218 26.183 1.00 48.31 A N
ANISOU 1322 N ILE A 143 7436 5732 5189 468 -476 -674 A N
ATOM 1323 CA ILE A 143 -0.079 16.893 25.212 1.00 44.63 A C
ANISOU 1323 CA ILE A 143 6946 5126 4887 239 -563 -747 A C
ATOM 1324 C ILE A 143 -0.919 17.269 24.001 1.00 48.65 A C
ANISOU 1324 C ILE A 143 7457 5649 5377 188 -413 -773 A C
ATOM 1325 O ILE A 143 -1.641 16.433 23.449 1.00 49.31 A O
ANISOU 1325 O ILE A 143 7436 5801 5500 185 -247 -718 A O
ATOM 1326 CB ILE A 143 1.104 15.992 24.827 1.00 47.91 A C
ANISOU 1326 CB ILE A 143 7112 5523 5567 77 -513 -672 A C
ATOM 1327 CG1 ILE A 143 2.061 15.805 26.016 1.00 50.34 A C
ANISOU 1327 CG1 ILE A 143 7414 5785 5930 87 -722 -632 A C
ATOM 1328 CG2 ILE A 143 1.870 16.555 23.631 1.00 52.14 A C
ANISOU 1328 CG2 ILE A 143 7545 5982 6282 -85 -487 -624 A C
ATOM 1329 CD1 ILE A 143 2.999 14.615 25.835 1.00 53.52 A C
ANISOU 1329 CD1 ILE A 143 7548 6231 6555 5 -602 -517 A C
ATOM 1330 N ARG A 144 -0.838 18.537 23.586 1.00 46.07 A N
ANISOU 1330 N ARG A 144 7272 5224 5009 137 -528 -845 A N
ATOM 1331 CA ARG A 144 -1.597 19.020 22.440 1.00 48.75 A C
ANISOU 1331 CA ARG A 144 7635 5569 5320 93 -401 -879 A C
ATOM 1332 C ARG A 144 -0.895 18.622 21.139 1.00 47.36 A C
ANISOU 1332 C ARG A 144 7289 5359 5348 -62 -270 -842 A C
ATOM 1333 O ARG A 144 0.338 18.569 21.084 1.00 46.43 A O
ANISOU 1333 O ARG A 144 7037 5198 5405 -146 -313 -756 A O
ATOM 1334 CB ARG A 144 -1.739 20.540 22.519 1.00 54.72 A C
ANISOU 1334 CB ARG A 144 8629 6221 5942 120 -587 -962 A C
ATOM 1335 CG ARG A 144 -2.339 21.028 23.851 1.00 71.56 A C
ANISOU 1335 CG ARG A 144 11060 8361 7770 407 -731 -1002 A C
ATOM 1336 CD ARG A 144 -3.740 21.649 23.812 1.00 96.85 A C
ANISOU 1336 CD ARG A 144 14444 11657 10697 643 -608 -999 A C
ATOM 1337 NE ARG A 144 -3.644 23.084 23.564 1.00115.75 A N
ANISOU 1337 NE ARG A 144 17121 13877 12981 639 -829 -1125 A N
ATOM 1338 CZ ARG A 144 -4.207 23.724 22.547 1.00132.51 A C
ANISOU 1338 CZ ARG A 144 19236 16000 15111 553 -734 -1153 A C
ATOM 1339 NH1 ARG A 144 -5.192 23.190 21.857 1.00125.08 A N
ANISOU 1339 NH1 ARG A 144 18104 15225 14196 551 -442 -1060 A N
ATOM 1340 NH2 ARG A 144 -3.799 24.954 22.249 1.00139.78 A N
ANISOU 1340 NH2 ARG A 144 20362 16722 16028 465 -991 -1253 A N
ATOM 1341 N PRO A 145 -1.647 18.318 20.077 1.00 44.35 A N
ANISOU 1341 N PRO A 145 6924 4988 4940 -57 -118 -863 A N
ATOM 1342 CA PRO A 145 -0.995 17.967 18.806 1.00 41.98 A C
ANISOU 1342 CA PRO A 145 6572 4643 4735 -78 19 -831 A C
ATOM 1343 C PRO A 145 -0.249 19.153 18.220 1.00 43.80 A C
ANISOU 1343 C PRO A 145 6761 4839 5043 -147 15 -771 A C
ATOM 1344 O PRO A 145 -0.611 20.312 18.427 1.00 48.44 A O
ANISOU 1344 O PRO A 145 7435 5388 5581 -208 -118 -822 A O
ATOM 1345 CB PRO A 145 -2.161 17.538 17.906 1.00 50.05 A C
ANISOU 1345 CB PRO A 145 7730 5620 5665 -36 70 -892 A C
ATOM 1346 CG PRO A 145 -3.340 18.201 18.482 1.00 49.78 A C
ANISOU 1346 CG PRO A 145 7745 5633 5537 -48 -7 -907 A C
ATOM 1347 CD PRO A 145 -3.118 18.227 19.965 1.00 47.18 A C
ANISOU 1347 CD PRO A 145 7359 5386 5182 4 -84 -867 A C
ATOM 1348 N LYS A 146 0.839 18.852 17.519 1.00 43.39 A N
ANISOU 1348 N LYS A 146 5882 4156 6449 564 642 -488 A N
ATOM 1349 CA ALYS A 146 1.684 19.877 16.929 0.40 47.92 A C
ANISOU 1349 CA ALYS A 146 6532 4621 7054 495 569 -501 A C
ATOM 1350 CA BLYS A 146 1.667 19.884 16.919 0.61 47.92 A C
ANISOU 1350 CA BLYS A 146 6531 4620 7056 497 569 -500 A C
ATOM 1351 C LYS A 146 2.152 19.408 15.561 1.00 44.90 A C
ANISOU 1351 C LYS A 146 6071 4305 6686 414 455 -386 A C
ATOM 1352 O LYS A 146 2.324 18.212 15.330 1.00 46.44 A O
ANISOU 1352 O LYS A 146 6192 4640 6813 372 413 -348 A O
ATOM 1353 CB ALYS A 146 2.936 20.192 17.771 0.40 49.67 A C
ANISOU 1353 CB ALYS A 146 6886 4820 7165 404 543 -639 A C
ATOM 1354 CB BLYS A 146 2.871 20.218 17.805 0.61 49.71 A C
ANISOU 1354 CB BLYS A 146 6892 4821 7173 412 549 -640 A C
ATOM 1355 CG ALYS A 146 2.770 20.095 19.273 0.40 51.07 A C
ANISOU 1355 CG ALYS A 146 7156 5011 7239 461 630 -768 A C
ATOM 1356 CG BLYS A 146 3.747 19.009 18.069 0.61 48.47 A C
ANISOU 1356 CG BLYS A 146 6713 4827 6877 323 488 -658 A C
ATOM 1357 CD ALYS A 146 2.314 21.404 19.889 0.40 53.83 A C
ANISOU 1357 CD ALYS A 146 7619 5185 7647 543 715 -861 A C
ATOM 1358 CD BLYS A 146 4.775 19.265 19.160 0.61 58.39 A C
ANISOU 1358 CD BLYS A 146 8093 6075 8016 264 463 -808 A C
ATOM 1359 CE ALYS A 146 1.803 21.170 21.303 0.40 51.09 A C
ANISOU 1359 CE ALYS A 146 7353 4867 7192 640 834 -964 A C
ATOM 1360 CE BLYS A 146 5.641 18.030 19.383 0.61 60.16 A C
ANISOU 1360 CE BLYS A 146 8285 6466 8108 192 395 -809 A C
ATOM 1361 NZ ALYS A 146 2.566 20.080 21.991 0.40 43.13 A N
ANISOU 1361 NZ ALYS A 146 6369 4017 6002 577 789 -1009 A N
ATOM 1362 NZ BLYS A 146 7.076 18.387 19.596 0.61 71.25 A N
ANISOU 1362 NZ BLYS A 146 9748 7863 9461 73 292 -900 A N
ATOM 1363 N ALA A 147 2.380 20.362 14.666 1.00 44.39 A N
ANISOU 1363 N ALA A 147 6035 4131 6703 397 414 -332 A N
ATOM 1364 CA ALA A 147 3.010 20.051 13.387 1.00 42.43 A C
ANISOU 1364 CA ALA A 147 5746 3934 6442 317 318 -230 A C
ATOM 1365 C ALA A 147 4.516 20.206 13.551 1.00 44.93 A C
ANISOU 1365 C ALA A 147 6136 4246 6690 182 280 -296 A C
ATOM 1366 O ALA A 147 4.983 21.205 14.106 1.00 47.80 A O
ANISOU 1366 O ALA A 147 6595 4484 7085 152 305 -381 A O
ATOM 1367 CB ALA A 147 2.491 20.966 12.279 1.00 48.50 A C
ANISOU 1367 CB ALA A 147 6511 4591 7324 374 298 -116 A C
ATOM 1368 N VAL A 148 5.273 19.219 13.080 1.00 40.47 A N
ANISOU 1368 N VAL A 148 5522 3814 6042 100 218 -262 A N
ATOM 1369 CA VAL A 148 6.717 19.215 13.277 1.00 43.01 A C
ANISOU 1369 CA VAL A 148 5881 4156 6307 -25 181 -322 A C
ATOM 1370 C VAL A 148 7.375 18.485 12.119 1.00 44.49 A C
ANISOU 1370 C VAL A 148 6008 4442 6455 -89 124 -223 A C
ATOM 1371 O VAL A 148 6.800 17.571 11.522 1.00 43.15 A O
ANISOU 1371 O VAL A 148 5772 4370 6252 -45 104 -148 A O
ATOM 1372 CB VAL A 148 7.081 18.561 14.634 1.00 49.20 A C
ANISOU 1372 CB VAL A 148 6683 5023 6986 -40 186 -449 A C
ATOM 1373 CG1 VAL A 148 6.419 17.200 14.764 1.00 48.96 A C
ANISOU 1373 CG1 VAL A 148 6578 5137 6888 17 197 -412 A C
ATOM 1374 CG2 VAL A 148 8.578 18.431 14.787 1.00 60.58 A C
ANISOU 1374 CG2 VAL A 148 8134 6508 8375 -165 125 -504 A C
ATOM 1375 N GLU A 149 8.608 18.880 11.811 1.00 44.11 A N
ANISOU 1375 N GLU A 149 5982 4366 6413 -196 103 -227 A N
ATOM 1376 CA GLU A 149 9.359 18.189 10.776 1.00 44.75 A C
ANISOU 1376 CA GLU A 149 6012 4542 6448 -255 70 -140 A C
ATOM 1377 C GLU A 149 10.029 16.948 11.358 1.00 42.15 A C
ANISOU 1377 C GLU A 149 5633 4366 6017 -294 39 -200 A C
ATOM 1378 O GLU A 149 10.694 17.021 12.396 1.00 43.31 A O
ANISOU 1378 O GLU A 149 5794 4519 6141 -342 28 -308 A O
ATOM 1379 CB GLU A 149 10.409 19.120 10.160 1.00 53.28 A C
ANISOU 1379 CB GLU A 149 7123 5528 7595 -353 81 -103 A C
ATOM 1380 CG GLU A 149 10.736 18.763 8.714 1.00 66.70 A C
ANISOU 1380 CG GLU A 149 8797 7280 9266 -367 80 36 A C
ATOM 1381 CD GLU A 149 10.760 19.964 7.784 1.00 84.48 A C
ANISOU 1381 CD GLU A 149 11109 9385 11605 -375 119 140 A C
ATOM 1382 OE1 GLU A 149 10.458 19.795 6.578 1.00 83.04 A O
ANISOU 1382 OE1 GLU A 149 10937 9228 11385 -328 118 269 A O
ATOM 1383 OE2 GLU A 149 11.084 21.072 8.262 1.00 82.41 A O
ANISOU 1383 OE2 GLU A 149 10893 8975 11443 -426 148 92 A O
ATOM 1384 N LYS A 150 9.864 15.815 10.676 1.00 41.68 A N
ANISOU 1384 N LYS A 150 5520 4424 5891 -269 20 -131 A N
ATOM 1385 CA LYS A 150 10.498 14.561 11.054 1.00 40.69 A C
ANISOU 1385 CA LYS A 150 5349 4437 5675 -295 -4 -165 A C
ATOM 1386 C LYS A 150 11.118 13.887 9.837 1.00 41.57 A C
ANISOU 1386 C LYS A 150 5424 4625 5747 -326 -18 -78 A C
ATOM 1387 O LYS A 150 10.709 14.120 8.695 1.00 42.08 A O
ANISOU 1387 O LYS A 150 5502 4660 5826 -301 -16 15 A O
ATOM 1388 CB LYS A 150 9.497 13.570 11.671 1.00 41.36 A C
ANISOU 1388 CB LYS A 150 5411 4593 5712 -216 3 -187 A C
ATOM 1389 CG LYS A 150 8.747 14.096 12.865 1.00 45.81 A C
ANISOU 1389 CG LYS A 150 6014 5094 6298 -163 41 -265 A C
ATOM 1390 CD LYS A 150 9.583 14.057 14.117 1.00 45.93 A C
ANISOU 1390 CD LYS A 150 6065 5137 6251 -201 32 -375 A C
ATOM 1391 CE LYS A 150 8.701 14.041 15.336 1.00 51.74 A C
ANISOU 1391 CE LYS A 150 6843 5858 6957 -122 83 -444 A C
ATOM 1392 NZ LYS A 150 9.405 14.593 16.503 1.00 53.04 A N
ANISOU 1392 NZ LYS A 150 7082 5998 7074 -151 69 -566 A N
ATOM 1393 N ILE A 151 12.088 13.016 10.108 1.00 38.45 A N
ANISOU 1393 N ILE A 151 4989 4330 5291 -368 -33 -108 A N
ATOM 1394 CA ILE A 151 12.534 12.002 9.160 1.00 39.21 A C
ANISOU 1394 CA ILE A 151 5050 4520 5326 -370 -37 -44 A C
ATOM 1395 C ILE A 151 11.751 10.730 9.451 1.00 37.92 A C
ANISOU 1395 C ILE A 151 4871 4437 5101 -305 -53 -57 A C
ATOM 1396 O ILE A 151 11.812 10.210 10.568 1.00 37.82 A O
ANISOU 1396 O ILE A 151 4847 4465 5059 -294 -56 -124 A O
ATOM 1397 CB ILE A 151 14.044 11.732 9.289 1.00 40.13 A C
ANISOU 1397 CB ILE A 151 5121 4698 5430 -442 -36 -65 A C
ATOM 1398 CG1 ILE A 151 14.865 13.014 9.180 1.00 52.15 A C
ANISOU 1398 CG1 ILE A 151 6643 6131 7041 -526 -17 -65 A C
ATOM 1399 CG2 ILE A 151 14.443 10.699 8.247 1.00 37.72 A C
ANISOU 1399 CG2 ILE A 151 4792 4481 5060 -427 -21 2 A C
ATOM 1400 CD1 ILE A 151 14.754 13.707 7.874 1.00 53.65 A C
ANISOU 1400 CD1 ILE A 151 6867 6250 7266 -534 28 42 A C
ATOM 1401 N VAL A 152 11.021 10.214 8.457 1.00 36.22 A N
ANISOU 1401 N VAL A 152 4658 4240 4866 -262 -65 7 A N
ATOM 1402 CA VAL A 152 10.235 8.994 8.618 1.00 35.97 A C
ANISOU 1402 CA VAL A 152 4602 4266 4798 -214 -82 -3 A C
ATOM 1403 C VAL A 152 11.016 7.823 8.034 1.00 38.25 A C
ANISOU 1403 C VAL A 152 4879 4641 5013 -226 -87 13 A C
ATOM 1404 O VAL A 152 11.569 7.922 6.933 1.00 38.78 A O
ANISOU 1404 O VAL A 152 4964 4718 5050 -242 -85 63 A O
ATOM 1405 CB VAL A 152 8.850 9.125 7.965 1.00 36.68 A C
ANISOU 1405 CB VAL A 152 4690 4317 4928 -160 -110 41 A C
ATOM 1406 CG1 VAL A 152 8.030 7.847 8.202 1.00 39.05 A C
ANISOU 1406 CG1 VAL A 152 4951 4668 5220 -127 -125 24 A C
ATOM 1407 CG2 VAL A 152 8.150 10.324 8.516 1.00 38.93 A C
ANISOU 1407 CG2 VAL A 152 4985 4511 5294 -135 -92 31 A C
ATOM 1408 N PHE A 153 11.094 6.737 8.807 1.00 35.29 A N
ANISOU 1408 N PHE A 153 4481 4322 4604 -212 -82 -28 A N
ATOM 1409 CA PHE A 153 11.814 5.505 8.499 1.00 36.18 A C
ANISOU 1409 CA PHE A 153 4584 4508 4654 -210 -80 -24 A C
ATOM 1410 C PHE A 153 10.791 4.385 8.326 1.00 36.04 A C
ANISOU 1410 C PHE A 153 4565 4499 4631 -172 -95 -23 A C
ATOM 1411 O PHE A 153 9.930 4.199 9.188 1.00 35.84 A O
ANISOU 1411 O PHE A 153 4523 4453 4641 -151 -86 -44 A O
ATOM 1412 CB PHE A 153 12.796 5.198 9.652 1.00 35.94 A C
ANISOU 1412 CB PHE A 153 4531 4524 4601 -221 -66 -69 A C
ATOM 1413 CG PHE A 153 13.461 3.837 9.598 1.00 37.57 A C
ANISOU 1413 CG PHE A 153 4723 4801 4752 -199 -58 -67 A C
ATOM 1414 CD1 PHE A 153 12.764 2.668 9.857 1.00 37.12 A C
ANISOU 1414 CD1 PHE A 153 4675 4751 4677 -158 -53 -70 A C
ATOM 1415 CD2 PHE A 153 14.829 3.748 9.364 1.00 40.56 A C
ANISOU 1415 CD2 PHE A 153 5071 5230 5112 -219 -48 -60 A C
ATOM 1416 CE1 PHE A 153 13.396 1.439 9.812 1.00 38.42 A C
ANISOU 1416 CE1 PHE A 153 4836 4962 4799 -132 -40 -66 A C
ATOM 1417 CE2 PHE A 153 15.466 2.528 9.339 1.00 37.54 A C
ANISOU 1417 CE2 PHE A 153 4672 4904 4685 -185 -35 -55 A C
ATOM 1418 CZ PHE A 153 14.754 1.372 9.567 1.00 40.94 A C
ANISOU 1418 CZ PHE A 153 5129 5333 5091 -138 -32 -59 A C
ATOM 1419 N PHE A 154 10.877 3.657 7.208 1.00 33.94 A N
ANISOU 1419 N PHE A 154 4318 4256 4322 -165 -114 0 A N
ATOM 1420 CA PHE A 154 10.089 2.451 6.965 1.00 34.55 A C
ANISOU 1420 CA PHE A 154 4394 4336 4397 -144 -138 -11 A C
ATOM 1421 C PHE A 154 11.035 1.316 6.595 1.00 41.62 A C
ANISOU 1421 C PHE A 154 5312 5277 5225 -136 -119 -20 A C
ATOM 1422 O PHE A 154 11.903 1.498 5.731 1.00 39.64 A O
ANISOU 1422 O PHE A 154 5089 5052 4920 -139 -108 1 A O
ATOM 1423 CB PHE A 154 9.120 2.602 5.802 1.00 37.13 A C
ANISOU 1423 CB PHE A 154 4738 4636 4734 -135 -202 10 A C
ATOM 1424 CG PHE A 154 7.718 2.889 6.205 1.00 38.75 A C
ANISOU 1424 CG PHE A 154 4895 4797 5031 -124 -232 8 A C
ATOM 1425 CD1 PHE A 154 7.401 4.094 6.790 1.00 44.78 A C
ANISOU 1425 CD1 PHE A 154 5640 5524 5852 -117 -212 20 A C
ATOM 1426 CD2 PHE A 154 6.723 1.957 6.002 1.00 47.16 A C
ANISOU 1426 CD2 PHE A 154 5929 5849 6139 -121 -275 -9 A C
ATOM 1427 CE1 PHE A 154 6.103 4.371 7.165 1.00 48.33 A C
ANISOU 1427 CE1 PHE A 154 6035 5932 6395 -94 -224 22 A C
ATOM 1428 CE2 PHE A 154 5.420 2.228 6.378 1.00 47.19 A C
ANISOU 1428 CE2 PHE A 154 5865 5815 6251 -110 -294 -5 A C
ATOM 1429 CZ PHE A 154 5.118 3.433 6.964 1.00 44.99 A C
ANISOU 1429 CZ PHE A 154 5564 5508 6024 -91 -262 13 A C
ATOM 1430 N SER A 155 10.853 0.146 7.199 1.00 35.08 A N
ANISOU 1430 N SER A 155 4474 4450 4403 -120 -104 -43 A N
ATOM 1431 CA ASER A 155 11.579 -1.055 6.791 0.70 34.92 A C
ANISOU 1431 CA ASER A 155 4482 4455 4330 -100 -86 -53 A C
ATOM 1432 CA BSER A 155 11.575 -1.052 6.786 0.30 35.16 A C
ANISOU 1432 CA BSER A 155 4512 4485 4360 -100 -86 -53 A C
ATOM 1433 C SER A 155 10.603 -2.221 6.768 1.00 41.88 A C
ANISOU 1433 C SER A 155 5372 5292 5247 -95 -104 -75 A C
ATOM 1434 O SER A 155 9.747 -2.335 7.647 1.00 41.33 A O
ANISOU 1434 O SER A 155 5267 5191 5245 -101 -94 -76 A O
ATOM 1435 CB ASER A 155 12.777 -1.358 7.715 0.70 35.92 A C
ANISOU 1435 CB ASER A 155 4587 4626 4433 -80 -37 -52 A C
ATOM 1436 CB BSER A 155 12.750 -1.361 7.716 0.30 35.88 A C
ANISOU 1436 CB BSER A 155 4584 4622 4429 -81 -37 -52 A C
ATOM 1437 OG ASER A 155 12.425 -1.678 9.053 0.70 36.57 A O
ANISOU 1437 OG ASER A 155 4651 4700 4543 -67 -19 -58 A O
ATOM 1438 OG BSER A 155 13.566 -2.384 7.169 0.30 40.40 A O
ANISOU 1438 OG BSER A 155 5180 5216 4954 -49 -12 -54 A O
ATOM 1439 N ASP A 156 10.740 -3.085 5.762 1.00 35.66 A N
ANISOU 1439 N ASP A 156 4633 4497 4417 -85 -123 -96 A N
ATOM 1440 CA ASP A 156 9.772 -4.152 5.523 1.00 35.85 A C
ANISOU 1440 CA ASP A 156 4669 4464 4487 -96 -158 -129 A C
ATOM 1441 C ASP A 156 10.504 -5.392 5.040 1.00 37.38 A C
ANISOU 1441 C ASP A 156 4926 4649 4626 -68 -132 -158 A C
ATOM 1442 O ASP A 156 11.379 -5.302 4.177 1.00 38.07 A O
ANISOU 1442 O ASP A 156 5065 4774 4627 -42 -121 -161 A O
ATOM 1443 CB ASP A 156 8.740 -3.630 4.501 1.00 37.50 A C
ANISOU 1443 CB ASP A 156 4883 4655 4711 -120 -252 -142 A C
ATOM 1444 CG ASP A 156 7.631 -4.607 4.174 1.00 39.25 A C
ANISOU 1444 CG ASP A 156 5098 4816 5001 -147 -316 -187 A C
ATOM 1445 OD1 ASP A 156 7.877 -5.764 3.805 1.00 38.09 A O
ANISOU 1445 OD1 ASP A 156 5004 4639 4831 -145 -314 -229 A O
ATOM 1446 OD2 ASP A 156 6.467 -4.154 4.215 1.00 43.09 A O
ANISOU 1446 OD2 ASP A 156 5519 5278 5573 -173 -374 -183 A O
ATOM 1447 N ILE A 157 10.156 -6.552 5.617 1.00 36.39 A N
ANISOU 1447 N ILE A 157 4801 4467 4559 -67 -107 -174 A N
ATOM 1448 CA ILE A 157 10.783 -7.814 5.233 1.00 37.45 A C
ANISOU 1448 CA ILE A 157 5001 4571 4658 -33 -76 -204 A C
ATOM 1449 C ILE A 157 10.433 -8.189 3.798 1.00 38.78 A C
ANISOU 1449 C ILE A 157 5243 4709 4782 -46 -146 -267 A C
ATOM 1450 O ILE A 157 9.273 -8.121 3.365 1.00 37.18 A O
ANISOU 1450 O ILE A 157 5029 4467 4630 -94 -233 -299 A O
ATOM 1451 CB ILE A 157 10.362 -8.941 6.204 1.00 34.92 A C
ANISOU 1451 CB ILE A 157 4670 4175 4424 -34 -31 -198 A C
ATOM 1452 CG1 ILE A 157 10.830 -8.594 7.622 1.00 38.29 A C
ANISOU 1452 CG1 ILE A 157 5049 4643 4856 -4 37 -135 A C
ATOM 1453 CG2 ILE A 157 10.882 -10.318 5.711 1.00 40.10 A C
ANISOU 1453 CG2 ILE A 157 5407 4770 5058 2 -2 -237 A C
ATOM 1454 CD1 ILE A 157 10.348 -9.550 8.670 1.00 38.32 A C
ANISOU 1454 CD1 ILE A 157 5050 4577 4934 2 95 -107 A C
ATOM 1455 N VAL A 158 11.451 -8.623 3.058 1.00 37.67 A N
ANISOU 1455 N VAL A 158 5180 4588 4546 5 -111 -288 A N
ATOM 1456 CA VAL A 158 11.281 -9.101 1.693 1.00 38.05 A C
ANISOU 1456 CA VAL A 158 5329 4608 4519 11 -165 -358 A C
ATOM 1457 C VAL A 158 10.674 -10.501 1.686 1.00 38.51 A C
ANISOU 1457 C VAL A 158 5430 4557 4644 -8 -188 -428 A C
ATOM 1458 O VAL A 158 11.196 -11.418 2.328 1.00 41.44 A O
ANISOU 1458 O VAL A 158 5810 4883 5052 25 -108 -420 A O
ATOM 1459 CB VAL A 158 12.633 -9.090 0.955 1.00 39.70 A C
ANISOU 1459 CB VAL A 158 5608 4874 4601 83 -90 -353 A C
ATOM 1460 CG1 VAL A 158 12.434 -9.579 -0.456 1.00 43.21 A C
ANISOU 1460 CG1 VAL A 158 6183 5291 4943 99 -141 -432 A C
ATOM 1461 CG2 VAL A 158 13.254 -7.692 1.018 1.00 41.69 A C
ANISOU 1461 CG2 VAL A 158 5805 5221 4815 86 -58 -279 A C
ATOM 1462 N SER A 159 9.548 -10.653 0.974 1.00 38.84 A N
ANISOU 1462 N SER A 159 5496 4550 4713 -64 -305 -493 A N
ATOM 1463 CA ASER A 159 8.931 -11.955 0.723 0.82 42.57 A C
ANISOU 1463 CA ASER A 159 6018 4905 5251 -98 -348 -580 A C
ATOM 1464 CA BSER A 159 8.920 -11.952 0.723 0.18 42.70 A C
ANISOU 1464 CA BSER A 159 6034 4921 5268 -98 -349 -580 A C
ATOM 1465 C SER A 159 8.595 -12.684 2.023 1.00 45.61 A C
ANISOU 1465 C SER A 159 6329 5208 5792 -127 -279 -543 A C
ATOM 1466 O SER A 159 8.742 -13.903 2.128 1.00 48.14 A O
ANISOU 1466 O SER A 159 6707 5429 6156 -120 -236 -582 A O
ATOM 1467 CB ASER A 159 9.833 -12.820 -0.170 0.82 45.92 A C
ANISOU 1467 CB ASER A 159 6588 5302 5557 -32 -311 -649 A C
ATOM 1468 CB BSER A 159 9.796 -12.821 -0.186 0.18 46.18 A C
ANISOU 1468 CB BSER A 159 6621 5334 5591 -34 -315 -651 A C
ATOM 1469 OG ASER A 159 9.060 -13.739 -0.920 0.82 60.64 A O
ANISOU 1469 OG ASER A 159 8530 7064 7444 -77 -410 -765 A O
ATOM 1470 OG BSER A 159 10.823 -13.457 0.551 0.18 52.50 A O
ANISOU 1470 OG BSER A 159 7427 6117 6404 30 -178 -610 A O
ATOM 1471 N PHE A 160 8.116 -11.937 3.017 1.00 42.77 A N
ANISOU 1471 N PHE A 160 5852 4883 5515 -156 -259 -467 A N
ATOM 1472 CA PHE A 160 7.694 -12.563 4.268 1.00 40.31 A C
ANISOU 1472 CA PHE A 160 5477 4498 5340 -180 -184 -421 A C
ATOM 1473 C PHE A 160 6.597 -13.599 4.057 1.00 46.75 A C
ANISOU 1473 C PHE A 160 6288 5180 6295 -260 -236 -485 A C
ATOM 1474 O PHE A 160 6.526 -14.586 4.799 1.00 47.65 A O
ANISOU 1474 O PHE A 160 6405 5195 6505 -268 -153 -463 A O
ATOM 1475 CB PHE A 160 7.190 -11.505 5.239 1.00 41.97 A C
ANISOU 1475 CB PHE A 160 5574 4768 5606 -198 -162 -342 A C
ATOM 1476 CG PHE A 160 6.721 -12.067 6.550 1.00 48.37 A C
ANISOU 1476 CG PHE A 160 6329 5511 6538 -215 -69 -284 A C
ATOM 1477 CD1 PHE A 160 7.632 -12.419 7.528 1.00 54.24 A C
ANISOU 1477 CD1 PHE A 160 7103 6266 7240 -147 42 -220 A C
ATOM 1478 CD2 PHE A 160 5.376 -12.252 6.795 1.00 54.98 A C
ANISOU 1478 CD2 PHE A 160 7082 6276 7533 -293 -91 -287 A C
ATOM 1479 CE1 PHE A 160 7.201 -12.937 8.739 1.00 52.60 A C
ANISOU 1479 CE1 PHE A 160 6864 5998 7124 -151 136 -155 A C
ATOM 1480 CE2 PHE A 160 4.945 -12.779 7.998 1.00 54.68 A C
ANISOU 1480 CE2 PHE A 160 7000 6172 7604 -304 19 -221 A C
ATOM 1481 CZ PHE A 160 5.866 -13.116 8.964 1.00 50.41 A C
ANISOU 1481 CZ PHE A 160 6513 5644 6998 -230 135 -153 A C
ATOM 1482 N SER A 161 5.722 -13.384 3.073 1.00 43.79 A N
ANISOU 1482 N SER A 161 5902 4796 5940 -320 -375 -560 A N
ATOM 1483 CA SER A 161 4.596 -14.293 2.870 1.00 51.09 A C
ANISOU 1483 CA SER A 161 6796 5593 7023 -414 -446 -630 A C
ATOM 1484 C SER A 161 5.081 -15.717 2.671 1.00 54.07 A C
ANISOU 1484 C SER A 161 7290 5847 7408 -405 -401 -693 A C
ATOM 1485 O SER A 161 4.365 -16.681 2.969 1.00 54.61 A O
ANISOU 1485 O SER A 161 7330 5777 7640 -479 -394 -720 A O
ATOM 1486 CB SER A 161 3.778 -13.842 1.663 1.00 59.84 A C
ANISOU 1486 CB SER A 161 7894 6727 8114 -463 -633 -716 A C
ATOM 1487 OG SER A 161 3.035 -12.675 1.965 1.00 64.55 A O
ANISOU 1487 OG SER A 161 8358 7402 8766 -482 -675 -654 A O
ATOM 1488 N THR A 162 6.302 -15.858 2.175 1.00 49.09 A N
ANISOU 1488 N THR A 162 6786 5256 6612 -314 -359 -713 A N
ATOM 1489 CA THR A 162 6.873 -17.174 1.941 1.00 57.85 A C
ANISOU 1489 CA THR A 162 8017 6247 7715 -282 -305 -774 A C
ATOM 1490 C THR A 162 7.161 -17.883 3.259 1.00 59.00 A C
ANISOU 1490 C THR A 162 8135 6315 7965 -258 -153 -679 A C
ATOM 1491 O THR A 162 6.863 -19.075 3.410 1.00 56.37 A O
ANISOU 1491 O THR A 162 7844 5824 7749 -294 -122 -714 A O
ATOM 1492 CB THR A 162 8.140 -17.010 1.105 1.00 64.99 A C
ANISOU 1492 CB THR A 162 9048 7231 8414 -175 -280 -804 A C
ATOM 1493 CG2 THR A 162 8.880 -18.334 0.971 1.00 79.30 A C
ANISOU 1493 CG2 THR A 162 10988 8926 10218 -114 -196 -854 A C
ATOM 1494 OG1 THR A 162 7.773 -16.543 -0.199 1.00 59.22 A O
ANISOU 1494 OG1 THR A 162 8374 6547 7579 -197 -422 -898 A O
ATOM 1495 N PHE A 163 7.766 -17.170 4.218 1.00 50.76 A N
ANISOU 1495 N PHE A 163 7032 5378 6875 -194 -61 -560 A N
ATOM 1496 CA PHE A 163 7.979 -17.734 5.547 1.00 48.96 A C
ANISOU 1496 CA PHE A 163 6781 5095 6726 -162 73 -457 A C
ATOM 1497 C PHE A 163 6.670 -18.290 6.092 1.00 46.05 A C
ANISOU 1497 C PHE A 163 6342 4596 6557 -269 80 -446 A C
ATOM 1498 O PHE A 163 6.600 -19.437 6.544 1.00 53.72 A O
ANISOU 1498 O PHE A 163 7357 5424 7631 -275 161 -428 A O
ATOM 1499 CB PHE A 163 8.502 -16.676 6.532 1.00 48.06 A C
ANISOU 1499 CB PHE A 163 6594 5125 6542 -103 132 -344 A C
ATOM 1500 CG PHE A 163 9.907 -16.195 6.271 1.00 48.78 A C
ANISOU 1500 CG PHE A 163 6728 5337 6470 1 153 -330 A C
ATOM 1501 CD1 PHE A 163 10.145 -15.146 5.399 1.00 62.02 A C
ANISOU 1501 CD1 PHE A 163 8396 7128 8042 0 78 -368 A C
ATOM 1502 CD2 PHE A 163 10.981 -16.755 6.943 1.00 49.90 A C
ANISOU 1502 CD2 PHE A 163 6907 5480 6573 103 251 -267 A C
ATOM 1503 CE1 PHE A 163 11.434 -14.687 5.181 1.00 56.40 A C
ANISOU 1503 CE1 PHE A 163 7706 6522 7203 87 113 -346 A C
ATOM 1504 CE2 PHE A 163 12.270 -16.308 6.724 1.00 51.70 A C
ANISOU 1504 CE2 PHE A 163 7146 5821 6676 194 270 -252 A C
ATOM 1505 CZ PHE A 163 12.496 -15.268 5.851 1.00 51.46 A C
ANISOU 1505 CZ PHE A 163 7098 5898 6556 180 208 -291 A C
ATOM 1506 N ALA A 164 5.621 -17.463 6.055 1.00 52.66 A N
ANISOU 1506 N ALA A 164 7065 5479 7463 -352 4 -449 A N
ATOM 1507 CA ALA A 164 4.337 -17.830 6.639 1.00 52.37 A C
ANISOU 1507 CA ALA A 164 6926 5338 7634 -455 24 -424 A C
ATOM 1508 C ALA A 164 3.752 -19.071 5.989 1.00 65.31 A C
ANISOU 1508 C ALA A 164 8606 6799 9411 -543 -27 -524 A C
ATOM 1509 O ALA A 164 3.001 -19.813 6.633 1.00 61.94 A O
ANISOU 1509 O ALA A 164 8126 6237 9172 -616 44 -487 A O
ATOM 1510 CB ALA A 164 3.363 -16.658 6.508 1.00 52.40 A C
ANISOU 1510 CB ALA A 164 6793 5433 7682 -515 -66 -424 A C
ATOM 1511 N GLU A 165 4.084 -19.318 4.723 1.00 62.39 A N
ANISOU 1511 N GLU A 165 8337 6418 8949 -539 -143 -653 A N
ATOM 1512 CA GLU A 165 3.492 -20.444 4.015 1.00 71.97 A C
ANISOU 1512 CA GLU A 165 9599 7458 10287 -631 -218 -775 A C
ATOM 1513 C GLU A 165 4.240 -21.744 4.273 1.00 68.75 A C
ANISOU 1513 C GLU A 165 9326 6902 9894 -580 -98 -774 A C
ATOM 1514 O GLU A 165 3.636 -22.820 4.208 1.00 68.36 A O
ANISOU 1514 O GLU A 165 9295 6663 10015 -669 -100 -831 A O
ATOM 1515 CB GLU A 165 3.454 -20.155 2.512 1.00 82.31 A C
ANISOU 1515 CB GLU A 165 10978 8818 11476 -644 -406 -925 A C
ATOM 1516 CG GLU A 165 2.056 -19.917 1.967 1.00105.64 A C
ANISOU 1516 CG GLU A 165 13816 11752 14570 -778 -580 -1005 A C
ATOM 1517 CD GLU A 165 1.173 -21.146 2.079 1.00142.94 A C
ANISOU 1517 CD GLU A 165 18507 16265 19538 -907 -594 -1069 A C
ATOM 1518 OE1 GLU A 165 0.168 -21.092 2.819 1.00143.73 A O
ANISOU 1518 OE1 GLU A 165 18437 16321 19852 -1001 -563 -1002 A O
ATOM 1519 OE2 GLU A 165 1.485 -22.167 1.430 1.00140.09 A O
ANISOU 1519 OE2 GLU A 165 18291 15774 19163 -916 -625 -1187 A O
ATOM 1520 N LYS A 166 5.533 -21.667 4.592 1.00 61.39 A N
ANISOU 1520 N LYS A 166 8480 6043 8802 -439 6 -708 A N
ATOM 1521 CA LYS A 166 6.399 -22.834 4.613 1.00 64.46 A C
ANISOU 1521 CA LYS A 166 9012 6307 9175 -360 102 -719 A C
ATOM 1522 C LYS A 166 6.824 -23.292 6.004 1.00 68.08 A C
ANISOU 1522 C LYS A 166 9462 6718 9686 -291 279 -561 A C
ATOM 1523 O LYS A 166 7.251 -24.442 6.147 1.00 66.90 A O
ANISOU 1523 O LYS A 166 9418 6416 9586 -246 365 -558 A O
ATOM 1524 CB LYS A 166 7.668 -22.550 3.794 1.00 72.34 A C
ANISOU 1524 CB LYS A 166 10123 7415 9949 -232 88 -770 A C
ATOM 1525 CG LYS A 166 7.406 -22.164 2.344 1.00 88.94 A C
ANISOU 1525 CG LYS A 166 12276 9565 11954 -273 -74 -923 A C
ATOM 1526 CD LYS A 166 6.795 -23.308 1.550 1.00107.43 A C
ANISOU 1526 CD LYS A 166 14716 11710 14394 -356 -152 -1079 A C
ATOM 1527 CE LYS A 166 6.362 -22.851 0.165 1.00112.18 A C
ANISOU 1527 CE LYS A 166 15364 12371 14891 -404 -341 -1231 A C
ATOM 1528 NZ LYS A 166 7.177 -23.474 -0.912 1.00118.85 A N
ANISOU 1528 NZ LYS A 166 16410 13169 15581 -319 -348 -1361 A N
ATOM 1529 N LEU A 167 6.726 -22.437 7.020 1.00 52.41 A N
ANISOU 1529 N LEU A 167 7369 4856 7687 -272 335 -431 A N
ATOM 1530 CA LEU A 167 7.249 -22.712 8.352 1.00 47.66 A C
ANISOU 1530 CA LEU A 167 6776 4250 7083 -182 490 -275 A C
ATOM 1531 C LEU A 167 6.121 -22.891 9.368 1.00 48.19 A C
ANISOU 1531 C LEU A 167 6752 4230 7327 -272 570 -180 A C
ATOM 1532 O LEU A 167 5.036 -22.329 9.196 1.00 50.46 A O
ANISOU 1532 O LEU A 167 6925 4537 7711 -387 504 -213 A O
ATOM 1533 CB LEU A 167 8.142 -21.564 8.838 1.00 50.47 A C
ANISOU 1533 CB LEU A 167 7095 4823 7259 -74 500 -196 A C
ATOM 1534 CG LEU A 167 9.398 -21.232 8.032 1.00 59.41 A C
ANISOU 1534 CG LEU A 167 8291 6068 8214 28 454 -253 A C
ATOM 1535 CD1 LEU A 167 10.101 -20.017 8.622 1.00 58.03 A C
ANISOU 1535 CD1 LEU A 167 8049 6097 7904 101 459 -173 A C
ATOM 1536 CD2 LEU A 167 10.315 -22.435 8.012 1.00 61.78 A C
ANISOU 1536 CD2 LEU A 167 8712 6257 8505 133 536 -247 A C
ATOM 1537 N PRO A 168 6.352 -23.648 10.445 1.00 48.55 A N
ANISOU 1537 N PRO A 168 6845 4183 7420 -213 721 -53 A N
ATOM 1538 CA PRO A 168 5.377 -23.678 11.542 1.00 52.17 A C
ANISOU 1538 CA PRO A 168 7220 4585 8016 -276 830 65 A C
ATOM 1539 C PRO A 168 5.212 -22.298 12.157 1.00 50.08 A C
ANISOU 1539 C PRO A 168 6852 4521 7654 -256 822 127 A C
ATOM 1540 O PRO A 168 6.118 -21.462 12.117 1.00 45.81 A O
ANISOU 1540 O PRO A 168 6326 4153 6926 -161 773 125 A O
ATOM 1541 CB PRO A 168 5.988 -24.671 12.541 1.00 53.38 A C
ANISOU 1541 CB PRO A 168 7483 4632 8169 -171 993 202 A C
ATOM 1542 CG PRO A 168 6.941 -25.483 11.731 1.00 59.86 A C
ANISOU 1542 CG PRO A 168 8431 5374 8939 -99 957 120 A C
ATOM 1543 CD PRO A 168 7.507 -24.515 10.739 1.00 52.42 A C
ANISOU 1543 CD PRO A 168 7467 4613 7837 -74 809 1 A C
ATOM 1544 N AVAL A 169 4.036 -22.072 12.743 0.65 48.08 A N
ANISOU 1544 N AVAL A 169 6489 4235 7543 -348 881 182 A N
ATOM 1545 N BVAL A 169 4.039 -22.079 12.757 0.35 48.11 A N
ANISOU 1545 N BVAL A 169 6494 4239 7547 -347 883 184 A N
ATOM 1546 CA AVAL A 169 3.673 -20.737 13.212 0.65 47.38 A C
ANISOU 1546 CA AVAL A 169 6296 4317 7390 -344 869 219 A C
ATOM 1547 CA BVAL A 169 3.669 -20.743 13.219 0.35 47.40 A C
ANISOU 1547 CA BVAL A 169 6298 4318 7394 -344 870 220 A C
ATOM 1548 C AVAL A 169 4.703 -20.198 14.202 0.65 45.58 A C
ANISOU 1548 C AVAL A 169 6133 4230 6956 -194 936 322 A C
ATOM 1549 C BVAL A 169 4.698 -20.198 14.203 0.35 45.62 A C
ANISOU 1549 C BVAL A 169 6137 4235 6961 -194 937 322 A C
ATOM 1550 O AVAL A 169 5.069 -19.018 14.154 0.65 44.25 A O
ANISOU 1550 O AVAL A 169 5930 4233 6651 -153 864 298 A O
ATOM 1551 O BVAL A 169 5.065 -19.019 14.148 0.35 44.45 A O
ANISOU 1551 O BVAL A 169 5954 4257 6676 -154 863 297 A O
ATOM 1552 CB AVAL A 169 2.260 -20.772 13.824 0.65 50.34 A C
ANISOU 1552 CB AVAL A 169 6547 4610 7970 -450 963 282 A C
ATOM 1553 CB BVAL A 169 2.257 -20.767 13.836 0.35 50.27 A C
ANISOU 1553 CB BVAL A 169 6538 4602 7961 -449 964 283 A C
ATOM 1554 CG1AVAL A 169 2.016 -19.564 14.688 0.65 45.16 A C
ANISOU 1554 CG1AVAL A 169 5818 4108 7231 -404 1015 357 A C
ATOM 1555 CG1BVAL A 169 1.271 -21.426 12.882 0.35 51.93 A C
ANISOU 1555 CG1BVAL A 169 6673 4658 8399 -606 884 178 A C
ATOM 1556 CG2AVAL A 169 1.217 -20.859 12.723 0.65 55.59 A C
ANISOU 1556 CG2AVAL A 169 7099 5198 8822 -604 835 156 A C
ATOM 1557 CG2BVAL A 169 2.263 -21.493 15.173 0.35 46.38 A C
ANISOU 1557 CG2BVAL A 169 6105 4019 7497 -394 1173 446 A C
ATOM 1558 N GLU A 170 5.173 -21.036 15.126 1.00 48.62 A N
ANISOU 1558 N GLU A 170 6615 4543 7317 -109 1070 438 A N
ATOM 1559 CA GLU A 170 6.121 -20.547 16.124 1.00 47.12 A C
ANISOU 1559 CA GLU A 170 6484 4491 6927 36 1116 533 A C
ATOM 1560 C GLU A 170 7.409 -20.046 15.490 1.00 48.69 A C
ANISOU 1560 C GLU A 170 6718 4826 6954 120 990 460 A C
ATOM 1561 O GLU A 170 8.016 -19.089 15.984 1.00 49.19 A O
ANISOU 1561 O GLU A 170 6772 5054 6863 193 960 483 A O
ATOM 1562 CB GLU A 170 6.438 -21.646 17.127 1.00 52.16 A C
ANISOU 1562 CB GLU A 170 7234 5019 7565 124 1266 674 A C
ATOM 1563 CG GLU A 170 5.261 -22.008 17.958 1.00 72.45 A C
ANISOU 1563 CG GLU A 170 9772 7474 10280 59 1423 777 A C
ATOM 1564 CD GLU A 170 5.639 -22.161 19.390 1.00 97.52 A C
ANISOU 1564 CD GLU A 170 13043 10681 13329 190 1563 944 A C
ATOM 1565 OE1 GLU A 170 6.430 -23.078 19.701 1.00121.28 A O
ANISOU 1565 OE1 GLU A 170 16173 13621 16287 292 1610 1019 A O
ATOM 1566 OE2 GLU A 170 5.134 -21.389 20.232 1.00 88.75 A O
ANISOU 1566 OE2 GLU A 170 11896 9660 12165 200 1632 1004 A O
ATOM 1567 N GLU A 171 7.845 -20.679 14.406 1.00 47.39 A N
ANISOU 1567 N GLU A 171 6596 4593 6818 109 922 368 A N
ATOM 1568 CA AGLU A 171 9.076 -20.241 13.763 0.44 45.43 A C
ANISOU 1568 CA AGLU A 171 6373 4468 6418 191 826 305 A C
ATOM 1569 CA BGLU A 171 9.072 -20.259 13.738 0.56 45.35 A C
ANISOU 1569 CA BGLU A 171 6365 4457 6411 190 825 303 A C
ATOM 1570 C GLU A 171 8.872 -18.955 12.978 1.00 50.08 A C
ANISOU 1570 C GLU A 171 6876 5192 6961 126 704 208 A C
ATOM 1571 O GLU A 171 9.776 -18.113 12.930 1.00 45.79 A O
ANISOU 1571 O GLU A 171 6321 4800 6277 192 650 200 A O
ATOM 1572 CB AGLU A 171 9.608 -21.346 12.854 0.44 55.27 A C
ANISOU 1572 CB AGLU A 171 7706 5593 7702 215 813 239 A C
ATOM 1573 CB BGLU A 171 9.542 -21.360 12.787 0.56 55.24 A C
ANISOU 1573 CB BGLU A 171 7701 5582 7707 206 809 232 A C
ATOM 1574 CG AGLU A 171 10.385 -22.418 13.596 0.44 63.93 A C
ANISOU 1574 CG AGLU A 171 8903 6606 8781 341 917 344 A C
ATOM 1575 CG BGLU A 171 10.962 -21.834 13.014 0.56 70.83 A C
ANISOU 1575 CG BGLU A 171 9756 7589 9568 364 840 280 A C
ATOM 1576 CD AGLU A 171 11.719 -22.718 12.942 0.44 76.14 A C
ANISOU 1576 CD AGLU A 171 10508 8190 10231 456 880 299 A C
ATOM 1577 CD BGLU A 171 11.166 -23.260 12.541 0.56 74.84 A C
ANISOU 1577 CD BGLU A 171 10368 7904 10164 392 890 256 A C
ATOM 1578 OE1AGLU A 171 12.681 -21.951 13.170 0.44 75.11 A O
ANISOU 1578 OE1AGLU A 171 10344 8234 9960 546 839 322 A O
ATOM 1579 OE1BGLU A 171 11.241 -23.469 11.311 0.56 67.00 A O
ANISOU 1579 OE1BGLU A 171 9402 6866 9188 354 824 126 A O
ATOM 1580 OE2AGLU A 171 11.804 -23.718 12.197 0.44 78.54 A O
ANISOU 1580 OE2AGLU A 171 10889 8344 10608 456 894 235 A O
ATOM 1581 OE2BGLU A 171 11.242 -24.169 13.397 0.56 74.13 A O
ANISOU 1581 OE2BGLU A 171 10345 7701 10120 456 999 367 A O
ATOM 1582 N VAL A 172 7.696 -18.775 12.376 1.00 42.78 A N
ANISOU 1582 N VAL A 172 5885 4212 6160 -1 657 141 A N
ATOM 1583 CA VAL A 172 7.387 -17.526 11.688 1.00 41.54 A C
ANISOU 1583 CA VAL A 172 5646 4174 5963 -56 544 66 A C
ATOM 1584 C VAL A 172 7.456 -16.355 12.660 1.00 40.90 A C
ANISOU 1584 C VAL A 172 5511 4232 5797 -16 570 137 A C
ATOM 1585 O VAL A 172 8.050 -15.313 12.364 1.00 40.12 A O
ANISOU 1585 O VAL A 172 5392 4268 5583 13 498 105 A O
ATOM 1586 CB VAL A 172 6.001 -17.609 11.022 1.00 43.19 A C
ANISOU 1586 CB VAL A 172 5779 4292 6338 -193 486 -3 A C
ATOM 1587 CG1 VAL A 172 5.662 -16.265 10.368 1.00 42.43 A C
ANISOU 1587 CG1 VAL A 172 5603 4324 6197 -232 368 -63 A C
ATOM 1588 CG2 VAL A 172 5.931 -18.756 10.018 1.00 48.07 A C
ANISOU 1588 CG2 VAL A 172 6463 4765 7034 -240 440 -97 A C
ATOM 1589 N VAL A 173 6.804 -16.493 13.819 1.00 39.18 A N
ANISOU 1589 N VAL A 173 5274 3976 5638 -18 680 230 A N
ATOM 1590 CA VAL A 173 6.809 -15.412 14.801 1.00 38.69 A C
ANISOU 1590 CA VAL A 173 5179 4035 5486 25 713 287 A C
ATOM 1591 C VAL A 173 8.227 -15.163 15.306 1.00 41.03 A C
ANISOU 1591 C VAL A 173 5544 4445 5602 145 702 320 A C
ATOM 1592 O VAL A 173 8.617 -14.017 15.557 1.00 40.62 A O
ANISOU 1592 O VAL A 173 5465 4522 5445 172 654 307 A O
ATOM 1593 CB VAL A 173 5.823 -15.738 15.945 1.00 43.28 A C
ANISOU 1593 CB VAL A 173 5743 4542 6160 9 856 386 A C
ATOM 1594 CG1 VAL A 173 5.912 -14.701 17.063 1.00 46.92 A C
ANISOU 1594 CG1 VAL A 173 6203 5125 6500 75 904 442 A C
ATOM 1595 CG2 VAL A 173 4.395 -15.799 15.405 1.00 44.14 A C
ANISOU 1595 CG2 VAL A 173 5743 4558 6470 -120 853 347 A C
ATOM 1596 N SER A 174 9.036 -16.216 15.422 1.00 43.64 A N
ANISOU 1596 N SER A 174 5956 4723 5903 219 737 357 A N
ATOM 1597 CA ASER A 174 10.409 -16.037 15.876 0.90 46.07 A C
ANISOU 1597 CA ASER A 174 6309 5141 6055 338 713 390 A C
ATOM 1598 CA BSER A 174 10.413 -16.041 15.874 0.10 46.15 A C
ANISOU 1598 CA BSER A 174 6319 5150 6065 338 713 390 A C
ATOM 1599 C SER A 174 11.216 -15.196 14.890 1.00 46.20 A C
ANISOU 1599 C SER A 174 6283 5269 6002 333 595 299 A C
ATOM 1600 O SER A 174 12.005 -14.336 15.298 1.00 42.93 A O
ANISOU 1600 O SER A 174 5849 4987 5477 384 551 305 A O
ATOM 1601 CB ASER A 174 11.060 -17.406 16.088 0.90 52.62 A C
ANISOU 1601 CB ASER A 174 7227 5877 6889 425 774 451 A C
ATOM 1602 CB BSER A 174 11.074 -17.405 16.076 0.10 52.52 A C
ANISOU 1602 CB BSER A 174 7214 5865 6876 426 773 450 A C
ATOM 1603 OG ASER A 174 12.385 -17.264 16.555 0.90 58.45 A O
ANISOU 1603 OG ASER A 174 7991 6728 7490 549 742 488 A O
ATOM 1604 OG BSER A 174 12.355 -17.270 16.665 0.10 57.94 A O
ANISOU 1604 OG BSER A 174 7929 6662 7422 552 748 497 A O
ATOM 1605 N VAL A 175 11.014 -15.414 13.587 1.00 40.99 A N
ANISOU 1605 N VAL A 175 5613 4555 5407 270 545 213 A N
ATOM 1606 CA VAL A 175 11.730 -14.641 12.571 1.00 41.31 A C
ANISOU 1606 CA VAL A 175 5624 4692 5379 266 453 137 A C
ATOM 1607 C VAL A 175 11.341 -13.169 12.638 1.00 42.56 A C
ANISOU 1607 C VAL A 175 5710 4953 5508 213 399 116 A C
ATOM 1608 O VAL A 175 12.200 -12.278 12.658 1.00 38.42 A O
ANISOU 1608 O VAL A 175 5159 4544 4894 245 355 109 A O
ATOM 1609 CB VAL A 175 11.466 -15.229 11.171 1.00 43.49 A C
ANISOU 1609 CB VAL A 175 5929 4881 5713 215 414 49 A C
ATOM 1610 CG1 VAL A 175 11.988 -14.284 10.080 1.00 46.53 A C
ANISOU 1610 CG1 VAL A 175 6289 5368 6021 202 331 -21 A C
ATOM 1611 CG2 VAL A 175 12.104 -16.610 11.067 1.00 47.66 A C
ANISOU 1611 CG2 VAL A 175 6541 5312 6255 287 470 60 A C
ATOM 1612 N VAL A 176 10.038 -12.879 12.664 1.00 38.23 A N
ANISOU 1612 N VAL A 176 5122 4355 5049 130 402 105 A N
ATOM 1613 CA VAL A 176 9.646 -11.474 12.628 1.00 34.88 A C
ANISOU 1613 CA VAL A 176 4633 4015 4607 89 351 82 A C
ATOM 1614 C VAL A 176 10.066 -10.773 13.915 1.00 36.17 A C
ANISOU 1614 C VAL A 176 4795 4262 4685 145 386 136 A C
ATOM 1615 O VAL A 176 10.513 -9.618 13.890 1.00 36.78 A O
ANISOU 1615 O VAL A 176 4844 4434 4697 146 333 111 A O
ATOM 1616 CB VAL A 176 8.136 -11.337 12.338 1.00 39.56 A C
ANISOU 1616 CB VAL A 176 5167 4535 5327 -2 343 61 A C
ATOM 1617 CG1 VAL A 176 7.300 -11.786 13.494 1.00 48.50 A C
ANISOU 1617 CG1 VAL A 176 6288 5603 6536 -5 450 131 A C
ATOM 1618 CG2 VAL A 176 7.801 -9.888 11.972 1.00 47.90 A C
ANISOU 1618 CG2 VAL A 176 6162 5669 6367 -36 274 27 A C
ATOM 1619 N ASN A 177 9.964 -11.457 15.053 1.00 37.32 A N
ANISOU 1619 N ASN A 177 4982 4373 4824 195 473 208 A N
ATOM 1620 CA ASN A 177 10.370 -10.836 16.308 1.00 38.65 A C
ANISOU 1620 CA ASN A 177 5170 4626 4887 258 497 252 A C
ATOM 1621 C ASN A 177 11.880 -10.606 16.345 1.00 39.96 A C
ANISOU 1621 C ASN A 177 5350 4895 4938 327 430 243 A C
ATOM 1622 O ASN A 177 12.339 -9.601 16.899 1.00 40.24 A O
ANISOU 1622 O ASN A 177 5372 5026 4891 345 387 228 A O
ATOM 1623 CB ASN A 177 9.910 -11.690 17.488 1.00 43.28 A C
ANISOU 1623 CB ASN A 177 5816 5151 5478 307 613 343 A C
ATOM 1624 CG ASN A 177 8.410 -11.565 17.754 1.00 40.49 A C
ANISOU 1624 CG ASN A 177 5425 4724 5236 241 696 361 A C
ATOM 1625 ND2 ASN A 177 7.920 -12.352 18.698 1.00 48.09 A N
ANISOU 1625 ND2 ASN A 177 6436 5617 6220 274 821 451 A N
ATOM 1626 OD1 ASN A 177 7.709 -10.777 17.118 1.00 42.62 A O
ANISOU 1626 OD1 ASN A 177 5620 4998 5578 167 653 304 A O
ATOM 1627 N SER A 178 12.665 -11.513 15.751 1.00 41.03 A N
ANISOU 1627 N SER A 178 5505 5008 5077 365 419 245 A N
ATOM 1628 CA SER A 178 14.110 -11.300 15.665 1.00 39.57 A C
ANISOU 1628 CA SER A 178 5304 4922 4809 429 359 237 A C
ATOM 1629 C SER A 178 14.431 -10.070 14.822 1.00 40.79 A C
ANISOU 1629 C SER A 178 5392 5151 4956 368 282 166 A C
ATOM 1630 O SER A 178 15.290 -9.262 15.182 1.00 40.13 A O
ANISOU 1630 O SER A 178 5272 5168 4810 388 229 156 A O
ATOM 1631 CB SER A 178 14.793 -12.528 15.060 1.00 43.41 A C
ANISOU 1631 CB SER A 178 5821 5356 5318 486 380 250 A C
ATOM 1632 OG SER A 178 14.696 -13.637 15.923 1.00 50.06 A O
ANISOU 1632 OG SER A 178 6731 6129 6160 559 451 330 A O
ATOM 1633 N TYR A 179 13.739 -9.918 13.695 1.00 37.71 A N
ANISOU 1633 N TYR A 179 4986 4708 4632 291 272 117 A N
ATOM 1634 CA TYR A 179 13.900 -8.736 12.851 1.00 36.06 A C
ANISOU 1634 CA TYR A 179 4729 4556 4417 234 211 65 A C
ATOM 1635 C TYR A 179 13.545 -7.457 13.601 1.00 39.10 A C
ANISOU 1635 C TYR A 179 5083 4989 4782 203 188 59 A C
ATOM 1636 O TYR A 179 14.290 -6.469 13.553 1.00 37.49 A O
ANISOU 1636 O TYR A 179 4843 4861 4542 193 141 37 A O
ATOM 1637 CB TYR A 179 13.032 -8.915 11.613 1.00 37.85 A C
ANISOU 1637 CB TYR A 179 4964 4710 4708 170 199 22 A C
ATOM 1638 CG TYR A 179 12.921 -7.711 10.734 1.00 37.84 A C
ANISOU 1638 CG TYR A 179 4928 4750 4701 114 142 -17 A C
ATOM 1639 CD1 TYR A 179 13.987 -7.292 9.952 1.00 37.74 A C
ANISOU 1639 CD1 TYR A 179 4904 4798 4638 126 121 -31 A C
ATOM 1640 CD2 TYR A 179 11.742 -6.990 10.679 1.00 40.02 A C
ANISOU 1640 CD2 TYR A 179 5180 4997 5028 55 120 -29 A C
ATOM 1641 CE1 TYR A 179 13.864 -6.196 9.135 1.00 38.98 A C
ANISOU 1641 CE1 TYR A 179 5041 4980 4787 77 82 -52 A C
ATOM 1642 CE2 TYR A 179 11.618 -5.907 9.872 1.00 40.06 A C
ANISOU 1642 CE2 TYR A 179 5163 5030 5027 14 68 -53 A C
ATOM 1643 CZ TYR A 179 12.679 -5.500 9.115 1.00 39.40 A C
ANISOU 1643 CZ TYR A 179 5083 5001 4885 24 51 -62 A C
ATOM 1644 OH TYR A 179 12.512 -4.404 8.298 1.00 43.38 A O
ANISOU 1644 OH TYR A 179 5577 5523 5383 -14 11 -71 A O
ATOM 1645 N PHE A 180 12.415 -7.453 14.313 1.00 37.43 A N
ANISOU 1645 N PHE A 180 4888 4730 4605 187 230 77 A N
ATOM 1646 CA PHE A 180 12.006 -6.252 15.028 1.00 36.14 A C
ANISOU 1646 CA PHE A 180 4709 4601 4423 168 221 64 A C
ATOM 1647 C PHE A 180 12.985 -5.906 16.145 1.00 37.54 A C
ANISOU 1647 C PHE A 180 4905 4860 4497 227 201 73 A C
ATOM 1648 O PHE A 180 13.209 -4.723 16.439 1.00 39.10 A O
ANISOU 1648 O PHE A 180 5087 5106 4664 206 158 35 A O
ATOM 1649 CB PHE A 180 10.595 -6.428 15.600 1.00 35.44 A C
ANISOU 1649 CB PHE A 180 4629 4442 4395 153 293 89 A C
ATOM 1650 CG PHE A 180 9.487 -6.382 14.572 1.00 34.85 A C
ANISOU 1650 CG PHE A 180 4508 4300 4435 83 283 66 A C
ATOM 1651 CD1 PHE A 180 9.632 -5.708 13.362 1.00 37.10 A C
ANISOU 1651 CD1 PHE A 180 4760 4601 4734 39 205 21 A C
ATOM 1652 CD2 PHE A 180 8.274 -6.991 14.842 1.00 41.76 A C
ANISOU 1652 CD2 PHE A 180 5367 5093 5405 63 351 95 A C
ATOM 1653 CE1 PHE A 180 8.596 -5.663 12.436 1.00 39.22 A C
ANISOU 1653 CE1 PHE A 180 4992 4816 5095 -16 175 1 A C
ATOM 1654 CE2 PHE A 180 7.236 -6.940 13.920 1.00 40.85 A C
ANISOU 1654 CE2 PHE A 180 5193 4922 5405 -3 320 69 A C
ATOM 1655 CZ PHE A 180 7.387 -6.273 12.732 1.00 39.07 A C
ANISOU 1655 CZ PHE A 180 4944 4723 5179 -38 224 20 A C
ATOM 1656 N ASER A 181 13.580 -6.920 16.776 0.64 37.66 A N
ANISOU 1656 N ASER A 181 4959 4887 4461 301 224 119 A N
ATOM 1657 N BSER A 181 13.553 -6.922 16.796 0.36 37.87 A N
ANISOU 1657 N BSER A 181 4987 4913 4488 301 225 120 A N
ATOM 1658 CA ASER A 181 14.542 -6.679 17.845 0.64 41.84 A C
ANISOU 1658 CA ASER A 181 5508 5505 4886 366 182 128 A C
ATOM 1659 CA BSER A 181 14.539 -6.676 17.841 0.36 41.90 A C
ANISOU 1659 CA BSER A 181 5515 5512 4893 366 182 128 A C
ATOM 1660 C ASER A 181 15.817 -6.038 17.315 0.64 39.21 A C
ANISOU 1660 C ASER A 181 5105 5252 4540 352 91 85 A C
ATOM 1661 C BSER A 181 15.771 -5.987 17.271 0.36 39.31 A C
ANISOU 1661 C BSER A 181 5117 5263 4556 346 91 83 A C
ATOM 1662 O ASER A 181 16.365 -5.121 17.938 0.64 41.45 A O
ANISOU 1662 O ASER A 181 5373 5605 4770 348 25 50 A O
ATOM 1663 O BSER A 181 16.234 -4.971 17.803 0.36 41.70 A O
ANISOU 1663 O BSER A 181 5401 5629 4815 333 28 42 A O
ATOM 1664 CB ASER A 181 14.864 -7.996 18.548 0.64 43.43 A C
ANISOU 1664 CB ASER A 181 5767 5694 5039 462 224 203 A C
ATOM 1665 CB BSER A 181 14.921 -7.997 18.510 0.36 43.42 A C
ANISOU 1665 CB BSER A 181 5763 5696 5038 462 221 202 A C
ATOM 1666 OG ASER A 181 13.758 -8.434 19.313 0.64 49.90 A O
ANISOU 1666 OG ASER A 181 6655 6448 5858 478 320 252 A O
ATOM 1667 OG BSER A 181 15.839 -7.781 19.566 0.36 46.59 A O
ANISOU 1667 OG BSER A 181 6184 6191 5326 536 161 211 A O
ATOM 1668 N VAL A 182 16.312 -6.532 16.180 1.00 38.10 A N
ANISOU 1668 N VAL A 182 4925 5100 4451 343 90 87 A N
ATOM 1669 CA VAL A 182 17.468 -5.928 15.515 1.00 39.48 A C
ANISOU 1669 CA VAL A 182 5021 5343 4636 322 32 56 A C
ATOM 1670 C VAL A 182 17.202 -4.466 15.167 1.00 42.36 A C
ANISOU 1670 C VAL A 182 5351 5714 5028 231 -3 3 A C
ATOM 1671 O VAL A 182 18.013 -3.584 15.471 1.00 40.83 A O
ANISOU 1671 O VAL A 182 5107 5584 4822 210 -64 -27 A O
ATOM 1672 CB VAL A 182 17.828 -6.733 14.253 1.00 42.84 A C
ANISOU 1672 CB VAL A 182 5430 5739 5107 333 68 67 A C
ATOM 1673 CG1 VAL A 182 18.816 -5.960 13.372 1.00 47.78 A C
ANISOU 1673 CG1 VAL A 182 5975 6424 5758 295 38 40 A C
ATOM 1674 CG2 VAL A 182 18.385 -8.082 14.655 1.00 47.42 A C
ANISOU 1674 CG2 VAL A 182 6035 6315 5665 435 95 117 A C
ATOM 1675 N CYS A 183 16.087 -4.190 14.485 1.00 37.86 A N
ANISOU 1675 N CYS A 183 4805 5075 4507 176 30 -8 A N
ATOM 1676 CA CYS A 183 15.838 -2.814 14.063 1.00 36.79 A C
ANISOU 1676 CA CYS A 183 4642 4935 4403 101 2 -47 A C
ATOM 1677 C CYS A 183 15.623 -1.891 15.252 1.00 38.55 A C
ANISOU 1677 C CYS A 183 4881 5172 4592 95 -24 -77 A C
ATOM 1678 O CYS A 183 16.122 -0.760 15.256 1.00 38.19 A O
ANISOU 1678 O CYS A 183 4804 5150 4557 49 -71 -116 A O
ATOM 1679 CB CYS A 183 14.626 -2.719 13.124 1.00 39.24 A C
ANISOU 1679 CB CYS A 183 4971 5170 4770 58 29 -47 A C
ATOM 1680 SG CYS A 183 14.711 -3.652 11.606 1.00 40.92 A S
ANISOU 1680 SG CYS A 183 5190 5354 5003 59 47 -35 A S
ATOM 1681 N THR A 184 14.851 -2.336 16.251 1.00 37.10 A N
ANISOU 1681 N THR A 184 4757 4967 4372 138 14 -62 A N
ATOM 1682 CA THR A 184 14.554 -1.480 17.391 1.00 39.17 A C
ANISOU 1682 CA THR A 184 5059 5240 4586 144 3 -98 A C
ATOM 1683 C THR A 184 15.824 -1.086 18.131 1.00 39.35 A C
ANISOU 1683 C THR A 184 5068 5345 4538 161 -82 -134 A C
ATOM 1684 O THR A 184 15.987 0.071 18.531 1.00 38.73 A O
ANISOU 1684 O THR A 184 4992 5274 4449 124 -131 -196 A O
ATOM 1685 CB THR A 184 13.597 -2.187 18.355 1.00 41.58 A C
ANISOU 1685 CB THR A 184 5434 5513 4849 203 81 -61 A C
ATOM 1686 CG2 THR A 184 13.481 -1.397 19.644 1.00 50.72 A C
ANISOU 1686 CG2 THR A 184 6655 6696 5921 231 74 -101 A C
ATOM 1687 OG1 THR A 184 12.303 -2.279 17.750 1.00 44.04 A O
ANISOU 1687 OG1 THR A 184 5736 5745 5252 170 148 -43 A O
ATOM 1688 N ALA A 185 16.730 -2.044 18.343 1.00 38.89 A N
ANISOU 1688 N ALA A 185 4995 5344 4437 220 -107 -98 A N
ATOM 1689 CA ALA A 185 17.935 -1.749 19.109 1.00 42.99 A C
ANISOU 1689 CA ALA A 185 5488 5952 4894 244 -207 -130 A C
ATOM 1690 C ALA A 185 18.768 -0.671 18.424 1.00 40.87 A C
ANISOU 1690 C ALA A 185 5124 5705 4700 157 -274 -183 A C
ATOM 1691 O ALA A 185 19.284 0.241 19.085 1.00 41.04 A O
ANISOU 1691 O ALA A 185 5133 5761 4698 126 -358 -249 A O
ATOM 1692 CB ALA A 185 18.744 -3.031 19.318 1.00 42.06 A C
ANISOU 1692 CB ALA A 185 5357 5888 4737 334 -220 -68 A C
ATOM 1693 N ILE A 186 18.888 -0.744 17.099 1.00 38.59 A N
ANISOU 1693 N ILE A 186 4774 5388 4501 113 -234 -157 A N
ATOM 1694 CA ILE A 186 19.751 0.185 16.378 1.00 37.60 A C
ANISOU 1694 CA ILE A 186 4554 5279 4453 33 -273 -186 A C
ATOM 1695 C ILE A 186 19.087 1.550 16.224 1.00 38.66 A C
ANISOU 1695 C ILE A 186 4714 5345 4629 -50 -271 -235 A C
ATOM 1696 O ILE A 186 19.732 2.588 16.404 1.00 38.03 A O
ANISOU 1696 O ILE A 186 4589 5274 4588 -115 -332 -287 A O
ATOM 1697 CB ILE A 186 20.132 -0.436 15.026 1.00 36.81 A C
ANISOU 1697 CB ILE A 186 4400 5176 4411 33 -213 -134 A C
ATOM 1698 CG1 ILE A 186 21.112 -1.597 15.284 1.00 44.41 A C
ANISOU 1698 CG1 ILE A 186 5316 6210 5348 119 -228 -96 A C
ATOM 1699 CG2 ILE A 186 20.755 0.621 14.121 1.00 43.62 A C
ANISOU 1699 CG2 ILE A 186 5183 6032 5358 -56 -215 -147 A C
ATOM 1700 CD1 ILE A 186 21.396 -2.466 14.090 1.00 45.73 A C
ANISOU 1700 CD1 ILE A 186 5458 6366 5550 150 -153 -48 A C
ATOM 1701 N ILE A 187 17.800 1.575 15.892 1.00 37.18 A N
ANISOU 1701 N ILE A 187 4594 5085 4449 -51 -205 -219 A N
ATOM 1702 CA ILE A 187 17.086 2.850 15.784 1.00 38.62 A C
ANISOU 1702 CA ILE A 187 4805 5195 4675 -111 -199 -258 A C
ATOM 1703 C ILE A 187 17.138 3.607 17.105 1.00 38.81 A C
ANISOU 1703 C ILE A 187 4873 5225 4649 -111 -253 -333 A C
ATOM 1704 O ILE A 187 17.394 4.818 17.144 1.00 40.22 A O
ANISOU 1704 O ILE A 187 5041 5367 4872 -177 -291 -389 A O
ATOM 1705 CB ILE A 187 15.636 2.616 15.325 1.00 36.74 A C
ANISOU 1705 CB ILE A 187 4618 4887 4455 -93 -127 -224 A C
ATOM 1706 CG1 ILE A 187 15.616 2.195 13.850 1.00 38.46 A C
ANISOU 1706 CG1 ILE A 187 4802 5090 4721 -111 -97 -172 A C
ATOM 1707 CG2 ILE A 187 14.792 3.884 15.562 1.00 39.94 A C
ANISOU 1707 CG2 ILE A 187 5060 5219 4895 -124 -119 -265 A C
ATOM 1708 CD1 ILE A 187 14.293 1.559 13.413 1.00 44.21 A C
ANISOU 1708 CD1 ILE A 187 5566 5767 5465 -85 -49 -140 A C
ATOM 1709 N THR A 188 16.894 2.902 18.215 1.00 39.19 A N
ANISOU 1709 N THR A 188 4982 5309 4597 -34 -253 -335 A N
ATOM 1710 CA THR A 188 16.899 3.552 19.520 1.00 40.59 A C
ANISOU 1710 CA THR A 188 5230 5499 4696 -18 -303 -413 A C
ATOM 1711 C THR A 188 18.292 4.071 19.872 1.00 42.21 A C
ANISOU 1711 C THR A 188 5374 5764 4898 -61 -427 -476 A C
ATOM 1712 O THR A 188 18.433 5.171 20.421 1.00 40.33 A O
ANISOU 1712 O THR A 188 5166 5501 4658 -107 -486 -566 A O
ATOM 1713 CB THR A 188 16.383 2.571 20.578 1.00 42.99 A C
ANISOU 1713 CB THR A 188 5622 5836 4878 86 -264 -383 A C
ATOM 1714 CG2 THR A 188 16.378 3.216 21.960 1.00 54.72 A C
ANISOU 1714 CG2 THR A 188 7205 7339 6248 118 -312 -466 A C
ATOM 1715 OG1 THR A 188 15.037 2.171 20.241 1.00 46.91 A O
ANISOU 1715 OG1 THR A 188 6152 6263 5407 109 -145 -328 A O
ATOM 1716 N ARG A 189 19.328 3.303 19.538 1.00 41.25 A N
ANISOU 1716 N ARG A 189 5163 5719 4790 -48 -468 -433 A N
ATOM 1717 CA ARG A 189 20.706 3.719 19.788 1.00 43.25 A C
ANISOU 1717 CA ARG A 189 5323 6039 5071 -92 -590 -484 A C
ATOM 1718 C ARG A 189 21.065 5.005 19.054 1.00 43.13 A C
ANISOU 1718 C ARG A 189 5236 5962 5188 -217 -604 -529 A C
ATOM 1719 O ARG A 189 21.880 5.794 19.550 1.00 47.59 A O
ANISOU 1719 O ARG A 189 5756 6545 5783 -279 -711 -610 A O
ATOM 1720 CB ARG A 189 21.636 2.582 19.369 1.00 47.62 A C
ANISOU 1720 CB ARG A 189 5777 6675 5639 -43 -599 -410 A C
ATOM 1721 CG ARG A 189 23.086 2.755 19.713 1.00 59.62 A C
ANISOU 1721 CG ARG A 189 7177 8284 7191 -65 -729 -448 A C
ATOM 1722 CD ARG A 189 23.814 1.455 19.384 1.00 58.83 A C
ANISOU 1722 CD ARG A 189 6996 8261 7094 20 -716 -362 A C
ATOM 1723 NE ARG A 189 23.316 0.359 20.209 1.00 48.16 A N
ANISOU 1723 NE ARG A 189 5755 6939 5606 147 -704 -318 A N
ATOM 1724 CZ ARG A 189 23.023 -0.858 19.771 1.00 51.10 A C
ANISOU 1724 CZ ARG A 189 6152 7300 5964 228 -610 -228 A C
ATOM 1725 NH1 ARG A 189 23.202 -1.203 18.508 1.00 50.44 A N
ANISOU 1725 NH1 ARG A 189 5996 7189 5979 206 -527 -180 A N
ATOM 1726 NH2 ARG A 189 22.548 -1.758 20.629 1.00 54.31 A N
ANISOU 1726 NH2 ARG A 189 6667 7718 6251 335 -595 -187 A N
ATOM 1727 N GLN A 190 20.472 5.236 17.882 1.00 41.40 A N
ANISOU 1727 N GLN A 190 5010 5667 5051 -256 -503 -476 A N
ATOM 1728 CA GLN A 190 20.711 6.439 17.102 1.00 41.96 A C
ANISOU 1728 CA GLN A 190 5032 5665 5247 -365 -493 -495 A C
ATOM 1729 C GLN A 190 19.708 7.551 17.392 1.00 43.38 A C
ANISOU 1729 C GLN A 190 5312 5735 5434 -396 -473 -552 A C
ATOM 1730 O GLN A 190 19.711 8.563 16.690 1.00 43.58 A O
ANISOU 1730 O GLN A 190 5319 5676 5564 -477 -448 -553 A O
ATOM 1731 CB GLN A 190 20.696 6.123 15.610 1.00 44.22 A C
ANISOU 1731 CB GLN A 190 5266 5932 5605 -380 -398 -399 A C
ATOM 1732 CG GLN A 190 21.836 5.251 15.145 1.00 45.12 A C
ANISOU 1732 CG GLN A 190 5267 6136 5741 -362 -400 -347 A C
ATOM 1733 CD GLN A 190 23.156 5.996 15.108 1.00 48.43 A C
ANISOU 1733 CD GLN A 190 5555 6579 6266 -452 -460 -378 A C
ATOM 1734 NE2 GLN A 190 24.244 5.270 15.272 1.00 49.95 A N
ANISOU 1734 NE2 GLN A 190 5637 6872 6469 -420 -503 -363 A N
ATOM 1735 OE1 GLN A 190 23.192 7.214 14.945 1.00 50.92 A O
ANISOU 1735 OE1 GLN A 190 5863 6817 6667 -549 -466 -415 A O
ATOM 1736 N GLY A 191 18.883 7.409 18.426 1.00 42.20 A N
ANISOU 1736 N GLY A 191 5273 5582 5179 -327 -475 -594 A N
ATOM 1737 CA GLY A 191 18.038 8.494 18.857 1.00 44.76 A C
ANISOU 1737 CA GLY A 191 5692 5806 5509 -343 -456 -662 A C
ATOM 1738 C GLY A 191 16.697 8.550 18.171 1.00 45.16 A C
ANISOU 1738 C GLY A 191 5788 5776 5592 -312 -343 -600 A C
ATOM 1739 O GLY A 191 15.972 9.540 18.343 1.00 45.26 A O
ANISOU 1739 O GLY A 191 5866 5693 5638 -323 -315 -645 A O
ATOM 1740 N GLY A 192 16.347 7.511 17.395 1.00 40.96 A N
ANISOU 1740 N GLY A 192 5224 5280 5061 -271 -284 -503 A N
ATOM 1741 CA GLY A 192 15.036 7.419 16.788 1.00 41.54 A C
ANISOU 1741 CA GLY A 192 5329 5291 5164 -238 -198 -447 A C
ATOM 1742 C GLY A 192 13.994 6.786 17.706 1.00 39.68 A C
ANISOU 1742 C GLY A 192 5163 5063 4849 -150 -146 -448 A C
ATOM 1743 O GLY A 192 14.298 6.214 18.744 1.00 40.37 A O
ANISOU 1743 O GLY A 192 5288 5213 4837 -103 -167 -474 A O
ATOM 1744 N GLU A 193 12.739 6.897 17.286 1.00 37.63 A N
ANISOU 1744 N GLU A 193 4918 4739 4641 -125 -74 -411 A N
ATOM 1745 CA GLU A 193 11.587 6.381 18.017 1.00 40.35 A C
ANISOU 1745 CA GLU A 193 5310 5074 4946 -50 2 -399 A C
ATOM 1746 C GLU A 193 10.885 5.362 17.134 1.00 40.26 A C
ANISOU 1746 C GLU A 193 5246 5066 4984 -35 45 -312 A C
ATOM 1747 O GLU A 193 10.451 5.692 16.029 1.00 40.36 A O
ANISOU 1747 O GLU A 193 5217 5034 5083 -64 43 -278 A O
ATOM 1748 CB GLU A 193 10.649 7.534 18.386 1.00 44.50 A C
ANISOU 1748 CB GLU A 193 5883 5510 5514 -32 48 -443 A C
ATOM 1749 CG GLU A 193 9.345 7.142 19.057 1.00 62.17 A C
ANISOU 1749 CG GLU A 193 8154 7729 7740 47 152 -423 A C
ATOM 1750 CD GLU A 193 9.510 6.794 20.527 1.00 67.22 A C
ANISOU 1750 CD GLU A 193 8884 8416 8242 108 181 -467 A C
ATOM 1751 OE1 GLU A 193 8.482 6.531 21.181 1.00 73.70 A O
ANISOU 1751 OE1 GLU A 193 9738 9218 9045 177 288 -448 A O
ATOM 1752 OE2 GLU A 193 10.652 6.810 21.030 1.00 60.40 A O
ANISOU 1752 OE2 GLU A 193 8054 7608 7287 91 97 -519 A O
ATOM 1753 N VAL A 194 10.774 4.127 17.606 1.00 36.56 A N
ANISOU 1753 N VAL A 194 4787 4644 4460 11 79 -277 A N
ATOM 1754 CA VAL A 194 9.973 3.141 16.890 1.00 35.68 A C
ANISOU 1754 CA VAL A 194 4632 4517 4406 20 122 -209 A C
ATOM 1755 C VAL A 194 8.528 3.369 17.312 1.00 38.93 A C
ANISOU 1755 C VAL A 194 5049 4870 4873 56 206 -200 A C
ATOM 1756 O VAL A 194 8.191 3.241 18.492 1.00 41.67 A O
ANISOU 1756 O VAL A 194 5449 5222 5162 108 274 -210 A O
ATOM 1757 CB VAL A 194 10.433 1.712 17.193 1.00 46.64 A C
ANISOU 1757 CB VAL A 194 6029 5958 5734 52 134 -171 A C
ATOM 1758 CG1 VAL A 194 9.537 0.714 16.501 1.00 47.87 A C
ANISOU 1758 CG1 VAL A 194 6147 6078 5964 51 178 -114 A C
ATOM 1759 CG2 VAL A 194 11.865 1.526 16.734 1.00 43.42 A C
ANISOU 1759 CG2 VAL A 194 5599 5610 5289 27 57 -178 A C
ATOM 1760 N THR A 195 7.680 3.745 16.368 1.00 36.39 A N
ANISOU 1760 N THR A 195 4672 4496 4659 35 205 -177 A N
ATOM 1761 CA THR A 195 6.323 4.126 16.742 1.00 37.02 A C
ANISOU 1761 CA THR A 195 4732 4519 4813 72 283 -169 A C
ATOM 1762 C THR A 195 5.272 3.069 16.426 1.00 41.03 A C
ANISOU 1762 C THR A 195 5171 5011 5407 78 330 -111 A C
ATOM 1763 O THR A 195 4.251 3.005 17.120 1.00 41.53 A O
ANISOU 1763 O THR A 195 5216 5044 5520 119 427 -95 A O
ATOM 1764 CB THR A 195 5.949 5.460 16.079 1.00 42.88 A C
ANISOU 1764 CB THR A 195 5454 5203 5635 60 250 -186 A C
ATOM 1765 CG2 THR A 195 5.758 5.335 14.572 1.00 40.29 A C
ANISOU 1765 CG2 THR A 195 5061 4865 5382 21 177 -141 A C
ATOM 1766 OG1 THR A 195 4.751 5.962 16.682 1.00 40.83 A O
ANISOU 1766 OG1 THR A 195 5182 4890 5441 114 336 -188 A O
ATOM 1767 N LYS A 196 5.484 2.222 15.430 1.00 35.82 A N
ANISOU 1767 N LYS A 196 4472 4366 4772 38 271 -83 A N
ATOM 1768 CA LYS A 196 4.472 1.228 15.114 1.00 36.82 A C
ANISOU 1768 CA LYS A 196 4530 4464 4995 30 302 -41 A C
ATOM 1769 C LYS A 196 5.080 0.062 14.349 1.00 37.82 A C
ANISOU 1769 C LYS A 196 4660 4611 5098 -6 247 -28 A C
ATOM 1770 O LYS A 196 5.975 0.249 13.524 1.00 37.59 A O
ANISOU 1770 O LYS A 196 4654 4611 5018 -30 166 -44 A O
ATOM 1771 CB LYS A 196 3.362 1.871 14.276 1.00 42.12 A C
ANISOU 1771 CB LYS A 196 5116 5090 5796 20 267 -31 A C
ATOM 1772 CG LYS A 196 2.070 1.113 14.243 1.00 51.63 A C
ANISOU 1772 CG LYS A 196 6225 6258 7136 14 311 4 A C
ATOM 1773 CD LYS A 196 0.998 1.883 13.462 1.00 53.83 A C
ANISOU 1773 CD LYS A 196 6407 6502 7545 17 258 12 A C
ATOM 1774 CE LYS A 196 0.757 3.309 13.950 1.00 63.12 A C
ANISOU 1774 CE LYS A 196 7596 7656 8729 72 299 0 A C
ATOM 1775 NZ LYS A 196 -0.260 3.335 15.027 1.00 44.84 A N
ANISOU 1775 NZ LYS A 196 5231 5311 6497 122 439 17 A N
ATOM 1776 N PHE A 197 4.560 -1.133 14.619 1.00 36.70 A N
ANISOU 1776 N PHE A 197 4496 4444 5003 -9 303 4 A N
ATOM 1777 CA PHE A 197 4.798 -2.311 13.793 1.00 35.16 A C
ANISOU 1777 CA PHE A 197 4297 4240 4825 -44 256 10 A C
ATOM 1778 C PHE A 197 3.558 -2.546 12.938 1.00 39.96 A C
ANISOU 1778 C PHE A 197 4811 4794 5576 -86 218 13 A C
ATOM 1779 O PHE A 197 2.428 -2.520 13.447 1.00 37.64 A O
ANISOU 1779 O PHE A 197 4447 4461 5393 -84 285 36 A O
ATOM 1780 CB PHE A 197 5.071 -3.549 14.639 1.00 38.64 A C
ANISOU 1780 CB PHE A 197 4779 4669 5233 -22 339 44 A C
ATOM 1781 CG PHE A 197 6.260 -3.413 15.538 1.00 38.84 A C
ANISOU 1781 CG PHE A 197 4890 4755 5114 29 360 44 A C
ATOM 1782 CD1 PHE A 197 7.508 -3.158 15.009 1.00 38.60 A C
ANISOU 1782 CD1 PHE A 197 4890 4778 4997 27 278 15 A C
ATOM 1783 CD2 PHE A 197 6.116 -3.515 16.906 1.00 47.34 A C
ANISOU 1783 CD2 PHE A 197 6011 5836 6141 81 460 74 A C
ATOM 1784 CE1 PHE A 197 8.612 -3.028 15.839 1.00 38.25 A C
ANISOU 1784 CE1 PHE A 197 4903 4795 4836 71 278 11 A C
ATOM 1785 CE2 PHE A 197 7.212 -3.379 17.744 1.00 43.43 A C
ANISOU 1785 CE2 PHE A 197 5596 5404 5502 133 454 68 A C
ATOM 1786 CZ PHE A 197 8.451 -3.137 17.213 1.00 40.95 A C
ANISOU 1786 CZ PHE A 197 5294 5146 5121 124 354 34 A C
ATOM 1787 N ILE A 198 3.759 -2.773 11.646 1.00 37.87 A N
ANISOU 1787 N ILE A 198 4546 4531 5312 -122 110 -12 A N
ATOM 1788 CA ILE A 198 2.656 -2.935 10.700 1.00 37.87 A C
ANISOU 1788 CA ILE A 198 4464 4492 5434 -162 33 -23 A C
ATOM 1789 C ILE A 198 2.914 -4.250 9.967 1.00 38.58 A C
ANISOU 1789 C ILE A 198 4584 4555 5520 -201 -15 -48 A C
ATOM 1790 O ILE A 198 3.553 -4.281 8.913 1.00 40.72 A O
ANISOU 1790 O ILE A 198 4910 4850 5710 -207 -103 -80 A O
ATOM 1791 CB ILE A 198 2.535 -1.754 9.733 1.00 39.80 A C
ANISOU 1791 CB ILE A 198 4695 4761 5666 -156 -70 -35 A C
ATOM 1792 CG1 ILE A 198 2.431 -0.439 10.512 1.00 41.16 A C
ANISOU 1792 CG1 ILE A 198 4859 4945 5837 -113 -13 -17 A C
ATOM 1793 CG2 ILE A 198 1.319 -1.916 8.843 1.00 41.41 A C
ANISOU 1793 CG2 ILE A 198 4805 4932 5995 -188 -166 -44 A C
ATOM 1794 CD1 ILE A 198 2.727 0.811 9.696 1.00 47.29 A C
ANISOU 1794 CD1 ILE A 198 5660 5740 6567 -98 -93 -18 A C
ATOM 1795 N GLY A 199 2.427 -5.354 10.529 1.00 39.97 A N
ANISOU 1795 N GLY A 199 4732 4672 5783 -225 55 -33 A N
ATOM 1796 CA GLY A 199 2.721 -6.650 9.947 1.00 40.03 A C
ANISOU 1796 CA GLY A 199 4783 4633 5791 -258 24 -62 A C
ATOM 1797 C GLY A 199 4.197 -6.976 10.068 1.00 38.93 A C
ANISOU 1797 C GLY A 199 4759 4533 5498 -213 52 -62 A C
ATOM 1798 O GLY A 199 4.697 -7.158 11.179 1.00 39.74 A O
ANISOU 1798 O GLY A 199 4896 4648 5556 -171 153 -19 A O
ATOM 1799 N ASP A 200 4.901 -7.048 8.935 1.00 34.07 A N
ANISOU 1799 N ASP A 200 4203 3943 4798 -213 -36 -107 A N
ATOM 1800 CA ASP A 200 6.338 -7.309 8.891 1.00 34.55 A C
ANISOU 1800 CA ASP A 200 4354 4048 4727 -165 -12 -108 A C
ATOM 1801 C ASP A 200 7.148 -6.034 8.694 1.00 38.49 A C
ANISOU 1801 C ASP A 200 4867 4635 5122 -136 -37 -102 A C
ATOM 1802 O ASP A 200 8.266 -6.080 8.168 1.00 37.86 A O
ANISOU 1802 O ASP A 200 4843 4597 4945 -109 -48 -113 A O
ATOM 1803 CB ASP A 200 6.647 -8.289 7.763 1.00 36.14 A C
ANISOU 1803 CB ASP A 200 4617 4211 4902 -177 -67 -161 A C
ATOM 1804 CG ASP A 200 6.437 -7.669 6.384 1.00 35.64 A C
ANISOU 1804 CG ASP A 200 4566 4177 4799 -198 -184 -208 A C
ATOM 1805 OD1 ASP A 200 5.642 -6.716 6.287 1.00 37.84 A O
ANISOU 1805 OD1 ASP A 200 4780 4474 5123 -218 -234 -197 A O
ATOM 1806 OD2 ASP A 200 7.022 -8.131 5.388 1.00 36.49 A O
ANISOU 1806 OD2 ASP A 200 4752 4285 4826 -185 -224 -252 A O
ATOM 1807 N CYS A 201 6.601 -4.895 9.100 1.00 37.24 A N
ANISOU 1807 N CYS A 201 4657 4497 4996 -140 -39 -83 A N
ATOM 1808 CA CYS A 201 7.163 -3.591 8.776 1.00 35.28 A C
ANISOU 1808 CA CYS A 201 4418 4307 4678 -128 -72 -80 A C
ATOM 1809 C CYS A 201 7.364 -2.779 10.045 1.00 41.29 A C
ANISOU 1809 C CYS A 201 5165 5093 5429 -104 -8 -57 A C
ATOM 1810 O CYS A 201 6.523 -2.804 10.948 1.00 36.32 A O
ANISOU 1810 O CYS A 201 4499 4433 4866 -99 46 -42 A O
ATOM 1811 CB CYS A 201 6.237 -2.848 7.802 1.00 41.19 A C
ANISOU 1811 CB CYS A 201 5133 5042 5475 -151 -158 -89 A C
ATOM 1812 SG CYS A 201 6.537 -1.098 7.677 1.00 44.87 A S
ANISOU 1812 SG CYS A 201 5599 5545 5903 -136 -175 -66 A S
ATOM 1813 N VAL A 202 8.498 -2.082 10.117 1.00 34.46 A N
ANISOU 1813 N VAL A 202 4330 4281 4481 -89 -9 -58 A N
ATOM 1814 CA AVAL A 202 8.841 -1.150 11.188 0.74 34.60 A C
ANISOU 1814 CA AVAL A 202 4348 4325 4474 -73 25 -57 A C
ATOM 1815 CA BVAL A 202 8.758 -1.157 11.209 0.26 34.82 A C
ANISOU 1815 CA BVAL A 202 4373 4349 4506 -73 26 -56 A C
ATOM 1816 C VAL A 202 8.616 0.271 10.691 1.00 35.78 A C
ANISOU 1816 C VAL A 202 4484 4466 4645 -92 -14 -62 A C
ATOM 1817 O VAL A 202 9.182 0.648 9.658 1.00 37.22 A O
ANISOU 1817 O VAL A 202 4681 4665 4797 -109 -57 -58 A O
ATOM 1818 CB AVAL A 202 10.318 -1.303 11.609 0.74 37.13 A C
ANISOU 1818 CB AVAL A 202 4697 4705 4706 -53 33 -61 A C
ATOM 1819 CB BVAL A 202 10.129 -1.406 11.862 0.26 38.27 A C
ANISOU 1819 CB BVAL A 202 4841 4842 4857 -48 45 -59 A C
ATOM 1820 CG1AVAL A 202 10.712 -0.160 12.531 0.74 35.09 A C
ANISOU 1820 CG1AVAL A 202 4441 4470 4421 -50 37 -78 A C
ATOM 1821 CG1BVAL A 202 11.243 -1.105 10.907 0.26 42.13 A C
ANISOU 1821 CG1BVAL A 202 5334 5371 5302 -63 5 -64 A C
ATOM 1822 CG2AVAL A 202 10.574 -2.631 12.256 0.74 39.57 A C
ANISOU 1822 CG2AVAL A 202 5027 5017 4991 -17 76 -45 A C
ATOM 1823 CG2BVAL A 202 10.266 -0.590 13.154 0.26 33.27 A C
ANISOU 1823 CG2BVAL A 202 4217 4227 4195 -30 70 -71 A C
ATOM 1824 N MET A 203 7.839 1.068 11.433 1.00 34.61 A N
ANISOU 1824 N MET A 203 4317 4290 4545 -81 14 -64 A N
ATOM 1825 CA AMET A 203 7.705 2.496 11.193 0.44 35.91 A C
ANISOU 1825 CA AMET A 203 4478 4432 4732 -88 -9 -69 A C
ATOM 1826 CA BMET A 203 7.694 2.498 11.197 0.56 35.87 A C
ANISOU 1826 CA BMET A 203 4473 4426 4728 -88 -9 -69 A C
ATOM 1827 C MET A 203 8.339 3.250 12.355 1.00 37.44 A C
ANISOU 1827 C MET A 203 4704 4636 4885 -78 26 -99 A C
ATOM 1828 O MET A 203 7.992 3.024 13.522 1.00 36.82 A O
ANISOU 1828 O MET A 203 4637 4556 4796 -47 83 -113 A O
ATOM 1829 CB AMET A 203 6.236 2.900 11.038 0.44 37.96 A C
ANISOU 1829 CB AMET A 203 4690 4639 5095 -73 -10 -54 A C
ATOM 1830 CB BMET A 203 6.218 2.874 11.059 0.56 37.96 A C
ANISOU 1830 CB BMET A 203 4688 4638 5095 -73 -9 -54 A C
ATOM 1831 CG AMET A 203 6.044 4.374 10.736 0.44 37.42 A C
ANISOU 1831 CG AMET A 203 4626 4534 5059 -67 -32 -50 A C
ATOM 1832 CG BMET A 203 5.933 4.363 11.090 0.56 38.40 A C
ANISOU 1832 CG BMET A 203 4748 4655 5189 -60 -12 -56 A C
ATOM 1833 SD AMET A 203 4.319 4.779 10.418 0.44 43.18 A S
ANISOU 1833 SD AMET A 203 5277 5207 5921 -33 -47 -23 A S
ATOM 1834 SD BMET A 203 4.160 4.665 11.144 0.56 39.16 A S
ANISOU 1834 SD BMET A 203 4763 4695 5422 -21 3 -34 A S
ATOM 1835 CE AMET A 203 4.377 6.542 10.687 0.44 40.20 A C
ANISOU 1835 CE AMET A 203 4934 4774 5566 -7 -28 -27 A C
ATOM 1836 CE BMET A 203 4.161 6.419 11.471 0.56 41.79 A C
ANISOU 1836 CE BMET A 203 5130 4972 5777 8 24 -46 A C
ATOM 1837 N ALA A 204 9.274 4.140 12.037 1.00 36.65 A N
ANISOU 1837 N ALA A 204 4623 4544 4759 -106 -5 -112 A N
ATOM 1838 CA ALA A 204 9.998 4.876 13.059 1.00 33.78 A C
ANISOU 1838 CA ALA A 204 4288 4187 4359 -111 4 -157 A C
ATOM 1839 C ALA A 204 10.196 6.305 12.587 1.00 33.98 A C
ANISOU 1839 C ALA A 204 4323 4161 4428 -145 -19 -165 A C
ATOM 1840 O ALA A 204 9.984 6.622 11.414 1.00 36.32 A O
ANISOU 1840 O ALA A 204 4607 4430 4761 -160 -40 -122 A O
ATOM 1841 CB ALA A 204 11.358 4.222 13.356 1.00 37.21 A C
ANISOU 1841 CB ALA A 204 4724 4695 4719 -121 -16 -170 A C
ATOM 1842 N TYR A 205 10.619 7.175 13.502 1.00 37.05 A N
ANISOU 1842 N TYR A 205 4742 4529 4806 -156 -17 -221 A N
ATOM 1843 CA TYR A 205 10.944 8.524 13.077 1.00 38.83 A C
ANISOU 1843 CA TYR A 205 4981 4689 5086 -199 -34 -231 A C
ATOM 1844 C TYR A 205 12.075 9.116 13.904 1.00 39.02 A C
ANISOU 1844 C TYR A 205 5022 4719 5085 -243 -62 -302 A C
ATOM 1845 O TYR A 205 12.366 8.686 15.027 1.00 39.69 A O
ANISOU 1845 O TYR A 205 5127 4853 5101 -222 -71 -356 A O
ATOM 1846 CB TYR A 205 9.709 9.448 13.106 1.00 39.39 A C
ANISOU 1846 CB TYR A 205 5073 4666 5228 -163 -4 -229 A C
ATOM 1847 CG TYR A 205 8.965 9.589 14.420 1.00 39.84 A C
ANISOU 1847 CG TYR A 205 5164 4700 5275 -108 44 -286 A C
ATOM 1848 CD1 TYR A 205 9.350 10.528 15.373 1.00 45.03 A C
ANISOU 1848 CD1 TYR A 205 5881 5312 5916 -117 48 -368 A C
ATOM 1849 CD2 TYR A 205 7.824 8.842 14.665 1.00 45.32 A C
ANISOU 1849 CD2 TYR A 205 5833 5407 5981 -48 93 -258 A C
ATOM 1850 CE1 TYR A 205 8.641 10.675 16.557 1.00 47.68 A C
ANISOU 1850 CE1 TYR A 205 6267 5626 6223 -54 106 -423 A C
ATOM 1851 CE2 TYR A 205 7.114 8.976 15.838 1.00 44.48 A C
ANISOU 1851 CE2 TYR A 205 5759 5279 5864 10 163 -299 A C
ATOM 1852 CZ TYR A 205 7.516 9.897 16.777 1.00 51.59 A C
ANISOU 1852 CZ TYR A 205 6736 6142 6726 14 173 -381 A C
ATOM 1853 OH TYR A 205 6.797 10.030 17.944 1.00 52.84 A O
ANISOU 1853 OH TYR A 205 6944 6279 6853 83 255 -425 A O
ATOM 1854 N PHE A 206 12.721 10.111 13.290 1.00 38.41 A N
ANISOU 1854 N PHE A 206 4938 4590 5066 -307 -79 -297 A N
ATOM 1855 CA PHE A 206 13.822 10.874 13.858 1.00 40.04 A C
ANISOU 1855 CA PHE A 206 5144 4780 5288 -375 -117 -365 A C
ATOM 1856 C PHE A 206 13.463 12.355 13.793 1.00 42.48 A C
ANISOU 1856 C PHE A 206 5500 4957 5684 -403 -103 -389 A C
ATOM 1857 O PHE A 206 12.620 12.768 12.992 1.00 42.63 A O
ANISOU 1857 O PHE A 206 5534 4908 5754 -376 -67 -326 A O
ATOM 1858 CB PHE A 206 15.135 10.644 13.080 1.00 39.19 A C
ANISOU 1858 CB PHE A 206 4965 4725 5199 -441 -138 -326 A C
ATOM 1859 CG PHE A 206 15.654 9.222 13.124 1.00 39.26 A C
ANISOU 1859 CG PHE A 206 4927 4856 5132 -409 -150 -304 A C
ATOM 1860 CD1 PHE A 206 15.041 8.215 12.389 1.00 39.25 A C
ANISOU 1860 CD1 PHE A 206 4926 4890 5096 -355 -117 -236 A C
ATOM 1861 CD2 PHE A 206 16.785 8.903 13.869 1.00 44.06 A C
ANISOU 1861 CD2 PHE A 206 5491 5538 5712 -431 -203 -354 A C
ATOM 1862 CE1 PHE A 206 15.523 6.908 12.422 1.00 40.55 A C
ANISOU 1862 CE1 PHE A 206 5059 5148 5200 -321 -121 -219 A C
ATOM 1863 CE2 PHE A 206 17.272 7.601 13.903 1.00 40.18 A C
ANISOU 1863 CE2 PHE A 206 4958 5150 5159 -388 -210 -326 A C
ATOM 1864 CZ PHE A 206 16.645 6.607 13.179 1.00 39.90 A C
ANISOU 1864 CZ PHE A 206 4934 5135 5091 -333 -162 -258 A C
ATOM 1865 N ASP A 207 14.127 13.161 14.623 1.00 43.41 A N
ANISOU 1865 N ASP A 207 5641 5031 5820 -456 -139 -484 A N
ATOM 1866 CA ASP A 207 14.005 14.608 14.499 1.00 44.66 A C
ANISOU 1866 CA ASP A 207 5845 5044 6079 -500 -126 -511 A C
ATOM 1867 C ASP A 207 14.392 15.049 13.092 1.00 42.09 A C
ANISOU 1867 C ASP A 207 5481 4671 5842 -557 -99 -406 A C
ATOM 1868 O ASP A 207 15.189 14.401 12.408 1.00 44.03 A O
ANISOU 1868 O ASP A 207 5657 4998 6073 -592 -103 -347 A O
ATOM 1869 CB ASP A 207 14.897 15.330 15.511 1.00 45.57 A C
ANISOU 1869 CB ASP A 207 5983 5123 6208 -573 -188 -639 A C
ATOM 1870 CG ASP A 207 14.359 15.272 16.920 1.00 63.13 A C
ANISOU 1870 CG ASP A 207 8291 7356 8339 -506 -203 -751 A C
ATOM 1871 OD1 ASP A 207 13.167 14.957 17.099 1.00 55.61 A O
ANISOU 1871 OD1 ASP A 207 7382 6402 7345 -406 -140 -725 A O
ATOM 1872 OD2 ASP A 207 15.138 15.561 17.853 1.00 58.89 A O
ANISOU 1872 OD2 ASP A 207 7776 6828 7771 -553 -278 -866 A O
ATOM 1873 N GLY A 208 13.839 16.189 12.671 1.00 44.53 A N
ANISOU 1873 N GLY A 208 5842 4839 6238 -558 -62 -381 A N
ATOM 1874 CA GLY A 208 14.006 16.640 11.301 1.00 42.61 A C
ANISOU 1874 CA GLY A 208 5586 4541 6063 -589 -23 -261 A C
ATOM 1875 C GLY A 208 15.426 17.005 10.932 1.00 47.11 A C
ANISOU 1875 C GLY A 208 6102 5100 6698 -709 -24 -250 A C
ATOM 1876 O GLY A 208 15.778 16.979 9.749 1.00 51.24 A O
ANISOU 1876 O GLY A 208 6601 5628 7241 -730 21 -136 A O
ATOM 1877 N ASP A 209 16.251 17.344 11.912 1.00 46.11 A N
ANISOU 1877 N ASP A 209 5955 4960 6606 -787 -73 -365 A N
ATOM 1878 CA ASP A 209 17.644 17.677 11.649 1.00 50.43 A C
ANISOU 1878 CA ASP A 209 6420 5500 7241 -912 -81 -363 A C
ATOM 1879 C ASP A 209 18.580 16.510 11.949 1.00 47.20 A C
ANISOU 1879 C ASP A 209 5908 5261 6765 -926 -130 -386 A C
ATOM 1880 O ASP A 209 19.789 16.714 12.101 1.00 48.69 A O
ANISOU 1880 O ASP A 209 6007 5464 7031 -1028 -162 -420 A O
ATOM 1881 CB ASP A 209 18.045 18.918 12.450 1.00 52.33 A C
ANISOU 1881 CB ASP A 209 6690 5599 7592 -1007 -119 -479 A C
ATOM 1882 CG ASP A 209 17.927 18.719 13.943 1.00 59.19 A C
ANISOU 1882 CG ASP A 209 7596 6509 8383 -981 -210 -641 A C
ATOM 1883 OD1 ASP A 209 17.354 17.697 14.370 1.00 61.84 A O
ANISOU 1883 OD1 ASP A 209 7946 6966 8584 -879 -224 -648 A O
ATOM 1884 OD2 ASP A 209 18.402 19.593 14.697 1.00 72.80 A O
ANISOU 1884 OD2 ASP A 209 9343 8139 10180 -1064 -265 -763 A O
ATOM 1885 N CYS A 210 18.053 15.289 12.010 1.00 41.65 A N
ANISOU 1885 N CYS A 210 5207 4682 5934 -825 -136 -364 A N
ATOM 1886 CA CYS A 210 18.848 14.101 12.317 1.00 45.08 A C
ANISOU 1886 CA CYS A 210 5556 5272 6300 -815 -179 -378 A C
ATOM 1887 C CYS A 210 18.937 13.142 11.128 1.00 44.56 A C
ANISOU 1887 C CYS A 210 5450 5291 6191 -772 -116 -257 A C
ATOM 1888 O CYS A 210 18.884 11.920 11.280 1.00 42.60 A O
ANISOU 1888 O CYS A 210 5183 5155 5847 -703 -130 -251 A O
ATOM 1889 CB CYS A 210 18.274 13.406 13.550 1.00 42.49 A C
ANISOU 1889 CB CYS A 210 5276 5013 5856 -734 -238 -465 A C
ATOM 1890 SG CYS A 210 18.564 14.400 15.030 1.00 50.27 A S
ANISOU 1890 SG CYS A 210 6307 5930 6863 -789 -329 -631 A S
ATOM 1891 N ALA A 211 19.124 13.686 9.926 1.00 44.52 A N
ANISOU 1891 N ALA A 211 5441 5224 6250 -810 -41 -159 A N
ATOM 1892 CA ALA A 211 19.257 12.828 8.754 1.00 40.79 A C
ANISOU 1892 CA ALA A 211 4949 4829 5721 -766 22 -52 A C
ATOM 1893 C ALA A 211 20.491 11.943 8.857 1.00 39.79 A C
ANISOU 1893 C ALA A 211 4708 4824 5588 -785 16 -59 A C
ATOM 1894 O ALA A 211 20.462 10.778 8.441 1.00 40.93 A O
ANISOU 1894 O ALA A 211 4846 5063 5643 -712 36 -21 A O
ATOM 1895 CB ALA A 211 19.331 13.672 7.482 1.00 47.14 A C
ANISOU 1895 CB ALA A 211 5782 5543 6584 -802 112 60 A C
ATOM 1896 N ASP A 212 21.598 12.488 9.373 1.00 44.32 A N
ANISOU 1896 N ASP A 212 5185 5388 6265 -881 -13 -107 A N
ATOM 1897 CA ASP A 212 22.816 11.691 9.484 1.00 43.14 A C
ANISOU 1897 CA ASP A 212 4904 5358 6130 -893 -24 -110 A C
ATOM 1898 C ASP A 212 22.576 10.457 10.344 1.00 47.31 A C
ANISOU 1898 C ASP A 212 5438 5998 6539 -798 -99 -166 A C
ATOM 1899 O ASP A 212 23.020 9.350 10.000 1.00 43.06 A O
ANISOU 1899 O ASP A 212 4849 5561 5951 -739 -72 -124 A O
ATOM 1900 CB ASP A 212 23.960 12.524 10.065 1.00 45.46 A C
ANISOU 1900 CB ASP A 212 5080 5624 6571 -1018 -73 -171 A C
ATOM 1901 CG ASP A 212 24.429 13.617 9.124 1.00 49.00 A C
ANISOU 1901 CG ASP A 212 5496 5962 7161 -1121 26 -94 A C
ATOM 1902 OD1 ASP A 212 24.705 13.316 7.951 1.00 47.19 A O
ANISOU 1902 OD1 ASP A 212 5247 5757 6926 -1101 145 24 A O
ATOM 1903 OD2 ASP A 212 24.536 14.781 9.561 1.00 55.89 A O
ANISOU 1903 OD2 ASP A 212 6370 6717 8147 -1222 -8 -150 A O
ATOM 1904 N GLN A 213 21.873 10.627 11.470 1.00 41.48 A N
ANISOU 1904 N GLN A 213 4771 5237 5753 -776 -182 -257 A N
ATOM 1905 CA GLN A 213 21.594 9.482 12.337 1.00 40.78 A C
ANISOU 1905 CA GLN A 213 4703 5244 5546 -682 -240 -298 A C
ATOM 1906 C GLN A 213 20.641 8.495 11.677 1.00 38.69 A C
ANISOU 1906 C GLN A 213 4511 5002 5188 -585 -176 -229 A C
ATOM 1907 O GLN A 213 20.785 7.280 11.848 1.00 40.06 A O
ANISOU 1907 O GLN A 213 4668 5264 5289 -513 -183 -217 A O
ATOM 1908 CB GLN A 213 21.036 9.943 13.688 1.00 41.17 A C
ANISOU 1908 CB GLN A 213 4828 5261 5554 -675 -324 -407 A C
ATOM 1909 CG GLN A 213 21.955 10.790 14.593 1.00 46.98 A C
ANISOU 1909 CG GLN A 213 5509 5983 6359 -765 -425 -510 A C
ATOM 1910 CD GLN A 213 22.377 12.148 14.036 1.00 62.58 A C
ANISOU 1910 CD GLN A 213 7448 7841 8489 -891 -400 -512 A C
ATOM 1911 NE2 GLN A 213 23.510 12.645 14.518 1.00 95.57 A N
ANISOU 1911 NE2 GLN A 213 11523 12027 12762 -988 -483 -581 A N
ATOM 1912 OE1 GLN A 213 21.688 12.756 13.224 1.00 53.88 A O
ANISOU 1912 OE1 GLN A 213 6410 6637 7426 -901 -314 -453 A O
ATOM 1913 N ALA A 214 19.648 8.988 10.932 1.00 40.17 A N
ANISOU 1913 N ALA A 214 4778 5105 5378 -579 -122 -185 A N
ATOM 1914 CA ALA A 214 18.737 8.089 10.229 1.00 41.04 A C
ANISOU 1914 CA ALA A 214 4948 5234 5412 -498 -80 -128 A C
ATOM 1915 C ALA A 214 19.475 7.268 9.175 1.00 38.29 A C
ANISOU 1915 C ALA A 214 4554 4952 5045 -480 -24 -59 A C
ATOM 1916 O ALA A 214 19.208 6.068 9.003 1.00 37.18 A O
ANISOU 1916 O ALA A 214 4432 4866 4830 -408 -15 -44 A O
ATOM 1917 CB ALA A 214 17.611 8.896 9.580 1.00 38.92 A C
ANISOU 1917 CB ALA A 214 4760 4866 5163 -496 -50 -92 A C
ATOM 1918 N ILE A 215 20.382 7.904 8.441 1.00 36.28 A N
ANISOU 1918 N ILE A 215 4242 4682 4859 -543 25 -14 A N
ATOM 1919 CA ILE A 215 21.171 7.187 7.441 1.00 34.14 A C
ANISOU 1919 CA ILE A 215 3929 4475 4570 -519 100 52 A C
ATOM 1920 C ILE A 215 22.053 6.151 8.120 1.00 38.24 A C
ANISOU 1920 C ILE A 215 4357 5095 5076 -483 70 19 A C
ATOM 1921 O ILE A 215 22.143 4.998 7.678 1.00 37.22 A O
ANISOU 1921 O ILE A 215 4237 5023 4882 -408 106 45 A O
ATOM 1922 CB ILE A 215 21.984 8.178 6.592 1.00 37.30 A C
ANISOU 1922 CB ILE A 215 4280 4832 5060 -598 179 116 A C
ATOM 1923 CG1 ILE A 215 21.049 9.012 5.698 1.00 40.23 A C
ANISOU 1923 CG1 ILE A 215 4764 5106 5415 -603 220 176 A C
ATOM 1924 CG2 ILE A 215 23.021 7.451 5.718 1.00 41.16 A C
ANISOU 1924 CG2 ILE A 215 4702 5398 5540 -572 273 179 A C
ATOM 1925 CD1 ILE A 215 21.732 10.173 4.973 1.00 42.07 A C
ANISOU 1925 CD1 ILE A 215 4971 5269 5746 -687 305 248 A C
ATOM 1926 N GLN A 216 22.714 6.546 9.212 1.00 40.06 A N
ANISOU 1926 N GLN A 216 4506 5346 5370 -531 -4 -43 A N
ATOM 1927 CA GLN A 216 23.624 5.634 9.899 1.00 38.27 A C
ANISOU 1927 CA GLN A 216 4183 5221 5136 -489 -49 -68 A C
ATOM 1928 C GLN A 216 22.875 4.436 10.468 1.00 40.07 A C
ANISOU 1928 C GLN A 216 4489 5485 5249 -385 -83 -87 A C
ATOM 1929 O GLN A 216 23.347 3.298 10.373 1.00 39.56 A O
ANISOU 1929 O GLN A 216 4392 5490 5151 -311 -63 -62 A O
ATOM 1930 CB GLN A 216 24.369 6.371 11.011 1.00 39.39 A C
ANISOU 1930 CB GLN A 216 4234 5376 5356 -562 -151 -142 A C
ATOM 1931 CG GLN A 216 25.449 5.531 11.688 1.00 44.86 A C
ANISOU 1931 CG GLN A 216 4807 6183 6055 -518 -215 -161 A C
ATOM 1932 CD GLN A 216 26.586 5.207 10.754 1.00 45.02 A C
ANISOU 1932 CD GLN A 216 4692 6255 6157 -522 -128 -90 A C
ATOM 1933 NE2 GLN A 216 26.707 3.937 10.392 1.00 49.07 A N
ANISOU 1933 NE2 GLN A 216 5209 6831 6604 -413 -77 -45 A N
ATOM 1934 OE1 GLN A 216 27.343 6.089 10.349 1.00 48.30 A O
ANISOU 1934 OE1 GLN A 216 5004 6647 6701 -620 -97 -75 A O
ATOM 1935 N ALA A 217 21.720 4.677 11.091 1.00 38.41 A N
ANISOU 1935 N ALA A 217 4381 5224 4990 -376 -123 -127 A N
ATOM 1936 CA ALA A 217 20.901 3.576 11.580 1.00 37.00 A C
ANISOU 1936 CA ALA A 217 4278 5063 4717 -286 -133 -132 A C
ATOM 1937 C ALA A 217 20.560 2.605 10.461 1.00 36.94 A C
ANISOU 1937 C ALA A 217 4310 5055 4672 -231 -58 -74 A C
ATOM 1938 O ALA A 217 20.594 1.380 10.652 1.00 37.65 A O
ANISOU 1938 O ALA A 217 4411 5183 4712 -156 -51 -64 A O
ATOM 1939 CB ALA A 217 19.614 4.119 12.205 1.00 38.87 A C
ANISOU 1939 CB ALA A 217 4611 5231 4927 -290 -156 -170 A C
ATOM 1940 N SER A 218 20.170 3.134 9.305 1.00 36.49 A N
ANISOU 1940 N SER A 218 4288 4946 4631 -264 -5 -37 A N
ATOM 1941 CA SER A 218 19.801 2.277 8.185 1.00 37.31 A C
ANISOU 1941 CA SER A 218 4446 5045 4682 -214 53 4 A C
ATOM 1942 C SER A 218 20.976 1.422 7.744 1.00 38.79 A C
ANISOU 1942 C SER A 218 4573 5300 4865 -171 104 30 A C
ATOM 1943 O SER A 218 20.824 0.221 7.485 1.00 36.90 A O
ANISOU 1943 O SER A 218 4375 5075 4572 -99 127 34 A O
ATOM 1944 CB SER A 218 19.307 3.130 7.014 1.00 39.62 A C
ANISOU 1944 CB SER A 218 4793 5281 4981 -252 90 43 A C
ATOM 1945 OG SER A 218 18.212 3.929 7.406 1.00 38.61 A O
ANISOU 1945 OG SER A 218 4712 5087 4870 -278 45 23 A O
ATOM 1946 N LEU A 219 22.152 2.033 7.631 1.00 36.26 A N
ANISOU 1946 N LEU A 219 4151 5014 4611 -215 128 48 A N
ATOM 1947 CA LEU A 219 23.335 1.300 7.203 1.00 37.95 A C
ANISOU 1947 CA LEU A 219 4285 5296 4840 -169 191 78 A C
ATOM 1948 C LEU A 219 23.696 0.226 8.220 1.00 40.23 A C
ANISOU 1948 C LEU A 219 4533 5642 5112 -95 138 52 A C
ATOM 1949 O LEU A 219 24.066 -0.896 7.852 1.00 39.22 A O
ANISOU 1949 O LEU A 219 4406 5543 4953 -11 189 72 A O
ATOM 1950 CB LEU A 219 24.488 2.284 7.020 1.00 38.58 A C
ANISOU 1950 CB LEU A 219 4237 5397 5026 -245 224 104 A C
ATOM 1951 CG LEU A 219 24.426 3.113 5.734 1.00 39.59 A C
ANISOU 1951 CG LEU A 219 4404 5475 5165 -295 322 163 A C
ATOM 1952 CD1 LEU A 219 25.567 4.134 5.732 1.00 42.47 A C
ANISOU 1952 CD1 LEU A 219 4626 5845 5663 -387 357 189 A C
ATOM 1953 CD2 LEU A 219 24.409 2.287 4.434 1.00 49.25 A C
ANISOU 1953 CD2 LEU A 219 5703 6710 6299 -217 432 211 A C
ATOM 1954 N ASP A 220 23.561 0.544 9.510 1.00 38.07 A N
ANISOU 1954 N ASP A 220 4238 5378 4849 -115 39 8 A N
ATOM 1955 CA ASP A 220 23.936 -0.403 10.555 1.00 36.46 A C
ANISOU 1955 CA ASP A 220 4004 5232 4617 -37 -18 -6 A C
ATOM 1956 C ASP A 220 22.951 -1.563 10.628 1.00 39.76 A C
ANISOU 1956 C ASP A 220 4542 5613 4951 43 1 -0 A C
ATOM 1957 O ASP A 220 23.351 -2.689 10.956 1.00 38.55 A O
ANISOU 1957 O ASP A 220 4380 5494 4774 133 5 17 A O
ATOM 1958 CB ASP A 220 24.047 0.311 11.913 1.00 40.11 A C
ANISOU 1958 CB ASP A 220 4433 5718 5091 -78 -134 -59 A C
ATOM 1959 CG ASP A 220 25.284 1.217 12.019 1.00 44.01 A C
ANISOU 1959 CG ASP A 220 4775 6257 5688 -152 -175 -75 A C
ATOM 1960 OD1 ASP A 220 26.266 1.001 11.290 1.00 44.59 A O
ANISOU 1960 OD1 ASP A 220 4741 6372 5828 -145 -115 -32 A O
ATOM 1961 OD2 ASP A 220 25.293 2.138 12.856 1.00 48.59 A O
ANISOU 1961 OD2 ASP A 220 5341 6830 6290 -219 -266 -133 A O
ATOM 1962 N ILE A 221 21.673 -1.315 10.327 1.00 36.17 A N
ANISOU 1962 N ILE A 221 4194 5085 4466 12 12 -11 A N
ATOM 1963 CA ILE A 221 20.694 -2.400 10.256 1.00 35.05 A C
ANISOU 1963 CA ILE A 221 4152 4896 4271 70 36 -6 A C
ATOM 1964 C ILE A 221 21.052 -3.351 9.119 1.00 37.05 A C
ANISOU 1964 C ILE A 221 4424 5145 4510 123 110 18 A C
ATOM 1965 O ILE A 221 21.060 -4.578 9.286 1.00 36.28 A O
ANISOU 1965 O ILE A 221 4360 5038 4388 200 130 26 A O
ATOM 1966 CB ILE A 221 19.270 -1.829 10.090 1.00 36.29 A C
ANISOU 1966 CB ILE A 221 4390 4979 4421 19 26 -24 A C
ATOM 1967 CG1 ILE A 221 18.724 -1.282 11.411 1.00 37.66 A C
ANISOU 1967 CG1 ILE A 221 4575 5145 4590 2 -28 -52 A C
ATOM 1968 CG2 ILE A 221 18.341 -2.887 9.493 1.00 40.37 A C
ANISOU 1968 CG2 ILE A 221 4990 5439 4910 56 59 -18 A C
ATOM 1969 CD1 ILE A 221 17.457 -0.401 11.204 1.00 38.98 A C
ANISOU 1969 CD1 ILE A 221 4793 5242 4775 -51 -31 -67 A C
ATOM 1970 N LEU A 222 21.367 -2.801 7.942 1.00 36.56 A N
ANISOU 1970 N LEU A 222 4351 5082 4458 88 161 32 A N
ATOM 1971 CA LEU A 222 21.733 -3.650 6.818 1.00 38.06 A C
ANISOU 1971 CA LEU A 222 4575 5269 4616 146 241 47 A C
ATOM 1972 C LEU A 222 22.970 -4.490 7.131 1.00 41.10 A C
ANISOU 1972 C LEU A 222 4878 5713 5024 228 275 66 A C
ATOM 1973 O LEU A 222 23.042 -5.658 6.735 1.00 39.73 A O
ANISOU 1973 O LEU A 222 4758 5519 4820 309 325 66 A O
ATOM 1974 CB LEU A 222 21.954 -2.812 5.555 1.00 39.82 A C
ANISOU 1974 CB LEU A 222 4806 5492 4832 102 301 70 A C
ATOM 1975 CG LEU A 222 20.737 -2.076 4.979 1.00 42.16 A C
ANISOU 1975 CG LEU A 222 5196 5728 5096 43 271 63 A C
ATOM 1976 CD1 LEU A 222 21.129 -1.196 3.791 1.00 49.32 A C
ANISOU 1976 CD1 LEU A 222 6112 6639 5988 10 338 105 A C
ATOM 1977 CD2 LEU A 222 19.665 -3.071 4.578 1.00 40.97 A C
ANISOU 1977 CD2 LEU A 222 5161 5523 4885 82 251 31 A C
ATOM 1978 N AMET A 223 23.966 -3.906 7.814 0.44 39.91 A N
ANISOU 1978 N AMET A 223 4595 5632 4935 210 245 79 A N
ATOM 1979 N BMET A 223 23.949 -3.918 7.843 0.56 39.87 A N
ANISOU 1979 N BMET A 223 4591 5627 4929 211 243 79 A N
ATOM 1980 CA AMET A 223 25.146 -4.672 8.212 0.44 40.56 A C
ANISOU 1980 CA AMET A 223 4578 5781 5053 296 258 102 A C
ATOM 1981 CA BMET A 223 25.150 -4.674 8.194 0.56 40.51 A C
ANISOU 1981 CA BMET A 223 4571 5773 5046 296 260 102 A C
ATOM 1982 C AMET A 223 24.768 -5.782 9.178 0.44 40.22 A C
ANISOU 1982 C AMET A 223 4590 5720 4970 379 211 98 A C
ATOM 1983 C BMET A 223 24.843 -5.751 9.226 0.56 40.17 A C
ANISOU 1983 C BMET A 223 4575 5721 4969 380 207 99 A C
ATOM 1984 O AMET A 223 25.190 -6.934 9.026 0.44 41.64 A O
ANISOU 1984 O AMET A 223 4781 5898 5143 483 260 118 A O
ATOM 1985 O BMET A 223 25.376 -6.866 9.147 0.56 41.25 A O
ANISOU 1985 O BMET A 223 4706 5864 5103 485 252 121 A O
ATOM 1986 CB AMET A 223 26.182 -3.766 8.884 0.44 43.92 A C
ANISOU 1986 CB AMET A 223 4840 6285 5563 247 201 107 A C
ATOM 1987 CB BMET A 223 26.229 -3.720 8.719 0.56 43.80 A C
ANISOU 1987 CB BMET A 223 4822 6269 5551 244 214 110 A C
ATOM 1988 CG AMET A 223 27.361 -3.352 8.030 0.44 54.87 A C
ANISOU 1988 CG AMET A 223 6098 7720 7030 231 287 142 A C
ATOM 1989 CG BMET A 223 27.443 -4.390 9.348 0.56 44.30 A C
ANISOU 1989 CG BMET A 223 4752 6415 5664 331 191 132 A C
ATOM 1990 SD AMET A 223 28.709 -4.538 7.746 0.44 61.51 A S
ANISOU 1990 SD AMET A 223 6824 8630 7917 369 371 185 A S
ATOM 1991 SD BMET A 223 28.670 -3.172 9.886 0.56 62.22 A S
ANISOU 1991 SD BMET A 223 6808 8773 8061 244 117 128 A S
ATOM 1992 CE AMET A 223 27.970 -6.170 7.693 0.44 40.35 A C
ANISOU 1992 CE AMET A 223 4312 5886 5133 501 401 178 A C
ATOM 1993 CE BMET A 223 27.857 -2.444 11.309 0.56 55.26 A C
ANISOU 1993 CE BMET A 223 5987 7877 7131 175 -47 66 A C
ATOM 1994 N GLU A 224 23.994 -5.435 10.209 1.00 37.43 A N
ANISOU 1994 N GLU A 224 4277 5351 4592 342 125 77 A N
ATOM 1995 CA GLU A 224 23.631 -6.418 11.218 1.00 39.14 A C
ANISOU 1995 CA GLU A 224 4553 5551 4768 420 91 88 A C
ATOM 1996 C GLU A 224 22.879 -7.593 10.597 1.00 39.87 A C
ANISOU 1996 C GLU A 224 4765 5553 4831 470 163 93 A C
ATOM 1997 O GLU A 224 23.106 -8.752 10.981 1.00 40.41 A O
ANISOU 1997 O GLU A 224 4860 5604 4890 569 183 121 A O
ATOM 1998 CB GLU A 224 22.808 -5.746 12.317 1.00 40.46 A C
ANISOU 1998 CB GLU A 224 4761 5709 4903 367 12 65 A C
ATOM 1999 CG GLU A 224 22.762 -6.534 13.602 1.00 41.78 A C
ANISOU 1999 CG GLU A 224 4965 5891 5020 452 -30 89 A C
ATOM 2000 CD GLU A 224 24.109 -6.596 14.323 1.00 47.72 A C
ANISOU 2000 CD GLU A 224 5604 6746 5780 516 -101 108 A C
ATOM 2001 OE1 GLU A 224 24.988 -5.726 14.110 1.00 49.22 A O
ANISOU 2001 OE1 GLU A 224 5672 7003 6026 464 -141 86 A O
ATOM 2002 OE2 GLU A 224 24.289 -7.551 15.094 1.00 55.03 A O
ANISOU 2002 OE2 GLU A 224 6561 7685 6664 621 -118 149 A O
ATOM 2003 N LEU A 225 22.004 -7.326 9.621 1.00 38.15 A N
ANISOU 2003 N LEU A 225 4622 5271 4603 407 198 65 A N
ATOM 2004 CA LEU A 225 21.281 -8.419 8.970 1.00 37.02 A C
ANISOU 2004 CA LEU A 225 4590 5037 4439 441 249 52 A C
ATOM 2005 C LEU A 225 22.223 -9.298 8.149 1.00 40.12 A C
ANISOU 2005 C LEU A 225 4979 5432 4832 530 327 60 A C
ATOM 2006 O LEU A 225 22.024 -10.516 8.061 1.00 40.98 A O
ANISOU 2006 O LEU A 225 5165 5471 4935 599 365 57 A O
ATOM 2007 CB LEU A 225 20.154 -7.859 8.097 1.00 35.91 A C
ANISOU 2007 CB LEU A 225 4521 4840 4285 354 242 16 A C
ATOM 2008 CG LEU A 225 19.034 -7.174 8.886 1.00 41.56 A C
ANISOU 2008 CG LEU A 225 5249 5531 5011 284 181 8 A C
ATOM 2009 CD1 LEU A 225 18.040 -6.568 7.902 1.00 47.02 A C
ANISOU 2009 CD1 LEU A 225 5991 6177 5698 210 168 -22 A C
ATOM 2010 CD2 LEU A 225 18.337 -8.134 9.829 1.00 46.29 A C
ANISOU 2010 CD2 LEU A 225 5899 6071 5617 319 180 19 A C
ATOM 2011 N GLU A 226 23.247 -8.715 7.524 1.00 38.86 A N
ANISOU 2011 N GLU A 226 4733 5344 4687 531 365 71 A N
ATOM 2012 CA AGLU A 226 24.202 -9.546 6.792 0.56 42.65 A C
ANISOU 2012 CA AGLU A 226 5202 5833 5171 630 459 82 A C
ATOM 2013 CA BGLU A 226 24.205 -9.541 6.795 0.44 42.68 A C
ANISOU 2013 CA BGLU A 226 5205 5837 5175 630 458 82 A C
ATOM 2014 C GLU A 226 24.957 -10.464 7.746 1.00 40.02 A C
ANISOU 2014 C GLU A 226 4810 5523 4872 742 451 120 A C
ATOM 2015 O GLU A 226 25.170 -11.643 7.443 1.00 43.46 A O
ANISOU 2015 O GLU A 226 5304 5905 5304 844 516 122 A O
ATOM 2016 CB AGLU A 226 25.180 -8.683 5.988 0.56 44.01 A C
ANISOU 2016 CB AGLU A 226 5274 6082 5365 608 520 100 A C
ATOM 2017 CB BGLU A 226 25.190 -8.672 6.012 0.44 44.03 A C
ANISOU 2017 CB BGLU A 226 5274 6086 5369 608 518 101 A C
ATOM 2018 CG AGLU A 226 26.378 -9.455 5.421 0.56 49.16 A C
ANISOU 2018 CG AGLU A 226 5875 6764 6039 725 630 123 A C
ATOM 2019 CG BGLU A 226 26.135 -9.493 5.149 0.44 48.63 A C
ANISOU 2019 CG BGLU A 226 5850 6677 5952 717 641 112 A C
ATOM 2020 CD AGLU A 226 26.116 -10.067 4.054 0.56 55.04 A C
ANISOU 2020 CD AGLU A 226 6758 7443 6711 768 736 88 A C
ATOM 2021 CD BGLU A 226 27.208 -8.665 4.472 0.44 54.88 A C
ANISOU 2021 CD BGLU A 226 6519 7550 6784 701 723 147 A C
ATOM 2022 OE1AGLU A 226 24.940 -10.103 3.630 0.56 48.52 A O
ANISOU 2022 OE1AGLU A 226 6075 6541 5818 714 701 41 A O
ATOM 2023 OE1BGLU A 226 27.235 -7.435 4.675 0.44 60.68 A O
ANISOU 2023 OE1BGLU A 226 7174 8327 7554 596 677 161 A O
ATOM 2024 OE2AGLU A 226 27.086 -10.542 3.419 0.56 63.25 A O
ANISOU 2024 OE2AGLU A 226 7765 8507 7760 862 851 104 A O
ATOM 2025 OE2BGLU A 226 28.030 -9.250 3.737 0.44 66.11 A O
ANISOU 2025 OE2BGLU A 226 7925 8986 8210 796 844 161 A O
ATOM 2026 N ILE A 227 25.384 -9.935 8.901 1.00 41.17 A N
ANISOU 2026 N ILE A 227 4849 5745 5048 732 367 149 A N
ATOM 2027 CA ILE A 227 26.059 -10.767 9.894 1.00 42.32 A C
ANISOU 2027 CA ILE A 227 4945 5921 5212 847 338 194 A C
ATOM 2028 C ILE A 227 25.132 -11.872 10.380 1.00 43.41 A C
ANISOU 2028 C ILE A 227 5228 5954 5313 897 341 201 A C
ATOM 2029 O ILE A 227 25.551 -13.022 10.561 1.00 44.20 A O
ANISOU 2029 O ILE A 227 5351 6020 5424 1019 381 236 A O
ATOM 2030 CB ILE A 227 26.563 -9.898 11.065 1.00 46.59 A C
ANISOU 2030 CB ILE A 227 5364 6567 5771 815 221 210 A C
ATOM 2031 CG1 ILE A 227 27.695 -8.985 10.576 1.00 51.51 A C
ANISOU 2031 CG1 ILE A 227 5819 7286 6468 775 228 210 A C
ATOM 2032 CG2 ILE A 227 27.032 -10.780 12.218 1.00 53.03 A C
ANISOU 2032 CG2 ILE A 227 6162 7410 6577 940 166 260 A C
ATOM 2033 CD1 ILE A 227 28.055 -7.864 11.540 1.00 54.73 A C
ANISOU 2033 CD1 ILE A 227 6112 7779 6903 699 101 198 A C
ATOM 2034 N LEU A 228 23.859 -11.541 10.598 1.00 38.75 A N
ANISOU 2034 N LEU A 228 4730 5302 4689 804 309 174 A N
ATOM 2035 CA LEU A 228 22.896 -12.516 11.102 1.00 39.06 A C
ANISOU 2035 CA LEU A 228 4894 5235 4714 832 321 187 A C
ATOM 2036 C LEU A 228 22.698 -13.650 10.107 1.00 43.29 A C
ANISOU 2036 C LEU A 228 5526 5658 5264 879 410 163 A C
ATOM 2037 O LEU A 228 22.680 -14.829 10.485 1.00 42.53 A O
ANISOU 2037 O LEU A 228 5495 5483 5181 968 446 195 A O
ATOM 2038 CB LEU A 228 21.568 -11.813 11.376 1.00 40.40 A C
ANISOU 2038 CB LEU A 228 5118 5367 4866 714 281 159 A C
ATOM 2039 CG LEU A 228 20.474 -12.605 12.077 1.00 50.03 A C
ANISOU 2039 CG LEU A 228 6442 6484 6085 719 297 181 A C
ATOM 2040 CD1 LEU A 228 20.868 -12.876 13.514 1.00 60.62 A C
ANISOU 2040 CD1 LEU A 228 7771 7868 7392 802 266 250 A C
ATOM 2041 CD2 LEU A 228 19.169 -11.810 12.023 1.00 49.77 A C
ANISOU 2041 CD2 LEU A 228 6438 6416 6057 597 273 144 A C
ATOM 2042 N ARG A 229 22.535 -13.298 8.826 1.00 39.54 A N
ANISOU 2042 N ARG A 229 5075 5168 4780 822 444 105 A N
ATOM 2043 CA ARG A 229 22.360 -14.288 7.769 1.00 40.71 A C
ANISOU 2043 CA ARG A 229 5330 5213 4925 863 519 61 A C
ATOM 2044 C ARG A 229 23.566 -15.218 7.661 1.00 42.20 A C
ANISOU 2044 C ARG A 229 5495 5406 5134 1011 595 90 A C
ATOM 2045 O ARG A 229 23.412 -16.435 7.513 1.00 43.33 A O
ANISOU 2045 O ARG A 229 5737 5434 5292 1084 648 80 A O
ATOM 2046 CB ARG A 229 22.146 -13.578 6.433 1.00 43.26 A C
ANISOU 2046 CB ARG A 229 5680 5551 5207 790 535 -0 A C
ATOM 2047 CG ARG A 229 20.772 -12.950 6.258 1.00 38.55 A C
ANISOU 2047 CG ARG A 229 5138 4913 4595 662 467 -41 A C
ATOM 2048 CD ARG A 229 20.543 -12.579 4.808 1.00 40.93 A C
ANISOU 2048 CD ARG A 229 5505 5208 4841 621 484 -100 A C
ATOM 2049 NE ARG A 229 21.482 -11.576 4.311 1.00 40.66 A N
ANISOU 2049 NE ARG A 229 5387 5283 4779 620 518 -74 A N
ATOM 2050 CZ ARG A 229 21.262 -10.266 4.344 1.00 41.80 A C
ANISOU 2050 CZ ARG A 229 5473 5489 4920 531 471 -57 A C
ATOM 2051 NH1 ARG A 229 20.147 -9.761 4.858 1.00 38.25 A N
ANISOU 2051 NH1 ARG A 229 5035 5011 4487 446 387 -66 A N
ATOM 2052 NH2 ARG A 229 22.161 -9.445 3.806 1.00 41.44 A N
ANISOU 2052 NH2 ARG A 229 5358 5525 4862 529 520 -29 A N
ATOM 2053 N ASN A 230 24.773 -14.656 7.729 1.00 41.33 A N
ANISOU 2053 N ASN A 230 5245 5420 5037 1056 603 128 A N
ATOM 2054 CA ASN A 230 25.980 -15.455 7.547 1.00 43.18 A C
ANISOU 2054 CA ASN A 230 5430 5672 5306 1205 681 159 A C
ATOM 2055 C ASN A 230 26.264 -16.353 8.746 1.00 47.52 A C
ANISOU 2055 C ASN A 230 5970 6199 5888 1317 654 228 A C
ATOM 2056 O ASN A 230 26.788 -17.460 8.576 1.00 45.06 A O
ANISOU 2056 O ASN A 230 5693 5824 5603 1452 728 246 A O
ATOM 2057 CB ASN A 230 27.180 -14.533 7.287 1.00 44.18 A C
ANISOU 2057 CB ASN A 230 5382 5943 5462 1210 697 185 A C
ATOM 2058 CG ASN A 230 27.098 -13.815 5.942 1.00 51.48 A C
ANISOU 2058 CG ASN A 230 6331 6880 6350 1134 764 135 A C
ATOM 2059 ND2 ASN A 230 27.986 -12.860 5.733 1.00 57.01 A N
ANISOU 2059 ND2 ASN A 230 6881 7695 7086 1107 782 163 A N
ATOM 2060 OD1 ASN A 230 26.232 -14.106 5.114 1.00 57.20 A O
ANISOU 2060 OD1 ASN A 230 7209 7511 7014 1098 794 74 A O
ATOM 2061 N ASER A 231 25.926 -15.915 9.957 0.53 46.13 A N
ANISOU 2061 N ASER A 231 5760 6067 5701 1276 553 270 A N
ATOM 2062 N BSER A 231 25.930 -15.899 9.954 0.47 46.14 A N
ANISOU 2062 N BSER A 231 5760 6070 5703 1275 552 269 A N
ATOM 2063 CA ASER A 231 26.288 -16.645 11.164 0.53 46.16 A C
ANISOU 2063 CA ASER A 231 5752 6072 5714 1392 517 350 A C
ATOM 2064 CA BSER A 231 26.279 -16.619 11.169 0.47 46.16 A C
ANISOU 2064 CA BSER A 231 5752 6074 5714 1390 515 350 A C
ATOM 2065 C ASER A 231 25.169 -17.530 11.701 0.53 46.47 A C
ANISOU 2065 C ASER A 231 5952 5966 5738 1392 531 368 A C
ATOM 2066 C BSER A 231 25.248 -17.665 11.572 0.47 46.54 A C
ANISOU 2066 C BSER A 231 5966 5965 5753 1407 545 366 A C
ATOM 2067 O ASER A 231 25.341 -18.153 12.753 0.53 48.77 A O
ANISOU 2067 O ASER A 231 6261 6245 6023 1490 509 448 A O
ATOM 2068 O BSER A 231 25.566 -18.541 12.384 0.47 48.01 A O
ANISOU 2068 O BSER A 231 6176 6117 5947 1530 549 443 A O
ATOM 2069 CB ASER A 231 26.720 -15.662 12.256 0.53 48.25 A C
ANISOU 2069 CB ASER A 231 5889 6483 5960 1366 395 388 A C
ATOM 2070 CB BSER A 231 26.464 -15.627 12.327 0.47 48.10 A C
ANISOU 2070 CB BSER A 231 5894 6449 5932 1346 390 384 A C
ATOM 2071 OG ASER A 231 25.592 -14.988 12.777 0.53 45.85 A O
ANISOU 2071 OG ASER A 231 5651 6163 5608 1241 336 365 A O
ATOM 2072 OG BSER A 231 27.464 -14.670 12.031 0.47 50.80 A O
ANISOU 2072 OG BSER A 231 6068 6928 6307 1321 357 370 A O
ATOM 2073 N ALA A 232 24.043 -17.609 11.012 1.00 44.26 A N
ANISOU 2073 N ALA A 232 5786 5576 5456 1288 566 302 A N
ATOM 2074 CA ALA A 232 22.950 -18.445 11.490 1.00 45.29 A C
ANISOU 2074 CA ALA A 232 6050 5558 5600 1272 588 320 A C
ATOM 2075 C ALA A 232 23.266 -19.932 11.317 1.00 46.92 A C
ANISOU 2075 C ALA A 232 6347 5629 5852 1403 676 346 A C
ATOM 2076 O ALA A 232 24.064 -20.321 10.458 1.00 50.23 A O
ANISOU 2076 O ALA A 232 6755 6042 6289 1484 734 314 A O
ATOM 2077 CB ALA A 232 21.659 -18.103 10.745 1.00 50.35 A C
ANISOU 2077 CB ALA A 232 6764 6120 6246 1118 587 235 A C
ATOM 2078 N PRO A 233 22.656 -20.789 12.133 1.00 52.53 A N
ANISOU 2078 N PRO A 233 7154 6220 6586 1433 700 408 A N
ATOM 2079 CA PRO A 233 22.913 -22.226 12.011 1.00 56.46 A C
ANISOU 2079 CA PRO A 233 7750 6562 7139 1558 788 437 A C
ATOM 2080 C PRO A 233 22.432 -22.778 10.678 1.00 52.47 A C
ANISOU 2080 C PRO A 233 7346 5912 6677 1505 852 322 A C
ATOM 2081 O PRO A 233 21.543 -22.223 10.023 1.00 49.16 A O
ANISOU 2081 O PRO A 233 6948 5480 6250 1355 822 232 A O
ATOM 2082 CB PRO A 233 22.116 -22.842 13.171 1.00 53.89 A C
ANISOU 2082 CB PRO A 233 7514 6131 6830 1561 803 531 A C
ATOM 2083 CG PRO A 233 21.453 -21.723 13.883 1.00 57.35 A C
ANISOU 2083 CG PRO A 233 7900 6679 7213 1445 728 543 A C
ATOM 2084 CD PRO A 233 22.025 -20.436 13.416 1.00 54.55 A C
ANISOU 2084 CD PRO A 233 7413 6505 6808 1394 651 481 A C
ATOM 2085 N GLU A 234 23.004 -23.917 10.297 1.00 50.74 A N
ANISOU 2085 N GLU A 234 7199 5579 6502 1635 937 322 A N
ATOM 2086 CA GLU A 234 22.560 -24.599 9.090 1.00 48.02 A C
ANISOU 2086 CA GLU A 234 6979 5073 6192 1599 997 203 A C
ATOM 2087 C GLU A 234 21.058 -24.822 9.144 1.00 52.27 A C
ANISOU 2087 C GLU A 234 7615 5466 6779 1441 976 160 A C
ATOM 2088 O GLU A 234 20.523 -25.272 10.160 1.00 53.79 A O
ANISOU 2088 O GLU A 234 7840 5577 7020 1436 988 249 A O
ATOM 2089 CB GLU A 234 23.263 -25.949 8.928 1.00 57.63 A C
ANISOU 2089 CB GLU A 234 8284 6147 7465 1772 1100 222 A C
ATOM 2090 CG GLU A 234 24.709 -25.974 9.335 1.00 73.28 A C
ANISOU 2090 CG GLU A 234 10154 8253 9435 1961 1123 316 A C
ATOM 2091 CD GLU A 234 25.454 -27.120 8.685 1.00 94.27 A C
ANISOU 2091 CD GLU A 234 12894 10784 12143 2127 1238 290 A C
ATOM 2092 OE1 GLU A 234 24.784 -28.040 8.161 1.00 71.63 A O
ANISOU 2092 OE1 GLU A 234 10194 7702 9322 2101 1297 214 A O
ATOM 2093 OE2 GLU A 234 26.702 -27.104 8.704 1.00118.11 A O
ANISOU 2093 OE2 GLU A 234 15805 13910 15161 2285 1269 342 A O
ATOM 2094 N GLY A 235 20.383 -24.517 8.042 1.00 50.76 A N
ANISOU 2094 N GLY A 235 7467 5243 6575 1317 948 28 A N
ATOM 2095 CA GLY A 235 18.960 -24.731 7.939 1.00 56.79 A C
ANISOU 2095 CA GLY A 235 8303 5870 7403 1162 916 -30 A C
ATOM 2096 C GLY A 235 18.101 -23.668 8.583 1.00 49.84 A C
ANISOU 2096 C GLY A 235 7332 5092 6514 1028 838 8 A C
ATOM 2097 O GLY A 235 16.871 -23.763 8.501 1.00 52.25 A O
ANISOU 2097 O GLY A 235 7670 5296 6887 893 810 -36 A O
ATOM 2098 N SER A 236 18.699 -22.656 9.207 1.00 45.66 A N
ANISOU 2098 N SER A 236 6683 4754 5910 1060 802 82 A N
ATOM 2099 CA SER A 236 17.913 -21.627 9.876 1.00 45.27 A C
ANISOU 2099 CA SER A 236 6557 4796 5848 946 737 115 A C
ATOM 2100 C SER A 236 17.217 -20.715 8.867 1.00 46.76 A C
ANISOU 2100 C SER A 236 6721 5031 6014 809 665 5 A C
ATOM 2101 O SER A 236 17.815 -20.299 7.868 1.00 41.91 A O
ANISOU 2101 O SER A 236 6098 4491 5337 826 649 -62 A O
ATOM 2102 CB SER A 236 18.802 -20.779 10.793 1.00 45.87 A C
ANISOU 2102 CB SER A 236 6522 5058 5847 1018 706 206 A C
ATOM 2103 OG SER A 236 18.090 -19.624 11.233 1.00 47.01 A O
ANISOU 2103 OG SER A 236 6600 5297 5966 906 642 210 A O
ATOM 2104 N PRO A 237 15.960 -20.343 9.118 1.00 44.64 A N
ANISOU 2104 N PRO A 237 6438 4729 5794 679 624 -5 A N
ATOM 2105 CA PRO A 237 15.299 -19.385 8.225 1.00 43.24 A C
ANISOU 2105 CA PRO A 237 6227 4609 5593 561 542 -95 A C
ATOM 2106 C PRO A 237 15.897 -17.987 8.281 1.00 44.18 A C
ANISOU 2106 C PRO A 237 6247 4922 5619 565 497 -73 A C
ATOM 2107 O PRO A 237 15.687 -17.208 7.341 1.00 44.05 A O
ANISOU 2107 O PRO A 237 6216 4961 5560 502 441 -142 A O
ATOM 2108 CB PRO A 237 13.839 -19.405 8.713 1.00 48.30 A C
ANISOU 2108 CB PRO A 237 6854 5164 6334 439 523 -87 A C
ATOM 2109 CG PRO A 237 13.923 -19.857 10.113 1.00 54.92 A C
ANISOU 2109 CG PRO A 237 7689 5973 7206 498 597 35 A C
ATOM 2110 CD PRO A 237 15.039 -20.849 10.153 1.00 51.22 A C
ANISOU 2110 CD PRO A 237 7288 5456 6717 637 662 67 A C
ATOM 2111 N LEU A 238 16.656 -17.653 9.331 1.00 42.84 A N
ANISOU 2111 N LEU A 238 6014 4850 5415 639 514 20 A N
ATOM 2112 CA LEU A 238 17.302 -16.348 9.399 1.00 39.26 A C
ANISOU 2112 CA LEU A 238 5463 4566 4889 637 468 33 A C
ATOM 2113 C LEU A 238 18.314 -16.148 8.275 1.00 39.66 A C
ANISOU 2113 C LEU A 238 5502 4679 4886 683 479 -14 A C
ATOM 2114 O LEU A 238 18.674 -15.003 7.965 1.00 39.61 A O
ANISOU 2114 O LEU A 238 5424 4792 4836 649 444 -23 A O
ATOM 2115 CB LEU A 238 17.989 -16.189 10.750 1.00 43.84 A C
ANISOU 2115 CB LEU A 238 5985 5228 5442 715 472 129 A C
ATOM 2116 CG LEU A 238 17.065 -16.215 11.974 1.00 47.13 A C
ANISOU 2116 CG LEU A 238 6417 5607 5882 681 476 190 A C
ATOM 2117 CD1 LEU A 238 17.887 -16.061 13.239 1.00 53.63 A C
ANISOU 2117 CD1 LEU A 238 7204 6528 6646 777 466 277 A C
ATOM 2118 CD2 LEU A 238 16.000 -15.144 11.876 1.00 49.94 A C
ANISOU 2118 CD2 LEU A 238 6738 5990 6249 554 429 150 A C
ATOM 2119 N ARG A 239 18.764 -17.232 7.646 1.00 39.81 A N
ANISOU 2119 N ARG A 239 5597 4614 4914 761 539 -44 A N
ATOM 2120 CA ARG A 239 19.691 -17.111 6.520 1.00 40.95 A C
ANISOU 2120 CA ARG A 239 5745 4812 5005 815 574 -90 A C
ATOM 2121 C ARG A 239 19.087 -16.333 5.352 1.00 42.35 A C
ANISOU 2121 C ARG A 239 5952 5010 5131 716 530 -171 A C
ATOM 2122 O ARG A 239 19.834 -15.753 4.550 1.00 37.59 A O
ANISOU 2122 O ARG A 239 5325 4493 4465 741 556 -186 A O
ATOM 2123 CB ARG A 239 20.129 -18.510 6.067 1.00 42.29 A C
ANISOU 2123 CB ARG A 239 6014 4861 5194 922 656 -119 A C
ATOM 2124 CG ARG A 239 21.043 -18.525 4.842 1.00 41.93 A C
ANISOU 2124 CG ARG A 239 5992 4853 5085 993 719 -172 A C
ATOM 2125 CD ARG A 239 22.006 -19.720 4.860 1.00 45.43 A C
ANISOU 2125 CD ARG A 239 6473 5230 5557 1154 819 -154 A C
ATOM 2126 NE ARG A 239 23.089 -19.464 5.799 1.00 42.41 A N
ANISOU 2126 NE ARG A 239 5949 4965 5199 1247 833 -46 A N
ATOM 2127 CZ ARG A 239 23.151 -19.926 7.043 1.00 43.54 A C
ANISOU 2127 CZ ARG A 239 6062 5087 5393 1299 816 40 A C
ATOM 2128 NH1 ARG A 239 22.395 -20.930 7.453 1.00 46.48 A N
ANISOU 2128 NH1 ARG A 239 6545 5301 5815 1300 827 44 A N
ATOM 2129 NH2 ARG A 239 23.968 -19.337 7.909 1.00 46.34 A N
ANISOU 2129 NH2 ARG A 239 6275 5583 5750 1346 782 126 A N
ATOM 2130 N VAL A 240 17.759 -16.287 5.228 1.00 40.48 A N
ANISOU 2130 N VAL A 240 5762 4696 4921 608 466 -217 A N
ATOM 2131 CA VAL A 240 17.171 -15.604 4.079 1.00 40.21 A C
ANISOU 2131 CA VAL A 240 5765 4682 4832 528 409 -291 A C
ATOM 2132 C VAL A 240 16.272 -14.460 4.544 1.00 42.04 A C
ANISOU 2132 C VAL A 240 5919 4968 5086 421 328 -265 A C
ATOM 2133 O VAL A 240 15.287 -14.130 3.887 1.00 43.47 A O
ANISOU 2133 O VAL A 240 6132 5122 5263 339 256 -320 A O
ATOM 2134 CB VAL A 240 16.401 -16.582 3.166 1.00 42.31 A C
ANISOU 2134 CB VAL A 240 6165 4807 5105 502 387 -395 A C
ATOM 2135 CG1 VAL A 240 17.380 -17.509 2.447 1.00 47.86 A C
ANISOU 2135 CG1 VAL A 240 6961 5466 5757 617 475 -438 A C
ATOM 2136 CG2 VAL A 240 15.354 -17.393 3.944 1.00 45.70 A C
ANISOU 2136 CG2 VAL A 240 6607 5101 5655 444 364 -394 A C
ATOM 2137 N LEU A 241 16.657 -13.811 5.635 1.00 38.76 A N
ANISOU 2137 N LEU A 241 5403 4636 4688 430 334 -185 A N
ATOM 2138 CA LEU A 241 15.990 -12.606 6.128 1.00 40.54 A C
ANISOU 2138 CA LEU A 241 5555 4921 4927 347 273 -159 A C
ATOM 2139 C LEU A 241 16.630 -11.380 5.477 1.00 39.15 A C
ANISOU 2139 C LEU A 241 5335 4856 4684 335 261 -156 A C
ATOM 2140 O LEU A 241 17.778 -11.030 5.781 1.00 40.17 A O
ANISOU 2140 O LEU A 241 5399 5069 4794 386 299 -113 A O
ATOM 2141 CB LEU A 241 16.096 -12.536 7.648 1.00 38.47 A C
ANISOU 2141 CB LEU A 241 5229 4684 4702 367 287 -86 A C
ATOM 2142 CG LEU A 241 15.562 -11.290 8.364 1.00 39.37 A C
ANISOU 2142 CG LEU A 241 5273 4862 4824 301 240 -59 A C
ATOM 2143 CD1 LEU A 241 14.117 -11.110 8.012 1.00 41.19 A C
ANISOU 2143 CD1 LEU A 241 5522 5025 5104 212 196 -96 A C
ATOM 2144 CD2 LEU A 241 15.729 -11.403 9.870 1.00 45.26 A C
ANISOU 2144 CD2 LEU A 241 5987 5628 5580 340 260 6 A C
ATOM 2145 N TYR A 242 15.876 -10.723 4.602 1.00 37.73 A N
ANISOU 2145 N TYR A 242 5184 4674 4479 268 206 -195 A N
ATOM 2146 CA TYR A 242 16.273 -9.502 3.921 1.00 37.92 A C
ANISOU 2146 CA TYR A 242 5182 4783 4444 247 197 -182 A C
ATOM 2147 C TYR A 242 15.219 -8.422 4.160 1.00 40.46 A C
ANISOU 2147 C TYR A 242 5465 5112 4798 163 121 -173 A C
ATOM 2148 O TYR A 242 14.041 -8.716 4.395 1.00 37.93 A O
ANISOU 2148 O TYR A 242 5156 4725 4532 119 69 -196 A O
ATOM 2149 CB TYR A 242 16.427 -9.731 2.425 1.00 38.68 A C
ANISOU 2149 CB TYR A 242 5377 4869 4452 271 210 -231 A C
ATOM 2150 CG TYR A 242 17.564 -10.651 2.039 1.00 40.06 A C
ANISOU 2150 CG TYR A 242 5591 5043 4586 367 306 -242 A C
ATOM 2151 CD1 TYR A 242 17.374 -12.023 1.934 1.00 42.84 A C
ANISOU 2151 CD1 TYR A 242 6028 5298 4952 410 322 -295 A C
ATOM 2152 CD2 TYR A 242 18.819 -10.139 1.754 1.00 43.16 A C
ANISOU 2152 CD2 TYR A 242 5935 5524 4942 415 387 -197 A C
ATOM 2153 CE1 TYR A 242 18.409 -12.867 1.573 1.00 46.41 A C
ANISOU 2153 CE1 TYR A 242 6521 5740 5372 512 418 -306 A C
ATOM 2154 CE2 TYR A 242 19.851 -10.970 1.388 1.00 40.79 A C
ANISOU 2154 CE2 TYR A 242 5658 5224 4615 514 486 -203 A C
ATOM 2155 CZ TYR A 242 19.648 -12.335 1.305 1.00 47.03 A C
ANISOU 2155 CZ TYR A 242 6540 5917 5411 569 502 -258 A C
ATOM 2156 OH TYR A 242 20.691 -13.180 0.944 1.00 51.61 A O
ANISOU 2156 OH TYR A 242 7149 6490 5971 683 610 -265 A O
ATOM 2157 N SER A 243 15.653 -7.167 4.079 1.00 39.16 A N
ANISOU 2157 N SER A 243 5249 5020 4611 142 121 -136 A N
ATOM 2158 CA SER A 243 14.786 -6.021 4.308 1.00 37.82 A C
ANISOU 2158 CA SER A 243 5043 4854 4474 76 60 -122 A C
ATOM 2159 C SER A 243 15.066 -4.945 3.274 1.00 46.17 A C
ANISOU 2159 C SER A 243 6118 5952 5471 61 58 -103 A C
ATOM 2160 O SER A 243 16.163 -4.861 2.725 1.00 41.41 A O
ANISOU 2160 O SER A 243 5521 5395 4818 94 123 -84 A O
ATOM 2161 CB SER A 243 15.008 -5.432 5.704 1.00 41.48 A C
ANISOU 2161 CB SER A 243 5421 5349 4991 64 68 -86 A C
ATOM 2162 OG SER A 243 14.112 -4.370 5.988 1.00 41.46 A O
ANISOU 2162 OG SER A 243 5391 5337 5026 10 20 -79 A O
ATOM 2163 N GLY A 244 14.051 -4.121 3.020 1.00 37.46 A N
ANISOU 2163 N GLY A 244 5020 4829 4383 15 -10 -100 A N
ATOM 2164 CA GLY A 244 14.235 -2.831 2.392 1.00 37.96 A C
ANISOU 2164 CA GLY A 244 5087 4924 4414 -5 -12 -59 A C
ATOM 2165 C GLY A 244 14.102 -1.730 3.432 1.00 38.98 A C
ANISOU 2165 C GLY A 244 5133 5056 4621 -46 -20 -29 A C
ATOM 2166 O GLY A 244 13.584 -1.947 4.525 1.00 40.48 A O
ANISOU 2166 O GLY A 244 5280 5226 4876 -56 -38 -45 A O
ATOM 2167 N ILE A 245 14.594 -0.539 3.086 1.00 33.61 A N
ANISOU 2167 N ILE A 245 4442 4396 3933 -67 2 15 A N
ATOM 2168 CA ILE A 245 14.491 0.628 3.955 1.00 33.00 A C
ANISOU 2168 CA ILE A 245 4303 4307 3927 -108 -7 34 A C
ATOM 2169 C ILE A 245 14.237 1.846 3.088 1.00 34.72 A C
ANISOU 2169 C ILE A 245 4556 4503 4134 -128 -17 81 A C
ATOM 2170 O ILE A 245 14.919 2.046 2.076 1.00 36.24 A O
ANISOU 2170 O ILE A 245 4789 4715 4264 -119 30 120 A O
ATOM 2171 CB ILE A 245 15.758 0.863 4.804 1.00 33.83 A C
ANISOU 2171 CB ILE A 245 4334 4454 4066 -122 43 39 A C
ATOM 2172 CG1 ILE A 245 16.080 -0.350 5.671 1.00 37.73 A C
ANISOU 2172 CG1 ILE A 245 4801 4973 4561 -85 50 7 A C
ATOM 2173 CG2 ILE A 245 15.563 2.094 5.680 1.00 38.85 A C
ANISOU 2173 CG2 ILE A 245 4926 5064 4770 -169 20 39 A C
ATOM 2174 CD1 ILE A 245 17.412 -0.231 6.407 1.00 43.59 A C
ANISOU 2174 CD1 ILE A 245 5463 5772 5328 -86 81 13 A C
ATOM 2175 N GLY A 246 13.257 2.647 3.481 1.00 33.41 A N
ANISOU 2175 N GLY A 246 4378 4291 4025 -147 -67 84 A N
ATOM 2176 CA GLY A 246 12.992 3.916 2.821 1.00 34.43 A C
ANISOU 2176 CA GLY A 246 4538 4385 4159 -159 -77 138 A C
ATOM 2177 C GLY A 246 12.936 5.020 3.854 1.00 38.22 A C
ANISOU 2177 C GLY A 246 4967 4823 4733 -195 -70 136 A C
ATOM 2178 O GLY A 246 12.421 4.828 4.952 1.00 37.55 A O
ANISOU 2178 O GLY A 246 4841 4727 4700 -196 -90 90 A O
ATOM 2179 N LEU A 247 13.500 6.187 3.494 1.00 35.48 A N
ANISOU 2179 N LEU A 247 4629 4445 4406 -225 -32 186 A N
ATOM 2180 CA LEU A 247 13.482 7.361 4.362 1.00 34.88 A C
ANISOU 2180 CA LEU A 247 4522 4310 4422 -265 -26 178 A C
ATOM 2181 C LEU A 247 12.927 8.560 3.609 1.00 39.46 A C
ANISOU 2181 C LEU A 247 5153 4814 5024 -259 -32 245 A C
ATOM 2182 O LEU A 247 13.260 8.766 2.439 1.00 37.93 A O
ANISOU 2182 O LEU A 247 5014 4624 4775 -251 -3 316 A O
ATOM 2183 CB LEU A 247 14.875 7.747 4.871 1.00 36.15 A C
ANISOU 2183 CB LEU A 247 4629 4484 4622 -324 28 167 A C
ATOM 2184 CG LEU A 247 15.815 6.676 5.421 1.00 39.99 A C
ANISOU 2184 CG LEU A 247 5057 5054 5084 -324 42 124 A C
ATOM 2185 CD1 LEU A 247 17.196 7.280 5.613 1.00 41.47 A C
ANISOU 2185 CD1 LEU A 247 5178 5251 5329 -388 87 132 A C
ATOM 2186 CD2 LEU A 247 15.292 6.137 6.721 1.00 40.12 A C
ANISOU 2186 CD2 LEU A 247 5050 5083 5111 -305 -4 54 A C
ATOM 2187 N ALA A 248 12.112 9.370 4.292 1.00 36.69 A N
ANISOU 2187 N ALA A 248 4795 4393 4752 -256 -59 227 A N
ATOM 2188 CA ALA A 248 11.589 10.611 3.732 1.00 37.35 A C
ANISOU 2188 CA ALA A 248 4926 4388 4877 -242 -61 293 A C
ATOM 2189 C ALA A 248 11.530 11.658 4.835 1.00 41.53 A C
ANISOU 2189 C ALA A 248 5435 4831 5513 -273 -44 250 A C
ATOM 2190 O ALA A 248 11.576 11.338 6.022 1.00 43.93 A O
ANISOU 2190 O ALA A 248 5696 5154 5841 -287 -48 166 A O
ATOM 2191 CB ALA A 248 10.200 10.398 3.100 1.00 41.91 A C
ANISOU 2191 CB ALA A 248 5531 4962 5432 -168 -137 323 A C
ATOM 2192 N LYS A 249 11.423 12.922 4.437 1.00 39.87 A N
ANISOU 2192 N LYS A 249 5268 4520 5359 -278 -23 309 A N
ATOM 2193 CA ALYS A 249 11.384 14.035 5.374 0.46 40.65 A C
ANISOU 2193 CA ALYS A 249 5367 4513 5563 -307 -2 265 A C
ATOM 2194 CA BLYS A 249 11.378 14.030 5.378 0.54 40.62 A C
ANISOU 2194 CA BLYS A 249 5364 4511 5560 -306 -3 264 A C
ATOM 2195 C LYS A 249 10.189 14.926 5.075 1.00 44.69 A C
ANISOU 2195 C LYS A 249 5924 4927 6131 -237 -21 315 A C
ATOM 2196 O LYS A 249 9.883 15.200 3.913 1.00 44.77 A O
ANISOU 2196 O LYS A 249 5981 4918 6112 -196 -32 418 A O
ATOM 2197 CB ALYS A 249 12.676 14.851 5.298 0.46 43.25 A C
ANISOU 2197 CB ALYS A 249 5701 4786 5945 -399 57 281 A C
ATOM 2198 CB BLYS A 249 12.666 14.855 5.330 0.54 43.23 A C
ANISOU 2198 CB BLYS A 249 5698 4784 5944 -399 57 279 A C
ATOM 2199 CG ALYS A 249 12.706 16.044 6.221 0.46 44.94 A C
ANISOU 2199 CG ALYS A 249 5928 4875 6273 -441 71 222 A C
ATOM 2200 CG BLYS A 249 12.685 15.991 6.325 0.54 44.94 A C
ANISOU 2200 CG BLYS A 249 5924 4879 6271 -440 68 212 A C
ATOM 2201 CD ALYS A 249 14.081 16.679 6.225 0.46 49.27 A C
ANISOU 2201 CD ALYS A 249 6455 5376 6889 -554 119 222 A C
ATOM 2202 CD BLYS A 249 13.921 16.840 6.167 0.54 49.78 A C
ANISOU 2202 CD BLYS A 249 6533 5421 6962 -545 121 230 A C
ATOM 2203 CE ALYS A 249 14.171 17.786 7.257 0.46 50.18 A C
ANISOU 2203 CE ALYS A 249 6587 5363 7117 -607 117 132 A C
ATOM 2204 CE BLYS A 249 13.853 18.047 7.082 0.54 49.31 A C
ANISOU 2204 CE BLYS A 249 6501 5215 7018 -587 123 155 A C
ATOM 2205 NZ ALYS A 249 13.757 19.091 6.680 0.46 51.87 A N
ANISOU 2205 NZ ALYS A 249 6878 5411 7421 -599 161 210 A N
ATOM 2206 NZ BLYS A 249 15.140 18.782 7.115 0.54 52.44 A N
ANISOU 2206 NZ BLYS A 249 6871 5542 7512 -713 162 147 A N
ATOM 2207 N GLY A 250 9.523 15.387 6.123 1.00 41.84 A N
ANISOU 2207 N GLY A 250 5552 4503 5844 -213 -23 246 A N
ATOM 2208 CA GLY A 250 8.450 16.338 5.903 1.00 45.10 A C
ANISOU 2208 CA GLY A 250 5998 4809 6329 -139 -30 294 A C
ATOM 2209 C GLY A 250 7.762 16.718 7.192 1.00 44.97 A C
ANISOU 2209 C GLY A 250 5968 4733 6387 -106 -12 201 A C
ATOM 2210 O GLY A 250 8.091 16.231 8.277 1.00 44.42 A O
ANISOU 2210 O GLY A 250 5872 4709 6296 -139 1 100 A O
ATOM 2211 N LYS A 251 6.790 17.614 7.047 1.00 45.41 A N
ANISOU 2211 N LYS A 251 5921 4359 6975 45 107 660 A N
ATOM 2212 CA LYS A 251 6.026 18.110 8.184 1.00 45.87 A C
ANISOU 2212 CA LYS A 251 5974 4333 7122 82 141 535 A C
ATOM 2213 C LYS A 251 4.912 17.121 8.490 1.00 46.56 A C
ANISOU 2213 C LYS A 251 6007 4647 7036 141 12 522 A C
ATOM 2214 O LYS A 251 4.099 16.814 7.611 1.00 50.46 A O
ANISOU 2214 O LYS A 251 6466 5283 7424 246 -31 686 A O
ATOM 2215 CB LYS A 251 5.459 19.494 7.876 1.00 49.70 A C
ANISOU 2215 CB LYS A 251 6494 4590 7800 217 307 670 A C
ATOM 2216 CG LYS A 251 4.501 20.042 8.927 1.00 60.76 A C
ANISOU 2216 CG LYS A 251 7886 5906 9295 289 358 557 A C
ATOM 2217 CD LYS A 251 3.497 21.026 8.325 1.00107.14 A C
ANISOU 2217 CD LYS A 251 13771 11656 15282 513 486 786 A C
ATOM 2218 CE LYS A 251 2.214 20.332 7.869 1.00125.19 A C
ANISOU 2218 CE LYS A 251 15973 14235 17360 670 357 938 A C
ATOM 2219 NZ LYS A 251 0.988 21.067 8.301 1.00107.81 A N
ANISOU 2219 NZ LYS A 251 13744 11972 15246 856 439 982 A N
ATOM 2220 N VAL A 252 4.854 16.638 9.730 1.00 41.81 A N
ANISOU 2220 N VAL A 252 5385 4104 6397 71 -41 327 A N
ATOM 2221 CA VAL A 252 3.838 15.679 10.141 1.00 40.13 A C
ANISOU 2221 CA VAL A 252 5126 4086 6038 105 -140 303 A C
ATOM 2222 C VAL A 252 3.156 16.197 11.403 1.00 45.07 A C
ANISOU 2222 C VAL A 252 5730 4667 6729 136 -105 165 A C
ATOM 2223 O VAL A 252 3.646 17.105 12.076 1.00 44.64 A O
ANISOU 2223 O VAL A 252 5693 4452 6814 97 -18 39 A O
ATOM 2224 CB VAL A 252 4.417 14.268 10.377 1.00 41.30 A C
ANISOU 2224 CB VAL A 252 5265 4389 6038 0 -232 233 A C
ATOM 2225 CG1 VAL A 252 5.050 13.715 9.088 1.00 46.21 A C
ANISOU 2225 CG1 VAL A 252 5903 5061 6593 -29 -256 349 A C
ATOM 2226 CG2 VAL A 252 5.432 14.259 11.528 1.00 42.36 A C
ANISOU 2226 CG2 VAL A 252 5399 4500 6197 -95 -224 61 A C
ATOM 2227 N ILE A 253 1.987 15.630 11.700 1.00 39.16 A N
ANISOU 2227 N ILE A 253 4932 4069 5878 195 -163 172 A N
ATOM 2228 CA ILE A 253 1.288 15.924 12.948 1.00 38.64 A C
ANISOU 2228 CA ILE A 253 4833 4010 5838 220 -144 35 A C
ATOM 2229 C ILE A 253 1.708 14.875 13.968 1.00 41.03 A C
ANISOU 2229 C ILE A 253 5116 4454 6019 112 -212 -101 A C
ATOM 2230 O ILE A 253 1.672 13.675 13.684 1.00 43.57 A O
ANISOU 2230 O ILE A 253 5431 4911 6211 76 -279 -45 A O
ATOM 2231 CB ILE A 253 -0.237 15.933 12.748 1.00 40.81 A C
ANISOU 2231 CB ILE A 253 5048 4392 6064 351 -157 124 A C
ATOM 2232 CG1 ILE A 253 -0.616 17.067 11.806 1.00 46.95 A C
ANISOU 2232 CG1 ILE A 253 5833 5046 6960 503 -70 292 A C
ATOM 2233 CG2 ILE A 253 -0.934 16.152 14.071 1.00 45.20 A C
ANISOU 2233 CG2 ILE A 253 5564 4975 6634 371 -137 -27 A C
ATOM 2234 CD1 ILE A 253 -2.040 16.999 11.283 1.00 55.04 A C
ANISOU 2234 CD1 ILE A 253 6767 6251 7893 654 -96 430 A C
ATOM 2235 N GLU A 254 2.136 15.323 15.144 1.00 39.49 A N
ANISOU 2235 N GLU A 254 4904 4233 5866 65 -176 -278 A N
ATOM 2236 CA GLU A 254 2.537 14.438 16.228 1.00 40.79 A C
ANISOU 2236 CA GLU A 254 5030 4572 5898 -4 -228 -385 A C
ATOM 2237 C GLU A 254 1.573 14.648 17.385 1.00 45.69 A C
ANISOU 2237 C GLU A 254 5593 5277 6492 38 -213 -498 A C
ATOM 2238 O GLU A 254 1.384 15.779 17.838 1.00 46.16 A O
ANISOU 2238 O GLU A 254 5638 5232 6669 56 -138 -623 A O
ATOM 2239 CB GLU A 254 3.973 14.722 16.668 1.00 44.34 A C
ANISOU 2239 CB GLU A 254 5467 5016 6364 -103 -209 -514 A C
ATOM 2240 CG GLU A 254 4.479 13.785 17.747 1.00 44.49 A C
ANISOU 2240 CG GLU A 254 5423 5267 6215 -139 -260 -584 A C
ATOM 2241 CD GLU A 254 5.949 13.994 18.045 1.00 59.95 A C
ANISOU 2241 CD GLU A 254 7337 7286 8156 -229 -253 -697 A C
ATOM 2242 OE1 GLU A 254 6.453 15.103 17.798 1.00 55.45 A O
ANISOU 2242 OE1 GLU A 254 6773 6567 7728 -294 -186 -806 A O
ATOM 2243 OE2 GLU A 254 6.612 13.025 18.460 1.00 59.80 A O
ANISOU 2243 OE2 GLU A 254 7276 7460 7987 -229 -300 -664 A O
ATOM 2244 N GLY A 255 0.948 13.578 17.858 1.00 39.51 A N
ANISOU 2244 N GLY A 255 4778 4667 5568 49 -263 -459 A N
ATOM 2245 CA GLY A 255 0.045 13.734 18.983 1.00 42.54 A C
ANISOU 2245 CA GLY A 255 5098 5157 5909 87 -246 -561 A C
ATOM 2246 C GLY A 255 -0.685 12.443 19.284 1.00 39.65 A C
ANISOU 2246 C GLY A 255 4707 4960 5399 91 -283 -475 A C
ATOM 2247 O GLY A 255 -0.351 11.383 18.757 1.00 37.87 A O
ANISOU 2247 O GLY A 255 4518 4759 5112 53 -307 -362 A O
ATOM 2248 N ASN A 256 -1.680 12.557 20.159 1.00 39.37 A N
ANISOU 2248 N ASN A 256 4609 5028 5322 131 -265 -541 A N
ATOM 2249 CA ASN A 256 -2.495 11.420 20.566 1.00 40.64 A C
ANISOU 2249 CA ASN A 256 4739 5343 5360 125 -270 -472 A C
ATOM 2250 C ASN A 256 -3.618 11.223 19.564 1.00 39.84 A C
ANISOU 2250 C ASN A 256 4632 5221 5285 145 -277 -377 A C
ATOM 2251 O ASN A 256 -4.478 12.098 19.399 1.00 41.48 A O
ANISOU 2251 O ASN A 256 4797 5409 5554 221 -266 -405 A O
ATOM 2252 CB ASN A 256 -3.075 11.624 21.961 1.00 40.04 A C
ANISOU 2252 CB ASN A 256 4581 5423 5210 155 -244 -585 A C
ATOM 2253 CG ASN A 256 -2.020 11.536 23.044 1.00 43.05 A C
ANISOU 2253 CG ASN A 256 4928 5932 5495 130 -242 -671 A C
ATOM 2254 ND2 ASN A 256 -1.834 12.627 23.760 1.00 47.29 A N
ANISOU 2254 ND2 ASN A 256 5410 6494 6062 136 -221 -865 A N
ATOM 2255 OD1 ASN A 256 -1.355 10.509 23.211 1.00 42.78 A O
ANISOU 2255 OD1 ASN A 256 4908 5984 5361 109 -249 -569 A O
ATOM 2256 N AILE A 257 -3.645 10.048 18.936 0.58 38.10 A N
ANISOU 2256 N AILE A 257 4439 5025 5011 79 -282 -276 A N
ATOM 2257 N BILE A 257 -3.608 10.078 18.902 0.42 38.28 A N
ANISOU 2257 N BILE A 257 4464 5042 5037 80 -283 -275 A N
ATOM 2258 CA AILE A 257 -4.558 9.740 17.841 0.58 41.75 A C
ANISOU 2258 CA AILE A 257 4875 5516 5472 64 -290 -212 A C
ATOM 2259 CA BILE A 257 -4.582 9.742 17.879 0.42 41.76 A C
ANISOU 2259 CA BILE A 257 4875 5520 5472 65 -290 -214 A C
ATOM 2260 C AILE A 257 -5.199 8.387 18.121 0.58 41.44 A C
ANISOU 2260 C AILE A 257 4814 5584 5348 -26 -246 -193 A C
ATOM 2261 C BILE A 257 -5.220 8.423 18.279 0.42 41.48 A C
ANISOU 2261 C BILE A 257 4816 5596 5350 -21 -244 -199 A C
ATOM 2262 O AILE A 257 -4.487 7.387 18.278 0.58 43.51 A O
ANISOU 2262 O AILE A 257 5139 5807 5587 -93 -206 -151 A O
ATOM 2263 O BILE A 257 -4.524 7.493 18.701 0.42 43.47 A O
ANISOU 2263 O BILE A 257 5123 5822 5570 -75 -202 -163 A O
ATOM 2264 CB AILE A 257 -3.818 9.719 16.489 0.58 43.57 A C
ANISOU 2264 CB AILE A 257 5163 5649 5744 40 -318 -140 A C
ATOM 2265 CB BILE A 257 -3.936 9.641 16.482 0.42 43.49 A C
ANISOU 2265 CB BILE A 257 5146 5652 5726 36 -316 -140 A C
ATOM 2266 CG1AILE A 257 -3.345 11.135 16.121 0.58 41.83 A C
ANISOU 2266 CG1AILE A 257 4961 5303 5629 131 -331 -139 A C
ATOM 2267 CG1BILE A 257 -2.929 10.780 16.254 0.42 41.38 A C
ANISOU 2267 CG1BILE A 257 4928 5237 5557 94 -331 -143 A C
ATOM 2268 CG2AILE A 257 -4.696 9.094 15.417 0.58 42.90 A C
ANISOU 2268 CG2AILE A 257 5026 5667 5607 -8 -323 -98 A C
ATOM 2269 CG2BILE A 257 -5.013 9.641 15.415 0.42 44.80 A C
ANISOU 2269 CG2BILE A 257 5237 5920 5863 46 -333 -99 A C
ATOM 2270 CD1AILE A 257 -2.054 11.172 15.328 0.58 49.29 A C
ANISOU 2270 CD1AILE A 257 5982 6126 6618 95 -343 -91 A C
ATOM 2271 CD1BILE A 257 -3.545 12.089 15.820 0.42 45.51 A C
ANISOU 2271 CD1BILE A 257 5415 5713 6164 210 -324 -127 A C
ATOM 2272 N GLY A 258 -6.528 8.350 18.173 1.00 40.90 A N
ANISOU 2272 N GLY A 258 4653 5644 5242 -26 -233 -218 A N
ATOM 2273 CA GLY A 258 -7.235 7.105 18.431 1.00 43.60 A C
ANISOU 2273 CA GLY A 258 4966 6079 5522 -138 -163 -218 A C
ATOM 2274 C GLY A 258 -8.637 7.346 18.959 1.00 42.87 A C
ANISOU 2274 C GLY A 258 4753 6155 5383 -116 -149 -271 A C
ATOM 2275 O GLY A 258 -9.244 8.391 18.725 1.00 48.61 A O
ANISOU 2275 O GLY A 258 5404 6944 6121 -10 -199 -296 A O
ATOM 2276 N SER A 259 -9.152 6.330 19.646 1.00 45.69 A N
ANISOU 2276 N SER A 259 5090 6580 5691 -210 -61 -275 A N
ATOM 2277 CA SER A 259 -10.501 6.333 20.192 1.00 49.61 A C
ANISOU 2277 CA SER A 259 5464 7256 6132 -220 -28 -327 A C
ATOM 2278 C SER A 259 -10.464 6.599 21.692 1.00 51.63 A C
ANISOU 2278 C SER A 259 5715 7554 6348 -144 -1 -334 A C
ATOM 2279 O SER A 259 -9.404 6.637 22.315 1.00 49.97 A O
ANISOU 2279 O SER A 259 5586 7263 6138 -100 -1 -300 A O
ATOM 2280 CB SER A 259 -11.186 4.987 19.926 1.00 51.45 A C
ANISOU 2280 CB SER A 259 5664 7544 6339 -406 81 -341 A C
ATOM 2281 OG SER A 259 -10.541 3.967 20.689 1.00 51.19 A O
ANISOU 2281 OG SER A 259 5737 7393 6321 -468 195 -268 A O
ATOM 2282 N GLU A 260 -11.649 6.752 22.288 1.00 55.38 A N
ANISOU 2282 N GLU A 260 6074 8200 6770 -132 27 -386 A N
ATOM 2283 CA GLU A 260 -11.700 6.812 23.746 1.00 57.46 A C
ANISOU 2283 CA GLU A 260 6317 8547 6969 -81 71 -395 A C
ATOM 2284 C GLU A 260 -11.178 5.521 24.365 1.00 51.51 A C
ANISOU 2284 C GLU A 260 5639 7756 6177 -169 181 -289 A C
ATOM 2285 O GLU A 260 -10.692 5.523 25.501 1.00 65.86 A O
ANISOU 2285 O GLU A 260 7467 9631 7924 -103 207 -255 A O
ATOM 2286 CB GLU A 260 -13.128 7.072 24.243 1.00 61.76 A C
ANISOU 2286 CB GLU A 260 6715 9295 7457 -65 97 -465 A C
ATOM 2287 CG GLU A 260 -13.869 8.183 23.538 1.00 79.30 A C
ANISOU 2287 CG GLU A 260 8840 11578 9713 40 20 -534 A C
ATOM 2288 CD GLU A 260 -14.734 7.669 22.408 1.00 88.74 A C
ANISOU 2288 CD GLU A 260 9947 12874 10895 -58 21 -530 A C
ATOM 2289 OE1 GLU A 260 -14.276 6.761 21.679 1.00 70.72 A O
ANISOU 2289 OE1 GLU A 260 7733 10506 8632 -196 46 -492 A O
ATOM 2290 OE2 GLU A 260 -15.877 8.157 22.263 1.00 94.36 A O
ANISOU 2290 OE2 GLU A 260 10508 13776 11568 3 6 -578 A O
ATOM 2291 N LEU A 261 -11.271 4.414 23.630 1.00 55.45 A N
ANISOU 2291 N LEU A 261 6181 8169 6718 -311 262 -237 A N
ATOM 2292 CA LEU A 261 -10.897 3.107 24.150 1.00 59.01 A C
ANISOU 2292 CA LEU A 261 6712 8544 7166 -388 415 -114 A C
ATOM 2293 C LEU A 261 -9.384 2.920 24.135 1.00 61.97 A C
ANISOU 2293 C LEU A 261 7212 8771 7561 -318 402 -12 A C
ATOM 2294 O LEU A 261 -8.807 2.354 25.072 1.00 55.37 A O
ANISOU 2294 O LEU A 261 6419 7946 6672 -262 488 118 A O
ATOM 2295 CB LEU A 261 -11.570 2.026 23.306 1.00 65.31 A C
ANISOU 2295 CB LEU A 261 7509 9275 8030 -585 536 -135 A C
ATOM 2296 CG LEU A 261 -12.903 1.401 23.736 1.00 79.56 A C
ANISOU 2296 CG LEU A 261 9213 11205 9810 -716 670 -172 A C
ATOM 2297 CD1 LEU A 261 -13.009 -0.007 23.131 1.00 75.12 A C
ANISOU 2297 CD1 LEU A 261 8714 10483 9346 -930 863 -164 A C
ATOM 2298 CD2 LEU A 261 -13.098 1.355 25.250 1.00 73.28 A C
ANISOU 2298 CD2 LEU A 261 8392 10522 8927 -630 741 -79 A C
ATOM 2299 N LYS A 262 -8.724 3.402 23.087 1.00 47.79 A N
ANISOU 2299 N LYS A 262 5464 6865 5829 -308 298 -55 A N
ATOM 2300 CA LYS A 262 -7.306 3.157 22.913 1.00 42.84 A C
ANISOU 2300 CA LYS A 262 4945 6103 5227 -260 291 33 A C
ATOM 2301 C LYS A 262 -6.731 4.242 22.020 1.00 46.98 A C
ANISOU 2301 C LYS A 262 5479 6573 5797 -212 141 -48 A C
ATOM 2302 O LYS A 262 -7.282 4.519 20.952 1.00 44.36 A O
ANISOU 2302 O LYS A 262 5120 6222 5514 -268 96 -116 A O
ATOM 2303 CB LYS A 262 -7.061 1.782 22.298 1.00 48.35 A C
ANISOU 2303 CB LYS A 262 5738 6632 6002 -374 437 118 A C
ATOM 2304 CG LYS A 262 -5.604 1.367 22.318 1.00 55.68 A C
ANISOU 2304 CG LYS A 262 6772 7441 6945 -296 461 241 A C
ATOM 2305 CD LYS A 262 -5.022 1.405 20.925 1.00 56.28 A C
ANISOU 2305 CD LYS A 262 6907 7371 7106 -353 407 188 A C
ATOM 2306 CE LYS A 262 -3.674 0.705 20.851 1.00 62.30 A C
ANISOU 2306 CE LYS A 262 7775 7999 7899 -295 475 318 A C
ATOM 2307 NZ LYS A 262 -2.562 1.626 21.169 1.00 61.82 A N
ANISOU 2307 NZ LYS A 262 7699 8014 7774 -158 336 331 A N
ATOM 2308 N ARG A 263 -5.643 4.860 22.454 1.00 44.41 A N
ANISOU 2308 N ARG A 263 5178 6246 5448 -112 75 -40 A N
ATOM 2309 CA AARG A 263 -4.936 5.886 21.701 0.50 43.41 A C
ANISOU 2309 CA AARG A 263 5073 6041 5380 -72 -37 -104 A C
ATOM 2310 CA BARG A 263 -4.964 5.802 21.582 0.50 43.55 A C
ANISOU 2310 CA BARG A 263 5095 6047 5404 -82 -33 -99 A C
ATOM 2311 C ARG A 263 -3.483 5.481 21.488 1.00 44.43 A C
ANISOU 2311 C ARG A 263 5285 6079 5518 -58 -34 -28 A C
ATOM 2312 O ARG A 263 -2.938 4.654 22.223 1.00 41.79 A O
ANISOU 2312 O ARG A 263 4973 5784 5121 -29 39 74 A O
ATOM 2313 CB AARG A 263 -4.994 7.239 22.427 0.50 49.19 A C
ANISOU 2313 CB AARG A 263 5736 6859 6094 17 -106 -221 A C
ATOM 2314 CB BARG A 263 -5.178 7.251 22.028 0.50 50.40 A C
ANISOU 2314 CB BARG A 263 5894 6981 6273 2 -113 -220 A C
ATOM 2315 CG AARG A 263 -6.213 8.083 22.066 0.50 50.56 A C
ANISOU 2315 CG AARG A 263 5839 7058 6312 38 -137 -305 A C
ATOM 2316 CG BARG A 263 -4.504 7.643 23.309 0.50 50.60 A C
ANISOU 2316 CG BARG A 263 5888 7118 6221 68 -117 -266 A C
ATOM 2317 CD AARG A 263 -6.677 8.948 23.223 0.50 56.80 A C
ANISOU 2317 CD AARG A 263 6548 7971 7062 115 -138 -416 A C
ATOM 2318 CD BARG A 263 -5.256 8.802 23.959 0.50 53.85 A C
ANISOU 2318 CD BARG A 263 6211 7619 6630 124 -140 -413 A C
ATOM 2319 NE AARG A 263 -8.103 9.237 23.120 0.50 61.50 A N
ANISOU 2319 NE AARG A 263 7058 8645 7663 136 -128 -454 A N
ATOM 2320 NE BARG A 263 -6.595 8.434 24.404 0.50 60.19 A N
ANISOU 2320 NE BARG A 263 6946 8541 7383 118 -93 -406 A N
ATOM 2321 CZ AARG A 263 -8.656 9.932 22.134 0.50 60.53 A C
ANISOU 2321 CZ AARG A 263 6911 8468 7619 180 -163 -463 A C
ATOM 2322 CZ BARG A 263 -7.438 9.262 25.010 0.50 58.51 A C
ANISOU 2322 CZ BARG A 263 6646 8426 7158 173 -94 -523 A C
ATOM 2323 NH1AARG A 263 -7.921 10.492 21.187 0.50 60.91 A N
ANISOU 2323 NH1AARG A 263 7023 8362 7757 205 -204 -438 A N
ATOM 2324 NH1BARG A 263 -7.101 10.512 25.287 0.50 62.00 A N
ANISOU 2324 NH1BARG A 263 7067 8841 7651 235 -123 -668 A N
ATOM 2325 NH2AARG A 263 -9.978 10.067 22.095 0.50 60.70 A N
ANISOU 2325 NH2AARG A 263 6831 8616 7618 209 -150 -483 A N
ATOM 2326 NH2BARG A 263 -8.648 8.826 25.347 0.50 64.29 A N
ANISOU 2326 NH2BARG A 263 7309 9281 7837 157 -48 -506 A N
ATOM 2327 N AASP A 264 -2.859 6.125 20.503 0.28 38.03 A N
ANISOU 2327 N AASP A 264 4509 5163 4779 -60 -109 -63 A N
ATOM 2328 N BASP A 264 -2.870 6.072 20.467 0.72 37.59 A N
ANISOU 2328 N BASP A 264 4455 5103 4723 -64 -106 -60 A N
ATOM 2329 CA AASP A 264 -1.447 5.968 20.190 0.28 41.21 A C
ANISOU 2329 CA AASP A 264 4973 5492 5194 -45 -123 -15 A C
ATOM 2330 CA BASP A 264 -1.447 5.996 20.209 0.72 41.16 A C
ANISOU 2330 CA BASP A 264 4965 5488 5187 -43 -125 -17 A C
ATOM 2331 C AASP A 264 -0.820 7.350 20.090 0.28 40.18 A C
ANISOU 2331 C AASP A 264 4821 5344 5102 -7 -211 -115 A C
ATOM 2332 C BASP A 264 -0.896 7.410 20.266 0.72 39.94 A C
ANISOU 2332 C BASP A 264 4779 5333 5062 -0 -211 -125 A C
ATOM 2333 O AASP A 264 -1.380 8.235 19.433 0.28 41.52 A O
ANISOU 2333 O AASP A 264 4977 5451 5345 -7 -251 -174 A O
ATOM 2334 O BASP A 264 -1.586 8.367 19.891 0.72 41.93 A O
ANISOU 2334 O BASP A 264 5005 5549 5378 8 -247 -200 A O
ATOM 2335 CB AASP A 264 -1.243 5.227 18.865 0.28 45.86 A C
ANISOU 2335 CB AASP A 264 5635 5942 5847 -118 -95 41 A C
ATOM 2336 CB BASP A 264 -1.106 5.424 18.817 0.72 46.76 A C
ANISOU 2336 CB BASP A 264 5748 6053 5966 -110 -112 32 A C
ATOM 2337 CG AASP A 264 -1.518 3.750 18.973 0.28 43.91 A C
ANISOU 2337 CG AASP A 264 5432 5659 5594 -172 37 128 A C
ATOM 2338 CG BASP A 264 -1.716 4.070 18.557 0.72 42.35 A C
ANISOU 2338 CG BASP A 264 5223 5452 5415 -191 2 90 A C
ATOM 2339 OD1AASP A 264 -0.832 3.072 19.765 0.28 43.59 A O
ANISOU 2339 OD1AASP A 264 5418 5632 5511 -112 109 232 A O
ATOM 2340 OD1BASP A 264 -1.802 3.248 19.496 0.72 44.53 A O
ANISOU 2340 OD1BASP A 264 5508 5762 5651 -173 101 166 A O
ATOM 2341 OD2AASP A 264 -2.420 3.267 18.258 0.28 45.16 A O
ANISOU 2341 OD2AASP A 264 5587 5781 5789 -274 83 94 A O
ATOM 2342 OD2BASP A 264 -2.065 3.816 17.382 0.72 39.10 A O
ANISOU 2342 OD2BASP A 264 4827 4979 5051 -277 7 58 A O
ATOM 2343 N TYR A 265 0.327 7.535 20.728 1.00 39.67 A N
ANISOU 2343 N TYR A 265 4742 5344 4989 28 -226 -133 A N
ATOM 2344 CA TYR A 265 1.095 8.768 20.595 1.00 37.50 A C
ANISOU 2344 CA TYR A 265 4448 5032 4769 28 -280 -250 A C
ATOM 2345 C TYR A 265 1.982 8.544 19.376 1.00 38.33 A C
ANISOU 2345 C TYR A 265 4625 5000 4939 -6 -294 -179 A C
ATOM 2346 O TYR A 265 2.903 7.724 19.428 1.00 41.33 A O
ANISOU 2346 O TYR A 265 5024 5418 5263 4 -276 -99 A O
ATOM 2347 CB TYR A 265 1.903 9.077 21.842 1.00 42.37 A C
ANISOU 2347 CB TYR A 265 4982 5836 5282 54 -286 -341 A C
ATOM 2348 CG TYR A 265 2.532 10.441 21.754 1.00 42.33 A C
ANISOU 2348 CG TYR A 265 4947 5777 5359 16 -311 -516 A C
ATOM 2349 CD1 TYR A 265 1.833 11.575 22.119 1.00 49.23 A C
ANISOU 2349 CD1 TYR A 265 5784 6616 6305 12 -296 -676 A C
ATOM 2350 CD2 TYR A 265 3.812 10.595 21.244 1.00 43.69 A C
ANISOU 2350 CD2 TYR A 265 5133 5910 5558 -22 -328 -524 A C
ATOM 2351 CE1 TYR A 265 2.408 12.834 22.011 1.00 54.21 A C
ANISOU 2351 CE1 TYR A 265 6402 7145 7050 -37 -277 -845 A C
ATOM 2352 CE2 TYR A 265 4.399 11.846 21.138 1.00 51.10 A C
ANISOU 2352 CE2 TYR A 265 6047 6774 6595 -84 -322 -695 A C
ATOM 2353 CZ TYR A 265 3.690 12.959 21.518 1.00 52.84 A C
ANISOU 2353 CZ TYR A 265 6242 6929 6905 -95 -286 -856 A C
ATOM 2354 OH TYR A 265 4.265 14.206 21.405 1.00 57.61 A O
ANISOU 2354 OH TYR A 265 6835 7412 7643 -169 -239 -1035 A O
ATOM 2355 N THR A 266 1.674 9.208 18.263 1.00 37.68 A N
ANISOU 2355 N THR A 266 4578 4775 4964 -28 -316 -188 A N
ATOM 2356 CA THR A 266 2.310 8.837 16.995 1.00 39.13 A C
ANISOU 2356 CA THR A 266 4825 4854 5190 -62 -323 -105 A C
ATOM 2357 C THR A 266 2.241 10.009 16.017 1.00 43.75 A C
ANISOU 2357 C THR A 266 5423 5317 5883 -60 -345 -123 A C
ATOM 2358 O THR A 266 1.920 11.139 16.399 1.00 40.49 A O
ANISOU 2358 O THR A 266 4981 4868 5535 -29 -338 -205 A O
ATOM 2359 CB THR A 266 1.655 7.557 16.450 1.00 39.30 A C
ANISOU 2359 CB THR A 266 4880 4873 5178 -94 -286 -16 A C
ATOM 2360 CG2 THR A 266 0.258 7.812 15.937 1.00 42.40 A C
ANISOU 2360 CG2 THR A 266 5242 5278 5591 -105 -294 -30 A C
ATOM 2361 OG1 THR A 266 2.460 7.006 15.396 1.00 41.11 A O
ANISOU 2361 OG1 THR A 266 5165 5027 5427 -131 -277 44 A O
ATOM 2362 N ILE A 267 2.582 9.753 14.748 1.00 37.10 A N
ANISOU 2362 N ILE A 267 4624 4407 5064 -86 -352 -42 A N
ATOM 2363 CA ILE A 267 2.624 10.806 13.741 1.00 36.77 A C
ANISOU 2363 CA ILE A 267 4595 4263 5114 -65 -357 -12 A C
ATOM 2364 C ILE A 267 1.675 10.476 12.598 1.00 41.29 A C
ANISOU 2364 C ILE A 267 5155 4878 5654 -52 -369 76 A C
ATOM 2365 O ILE A 267 1.330 9.321 12.344 1.00 42.86 A O
ANISOU 2365 O ILE A 267 5351 5158 5776 -103 -368 90 A O
ATOM 2366 CB ILE A 267 4.049 11.068 13.183 1.00 35.67 A C
ANISOU 2366 CB ILE A 267 4493 4044 5017 -104 -352 3 A C
ATOM 2367 CG1 ILE A 267 4.638 9.784 12.586 1.00 40.46 A C
ANISOU 2367 CG1 ILE A 267 5130 4695 5548 -146 -360 66 A C
ATOM 2368 CG2 ILE A 267 4.959 11.657 14.245 1.00 40.65 A C
ANISOU 2368 CG2 ILE A 267 5100 4671 5677 -129 -337 -118 A C
ATOM 2369 CD1 ILE A 267 5.898 10.036 11.775 1.00 44.93 A C
ANISOU 2369 CD1 ILE A 267 5722 5200 6148 -178 -357 98 A C
ATOM 2370 N LEU A 268 1.281 11.538 11.891 1.00 39.90 A N
ANISOU 2370 N LEU A 268 4964 4656 5542 17 -363 134 A N
ATOM 2371 CA ALEU A 268 0.359 11.489 10.765 0.59 40.99 A C
ANISOU 2371 CA ALEU A 268 5052 4897 5626 60 -379 229 A C
ATOM 2372 CA BLEU A 268 0.373 11.475 10.756 0.41 41.00 A C
ANISOU 2372 CA BLEU A 268 5054 4898 5626 59 -380 229 A C
ATOM 2373 C LEU A 268 0.838 12.478 9.710 1.00 41.37 A C
ANISOU 2373 C LEU A 268 5117 4861 5740 126 -357 347 A C
ATOM 2374 O LEU A 268 1.109 13.633 10.042 1.00 46.62 A O
ANISOU 2374 O LEU A 268 5810 5369 6533 187 -305 354 A O
ATOM 2375 CB ALEU A 268 -1.059 11.883 11.207 0.59 46.22 A C
ANISOU 2375 CB ALEU A 268 5639 5648 6276 144 -378 219 A C
ATOM 2376 CB BLEU A 268 -1.056 11.800 11.209 0.41 46.19 A C
ANISOU 2376 CB BLEU A 268 5634 5649 6265 137 -379 216 A C
ATOM 2377 CG ALEU A 268 -2.123 10.862 11.565 0.59 47.84 A C
ANISOU 2377 CG ALEU A 268 5778 6027 6373 91 -395 161 A C
ATOM 2378 CG BLEU A 268 -2.243 11.365 10.367 0.41 49.34 A C
ANISOU 2378 CG BLEU A 268 5935 6264 6550 155 -406 267 A C
ATOM 2379 CD1ALEU A 268 -3.346 11.613 12.099 0.59 45.21 A C
ANISOU 2379 CD1ALEU A 268 5366 5758 6053 201 -386 154 A C
ATOM 2380 CD1BLEU A 268 -2.394 9.873 10.451 0.41 54.14 A C
ANISOU 2380 CD1BLEU A 268 6533 6978 7061 10 -413 180 A C
ATOM 2381 CD2ALEU A 268 -2.492 10.053 10.346 0.59 54.80 A C
ANISOU 2381 CD2ALEU A 268 6605 7072 7145 31 -416 195 A C
ATOM 2382 CD2BLEU A 268 -3.494 12.048 10.878 0.41 47.54 A C
ANISOU 2382 CD2BLEU A 268 5623 6109 6329 271 -397 270 A C
ATOM 2383 N GLY A 269 0.919 12.063 8.448 1.00 43.66 A N
ANISOU 2383 N GLY A 269 5386 5256 5947 113 -379 434 A N
ATOM 2384 CA GLY A 269 1.232 13.025 7.401 1.00 43.45 A C
ANISOU 2384 CA GLY A 269 5362 5184 5965 200 -346 586 A C
ATOM 2385 C GLY A 269 1.782 12.393 6.140 1.00 42.09 A C
ANISOU 2385 C GLY A 269 5178 5126 5687 145 -370 647 A C
ATOM 2386 O GLY A 269 2.137 11.217 6.104 1.00 39.07 A O
ANISOU 2386 O GLY A 269 4807 4809 5230 25 -399 550 A O
ATOM 2387 N ASP A 270 1.907 13.240 5.102 1.00 43.62 A N
ANISOU 2387 N ASP A 270 5354 5331 5890 244 -337 819 A N
ATOM 2388 CA AASP A 270 2.259 12.748 3.772 0.35 46.82 A C
ANISOU 2388 CA AASP A 270 5718 5908 6162 214 -359 892 A C
ATOM 2389 CA BASP A 270 2.258 12.750 3.771 0.65 46.83 A C
ANISOU 2389 CA BASP A 270 5720 5909 6164 214 -359 893 A C
ATOM 2390 C ASP A 270 3.641 12.110 3.738 1.00 43.30 A C
ANISOU 2390 C ASP A 270 5353 5358 5741 78 -357 808 A C
ATOM 2391 O ASP A 270 3.875 11.184 2.954 1.00 44.12 A O
ANISOU 2391 O ASP A 270 5427 5615 5721 -0 -383 771 A O
ATOM 2392 CB AASP A 270 2.192 13.884 2.745 0.35 48.76 A C
ANISOU 2392 CB AASP A 270 5929 6183 6413 372 -306 1132 A C
ATOM 2393 CB BASP A 270 2.188 13.898 2.752 0.65 48.74 A C
ANISOU 2393 CB BASP A 270 5928 6179 6413 374 -305 1133 A C
ATOM 2394 CG AASP A 270 2.429 13.401 1.323 0.35 51.43 A C
ANISOU 2394 CG AASP A 270 6196 6773 6573 356 -333 1214 A C
ATOM 2395 CG BASP A 270 0.773 14.404 2.526 0.65 53.20 A C
ANISOU 2395 CG BASP A 270 6377 6932 6903 546 -308 1255 A C
ATOM 2396 OD1AASP A 270 1.677 12.517 0.861 0.35 50.40 A O
ANISOU 2396 OD1AASP A 270 5954 6939 6255 313 -397 1138 A O
ATOM 2397 OD1BASP A 270 -0.184 13.634 2.719 0.65 55.36 A O
ANISOU 2397 OD1BASP A 270 6559 7425 7050 508 -375 1145 A O
ATOM 2398 OD2AASP A 270 3.373 13.898 0.671 0.35 48.76 A O
ANISOU 2398 OD2AASP A 270 5902 6347 6277 372 -281 1336 A O
ATOM 2399 OD2BASP A 270 0.615 15.582 2.149 0.65 58.96 A O
ANISOU 2399 OD2BASP A 270 7103 7592 7708 726 -226 1471 A O
ATOM 2400 N ALA A 271 4.575 12.591 4.563 1.00 40.82 A N
ANISOU 2400 N ALA A 271 5126 4807 5578 46 -318 763 A N
ATOM 2401 CA ALA A 271 5.917 12.007 4.565 1.00 41.79 A C
ANISOU 2401 CA ALA A 271 5302 4866 5710 -65 -317 692 A C
ATOM 2402 C ALA A 271 5.879 10.521 4.878 1.00 41.41 A C
ANISOU 2402 C ALA A 271 5253 4914 5568 -155 -357 559 A C
ATOM 2403 O ALA A 271 6.782 9.775 4.486 1.00 39.86 A O
ANISOU 2403 O ALA A 271 5079 4732 5335 -223 -351 525 A O
ATOM 2404 CB ALA A 271 6.810 12.722 5.578 1.00 41.38 A C
ANISOU 2404 CB ALA A 271 5308 4605 5811 -95 -273 625 A C
ATOM 2405 N VAL A 272 4.857 10.068 5.604 1.00 42.60 A N
ANISOU 2405 N VAL A 272 5378 5115 5691 -154 -377 485 A N
ATOM 2406 CA VAL A 272 4.751 8.645 5.887 1.00 39.31 A C
ANISOU 2406 CA VAL A 272 4969 4756 5210 -241 -375 375 A C
ATOM 2407 C VAL A 272 4.492 7.864 4.603 1.00 41.26 A C
ANISOU 2407 C VAL A 272 5168 5169 5339 -299 -372 361 A C
ATOM 2408 O VAL A 272 5.127 6.829 4.362 1.00 39.01 A O
ANISOU 2408 O VAL A 272 4918 4872 5034 -379 -335 291 A O
ATOM 2409 CB VAL A 272 3.655 8.365 6.931 1.00 41.09 A C
ANISOU 2409 CB VAL A 272 5173 5003 5435 -236 -379 307 A C
ATOM 2410 CG1 VAL A 272 3.487 6.862 7.097 1.00 41.99 A C
ANISOU 2410 CG1 VAL A 272 5301 5152 5501 -332 -338 211 A C
ATOM 2411 CG2 VAL A 272 3.979 9.038 8.272 1.00 39.81 A C
ANISOU 2411 CG2 VAL A 272 5046 4711 5368 -192 -377 286 A C
ATOM 2412 N ASN A 273 3.528 8.320 3.777 1.00 41.05 A N
ANISOU 2412 N ASN A 273 5049 5324 5225 -254 -399 419 A N
ATOM 2413 CA AASN A 273 3.285 7.580 2.549 0.55 43.10 A C
ANISOU 2413 CA AASN A 273 5231 5802 5341 -325 -397 373 A C
ATOM 2414 CA BASN A 273 3.260 7.685 2.483 0.46 43.00 A C
ANISOU 2414 CA BASN A 273 5214 5801 5325 -314 -400 387 A C
ATOM 2415 C ASN A 273 4.513 7.628 1.640 1.00 41.07 A C
ANISOU 2415 C ASN A 273 5006 5527 5070 -337 -381 426 A C
ATOM 2416 O ASN A 273 4.768 6.654 0.924 1.00 41.11 A O
ANISOU 2416 O ASN A 273 4993 5633 4995 -436 -353 324 A O
ATOM 2417 CB AASN A 273 2.041 8.106 1.830 0.55 44.94 A C
ANISOU 2417 CB AASN A 273 5323 6309 5445 -254 -436 438 A C
ATOM 2418 CB BASN A 273 2.245 8.448 1.622 0.46 43.18 A C
ANISOU 2418 CB BASN A 273 5102 6079 5226 -217 -440 496 A C
ATOM 2419 CG AASN A 273 0.766 7.265 2.112 0.55 45.86 A C
ANISOU 2419 CG AASN A 273 5349 6595 5481 -342 -436 283 A C
ATOM 2420 CG BASN A 273 1.058 8.882 2.363 0.46 49.50 A C
ANISOU 2420 CG BASN A 273 5851 6916 6041 -145 -461 508 A C
ATOM 2421 ND2AASN A 273 -0.282 7.563 1.352 0.55 51.13 A N
ANISOU 2421 ND2AASN A 273 5855 7580 5993 -294 -474 316 A N
ATOM 2422 ND2BASN A 273 -0.121 8.546 1.853 0.46 43.60 A N
ANISOU 2422 ND2BASN A 273 4956 6470 5139 -161 -485 458 A N
ATOM 2423 OD1AASN A 273 0.723 6.367 2.983 0.55 48.19 A O
ANISOU 2423 OD1AASN A 273 5707 6757 5846 -447 -393 146 A O
ATOM 2424 OD1BASN A 273 1.181 9.568 3.363 0.46 52.74 A O
ANISOU 2424 OD1BASN A 273 6336 7114 6590 -75 -452 552 A O
ATOM 2425 N VAL A 274 5.265 8.731 1.649 1.00 40.21 A N
ANISOU 2425 N VAL A 274 4942 5290 5044 -250 -382 569 A N
ATOM 2426 CA VAL A 274 6.435 8.822 0.789 1.00 38.40 A C
ANISOU 2426 CA VAL A 274 4736 5055 4801 -266 -360 628 A C
ATOM 2427 C VAL A 274 7.489 7.814 1.227 1.00 40.28 A C
ANISOU 2427 C VAL A 274 5050 5166 5089 -359 -328 503 A C
ATOM 2428 O VAL A 274 8.078 7.118 0.389 1.00 39.95 A O
ANISOU 2428 O VAL A 274 4999 5204 4977 -418 -302 457 A O
ATOM 2429 CB VAL A 274 6.992 10.261 0.767 1.00 44.42 A C
ANISOU 2429 CB VAL A 274 5530 5679 5668 -170 -337 802 A C
ATOM 2430 CG1 VAL A 274 8.282 10.314 -0.055 1.00 43.38 A C
ANISOU 2430 CG1 VAL A 274 5419 5535 5527 -205 -304 856 A C
ATOM 2431 CG2 VAL A 274 5.968 11.225 0.170 1.00 48.98 A C
ANISOU 2431 CG2 VAL A 274 6029 6387 6194 -37 -339 973 A C
ATOM 2432 N ALA A 275 7.741 7.712 2.537 1.00 39.11 A N
ANISOU 2432 N ALA A 275 4967 4843 5050 -359 -322 452 A N
ATOM 2433 CA ALA A 275 8.717 6.743 3.032 1.00 38.95 A C
ANISOU 2433 CA ALA A 275 5004 4730 5065 -407 -282 370 A C
ATOM 2434 C ALA A 275 8.291 5.322 2.699 1.00 39.23 A C
ANISOU 2434 C ALA A 275 5037 4828 5039 -482 -231 252 A C
ATOM 2435 O ALA A 275 9.117 4.483 2.333 1.00 37.34 A O
ANISOU 2435 O ALA A 275 4828 4564 4797 -518 -172 203 A O
ATOM 2436 CB ALA A 275 8.906 6.897 4.540 1.00 37.42 A C
ANISOU 2436 CB ALA A 275 4850 4406 4961 -374 -286 350 A C
ATOM 2437 N ALA A 276 6.999 5.026 2.819 1.00 38.50 A N
ANISOU 2437 N ALA A 276 4906 4814 4909 -514 -234 191 A N
ATOM 2438 CA ALA A 276 6.530 3.680 2.520 1.00 39.06 A C
ANISOU 2438 CA ALA A 276 4970 4928 4943 -621 -153 44 A C
ATOM 2439 C ALA A 276 6.660 3.367 1.039 1.00 41.79 A C
ANISOU 2439 C ALA A 276 5253 5448 5178 -691 -136 -20 A C
ATOM 2440 O ALA A 276 6.999 2.235 0.669 1.00 41.81 A O
ANISOU 2440 O ALA A 276 5281 5419 5185 -780 -36 -150 A O
ATOM 2441 CB ALA A 276 5.084 3.520 2.996 1.00 39.94 A C
ANISOU 2441 CB ALA A 276 5032 5109 5034 -659 -157 -21 A C
ATOM 2442 N ARG A 277 6.404 4.355 0.170 1.00 40.03 A N
ANISOU 2442 N ARG A 277 4943 5414 4852 -644 -214 75 A N
ATOM 2443 CA ARG A 277 6.558 4.142 -1.264 1.00 41.98 A C
ANISOU 2443 CA ARG A 277 5107 5886 4957 -696 -204 31 A C
ATOM 2444 C ARG A 277 8.022 3.945 -1.637 1.00 41.30 A C
ANISOU 2444 C ARG A 277 5087 5695 4910 -693 -163 53 A C
ATOM 2445 O ARG A 277 8.346 3.131 -2.510 1.00 43.63 A O
ANISOU 2445 O ARG A 277 5355 6088 5134 -778 -101 -73 A O
ATOM 2446 CB ARG A 277 5.974 5.330 -2.024 1.00 49.41 A C
ANISOU 2446 CB ARG A 277 5934 7066 5772 -602 -288 187 A C
ATOM 2447 CG ARG A 277 6.378 5.407 -3.476 1.00 69.42 A C
ANISOU 2447 CG ARG A 277 8379 9851 8146 -611 -288 214 A C
ATOM 2448 CD ARG A 277 5.318 6.136 -4.263 1.00 97.31 A C
ANISOU 2448 CD ARG A 277 11750 13728 11495 -534 -350 321 A C
ATOM 2449 NE ARG A 277 5.637 7.557 -4.302 1.00 99.66 A N
ANISOU 2449 NE ARG A 277 12071 13957 11840 -360 -379 607 A N
ATOM 2450 CZ ARG A 277 4.964 8.498 -3.652 1.00 90.37 A C
ANISOU 2450 CZ ARG A 277 10899 12702 10737 -234 -406 754 A C
ATOM 2451 NH1 ARG A 277 3.908 8.209 -2.908 1.00 89.28 A N
ANISOU 2451 NH1 ARG A 277 10733 12579 10613 -254 -429 653 A N
ATOM 2452 NH2 ARG A 277 5.374 9.760 -3.733 1.00 79.81 A N
ANISOU 2452 NH2 ARG A 277 9599 11248 9476 -89 -389 1001 A N
ATOM 2453 N LEU A 278 8.917 4.693 -1.002 1.00 40.31 A N
ANISOU 2453 N LEU A 278 5035 5389 4891 -603 -189 193 A N
ATOM 2454 CA LEU A 278 10.331 4.528 -1.312 1.00 38.23 A C
ANISOU 2454 CA LEU A 278 4815 5051 4658 -599 -151 213 A C
ATOM 2455 C LEU A 278 10.837 3.159 -0.872 1.00 39.93 A C
ANISOU 2455 C LEU A 278 5100 5131 4941 -646 -52 76 A C
ATOM 2456 O LEU A 278 11.625 2.527 -1.592 1.00 41.02 A O
ANISOU 2456 O LEU A 278 5240 5294 5052 -678 13 13 A O
ATOM 2457 CB LEU A 278 11.151 5.643 -0.672 1.00 40.57 A C
ANISOU 2457 CB LEU A 278 5153 5210 5054 -518 -189 363 A C
ATOM 2458 CG LEU A 278 10.905 7.055 -1.225 1.00 44.87 A C
ANISOU 2458 CG LEU A 278 5650 5829 5571 -459 -235 528 A C
ATOM 2459 CD1 LEU A 278 11.653 8.123 -0.392 1.00 46.80 A C
ANISOU 2459 CD1 LEU A 278 5943 5883 5956 -415 -238 622 A C
ATOM 2460 CD2 LEU A 278 11.262 7.142 -2.696 1.00 58.29 A C
ANISOU 2460 CD2 LEU A 278 7285 7723 7141 -469 -221 584 A C
ATOM 2461 N GLU A 279 10.412 2.689 0.310 1.00 37.81 A N
ANISOU 2461 N GLU A 279 4887 4715 4764 -636 -24 42 A N
ATOM 2462 CA GLU A 279 10.822 1.360 0.763 1.00 40.11 A C
ANISOU 2462 CA GLU A 279 5250 4856 5134 -652 104 -50 A C
ATOM 2463 C GLU A 279 10.388 0.300 -0.242 1.00 39.05 A C
ANISOU 2463 C GLU A 279 5093 4794 4952 -777 211 -235 A C
ATOM 2464 O GLU A 279 11.150 -0.619 -0.574 1.00 41.55 A O
ANISOU 2464 O GLU A 279 5451 5027 5308 -792 332 -311 A O
ATOM 2465 CB GLU A 279 10.232 1.080 2.151 1.00 38.47 A C
ANISOU 2465 CB GLU A 279 5093 4513 5013 -618 127 -32 A C
ATOM 2466 CG GLU A 279 10.762 -0.176 2.849 1.00 35.81 A C
ANISOU 2466 CG GLU A 279 4840 3992 4774 -581 277 -51 A C
ATOM 2467 CD GLU A 279 10.231 -1.478 2.277 1.00 46.43 A C
ANISOU 2467 CD GLU A 279 6213 5277 6153 -697 443 -220 A C
ATOM 2468 OE1 GLU A 279 9.070 -1.521 1.810 1.00 40.47 A O
ANISOU 2468 OE1 GLU A 279 5404 4625 5347 -824 437 -345 A O
ATOM 2469 OE2 GLU A 279 10.977 -2.485 2.299 1.00 40.97 A O
ANISOU 2469 OE2 GLU A 279 5588 4436 5543 -663 598 -239 A O
ATOM 2470 N ALA A 280 9.171 0.433 -0.768 1.00 40.08 A N
ANISOU 2470 N ALA A 280 5139 5101 4988 -869 176 -324 A N
ATOM 2471 CA ALA A 280 8.667 -0.538 -1.729 1.00 43.10 A C
ANISOU 2471 CA ALA A 280 5468 5603 5305 -1023 280 -550 A C
ATOM 2472 C ALA A 280 9.472 -0.524 -3.023 1.00 42.13 A C
ANISOU 2472 C ALA A 280 5292 5638 5077 -1044 286 -591 A C
ATOM 2473 O ALA A 280 9.606 -1.564 -3.681 1.00 45.72 A O
ANISOU 2473 O ALA A 280 5742 6103 5527 -1156 422 -797 A O
ATOM 2474 CB ALA A 280 7.185 -0.258 -2.002 1.00 46.80 A C
ANISOU 2474 CB ALA A 280 5816 6308 5657 -1109 218 -631 A C
ATOM 2475 N LEU A 281 10.017 0.634 -3.399 1.00 42.81 A N
ANISOU 2475 N LEU A 281 5340 5838 5087 -944 161 -406 A N
ATOM 2476 CA LEU A 281 10.835 0.732 -4.599 1.00 45.21 A C
ANISOU 2476 CA LEU A 281 5591 6305 5283 -953 166 -413 A C
ATOM 2477 C LEU A 281 12.090 -0.136 -4.536 1.00 47.41 A C
ANISOU 2477 C LEU A 281 5959 6389 5667 -940 289 -472 A C
ATOM 2478 O LEU A 281 12.631 -0.502 -5.589 1.00 48.82 A O
ANISOU 2478 O LEU A 281 6091 6697 5761 -988 345 -570 A O
ATOM 2479 CB LEU A 281 11.249 2.185 -4.827 1.00 52.36 A C
ANISOU 2479 CB LEU A 281 6461 7303 6131 -838 39 -165 A C
ATOM 2480 CG LEU A 281 10.346 3.090 -5.657 1.00 71.31 A C
ANISOU 2480 CG LEU A 281 8728 10013 8353 -821 -53 -77 A C
ATOM 2481 CD1 LEU A 281 10.983 4.478 -5.690 1.00 66.58 A C
ANISOU 2481 CD1 LEU A 281 8141 9383 7773 -693 -122 194 A C
ATOM 2482 CD2 LEU A 281 10.139 2.545 -7.064 1.00 62.88 A C
ANISOU 2482 CD2 LEU A 281 7530 9281 7080 -918 -18 -232 A C
ATOM 2483 N THR A 282 12.566 -0.471 -3.332 1.00 42.34 A N
ANISOU 2483 N THR A 282 5429 5468 5192 -861 337 -408 A N
ATOM 2484 CA THR A 282 13.779 -1.266 -3.225 1.00 40.79 A C
ANISOU 2484 CA THR A 282 5303 5107 5089 -807 459 -426 A C
ATOM 2485 C THR A 282 13.614 -2.657 -3.811 1.00 43.75 A C
ANISOU 2485 C THR A 282 5698 5429 5496 -916 651 -670 A C
ATOM 2486 O THR A 282 14.619 -3.315 -4.088 1.00 52.67 A O
ANISOU 2486 O THR A 282 6866 6469 6679 -874 769 -710 A O
ATOM 2487 CB THR A 282 14.230 -1.417 -1.762 1.00 40.16 A C
ANISOU 2487 CB THR A 282 5316 4789 5155 -679 482 -295 A C
ATOM 2488 CG2 THR A 282 14.517 -0.064 -1.142 1.00 41.78 A C
ANISOU 2488 CG2 THR A 282 5495 5040 5341 -594 317 -102 A C
ATOM 2489 OG1 THR A 282 13.213 -2.073 -1.001 1.00 40.20 A O
ANISOU 2489 OG1 THR A 282 5371 4661 5242 -719 557 -362 A O
ATOM 2490 N ARG A 283 12.375 -3.147 -3.943 1.00 44.00 A N
ANISOU 2490 N ARG A 283 5702 5502 5514 -1057 704 -848 A N
ATOM 2491 CA ARG A 283 12.167 -4.448 -4.560 1.00 43.39 A C
ANISOU 2491 CA ARG A 283 5634 5372 5479 -1201 913 -1130 A C
ATOM 2492 C ARG A 283 12.542 -4.446 -6.039 1.00 58.42 A C
ANISOU 2492 C ARG A 283 7431 7545 7219 -1286 916 -1279 A C
ATOM 2493 O ARG A 283 12.804 -5.513 -6.602 1.00 57.89 A O
ANISOU 2493 O ARG A 283 7381 7410 7204 -1379 1111 -1513 A O
ATOM 2494 CB ARG A 283 10.717 -4.898 -4.417 1.00 48.46 A C
ANISOU 2494 CB ARG A 283 6242 6044 6127 -1370 970 -1317 A C
ATOM 2495 CG ARG A 283 10.184 -4.947 -2.985 1.00 51.74 A C
ANISOU 2495 CG ARG A 283 6750 6223 6688 -1306 980 -1187 A C
ATOM 2496 CD ARG A 283 10.980 -5.913 -2.141 1.00 50.38 A C
ANISOU 2496 CD ARG A 283 6733 5677 6733 -1199 1179 -1124 A C
ATOM 2497 NE ARG A 283 10.380 -6.119 -0.823 1.00 44.95 A N
ANISOU 2497 NE ARG A 283 6123 4787 6169 -1152 1223 -1018 A N
ATOM 2498 CZ ARG A 283 10.532 -5.308 0.215 1.00 40.92 A C
ANISOU 2498 CZ ARG A 283 5631 4264 5653 -993 1072 -766 A C
ATOM 2499 NH1 ARG A 283 11.262 -4.209 0.136 1.00 44.70 A N
ANISOU 2499 NH1 ARG A 283 6064 4889 6030 -875 877 -601 A N
ATOM 2500 NH2 ARG A 283 9.927 -5.603 1.359 1.00 40.34 A N
ANISOU 2500 NH2 ARG A 283 5617 4031 5678 -964 1133 -693 A N
ATOM 2501 N GLN A 284 12.566 -3.279 -6.679 1.00 52.04 A N
ANISOU 2501 N GLN A 284 6512 7038 6221 -1252 724 -1148 A N
ATOM 2502 CA GLN A 284 12.894 -3.195 -8.099 1.00 56.96 A C
ANISOU 2502 CA GLN A 284 7015 7972 6654 -1318 717 -1258 A C
ATOM 2503 C GLN A 284 14.309 -2.704 -8.364 1.00 59.99 A C
ANISOU 2503 C GLN A 284 7421 8343 7029 -1184 679 -1078 A C
ATOM 2504 O GLN A 284 14.722 -2.661 -9.525 1.00 57.23 A O
ANISOU 2504 O GLN A 284 6978 8243 6525 -1225 687 -1153 A O
ATOM 2505 CB GLN A 284 11.905 -2.280 -8.836 1.00 55.67 A C
ANISOU 2505 CB GLN A 284 6684 8220 6249 -1367 557 -1228 A C
ATOM 2506 CG GLN A 284 10.462 -2.334 -8.367 1.00 79.55 A C
ANISOU 2506 CG GLN A 284 9663 11300 9263 -1453 529 -1310 A C
ATOM 2507 CD GLN A 284 9.667 -1.126 -8.834 1.00111.46 A C
ANISOU 2507 CD GLN A 284 13552 15714 13085 -1403 342 -1149 A C
ATOM 2508 NE2 GLN A 284 8.526 -0.883 -8.199 1.00104.86 A N
ANISOU 2508 NE2 GLN A 284 12687 14896 12258 -1415 284 -1129 A N
ATOM 2509 OE1 GLN A 284 10.076 -0.421 -9.759 1.00109.84 A O
ANISOU 2509 OE1 GLN A 284 13251 15779 12704 -1341 265 -1027 A O
ATOM 2510 N LEU A 285 15.061 -2.350 -7.330 1.00 54.36 A N
ANISOU 2510 N LEU A 285 6812 7380 6462 -1034 644 -858 A N
ATOM 2511 CA LEU A 285 16.410 -1.820 -7.454 1.00 54.26 A C
ANISOU 2511 CA LEU A 285 6805 7364 6447 -916 606 -688 A C
ATOM 2512 C LEU A 285 17.401 -2.799 -6.843 1.00 60.22 A C
ANISOU 2512 C LEU A 285 7662 7843 7374 -829 760 -716 A C
ATOM 2513 O LEU A 285 17.033 -3.683 -6.070 1.00 59.29 A O
ANISOU 2513 O LEU A 285 7634 7490 7404 -824 880 -789 A O
ATOM 2514 CB LEU A 285 16.510 -0.465 -6.748 1.00 56.89 A C
ANISOU 2514 CB LEU A 285 7142 7685 6790 -817 437 -414 A C
ATOM 2515 CG LEU A 285 15.577 0.614 -7.298 1.00 60.33 A C
ANISOU 2515 CG LEU A 285 7483 8366 7075 -853 303 -325 A C
ATOM 2516 CD1 LEU A 285 15.622 1.855 -6.426 1.00 67.84 A C
ANISOU 2516 CD1 LEU A 285 8465 9217 8096 -758 185 -84 A C
ATOM 2517 CD2 LEU A 285 15.959 0.966 -8.727 1.00 67.17 A C
ANISOU 2517 CD2 LEU A 285 8238 9533 7751 -882 291 -319 A C
ATOM 2518 N SER A 286 18.677 -2.633 -7.184 1.00 59.37 A N
ANISOU 2518 N SER A 286 7535 7774 7248 -747 768 -637 A N
ATOM 2519 CA SER A 286 19.698 -3.405 -6.485 1.00 63.80 A C
ANISOU 2519 CA SER A 286 8174 8107 7961 -613 896 -602 A C
ATOM 2520 C SER A 286 19.905 -2.901 -5.060 1.00 63.74 A C
ANISOU 2520 C SER A 286 8212 7959 8047 -482 811 -386 A C
ATOM 2521 O SER A 286 20.333 -3.675 -4.196 1.00 59.74 A O
ANISOU 2521 O SER A 286 7774 7255 7670 -360 925 -346 A O
ATOM 2522 CB SER A 286 21.017 -3.370 -7.262 1.00 70.75 A C
ANISOU 2522 CB SER A 286 8997 9108 8778 -559 929 -587 A C
ATOM 2523 OG SER A 286 21.425 -2.040 -7.523 1.00 75.38 A O
ANISOU 2523 OG SER A 286 9502 9890 9250 -556 757 -415 A O
ATOM 2524 N GLN A 287 19.581 -1.637 -4.793 1.00 54.20 A N
ANISOU 2524 N GLN A 287 6961 6856 6776 -501 629 -247 A N
ATOM 2525 CA GLN A 287 19.832 -1.032 -3.495 1.00 46.35 A C
ANISOU 2525 CA GLN A 287 5986 5775 5850 -400 543 -76 A C
ATOM 2526 C GLN A 287 18.722 -1.368 -2.504 1.00 42.86 A C
ANISOU 2526 C GLN A 287 5614 5182 5490 -402 553 -88 A C
ATOM 2527 O GLN A 287 17.541 -1.358 -2.851 1.00 48.11 A O
ANISOU 2527 O GLN A 287 6280 5876 6122 -513 535 -179 A O
ATOM 2528 CB GLN A 287 19.947 0.486 -3.643 1.00 49.18 A C
ANISOU 2528 CB GLN A 287 6277 6276 6134 -434 380 53 A C
ATOM 2529 CG GLN A 287 21.236 0.927 -4.344 1.00 50.19 A C
ANISOU 2529 CG GLN A 287 6333 6535 6203 -420 376 106 A C
ATOM 2530 CD GLN A 287 21.124 0.941 -5.858 1.00 60.59 A C
ANISOU 2530 CD GLN A 287 7600 8027 7395 -509 397 35 A C
ATOM 2531 NE2 GLN A 287 22.240 1.215 -6.522 1.00 74.15 A N
ANISOU 2531 NE2 GLN A 287 9255 9864 9056 -499 413 75 A N
ATOM 2532 OE1 GLN A 287 20.061 0.707 -6.426 1.00 53.51 A O
ANISOU 2532 OE1 GLN A 287 6703 7191 6436 -588 401 -61 A O
ATOM 2533 N ALA A 288 19.116 -1.642 -1.261 1.00 41.50 A N
ANISOU 2533 N ALA A 288 5479 4884 5405 -273 581 13 A N
ATOM 2534 CA ALA A 288 18.177 -1.968 -0.194 1.00 42.85 A C
ANISOU 2534 CA ALA A 288 5712 4917 5651 -254 602 31 A C
ATOM 2535 C ALA A 288 17.760 -0.755 0.619 1.00 37.26 A C
ANISOU 2535 C ALA A 288 4970 4273 4914 -257 432 134 A C
ATOM 2536 O ALA A 288 16.888 -0.891 1.484 1.00 41.43 A O
ANISOU 2536 O ALA A 288 5538 4718 5486 -251 431 147 A O
ATOM 2537 CB ALA A 288 18.784 -3.001 0.756 1.00 46.17 A C
ANISOU 2537 CB ALA A 288 6186 5186 6170 -86 750 108 A C
ATOM 2538 N LEU A 289 18.402 0.398 0.391 1.00 38.42 A N
ANISOU 2538 N LEU A 289 5045 4551 5000 -267 311 201 A N
ATOM 2539 CA LEU A 289 18.123 1.662 1.070 1.00 37.15 A C
ANISOU 2539 CA LEU A 289 4850 4432 4833 -283 176 276 A C
ATOM 2540 C LEU A 289 17.919 2.745 0.022 1.00 43.98 A C
ANISOU 2540 C LEU A 289 5674 5397 5641 -380 97 287 A C
ATOM 2541 O LEU A 289 18.775 2.939 -0.846 1.00 40.45 A O
ANISOU 2541 O LEU A 289 5185 5035 5149 -397 110 299 A O
ATOM 2542 CB LEU A 289 19.289 2.043 2.001 1.00 38.82 A C
ANISOU 2542 CB LEU A 289 5004 4696 5050 -193 146 353 A C
ATOM 2543 CG LEU A 289 19.349 3.468 2.532 1.00 37.48 A C
ANISOU 2543 CG LEU A 289 4778 4582 4881 -241 33 387 A C
ATOM 2544 CD1 LEU A 289 18.185 3.686 3.526 1.00 41.15 A C
ANISOU 2544 CD1 LEU A 289 5279 4978 5379 -239 -11 383 A C
ATOM 2545 CD2 LEU A 289 20.693 3.695 3.216 1.00 44.66 A C
ANISOU 2545 CD2 LEU A 289 5595 5606 5769 -181 24 412 A C
ATOM 2546 N AVAL A 290 16.801 3.459 0.084 0.47 36.76 A N
ANISOU 2546 N AVAL A 290 4764 4481 4723 -428 28 301 A N
ATOM 2547 N BVAL A 290 16.785 3.438 0.111 0.53 36.71 A N
ANISOU 2547 N BVAL A 290 4759 4471 4717 -427 29 300 A N
ATOM 2548 CA AVAL A 290 16.601 4.604 -0.800 0.47 38.30 A C
ANISOU 2548 CA AVAL A 290 4917 4765 4869 -479 -31 367 A C
ATOM 2549 CA BVAL A 290 16.449 4.562 -0.754 0.53 38.26 A C
ANISOU 2549 CA BVAL A 290 4915 4755 4865 -480 -32 361 A C
ATOM 2550 C AVAL A 290 15.888 5.706 -0.036 0.47 39.95 A C
ANISOU 2550 C AVAL A 290 5130 4916 5135 -472 -101 431 A C
ATOM 2551 C BVAL A 290 16.003 5.717 0.129 0.53 39.83 A C
ANISOU 2551 C BVAL A 290 5116 4888 5130 -467 -101 430 A C
ATOM 2552 O AVAL A 290 15.002 5.442 0.784 0.47 40.35 A O
ANISOU 2552 O AVAL A 290 5209 4907 5215 -456 -117 395 A O
ATOM 2553 O BVAL A 290 15.426 5.510 1.202 0.53 38.66 A O
ANISOU 2553 O BVAL A 290 4996 4666 5028 -440 -116 400 A O
ATOM 2554 CB AVAL A 290 15.819 4.225 -2.074 0.47 41.93 A C
ANISOU 2554 CB AVAL A 290 5354 5352 5225 -534 -13 315 A C
ATOM 2555 CB BVAL A 290 15.342 4.177 -1.761 0.53 42.88 A C
ANISOU 2555 CB BVAL A 290 5486 5446 5360 -534 -24 302 A C
ATOM 2556 CG1AVAL A 290 16.616 3.224 -2.897 0.47 44.40 A C
ANISOU 2556 CG1AVAL A 290 5658 5723 5490 -553 73 226 A C
ATOM 2557 CG1BVAL A 290 14.763 5.408 -2.420 0.53 44.82 A C
ANISOU 2557 CG1BVAL A 290 5682 5797 5549 -540 -88 416 A C
ATOM 2558 CG2AVAL A 290 14.449 3.679 -1.716 0.47 38.22 A C
ANISOU 2558 CG2AVAL A 290 4905 4864 4755 -560 -13 232 A C
ATOM 2559 CG2BVAL A 290 15.883 3.205 -2.798 0.53 45.63 A C
ANISOU 2559 CG2BVAL A 290 5818 5881 5639 -570 57 205 A C
ATOM 2560 N PHE A 291 16.267 6.944 -0.315 1.00 37.80 A N
ANISOU 2560 N PHE A 291 4829 4648 4885 -486 -122 524 A N
ATOM 2561 CA PHE A 291 15.731 8.092 0.400 1.00 36.01 A C
ANISOU 2561 CA PHE A 291 4610 4330 4741 -479 -156 575 A C
ATOM 2562 C PHE A 291 15.587 9.278 -0.537 1.00 42.55 A C
ANISOU 2562 C PHE A 291 5419 5173 5574 -485 -140 708 A C
ATOM 2563 O PHE A 291 16.194 9.339 -1.610 1.00 41.08 A O
ANISOU 2563 O PHE A 291 5205 5076 5328 -502 -108 770 A O
ATOM 2564 CB PHE A 291 16.576 8.447 1.649 1.00 38.69 A C
ANISOU 2564 CB PHE A 291 4939 4595 5168 -486 -157 526 A C
ATOM 2565 CG PHE A 291 18.079 8.481 1.421 1.00 36.83 A C
ANISOU 2565 CG PHE A 291 4656 4410 4928 -518 -124 518 A C
ATOM 2566 CD1 PHE A 291 18.689 9.625 0.949 1.00 36.67 A C
ANISOU 2566 CD1 PHE A 291 4607 4364 4961 -581 -88 575 A C
ATOM 2567 CD2 PHE A 291 18.869 7.376 1.716 1.00 38.82 A C
ANISOU 2567 CD2 PHE A 291 4887 4732 5130 -478 -109 463 A C
ATOM 2568 CE1 PHE A 291 20.072 9.671 0.752 1.00 43.07 A C
ANISOU 2568 CE1 PHE A 291 5357 5242 5764 -627 -52 555 A C
ATOM 2569 CE2 PHE A 291 20.247 7.405 1.506 1.00 42.89 A C
ANISOU 2569 CE2 PHE A 291 5338 5330 5629 -495 -80 457 A C
ATOM 2570 CZ PHE A 291 20.843 8.557 1.041 1.00 42.58 A C
ANISOU 2570 CZ PHE A 291 5258 5287 5632 -582 -59 491 A C
ATOM 2571 N SER A 292 14.745 10.219 -0.116 1.00 41.70 A N
ANISOU 2571 N SER A 292 5326 4979 5539 -455 -148 767 A N
ATOM 2572 CA SER A 292 14.420 11.381 -0.919 1.00 41.46 A C
ANISOU 2572 CA SER A 292 5286 4936 5530 -420 -106 934 A C
ATOM 2573 C SER A 292 15.531 12.425 -0.869 1.00 45.06 A C
ANISOU 2573 C SER A 292 5749 5258 6113 -472 -25 985 A C
ATOM 2574 O SER A 292 16.384 12.425 0.019 1.00 42.03 A O
ANISOU 2574 O SER A 292 5364 4798 5806 -542 -18 864 A O
ATOM 2575 CB SER A 292 13.134 12.013 -0.418 1.00 47.00 A C
ANISOU 2575 CB SER A 292 6003 5571 6286 -349 -119 981 A C
ATOM 2576 OG SER A 292 13.359 12.516 0.884 1.00 46.75 A O
ANISOU 2576 OG SER A 292 6003 5358 6401 -380 -105 889 A O
ATOM 2577 N SER A 293 15.472 13.358 -1.815 1.00 44.66 A N
ANISOU 2577 N SER A 293 5694 5194 6081 -438 49 1172 A N
ATOM 2578 CA SER A 293 16.475 14.416 -1.868 1.00 43.46 A C
ANISOU 2578 CA SER A 293 5553 4888 6072 -506 163 1230 A C
ATOM 2579 C SER A 293 16.429 15.309 -0.634 1.00 47.82 A C
ANISOU 2579 C SER A 293 6141 5204 6825 -552 218 1138 A C
ATOM 2580 O SER A 293 17.450 15.898 -0.261 1.00 48.70 A O
ANISOU 2580 O SER A 293 6244 5201 7060 -667 300 1061 A O
ATOM 2581 CB SER A 293 16.271 15.251 -3.131 1.00 53.34 A C
ANISOU 2581 CB SER A 293 6799 6158 7309 -432 259 1491 A C
ATOM 2582 OG SER A 293 14.961 15.782 -3.149 1.00 58.12 A O
ANISOU 2582 OG SER A 293 7421 6731 7930 -301 268 1624 A O
ATOM 2583 N GLU A 294 15.258 15.447 -0.001 1.00 47.60 A N
ANISOU 2583 N GLU A 294 6140 5117 6829 -474 183 1124 A N
ATOM 2584 CA GLU A 294 15.192 16.251 1.218 1.00 49.17 A C
ANISOU 2584 CA GLU A 294 6365 5107 7209 -524 239 1001 A C
ATOM 2585 C GLU A 294 16.011 15.629 2.343 1.00 47.40 A C
ANISOU 2585 C GLU A 294 6101 4940 6969 -635 174 755 A C
ATOM 2586 O GLU A 294 16.605 16.351 3.150 1.00 47.40 A O
ANISOU 2586 O GLU A 294 6085 4822 7103 -742 247 617 A O
ATOM 2587 CB GLU A 294 13.741 16.447 1.657 1.00 53.27 A C
ANISOU 2587 CB GLU A 294 6911 5583 7747 -404 211 1035 A C
ATOM 2588 CG GLU A 294 12.932 17.349 0.713 1.00 62.81 A C
ANISOU 2588 CG GLU A 294 8142 6724 8998 -265 307 1298 A C
ATOM 2589 CD GLU A 294 12.478 16.658 -0.566 1.00 84.22 A C
ANISOU 2589 CD GLU A 294 10807 9702 11492 -165 235 1469 A C
ATOM 2590 OE1 GLU A 294 12.549 15.413 -0.648 1.00 64.78 A O
ANISOU 2590 OE1 GLU A 294 8307 7446 8861 -206 110 1355 A O
ATOM 2591 OE2 GLU A 294 12.056 17.373 -1.500 1.00105.48 A O
ANISOU 2591 OE2 GLU A 294 13492 12404 14180 -42 319 1719 A O
ATOM 2592 N VAL A 295 16.074 14.299 2.398 1.00 43.91 A N
ANISOU 2592 N VAL A 295 5632 4690 6362 -611 57 697 A N
ATOM 2593 CA VAL A 295 16.947 13.637 3.365 1.00 40.38 A C
ANISOU 2593 CA VAL A 295 5132 4336 5873 -676 7 517 A C
ATOM 2594 C VAL A 295 18.408 13.856 2.995 1.00 44.55 A C
ANISOU 2594 C VAL A 295 5605 4905 6417 -778 64 489 A C
ATOM 2595 O VAL A 295 19.241 14.192 3.847 1.00 45.27 A O
ANISOU 2595 O VAL A 295 5630 5013 6557 -876 88 336 A O
ATOM 2596 CB VAL A 295 16.604 12.140 3.446 1.00 41.18 A C
ANISOU 2596 CB VAL A 295 5234 4593 5820 -600 -92 499 A C
ATOM 2597 CG1 VAL A 295 17.596 11.407 4.317 1.00 40.77 A C
ANISOU 2597 CG1 VAL A 295 5120 4659 5711 -622 -123 374 A C
ATOM 2598 CG2 VAL A 295 15.169 11.950 3.965 1.00 43.47 A C
ANISOU 2598 CG2 VAL A 295 5563 4853 6102 -525 -139 499 A C
ATOM 2599 N LYS A 296 18.741 13.669 1.719 1.00 42.60 A N
ANISOU 2599 N LYS A 296 5365 4709 6112 -764 88 624 A N
ATOM 2600 CA LYS A 296 20.111 13.892 1.265 1.00 42.32 A C
ANISOU 2600 CA LYS A 296 5271 4721 6087 -862 151 611 A C
ATOM 2601 C LYS A 296 20.568 15.313 1.570 1.00 47.21 A C
ANISOU 2601 C LYS A 296 5880 5164 6893 -991 282 568 A C
ATOM 2602 O LYS A 296 21.703 15.533 2.021 1.00 47.89 A O
ANISOU 2602 O LYS A 296 5881 5302 7011 -1119 321 426 A O
ATOM 2603 CB LYS A 296 20.196 13.590 -0.234 1.00 48.69 A C
ANISOU 2603 CB LYS A 296 6092 5608 6800 -817 169 781 A C
ATOM 2604 CG LYS A 296 21.600 13.679 -0.834 1.00 48.78 A C
ANISOU 2604 CG LYS A 296 6038 5699 6797 -908 232 782 A C
ATOM 2605 CD LYS A 296 21.709 14.810 -1.821 1.00 51.10 A C
ANISOU 2605 CD LYS A 296 6354 5881 7179 -948 363 957 A C
ATOM 2606 CE LYS A 296 23.095 14.873 -2.446 1.00 57.19 A C
ANISOU 2606 CE LYS A 296 7054 6746 7930 -1049 433 958 A C
ATOM 2607 NZ LYS A 296 23.570 16.281 -2.518 1.00 66.58 A N
ANISOU 2607 NZ LYS A 296 8247 7740 9312 -1177 605 1005 A N
ATOM 2608 N ASN A 297 19.703 16.296 1.343 1.00 49.32 A N
ANISOU 2608 N ASN A 297 6222 5224 7292 -961 368 681 A N
ATOM 2609 CA ASN A 297 20.124 17.681 1.488 1.00 50.33 A C
ANISOU 2609 CA ASN A 297 6359 5126 7637 -1087 544 654 A C
ATOM 2610 C ASN A 297 20.214 18.116 2.942 1.00 51.80 A C
ANISOU 2610 C ASN A 297 6506 5245 7931 -1196 562 392 A C
ATOM 2611 O ASN A 297 20.902 19.099 3.234 1.00 51.86 A O
ANISOU 2611 O ASN A 297 6484 5112 8107 -1362 712 269 A O
ATOM 2612 CB ASN A 297 19.171 18.595 0.715 1.00 54.96 A C
ANISOU 2612 CB ASN A 297 7042 5501 8341 -983 663 899 A C
ATOM 2613 CG ASN A 297 19.361 18.477 -0.783 1.00 58.45 A C
ANISOU 2613 CG ASN A 297 7491 6030 8688 -914 695 1156 A C
ATOM 2614 ND2 ASN A 297 18.291 18.693 -1.539 1.00 64.86 A N
ANISOU 2614 ND2 ASN A 297 8352 6825 9465 -745 711 1399 A N
ATOM 2615 OD1 ASN A 297 20.469 18.216 -1.256 1.00 65.84 A O
ANISOU 2615 OD1 ASN A 297 8372 7076 9568 -1007 710 1135 A O
ATOM 2616 N SER A 298 19.564 17.394 3.852 1.00 50.75 A N
ANISOU 2616 N SER A 298 6362 5223 7698 -1118 424 290 A N
ATOM 2617 CA SER A 298 19.615 17.686 5.278 1.00 54.86 A C
ANISOU 2617 CA SER A 298 6823 5751 8270 -1207 422 34 A C
ATOM 2618 C SER A 298 20.773 17.002 6.000 1.00 52.72 A C
ANISOU 2618 C SER A 298 6410 5761 7861 -1293 342 -162 A C
ATOM 2619 O SER A 298 21.030 17.324 7.164 1.00 57.25 A O
ANISOU 2619 O SER A 298 6893 6404 8453 -1393 351 -397 A O
ATOM 2620 CB SER A 298 18.298 17.266 5.945 1.00 58.37 A C
ANISOU 2620 CB SER A 298 7315 6199 8663 -1068 322 39 A C
ATOM 2621 OG SER A 298 17.195 17.939 5.367 1.00 64.03 A O
ANISOU 2621 OG SER A 298 8139 6695 9496 -970 396 214 A O
ATOM 2622 N ALA A 299 21.464 16.064 5.359 1.00 48.74 A N
ANISOU 2622 N ALA A 299 5868 5445 7208 -1247 270 -73 A N
ATOM 2623 CA ALA A 299 22.623 15.441 5.987 1.00 53.26 A C
ANISOU 2623 CA ALA A 299 6289 6304 7645 -1298 210 -226 A C
ATOM 2624 C ALA A 299 23.796 16.415 6.029 1.00 52.14 A C
ANISOU 2624 C ALA A 299 6039 6168 7604 -1517 335 -387 A C
ATOM 2625 O ALA A 299 23.936 17.291 5.170 1.00 55.31 A O
ANISOU 2625 O ALA A 299 6500 6352 8162 -1610 474 -309 A O
ATOM 2626 CB ALA A 299 23.020 14.173 5.232 1.00 51.74 A C
ANISOU 2626 CB ALA A 299 6093 6281 7286 -1172 126 -81 A C
ATOM 2627 N THR A 300 24.656 16.261 7.044 1.00 52.60 A N
ANISOU 2627 N THR A 300 5920 6499 7565 -1602 299 -612 A N
ATOM 2628 CA THR A 300 25.819 17.126 7.176 1.00 56.36 A C
ANISOU 2628 CA THR A 300 6256 7041 8117 -1841 419 -817 A C
ATOM 2629 C THR A 300 27.145 16.424 6.904 1.00 59.99 A C
ANISOU 2629 C THR A 300 6558 7830 8408 -1849 370 -827 A C
ATOM 2630 O THR A 300 28.144 17.105 6.657 1.00 63.53 A O
ANISOU 2630 O THR A 300 6899 8315 8923 -2051 482 -950 A O
ATOM 2631 CB THR A 300 25.879 17.759 8.579 1.00 63.20 A C
ANISOU 2631 CB THR A 300 6993 8014 9007 -1990 446 -1138 A C
ATOM 2632 CG2 THR A 300 24.558 18.418 8.925 1.00 63.67 A C
ANISOU 2632 CG2 THR A 300 7201 7758 9231 -1965 499 -1142 A C
ATOM 2633 OG1 THR A 300 26.150 16.760 9.564 1.00 60.37 A O
ANISOU 2633 OG1 THR A 300 6483 8061 8396 -1876 288 -1215 A O
ATOM 2634 N LYS A 301 27.183 15.094 6.937 1.00 52.79 A N
ANISOU 2634 N LYS A 301 5625 7143 7291 -1635 227 -701 A N
ATOM 2635 CA LYS A 301 28.403 14.347 6.665 1.00 56.77 A C
ANISOU 2635 CA LYS A 301 5981 7957 7633 -1597 189 -685 A C
ATOM 2636 C LYS A 301 28.530 14.052 5.176 1.00 53.34 A C
ANISOU 2636 C LYS A 301 5660 7378 7228 -1543 225 -463 A C
ATOM 2637 O LYS A 301 27.549 14.064 4.435 1.00 51.81 A O
ANISOU 2637 O LYS A 301 5655 6915 7117 -1468 236 -290 A O
ATOM 2638 CB LYS A 301 28.431 13.042 7.467 1.00 55.75 A C
ANISOU 2638 CB LYS A 301 5771 8129 7280 -1372 53 -645 A C
ATOM 2639 CG LYS A 301 28.324 13.254 8.971 1.00 65.13 A C
ANISOU 2639 CG LYS A 301 6821 9536 8390 -1401 8 -848 A C
ATOM 2640 CD LYS A 301 27.659 12.091 9.689 1.00 82.53 A C
ANISOU 2640 CD LYS A 301 9056 11858 10443 -1143 -101 -723 A C
ATOM 2641 CE LYS A 301 28.667 11.308 10.526 1.00 90.20 A C
ANISOU 2641 CE LYS A 301 9788 13314 11170 -1020 -162 -758 A C
ATOM 2642 NZ LYS A 301 28.017 10.266 11.376 1.00 96.16 A N
ANISOU 2642 NZ LYS A 301 10566 14183 11788 -769 -237 -627 A N
ATOM 2643 N SER A 302 29.767 13.798 4.742 1.00 50.14 A N
ANISOU 2643 N SER A 302 5118 7195 6737 -1581 245 -479 A N
ATOM 2644 CA SER A 302 30.058 13.553 3.324 1.00 52.55 A C
ANISOU 2644 CA SER A 302 5498 7417 7052 -1549 291 -296 A C
ATOM 2645 C SER A 302 29.848 12.074 2.992 1.00 52.07 A C
ANISOU 2645 C SER A 302 5490 7456 6837 -1291 192 -138 A C
ATOM 2646 O SER A 302 30.777 11.315 2.701 1.00 53.50 A O
ANISOU 2646 O SER A 302 5568 7866 6894 -1212 179 -113 A O
ATOM 2647 CB SER A 302 31.475 14.000 2.982 1.00 64.91 A C
ANISOU 2647 CB SER A 302 6888 9169 8607 -1721 376 -395 A C
ATOM 2648 OG SER A 302 31.682 15.353 3.336 1.00 87.29 A O
ANISOU 2648 OG SER A 302 9670 11888 11607 -1987 500 -574 A O
ATOM 2649 N TRP A 303 28.581 11.684 3.023 1.00 45.48 A N
ANISOU 2649 N TRP A 303 4821 6435 6026 -1166 141 -38 A N
ATOM 2650 CA TRP A 303 28.187 10.337 2.657 1.00 43.57 A C
ANISOU 2650 CA TRP A 303 4659 6216 5680 -953 83 93 A C
ATOM 2651 C TRP A 303 28.496 10.053 1.193 1.00 43.75 A C
ANISOU 2651 C TRP A 303 4730 6207 5686 -940 133 212 A C
ATOM 2652 O TRP A 303 28.568 10.959 0.354 1.00 42.52 A O
ANISOU 2652 O TRP A 303 4603 5940 5612 -1071 204 256 A O
ATOM 2653 CB TRP A 303 26.690 10.141 2.874 1.00 43.81 A C
ANISOU 2653 CB TRP A 303 4851 6038 5757 -871 39 155 A C
ATOM 2654 CG TRP A 303 26.252 10.315 4.289 1.00 47.49 A C
ANISOU 2654 CG TRP A 303 5281 6538 6226 -862 -10 49 A C
ATOM 2655 CD1 TRP A 303 25.643 11.406 4.839 1.00 48.15 A C
ANISOU 2655 CD1 TRP A 303 5389 6482 6424 -981 6 -37 A C
ATOM 2656 CD2 TRP A 303 26.382 9.353 5.336 1.00 42.46 A C
ANISOU 2656 CD2 TRP A 303 4571 6096 5467 -713 -69 28 A C
ATOM 2657 CE2 TRP A 303 25.825 9.924 6.504 1.00 43.54 A C
ANISOU 2657 CE2 TRP A 303 4682 6234 5628 -759 -101 -80 A C
ATOM 2658 CE3 TRP A 303 26.913 8.064 5.402 1.00 42.06 A C
ANISOU 2658 CE3 TRP A 303 4475 6214 5292 -530 -78 103 A C
ATOM 2659 NE1 TRP A 303 25.381 11.178 6.176 1.00 45.95 A N
ANISOU 2659 NE1 TRP A 303 5049 6322 6086 -929 -52 -134 A N
ATOM 2660 CZ2 TRP A 303 25.793 9.247 7.721 1.00 45.61 A C
ANISOU 2660 CZ2 TRP A 303 4863 6696 5770 -629 -154 -104 A C
ATOM 2661 CZ3 TRP A 303 26.883 7.396 6.617 1.00 47.92 A C
ANISOU 2661 CZ3 TRP A 303 5147 7126 5934 -386 -116 102 A C
ATOM 2662 CH2 TRP A 303 26.332 7.990 7.758 1.00 50.74 A C
ANISOU 2662 CH2 TRP A 303 5468 7516 6294 -437 -160 4 A C
ATOM 2663 N ASN A 304 28.622 8.764 0.875 1.00 42.81 A N
ANISOU 2663 N ASN A 304 4626 6177 5463 -772 112 272 A N
ATOM 2664 CA ASN A 304 28.896 8.336 -0.500 1.00 42.89 A C
ANISOU 2664 CA ASN A 304 4673 6191 5433 -748 161 357 A C
ATOM 2665 C ASN A 304 27.572 8.189 -1.255 1.00 40.75 A C
ANISOU 2665 C ASN A 304 4566 5727 5188 -719 154 444 A C
ATOM 2666 O ASN A 304 27.125 7.096 -1.602 1.00 42.98 A O
ANISOU 2666 O ASN A 304 4916 6000 5416 -602 150 463 A O
ATOM 2667 CB ASN A 304 29.689 7.035 -0.510 1.00 46.43 A C
ANISOU 2667 CB ASN A 304 5053 6817 5772 -585 172 356 A C
ATOM 2668 CG ASN A 304 31.109 7.197 0.025 1.00 50.45 A C
ANISOU 2668 CG ASN A 304 5359 7589 6219 -604 182 286 A C
ATOM 2669 ND2 ASN A 304 31.607 6.152 0.662 1.00 51.25 A N
ANISOU 2669 ND2 ASN A 304 5383 7858 6230 -416 175 292 A N
ATOM 2670 OD1 ASN A 304 31.748 8.246 -0.132 1.00 51.16 A O
ANISOU 2670 OD1 ASN A 304 5356 7740 6343 -782 210 232 A O
ATOM 2671 N PHE A 305 26.948 9.340 -1.518 1.00 41.05 A N
ANISOU 2671 N PHE A 305 4661 5622 5316 -831 169 490 A N
ATOM 2672 CA PHE A 305 25.643 9.355 -2.160 1.00 41.50 A C
ANISOU 2672 CA PHE A 305 4841 5546 5380 -798 155 581 A C
ATOM 2673 C PHE A 305 25.739 8.886 -3.604 1.00 43.47 A C
ANISOU 2673 C PHE A 305 5102 5882 5531 -773 192 656 A C
ATOM 2674 O PHE A 305 26.702 9.208 -4.314 1.00 39.69 A O
ANISOU 2674 O PHE A 305 4556 5498 5028 -833 251 690 A O
ATOM 2675 CB PHE A 305 25.046 10.765 -2.176 1.00 44.91 A C
ANISOU 2675 CB PHE A 305 5318 5815 5932 -893 189 649 A C
ATOM 2676 CG PHE A 305 24.744 11.342 -0.821 1.00 45.76 A C
ANISOU 2676 CG PHE A 305 5424 5819 6145 -932 166 553 A C
ATOM 2677 CD1 PHE A 305 23.757 10.797 -0.011 1.00 45.19 A C
ANISOU 2677 CD1 PHE A 305 5407 5702 6061 -843 90 514 A C
ATOM 2678 CD2 PHE A 305 25.428 12.463 -0.379 1.00 49.10 A C
ANISOU 2678 CD2 PHE A 305 5782 6194 6680 -1076 236 487 A C
ATOM 2679 CE1 PHE A 305 23.478 11.359 1.233 1.00 44.95 A C
ANISOU 2679 CE1 PHE A 305 5364 5603 6113 -881 73 416 A C
ATOM 2680 CE2 PHE A 305 25.151 13.015 0.861 1.00 49.62 A C
ANISOU 2680 CE2 PHE A 305 5833 6186 6835 -1129 225 362 A C
ATOM 2681 CZ PHE A 305 24.180 12.471 1.654 1.00 45.27 A C
ANISOU 2681 CZ PHE A 305 5334 5612 6255 -1024 138 332 A C
ATOM 2682 N ILE A 306 24.704 8.185 -4.053 1.00 39.69 A N
ANISOU 2682 N ILE A 306 4698 5389 4993 -701 164 671 A N
ATOM 2683 CA ILE A 306 24.500 7.884 -5.465 1.00 39.05 A C
ANISOU 2683 CA ILE A 306 4621 5417 4801 -694 196 726 A C
ATOM 2684 C ILE A 306 23.087 8.312 -5.848 1.00 41.33 A C
ANISOU 2684 C ILE A 306 4969 5663 5073 -685 166 809 A C
ATOM 2685 O ILE A 306 22.121 8.014 -5.131 1.00 42.42 A O
ANISOU 2685 O ILE A 306 5161 5712 5244 -647 115 759 A O
ATOM 2686 CB ILE A 306 24.740 6.390 -5.767 1.00 39.26 A C
ANISOU 2686 CB ILE A 306 4643 5534 4739 -623 215 612 A C
ATOM 2687 CG1 ILE A 306 24.501 6.105 -7.248 1.00 40.94 A C
ANISOU 2687 CG1 ILE A 306 4839 5898 4818 -638 251 628 A C
ATOM 2688 CG2 ILE A 306 23.881 5.490 -4.860 1.00 43.13 A C
ANISOU 2688 CG2 ILE A 306 5204 5915 5268 -554 184 522 A C
ATOM 2689 CD1 ILE A 306 25.039 4.787 -7.701 1.00 48.43 A C
ANISOU 2689 CD1 ILE A 306 5769 6936 5698 -593 311 496 A C
ATOM 2690 N TRP A 307 22.982 9.059 -6.944 1.00 42.50 A N
ANISOU 2690 N TRP A 307 5093 5891 5164 -707 205 952 A N
ATOM 2691 CA TRP A 307 21.708 9.503 -7.509 1.00 44.08 A C
ANISOU 2691 CA TRP A 307 5315 6125 5307 -668 186 1070 A C
ATOM 2692 C TRP A 307 21.130 8.392 -8.378 1.00 49.95 A C
ANISOU 2692 C TRP A 307 6030 7079 5870 -639 163 983 A C
ATOM 2693 O TRP A 307 21.792 7.933 -9.311 1.00 49.79 A O
ANISOU 2693 O TRP A 307 5953 7230 5733 -656 203 955 A O
ATOM 2694 CB TRP A 307 21.955 10.770 -8.330 1.00 49.79 A C
ANISOU 2694 CB TRP A 307 6012 6869 6037 -682 264 1294 A C
ATOM 2695 CG TRP A 307 20.735 11.482 -8.827 1.00 57.07 A C
ANISOU 2695 CG TRP A 307 6943 7823 6915 -605 266 1478 A C
ATOM 2696 CD1 TRP A 307 19.437 11.117 -8.646 1.00 63.64 A C
ANISOU 2696 CD1 TRP A 307 7789 8702 7689 -540 191 1444 A C
ATOM 2697 CD2 TRP A 307 20.711 12.688 -9.603 1.00 72.27 A C
ANISOU 2697 CD2 TRP A 307 8854 9756 8848 -570 363 1747 A C
ATOM 2698 CE2 TRP A 307 19.360 12.997 -9.852 1.00 77.93 A C
ANISOU 2698 CE2 TRP A 307 9569 10543 9499 -456 334 1879 A C
ATOM 2699 CE3 TRP A 307 21.703 13.538 -10.107 1.00 78.34 A C
ANISOU 2699 CE3 TRP A 307 9606 10480 9679 -619 487 1899 A C
ATOM 2700 NE1 TRP A 307 18.600 12.024 -9.259 1.00 69.03 A N
ANISOU 2700 NE1 TRP A 307 8452 9449 8326 -452 221 1675 A N
ATOM 2701 CZ2 TRP A 307 18.973 14.122 -10.584 1.00 82.10 A C
ANISOU 2701 CZ2 TRP A 307 10082 11097 10016 -359 429 2186 A C
ATOM 2702 CZ3 TRP A 307 21.317 14.653 -10.834 1.00 79.90 A C
ANISOU 2702 CZ3 TRP A 307 9803 10672 9884 -542 595 2199 A C
ATOM 2703 CH2 TRP A 307 19.964 14.933 -11.066 1.00 80.08 A C
ANISOU 2703 CH2 TRP A 307 9827 10765 9836 -398 567 2353 A C
ATOM 2704 N LEU A 308 19.893 7.967 -8.094 1.00 48.77 A N
ANISOU 2704 N LEU A 308 5908 6929 5694 -609 108 919 A N
ATOM 2705 CA LEU A 308 19.260 6.863 -8.814 1.00 56.70 A C
ANISOU 2705 CA LEU A 308 6874 8127 6540 -617 101 778 A C
ATOM 2706 C LEU A 308 18.258 7.375 -9.846 1.00 68.13 A C
ANISOU 2706 C LEU A 308 8247 9821 7819 -588 80 899 A C
ATOM 2707 O LEU A 308 17.413 8.222 -9.538 1.00 65.02 A O
ANISOU 2707 O LEU A 308 7863 9377 7462 -534 46 1041 A O
ATOM 2708 CB LEU A 308 18.551 5.912 -7.843 1.00 49.43 A C
ANISOU 2708 CB LEU A 308 6014 7075 5691 -621 74 601 A C
ATOM 2709 CG LEU A 308 19.403 5.262 -6.754 1.00 50.09 A C
ANISOU 2709 CG LEU A 308 6160 6955 5916 -611 101 501 A C
ATOM 2710 CD1 LEU A 308 18.515 4.506 -5.786 1.00 62.06 A C
ANISOU 2710 CD1 LEU A 308 7738 8339 7502 -600 88 386 A C
ATOM 2711 CD2 LEU A 308 20.435 4.340 -7.357 1.00 56.13 A C
ANISOU 2711 CD2 LEU A 308 6899 7798 6632 -620 178 395 A C
ATOM 2712 N THR A 309 18.333 6.830 -11.059 1.00 86.05 A N
ANISOU 2712 N THR A 309 10425 12378 9890 -613 106 837 A N
ATOM 2713 CA THR A 309 17.466 7.237 -12.169 1.00101.59 A C
ANISOU 2713 CA THR A 309 12279 14682 11638 -574 88 952 A C
ATOM 2714 C THR A 309 16.215 6.367 -12.269 1.00101.67 A C
ANISOU 2714 C THR A 309 12233 14871 11526 -612 46 748 A C
ATOM 2715 O THR A 309 15.875 5.858 -13.339 1.00103.00 A O
ANISOU 2715 O THR A 309 12276 15395 11465 -651 54 642 A O
ATOM 2716 CB THR A 309 18.252 7.198 -13.475 1.00 78.16 A C
ANISOU 2716 CB THR A 309 9215 11995 8488 -587 143 994 A C
ATOM 2717 N ASP A 310 15.506 6.201 -11.152 0.00 82.60 A N
ANISOU 2717 N ASP A 310 9895 12233 9256 -615 7 677 A N
ATOM 2718 CA ASP A 310 14.318 5.355 -11.095 0.00 77.16 A C
ANISOU 2718 CA ASP A 310 9158 11673 8486 -675 -18 464 A C
ATOM 2719 C ASP A 310 13.200 6.052 -10.331 0.00 70.53 A C
ANISOU 2719 C ASP A 310 8334 10754 7709 -605 -86 586 A C
ATOM 2720 O ASP A 310 12.525 5.448 -9.491 0.00 67.66 A O
ANISOU 2720 O ASP A 310 8016 10257 7434 -653 -98 428 A O
ATOM 2721 CB ASP A 310 14.636 4.002 -10.457 0.00 76.68 A C
ANISOU 2721 CB ASP A 310 9184 11397 8553 -775 45 177 A C
ATOM 2722 N SER A 311 12.985 7.337 -10.618 0.00 68.62 A N
ANISOU 2722 N SER A 311 8054 10587 7430 -483 -112 879 A N
ATOM 2723 CA SER A 311 11.941 8.118 -9.954 0.00 63.72 A C
ANISOU 2723 CA SER A 311 7443 9893 6874 -388 -159 1019 A C
ATOM 2724 C SER A 311 10.640 7.962 -10.738 0.00 60.61 A C
ANISOU 2724 C SER A 311 6876 9927 6225 -360 -205 999 A C
ATOM 2725 O SER A 311 10.256 8.803 -11.554 0.00 59.05 A O
ANISOU 2725 O SER A 311 6566 10004 5867 -231 -212 1242 A O
ATOM 2726 CB SER A 311 12.357 9.579 -9.835 0.00 64.14 A C
ANISOU 2726 CB SER A 311 7549 9773 7047 -261 -126 1342 A C
ATOM 2727 N GLU A 312 9.953 6.853 -10.478 0.00 60.26 A N
ANISOU 2727 N GLU A 312 6800 9955 6141 -483 -223 705 A N
ATOM 2728 CA GLU A 312 8.660 6.547 -11.077 0.00 59.01 A C
ANISOU 2728 CA GLU A 312 6457 10221 5744 -501 -266 607 A C
ATOM 2729 C GLU A 312 7.586 6.443 -10.000 0.00 59.24 A C
ANISOU 2729 C GLU A 312 6516 10108 5883 -509 -304 532 A C
ATOM 2730 O GLU A 312 6.756 5.531 -10.005 0.00 59.06 A O
ANISOU 2730 O GLU A 312 6408 10259 5773 -638 -306 267 A O
ATOM 2731 CB GLU A 312 8.730 5.258 -11.893 0.00 57.48 A C
ANISOU 2731 CB GLU A 312 6161 10299 5378 -683 -225 271 A C
ATOM 2732 N LEU A 313 7.595 7.388 -9.064 0.00 60.68 A N
ANISOU 2732 N LEU A 313 6814 9976 6263 -383 -321 748 A N
ATOM 2733 CA LEU A 313 6.688 7.344 -7.931 0.00 65.73 A C
ANISOU 2733 CA LEU A 313 7499 10448 7029 -383 -351 685 A C
ATOM 2734 C LEU A 313 5.241 7.538 -8.384 0.00 65.81 A C
ANISOU 2734 C LEU A 313 7313 10868 6823 -323 -406 710 A C
ATOM 2735 O LEU A 313 4.958 7.964 -9.508 0.00 62.24 A O
ANISOU 2735 O LEU A 313 6694 10822 6132 -232 -425 848 A O
ATOM 2736 CB LEU A 313 7.067 8.415 -6.909 0.00 69.36 A C
ANISOU 2736 CB LEU A 313 8108 10515 7732 -260 -346 901 A C
ATOM 2737 N LYS A 314 4.318 7.214 -7.480 0.00 68.61 A N
ANISOU 2737 N LYS A 314 7674 11143 7251 -366 -428 581 A N
ATOM 2738 CA LYS A 314 2.892 7.380 -7.716 0.00 67.25 A C
ANISOU 2738 CA LYS A 314 7310 11349 6894 -313 -481 586 A C
ATOM 2739 C LYS A 314 2.244 7.917 -6.449 0.00 68.95 A C
ANISOU 2739 C LYS A 314 7608 11295 7295 -223 -501 669 A C
ATOM 2740 O LYS A 314 2.668 7.601 -5.334 0.00 71.98 A O
ANISOU 2740 O LYS A 314 8168 11268 7912 -297 -473 573 A O
ATOM 2741 CB LYS A 314 2.228 6.060 -8.129 0.00 64.18 A C
ANISOU 2741 CB LYS A 314 6778 11273 6336 -537 -470 221 A C
ATOM 2742 N GLY A 315 1.209 8.736 -6.631 0.00 65.17 A N
ANISOU 2742 N GLY A 315 6987 11077 6697 -49 -543 854 A N
ATOM 2743 CA GLY A 315 0.523 9.360 -5.522 0.00 64.29 A C
ANISOU 2743 CA GLY A 315 6933 10750 6744 62 -555 946 A C
ATOM 2744 C GLY A 315 1.173 10.616 -4.990 0.00 63.83 A C
ANISOU 2744 C GLY A 315 7038 10302 6912 243 -513 1227 A C
ATOM 2745 O GLY A 315 0.573 11.294 -4.145 0.00 61.89 A O
ANISOU 2745 O GLY A 315 6826 9895 6793 361 -508 1320 A O
ATOM 2746 N LYS A 316 2.373 10.954 -5.450 0.00 64.77 A N
ANISOU 2746 N LYS A 316 7252 10265 7092 256 -468 1346 A N
ATOM 2747 CA LYS A 316 3.062 12.150 -4.989 0.00 62.50 A C
ANISOU 2747 CA LYS A 316 7115 9599 7035 390 -399 1580 A C
ATOM 2748 C LYS A 316 2.413 13.385 -5.613 0.00 57.95 A C
ANISOU 2748 C LYS A 316 6436 9198 6384 657 -360 1926 A C
ATOM 2749 O LYS A 316 1.376 13.313 -6.280 0.00 57.17 A O
ANISOU 2749 O LYS A 316 6140 9540 6043 756 -405 1987 A O
ATOM 2750 CB LYS A 316 4.548 12.067 -5.327 0.00 65.20 A C
ANISOU 2750 CB LYS A 316 7569 9751 7454 300 -352 1583 A C
ATOM 2751 N SER A 317 3.033 14.544 -5.397 0.00 56.71 A N
ANISOU 2751 N SER A 317 6406 8702 6439 782 -256 2159 A N
ATOM 2752 CA SER A 317 2.575 15.803 -5.969 0.00 55.26 A C
ANISOU 2752 CA SER A 317 6162 8595 6241 1061 -166 2535 A C
ATOM 2753 C SER A 317 3.416 16.251 -7.156 0.00 55.48 A C
ANISOU 2753 C SER A 317 6174 8719 6189 1132 -89 2783 A C
ATOM 2754 O SER A 317 2.867 16.752 -8.142 0.00 55.89 A O
ANISOU 2754 O SER A 317 6075 9119 6043 1348 -59 3072 A O
ATOM 2755 CB SER A 317 2.583 16.901 -4.901 0.00 53.63 A C
ANISOU 2755 CB SER A 317 6111 7907 6360 1163 -54 2635 A C
ATOM 2756 N GLU A 318 4.732 16.080 -7.088 0.00 57.01 A N
ANISOU 2756 N GLU A 318 6505 8642 6516 964 -51 2689 A N
ATOM 2757 CA GLU A 318 5.617 16.486 -8.173 0.00 58.60 A C
ANISOU 2757 CA GLU A 318 6698 8915 6654 1009 33 2912 A C
ATOM 2758 C GLU A 318 6.835 15.564 -8.216 0.00 61.33 A C
ANISOU 2758 C GLU A 318 7113 9185 7006 754 -8 2653 A C
ATOM 2759 O GLU A 318 7.980 16.010 -8.306 0.00 62.41 A O
ANISOU 2759 O GLU A 318 7355 9067 7291 705 87 2730 A O
ATOM 2760 CB GLU A 318 6.030 17.949 -8.016 0.00 57.89 A C
ANISOU 2760 CB GLU A 318 6732 8431 6831 1166 225 3226 A C
ATOM 2761 N SER A 319 6.595 14.254 -8.153 0.00 62.69 A N
ANISOU 2761 N SER A 319 7221 9575 7025 590 -134 2340 A N
ATOM 2762 CA SER A 319 7.669 13.272 -8.243 0.00 65.65 A C
ANISOU 2762 CA SER A 319 7648 9904 7392 375 -161 2096 A C
ATOM 2763 C SER A 319 8.665 13.442 -7.101 0.00 68.65 A C
ANISOU 2763 C SER A 319 8217 9791 8076 267 -117 1990 A C
ATOM 2764 O SER A 319 8.332 14.027 -6.065 0.00 67.26 A O
ANISOU 2764 O SER A 319 8124 9334 8098 308 -94 2001 A O
ATOM 2765 CB SER A 319 8.380 13.389 -9.593 1.00 76.01 A C
ANISOU 2765 CB SER A 319 8884 11467 8530 403 -116 2255 A C
ATOM 2766 N ILE A 320 9.886 12.934 -7.277 1.00 82.83 A N
ANISOU 2766 N ILE A 320 10066 11511 9896 130 -101 1876 A N
ATOM 2767 CA ILE A 320 10.904 13.006 -6.234 1.00 73.37 A C
ANISOU 2767 CA ILE A 320 9009 9927 8942 21 -68 1757 A C
ATOM 2768 C ILE A 320 12.231 12.461 -6.747 1.00 67.23 A C
ANISOU 2768 C ILE A 320 8243 9171 8130 -95 -46 1677 A C
ATOM 2769 O ILE A 320 12.282 11.377 -7.340 1.00 66.45 A O
ANISOU 2769 O ILE A 320 8081 9310 7858 -163 -94 1530 A O
ATOM 2770 CB ILE A 320 10.454 12.236 -4.976 1.00 64.03 A C
ANISOU 2770 CB ILE A 320 7875 8614 7838 -58 -141 1505 A C
ATOM 2771 N ASP A 321 13.314 13.213 -6.535 1.00 64.58 A N
ANISOU 2771 N ASP A 321 7980 8593 7963 -126 41 1758 A N
ATOM 2772 CA ASP A 321 14.649 12.683 -6.780 1.00 56.26 A C
ANISOU 2772 CA ASP A 321 6938 7536 6905 -242 59 1655 A C
ATOM 2773 C ASP A 321 15.005 11.666 -5.703 1.00 53.62 A C
ANISOU 2773 C ASP A 321 6652 7085 6638 -345 -3 1380 A C
ATOM 2774 O ASP A 321 14.783 11.906 -4.510 1.00 56.02 A O
ANISOU 2774 O ASP A 321 7015 7179 7092 -353 -17 1309 A O
ATOM 2775 CB ASP A 321 15.692 13.799 -6.802 1.00 64.95 A C
ANISOU 2775 CB ASP A 321 8083 8423 8170 -266 181 1802 A C
ATOM 2776 CG ASP A 321 15.630 14.625 -8.062 1.00 77.95 A C
ANISOU 2776 CG ASP A 321 9680 10207 9731 -165 274 2101 A C
ATOM 2777 OD1 ASP A 321 15.837 14.051 -9.150 1.00 80.36 A O
ANISOU 2777 OD1 ASP A 321 9903 10811 9822 -162 252 2126 A O
ATOM 2778 OD2 ASP A 321 15.387 15.846 -7.962 1.00 88.37 A O
ANISOU 2778 OD2 ASP A 321 11042 11336 11199 -83 386 2314 A O
ATOM 2779 N ILE A 322 15.561 10.534 -6.125 1.00 52.36 A N
ANISOU 2779 N ILE A 322 6463 7065 6365 -410 -25 1234 A N
ATOM 2780 CA ILE A 322 15.819 9.391 -5.256 1.00 47.05 A C
ANISOU 2780 CA ILE A 322 5829 6315 5733 -472 -61 1005 A C
ATOM 2781 C ILE A 322 17.326 9.187 -5.123 1.00 42.51 A C
ANISOU 2781 C ILE A 322 5266 5671 5215 -528 -20 952 A C
ATOM 2782 O ILE A 322 18.055 9.260 -6.116 1.00 44.54 A O
ANISOU 2782 O ILE A 322 5479 6050 5394 -545 23 1013 A O
ATOM 2783 CB ILE A 322 15.161 8.122 -5.828 1.00 53.23 A C
ANISOU 2783 CB ILE A 322 6568 7301 6355 -495 -88 857 A C
ATOM 2784 CG1 ILE A 322 13.627 8.212 -5.834 1.00 65.42 A C
ANISOU 2784 CG1 ILE A 322 8074 8954 7829 -455 -137 870 A C
ATOM 2785 CG2 ILE A 322 15.616 6.928 -5.041 1.00 56.27 A C
ANISOU 2785 CG2 ILE A 322 7005 7570 6804 -543 -77 659 A C
ATOM 2786 CD1 ILE A 322 13.032 9.085 -4.774 1.00 65.61 A C
ANISOU 2786 CD1 ILE A 322 8149 8783 7997 -396 -160 953 A C
ATOM 2787 N TYR A 323 17.784 8.898 -3.905 1.00 39.44 A N
ANISOU 2787 N TYR A 323 4918 5125 4942 -548 -32 841 A N
ATOM 2788 CA TYR A 323 19.202 8.678 -3.632 1.00 37.68 A C
ANISOU 2788 CA TYR A 323 4680 4877 4760 -585 2 785 A C
ATOM 2789 C TYR A 323 19.410 7.407 -2.820 1.00 40.98 A C
ANISOU 2789 C TYR A 323 5117 5274 5181 -561 -12 634 A C
ATOM 2790 O TYR A 323 18.498 6.920 -2.150 1.00 41.32 A O
ANISOU 2790 O TYR A 323 5200 5260 5240 -532 -42 576 A O
ATOM 2791 CB TYR A 323 19.813 9.846 -2.851 1.00 41.62 A C
ANISOU 2791 CB TYR A 323 5178 5235 5403 -627 25 824 A C
ATOM 2792 CG TYR A 323 19.978 11.087 -3.674 1.00 41.01 A C
ANISOU 2792 CG TYR A 323 5088 5133 5361 -656 94 988 A C
ATOM 2793 CD1 TYR A 323 18.934 11.977 -3.843 1.00 45.19 A C
ANISOU 2793 CD1 TYR A 323 5650 5587 5934 -610 110 1122 A C
ATOM 2794 CD2 TYR A 323 21.191 11.377 -4.277 1.00 46.09 A C
ANISOU 2794 CD2 TYR A 323 5684 5827 6001 -718 162 1026 A C
ATOM 2795 CE1 TYR A 323 19.088 13.120 -4.606 1.00 51.75 A C
ANISOU 2795 CE1 TYR A 323 6477 6374 6813 -610 207 1314 A C
ATOM 2796 CE2 TYR A 323 21.361 12.516 -5.022 1.00 46.77 A C
ANISOU 2796 CE2 TYR A 323 5766 5871 6135 -744 254 1199 A C
ATOM 2797 CZ TYR A 323 20.307 13.386 -5.185 1.00 55.43 A C
ANISOU 2797 CZ TYR A 323 6906 6871 7284 -683 285 1354 A C
ATOM 2798 OH TYR A 323 20.481 14.520 -5.946 1.00 57.52 A O
ANISOU 2798 OH TYR A 323 7172 7072 7609 -684 410 1566 A O
ATOM 2799 N SER A 324 20.634 6.886 -2.856 1.00 40.12 A N
ANISOU 2799 N SER A 324 4974 5212 5058 -560 25 588 A N
ATOM 2800 CA SER A 324 21.042 5.833 -1.936 1.00 37.64 A C
ANISOU 2800 CA SER A 324 4669 4868 4766 -501 36 493 A C
ATOM 2801 C SER A 324 22.490 6.105 -1.522 1.00 39.36 A C
ANISOU 2801 C SER A 324 4813 5139 5004 -500 53 494 A C
ATOM 2802 O SER A 324 23.030 7.193 -1.754 1.00 38.92 A O
ANISOU 2802 O SER A 324 4710 5103 4976 -576 56 543 A O
ATOM 2803 CB SER A 324 20.858 4.442 -2.560 1.00 38.76 A C
ANISOU 2803 CB SER A 324 4838 5045 4844 -466 95 411 A C
ATOM 2804 OG SER A 324 21.159 3.409 -1.635 1.00 40.32 A O
ANISOU 2804 OG SER A 324 5060 5175 5085 -380 138 359 A O
ATOM 2805 N ILE A 325 23.088 5.128 -0.843 1.00 38.79 A N
ANISOU 2805 N ILE A 325 4722 5095 4924 -412 79 445 A N
ATOM 2806 CA ILE A 325 24.503 5.130 -0.487 1.00 40.09 A C
ANISOU 2806 CA ILE A 325 4784 5378 5070 -383 98 438 A C
ATOM 2807 C ILE A 325 25.174 4.018 -1.283 1.00 47.07 A C
ANISOU 2807 C ILE A 325 5658 6330 5897 -307 178 423 A C
ATOM 2808 O ILE A 325 24.684 2.883 -1.299 1.00 45.05 A O
ANISOU 2808 O ILE A 325 5473 6000 5645 -224 233 393 A O
ATOM 2809 CB ILE A 325 24.703 4.902 1.023 1.00 42.52 A C
ANISOU 2809 CB ILE A 325 5049 5717 5390 -298 71 419 A C
ATOM 2810 CG1 ILE A 325 24.090 6.027 1.855 1.00 49.98 A C
ANISOU 2810 CG1 ILE A 325 5992 6605 6391 -384 4 398 A C
ATOM 2811 CG2 ILE A 325 26.188 4.749 1.360 1.00 46.14 A C
ANISOU 2811 CG2 ILE A 325 5368 6371 5793 -243 93 411 A C
ATOM 2812 CD1 ILE A 325 24.602 7.406 1.530 1.00 50.88 A C
ANISOU 2812 CD1 ILE A 325 6046 6737 6549 -533 2 384 A C
ATOM 2813 N ASP A 326 26.310 4.318 -1.901 1.00 44.71 A N
ANISOU 2813 N ASP A 326 5269 6162 5557 -339 205 432 A N
ATOM 2814 CA AASP A 326 27.057 3.334 -2.683 0.68 49.88 A C
ANISOU 2814 CA AASP A 326 5900 6895 6156 -264 291 408 A C
ATOM 2815 CA BASP A 326 27.054 3.333 -2.681 0.32 50.06 A C
ANISOU 2815 CA BASP A 326 5924 6918 6180 -263 291 408 A C
ATOM 2816 C ASP A 326 28.191 2.802 -1.814 1.00 57.49 A C
ANISOU 2816 C ASP A 326 6766 7974 7104 -129 320 416 A C
ATOM 2817 O ASP A 326 29.241 3.436 -1.695 1.00 61.88 A O
ANISOU 2817 O ASP A 326 7192 8693 7626 -167 301 422 A O
ATOM 2818 CB AASP A 326 27.584 3.950 -3.975 0.68 46.95 A C
ANISOU 2818 CB AASP A 326 5479 6630 5730 -369 310 425 A C
ATOM 2819 CB BASP A 326 27.574 3.942 -3.978 0.32 47.11 A C
ANISOU 2819 CB BASP A 326 5500 6649 5750 -369 310 425 A C
ATOM 2820 CG AASP A 326 28.319 2.947 -4.843 0.68 52.89 A C
ANISOU 2820 CG AASP A 326 6203 7476 6419 -297 405 379 A C
ATOM 2821 CG BASP A 326 28.246 2.918 -4.872 0.32 52.99 A C
ANISOU 2821 CG BASP A 326 6222 7481 6431 -298 405 377 A C
ATOM 2822 OD1AASP A 326 28.274 1.741 -4.531 0.68 52.35 A O
ANISOU 2822 OD1AASP A 326 6176 7344 6371 -167 473 331 A O
ATOM 2823 OD1BASP A 326 27.606 1.892 -5.188 0.32 55.81 A O
ANISOU 2823 OD1BASP A 326 6661 7754 6790 -244 465 310 A O
ATOM 2824 OD2AASP A 326 28.937 3.365 -5.842 0.68 46.96 A O
ANISOU 2824 OD2AASP A 326 5388 6849 5604 -367 429 395 A O
ATOM 2825 OD2BASP A 326 29.412 3.141 -5.257 0.32 50.59 A O
ANISOU 2825 OD2BASP A 326 5813 7328 6082 -306 435 390 A O
ATOM 2826 N ASN A 327 27.969 1.639 -1.205 1.00 72.17 A N
ANISOU 2826 N ASN A 327 8675 9760 8986 32 379 422 A N
ATOM 2827 CA AASN A 327 28.970 0.937 -0.414 0.55 82.33 A C
ANISOU 2827 CA AASN A 327 9869 11171 10243 221 430 470 A C
ATOM 2828 CA BASN A 327 29.009 0.948 -0.451 0.45 82.29 A C
ANISOU 2828 CA BASN A 327 9860 11171 10236 219 431 469 A C
ATOM 2829 C ASN A 327 28.914 -0.540 -0.794 1.00 95.85 A C
ANISOU 2829 C ASN A 327 11667 12756 11994 380 584 470 A C
ATOM 2830 O ASN A 327 28.190 -0.939 -1.712 1.00100.16 A O
ANISOU 2830 O ASN A 327 12325 13152 12579 305 642 394 A O
ATOM 2831 CB AASN A 327 28.745 1.160 1.091 0.55 79.08 A C
ANISOU 2831 CB AASN A 327 9417 10802 9829 287 364 517 A C
ATOM 2832 CB BASN A 327 28.883 1.227 1.057 0.45 79.14 A C
ANISOU 2832 CB BASN A 327 9408 10834 9828 282 361 515 A C
ATOM 2833 CG AASN A 327 27.529 0.412 1.633 0.55 72.67 A C
ANISOU 2833 CG AASN A 327 8751 9774 9086 360 402 544 A C
ATOM 2834 CG BASN A 327 29.458 2.590 1.461 0.45 67.04 A C
ANISOU 2834 CG BASN A 327 7732 9490 8252 138 254 476 A C
ATOM 2835 ND2AASN A 327 27.227 0.637 2.906 0.55 69.03 A N
ANISOU 2835 ND2AASN A 327 8259 9359 8611 410 343 586 A N
ATOM 2836 ND2BASN A 327 29.055 3.081 2.634 0.45 52.31 A N
ANISOU 2836 ND2BASN A 327 5835 7657 6383 123 180 466 A N
ATOM 2837 OD1AASN A 327 26.877 -0.356 0.927 0.55 79.18 A O
ANISOU 2837 OD1AASN A 327 9703 10411 9971 360 491 511 A O
ATOM 2838 OD1BASN A 327 30.266 3.178 0.740 0.45 58.92 A O
ANISOU 2838 OD1BASN A 327 6617 8576 7195 34 254 442 A O
ATOM 2839 N GLU A 328 29.659 -1.369 -0.060 1.00101.99 A N
ANISOU 2839 N GLU A 328 12386 13604 12762 606 667 553 A N
ATOM 2840 CA GLU A 328 29.696 -2.795 -0.372 1.00112.82 A C
ANISOU 2840 CA GLU A 328 13845 14817 14204 779 858 564 A C
ATOM 2841 C GLU A 328 28.320 -3.446 -0.258 1.00124.95 A C
ANISOU 2841 C GLU A 328 15564 16059 15854 749 932 526 A C
ATOM 2842 O GLU A 328 28.031 -4.412 -0.973 1.00125.92 A O
ANISOU 2842 O GLU A 328 15791 15995 16058 764 1095 445 A O
ATOM 2843 CB GLU A 328 30.694 -3.502 0.548 1.00112.67 A C
ANISOU 2843 CB GLU A 328 13722 14932 14154 1068 943 712 A C
ATOM 2844 CG GLU A 328 30.325 -3.467 2.028 1.00124.33 A C
ANISOU 2844 CG GLU A 328 15177 16449 15614 1183 894 836 A C
ATOM 2845 CD GLU A 328 30.990 -2.327 2.776 1.00122.30 A C
ANISOU 2845 CD GLU A 328 14720 16532 15216 1132 717 852 A C
ATOM 2846 OE1 GLU A 328 31.533 -1.415 2.117 1.00121.33 A O
ANISOU 2846 OE1 GLU A 328 14505 16553 15041 955 627 755 A O
ATOM 2847 OE2 GLU A 328 30.962 -2.340 4.025 1.00109.03 A O
ANISOU 2847 OE2 GLU A 328 12967 14983 13477 1259 681 952 A O
ATOM 2848 N MET A 329 27.462 -2.937 0.626 1.00121.91 A N
ANISOU 2848 N MET A 329 17299 15451 13568 -1288 5199 1036 A N
ATOM 2849 CA MET A 329 26.167 -3.557 0.873 1.00118.45 A C
ANISOU 2849 CA MET A 329 16760 14815 13429 -722 4830 1050 A C
ATOM 2850 C MET A 329 25.191 -3.322 -0.272 1.00133.91 A C
ANISOU 2850 C MET A 329 18991 16797 15094 -481 4636 1466 A C
ATOM 2851 O MET A 329 24.816 -4.264 -0.979 1.00139.19 A O
ANISOU 2851 O MET A 329 19409 17875 15601 -229 4397 1322 A O
ATOM 2852 CB MET A 329 25.570 -3.025 2.177 1.00107.28 A C
ANISOU 2852 CB MET A 329 15524 12702 12534 -558 4805 1169 A C
ATOM 2853 CG MET A 329 24.710 -4.035 2.908 1.00106.12 A C
ANISOU 2853 CG MET A 329 15046 12447 12827 -51 4483 914 A C
ATOM 2854 SD MET A 329 25.640 -5.159 3.964 1.00108.85 A S
ANISOU 2854 SD MET A 329 14812 13067 13480 -125 4524 233 A S
ATOM 2855 CE MET A 329 26.612 -4.015 4.929 1.00 92.06 A C
ANISOU 2855 CE MET A 329 12950 10544 11486 -637 4904 295 A C
ATOM 2856 N THR A 330 24.775 -2.070 -0.464 1.00128.32 A N
ANISOU 2856 N THR A 330 18800 15649 14306 -560 4737 1988 A N
ATOM 2857 CA THR A 330 23.788 -1.756 -1.486 1.00120.86 A C
ANISOU 2857 CA THR A 330 18139 14675 13109 -318 4548 2432 A C
ATOM 2858 C THR A 330 24.259 -2.110 -2.888 1.00125.76 A C
ANISOU 2858 C THR A 330 18693 15930 13159 -492 4563 2402 A C
ATOM 2859 O THR A 330 23.452 -2.070 -3.823 1.00121.60 A O
ANISOU 2859 O THR A 330 18330 15482 12391 -274 4361 2710 A O
ATOM 2860 CB THR A 330 23.437 -0.267 -1.429 1.00118.32 A C
ANISOU 2860 CB THR A 330 18402 13776 12780 -433 4719 2996 A C
ATOM 2861 CG2 THR A 330 22.634 0.045 -0.173 1.00113.53 A C
ANISOU 2861 CG2 THR A 330 17905 12500 12733 -142 4639 3104 A C
ATOM 2862 OG1 THR A 330 24.643 0.510 -1.436 1.00119.79 A O
ANISOU 2862 OG1 THR A 330 18774 13994 12747 -987 5111 2998 A O
ATOM 2863 N ARG A 331 25.533 -2.456 -3.058 1.00134.75 A N
ANISOU 2863 N ARG A 331 19598 17522 14079 -874 4797 2048 A N
ATOM 2864 CA ARG A 331 26.086 -2.736 -4.378 1.00141.34 A C
ANISOU 2864 CA ARG A 331 20394 18951 14357 -1077 4861 2016 A C
ATOM 2865 C ARG A 331 25.953 -4.215 -4.736 1.00145.25 A C
ANISOU 2865 C ARG A 331 20417 19970 14803 -807 4608 1598 A C
ATOM 2866 O ARG A 331 25.349 -4.562 -5.757 1.00145.09 A O
ANISOU 2866 O ARG A 331 20441 20204 14482 -613 4396 1734 A O
ATOM 2867 CB ARG A 331 27.553 -2.288 -4.429 1.00126.99 A C
ANISOU 2867 CB ARG A 331 18587 17353 12310 -1645 5273 1883 A C
ATOM 2868 CG ARG A 331 28.199 -2.478 -5.786 1.00129.89 A C
ANISOU 2868 CG ARG A 331 18948 18312 12093 -1889 5389 1871 A C
ATOM 2869 CD ARG A 331 29.608 -1.886 -5.887 1.00132.00 A C
ANISOU 2869 CD ARG A 331 19274 18760 12120 -2466 5812 1813 A C
ATOM 2870 NE ARG A 331 29.791 -0.618 -5.187 1.00132.24 A N
ANISOU 2870 NE ARG A 331 19673 18248 12323 -2730 6041 2101 A N
ATOM 2871 CZ ARG A 331 30.476 -0.461 -4.060 1.00130.01 A C
ANISOU 2871 CZ ARG A 331 19259 17774 12364 -2953 6222 1880 A C
ATOM 2872 NH1 ARG A 331 31.024 -1.489 -3.432 1.00126.20 A N
ANISOU 2872 NH1 ARG A 331 18267 17579 12106 -2924 6195 1372 A N
ATOM 2873 NH2 ARG A 331 30.626 0.761 -3.559 1.00131.78 A N
ANISOU 2873 NH2 ARG A 331 19882 17508 12681 -3221 6440 2181 A N
ATOM 2874 N LYS A 332 26.500 -5.098 -3.897 0.81147.57 A N
ANISOU 2874 N LYS A 332 20265 20419 15385 -791 4625 1092 A N
ATOM 2875 CA LYS A 332 26.558 -6.529 -4.199 0.81140.00 A C
ANISOU 2875 CA LYS A 332 18843 19982 14367 -584 4441 646 A C
ATOM 2876 C LYS A 332 25.277 -7.201 -3.712 0.81138.49 A C
ANISOU 2876 C LYS A 332 18509 19557 14553 -41 4045 607 A C
ATOM 2877 O LYS A 332 25.212 -7.798 -2.635 0.81134.42 A O
ANISOU 2877 O LYS A 332 17692 18899 14483 142 3965 286 A O
ATOM 2878 CB LYS A 332 27.796 -7.157 -3.569 0.81126.57 A C
ANISOU 2878 CB LYS A 332 16728 18583 12781 -829 4665 132 A C
ATOM 2879 N SER A 333 24.239 -7.102 -4.539 0.93142.33 A N
ANISOU 2879 N SER A 333 19215 20014 14850 216 3790 949 A N
ATOM 2880 CA SER A 333 22.976 -7.779 -4.290 0.93144.35 A C
ANISOU 2880 CA SER A 333 19335 20119 15394 728 3390 945 A C
ATOM 2881 C SER A 333 22.487 -8.402 -5.590 0.93146.42 A C
ANISOU 2881 C SER A 333 19578 20825 15230 879 3152 999 A C
ATOM 2882 O SER A 333 22.854 -7.971 -6.686 0.93155.00 A O
ANISOU 2882 O SER A 333 20898 22177 15819 625 3277 1210 A O
ATOM 2883 CB SER A 333 21.916 -6.817 -3.733 0.93134.12 A C
ANISOU 2883 CB SER A 333 18387 18150 14423 952 3279 1419 A C
ATOM 2884 N SER A 334 21.656 -9.434 -5.457 0.79141.89 A N
ANISOU 2884 N SER A 334 18729 20332 14850 1288 2806 802 A N
ATOM 2885 CA SER A 334 20.955 -10.004 -6.600 0.79143.59 A C
ANISOU 2885 CA SER A 334 18955 20889 14715 1485 2516 899 A C
ATOM 2886 C SER A 334 19.750 -9.171 -7.014 0.79164.18 A C
ANISOU 2886 C SER A 334 21948 23138 17293 1693 2296 1500 A C
ATOM 2887 O SER A 334 18.971 -9.611 -7.866 0.79163.46 A O
ANISOU 2887 O SER A 334 21873 23265 16969 1904 1998 1629 A O
ATOM 2888 CB SER A 334 20.504 -11.434 -6.290 0.79128.55 A C
ANISOU 2888 CB SER A 334 16612 19201 13030 1837 2224 461 A C
ATOM 2889 OG SER A 334 21.606 -12.319 -6.228 0.79109.60 A O
ANISOU 2889 OG SER A 334 13861 17248 10532 1651 2412 -79 A O
ATOM 2890 N GLY A 335 19.586 -7.985 -6.436 0.93154.58 A N
ANISOU 2890 N GLY A 335 21046 21384 16302 1634 2439 1874 A N
ATOM 2891 CA GLY A 335 18.409 -7.180 -6.686 0.93141.15 A C
ANISOU 2891 CA GLY A 335 19697 19289 14643 1868 2243 2454 A C
ATOM 2892 C GLY A 335 17.176 -7.820 -6.075 0.93146.93 A C
ANISOU 2892 C GLY A 335 20223 19787 15816 2374 1861 2435 A C
ATOM 2893 O GLY A 335 17.229 -8.852 -5.408 0.93149.35 A O
ANISOU 2893 O GLY A 335 20132 20204 16412 2541 1755 1971 A O
ATOM 2894 N GLY A 336 16.040 -7.173 -6.307 0.62138.51 A N
ANISOU 2894 N GLY A 336 19438 18385 14806 2625 1657 2965 A N
ATOM 2895 CA GLY A 336 14.769 -7.739 -5.914 0.62135.65 A C
ANISOU 2895 CA GLY A 336 18903 17831 14807 3112 1268 3021 A C
ATOM 2896 C GLY A 336 14.211 -8.659 -6.982 0.62145.33 A C
ANISOU 2896 C GLY A 336 19971 19549 15698 3278 919 2973 A C
ATOM 2897 O GLY A 336 14.716 -8.724 -8.101 0.62148.15 A O
ANISOU 2897 O GLY A 336 20420 20355 15517 3027 976 2975 A O
ATOM 2898 N LEU A 337 13.154 -9.383 -6.613 1.00146.03 A N
ANISOU 2898 N LEU A 337 19826 19545 16113 3702 555 2926 A N
ATOM 2899 CA LEU A 337 12.568 -10.392 -7.490 1.00142.33 A C
ANISOU 2899 CA LEU A 337 19166 19530 15383 3882 192 2826 A C
ATOM 2900 C LEU A 337 13.475 -11.616 -7.557 1.00135.47 A C
ANISOU 2900 C LEU A 337 17928 19180 14366 3735 256 2165 A C
ATOM 2901 O LEU A 337 13.012 -12.748 -7.384 1.00127.22 A O
ANISOU 2901 O LEU A 337 16550 18313 13476 3995 -17 1846 A O
ATOM 2902 CB LEU A 337 12.323 -9.825 -8.890 1.00137.00 A C
ANISOU 2902 CB LEU A 337 18827 19082 14145 3751 117 3283 A C
ATOM 2903 N GLU A 338 14.767 -11.403 -7.820 0.78139.20 A N
ANISOU 2903 N GLU A 338 18456 19899 14537 3321 621 1962 A N
ATOM 2904 CA GLU A 338 15.726 -12.497 -7.716 0.78138.36 A C
ANISOU 2904 CA GLU A 338 17987 20232 14352 3181 741 1329 A C
ATOM 2905 C GLU A 338 15.846 -12.977 -6.275 0.78132.98 A C
ANISOU 2905 C GLU A 338 16984 19279 14264 3347 783 946 A C
ATOM 2906 O GLU A 338 15.983 -14.179 -6.022 0.78123.45 A O
ANISOU 2906 O GLU A 338 15398 18347 13160 3472 679 455 A O
ATOM 2907 CB GLU A 338 17.088 -12.057 -8.251 0.78139.15 A C
ANISOU 2907 CB GLU A 338 18223 20617 14032 2699 1147 1241 A C
ATOM 2908 N ILE A 339 15.791 -12.051 -5.315 1.00134.79 A N
ANISOU 2908 N ILE A 339 17371 18960 14882 3351 939 1163 A N
ATOM 2909 CA ILE A 339 15.848 -12.444 -3.911 1.00128.12 A C
ANISOU 2909 CA ILE A 339 16251 17818 14612 3515 971 830 A C
ATOM 2910 C ILE A 339 14.601 -13.238 -3.536 1.00108.88 A C
ANISOU 2910 C ILE A 339 13592 15251 12526 4000 563 790 A C
ATOM 2911 O ILE A 339 14.683 -14.252 -2.834 1.00101.62 A O
ANISOU 2911 O ILE A 339 12299 14415 11899 4162 487 321 A O
ATOM 2912 CB ILE A 339 16.036 -11.202 -3.018 1.00125.98 A C
ANISOU 2912 CB ILE A 339 16253 16966 14646 3394 1234 1109 A C
ATOM 2913 CG1 ILE A 339 17.513 -10.791 -2.979 1.00131.16 A C
ANISOU 2913 CG1 ILE A 339 16956 17787 15092 2908 1663 912 A C
ATOM 2914 CG2 ILE A 339 15.557 -11.470 -1.600 1.00102.38 A C
ANISOU 2914 CG2 ILE A 339 13067 13530 12302 3695 1150 940 A C
ATOM 2915 CD1 ILE A 339 17.768 -9.407 -2.398 1.00126.63 A C
ANISOU 2915 CD1 ILE A 339 16748 16693 14672 2699 1947 1260 A C
ATOM 2916 N ALA A 340 13.431 -12.809 -4.020 0.79110.11 A N
ANISOU 2916 N ALA A 340 16369 15999 9467 4027 -849 -2318 A N
ATOM 2917 CA ALA A 340 12.189 -13.495 -3.673 0.79 92.61 A C
ANISOU 2917 CA ALA A 340 13682 13929 7576 4062 -788 -2954 A C
ATOM 2918 C ALA A 340 12.195 -14.941 -4.159 0.79101.08 A C
ANISOU 2918 C ALA A 340 14433 15161 8813 3946 -789 -3157 A C
ATOM 2919 O ALA A 340 11.666 -15.832 -3.484 0.79 80.56 A O
ANISOU 2919 O ALA A 340 11501 12547 6560 3610 -560 -3438 A O
ATOM 2920 CB ALA A 340 10.991 -12.743 -4.255 0.79 91.32 A C
ANISOU 2920 CB ALA A 340 13315 13840 7541 4586 -1146 -3405 A C
ATOM 2921 N ARG A 341 12.773 -15.194 -5.336 0.91 99.52 A N
ANISOU 2921 N ARG A 341 14293 15060 8462 4129 -1033 -2964 A N
ATOM 2922 CA ARG A 341 12.892 -16.570 -5.808 0.91 96.10 A C
ANISOU 2922 CA ARG A 341 13565 14761 8189 4043 -1075 -3165 A C
ATOM 2923 C ARG A 341 13.832 -17.370 -4.913 0.91 97.43 A C
ANISOU 2923 C ARG A 341 13863 14786 8371 3565 -810 -2957 A C
ATOM 2924 O ARG A 341 13.564 -18.538 -4.605 0.91 89.09 A O
ANISOU 2924 O ARG A 341 12533 13692 7624 3318 -766 -3203 A O
ATOM 2925 CB ARG A 341 13.381 -16.594 -7.258 0.91 88.30 A C
ANISOU 2925 CB ARG A 341 12630 13913 7007 4332 -1351 -3011 A C
ATOM 2926 N ASN A 342 14.933 -16.754 -4.477 0.89 98.28 A N
ANISOU 2926 N ASN A 342 14360 14715 8265 3365 -674 -2451 A N
ATOM 2927 CA ASN A 342 15.889 -17.462 -3.633 0.89 95.78 A C
ANISOU 2927 CA ASN A 342 14209 14200 7983 2958 -530 -2260 A C
ATOM 2928 C ASN A 342 15.247 -17.896 -2.321 0.89100.11 A C
ANISOU 2928 C ASN A 342 14715 14512 8811 2536 -309 -2359 A C
ATOM 2929 O ASN A 342 15.504 -19.003 -1.832 0.89 91.18 A O
ANISOU 2929 O ASN A 342 13565 13200 7878 2188 -303 -2381 A O
ATOM 2930 CB ASN A 342 17.105 -16.575 -3.366 0.89 95.24 A C
ANISOU 2930 CB ASN A 342 14505 13950 7731 2825 -443 -1750 A C
ATOM 2931 N ILE A 343 14.402 -17.041 -1.741 0.82 87.03 A N
ANISOU 2931 N ILE A 343 13067 12843 7157 2546 -136 -2442 A N
ATOM 2932 CA ILE A 343 13.810 -17.347 -0.442 0.82 86.83 A C
ANISOU 2932 CA ILE A 343 13045 12638 7310 2081 176 -2544 A C
ATOM 2933 C ILE A 343 12.893 -18.562 -0.539 0.82 83.52 A C
ANISOU 2933 C ILE A 343 12203 12290 7239 1889 216 -2973 A C
ATOM 2934 O ILE A 343 12.912 -19.438 0.334 0.82 79.80 A O
ANISOU 2934 O ILE A 343 11845 11593 6881 1362 392 -2932 A O
ATOM 2935 CB ILE A 343 13.068 -16.111 0.099 0.82 73.64 A C
ANISOU 2935 CB ILE A 343 11391 11003 5585 2188 357 -2655 A C
ATOM 2936 CG1 ILE A 343 14.078 -15.079 0.614 0.82 82.12 A C
ANISOU 2936 CG1 ILE A 343 12972 11873 6357 2181 368 -2172 A C
ATOM 2937 CG2 ILE A 343 12.116 -16.493 1.225 0.82 78.82 A C
ANISOU 2937 CG2 ILE A 343 11892 11617 6441 1729 751 -2960 A C
ATOM 2938 CD1 ILE A 343 13.836 -13.664 0.141 0.82 86.84 A C
ANISOU 2938 CD1 ILE A 343 13625 12552 6816 2645 207 -2170 A C
ATOM 2939 N GLY A 344 12.088 -18.644 -1.600 0.84 81.69 A N
ANISOU 2939 N GLY A 344 11524 12336 7179 2298 16 -3388 A N
ATOM 2940 CA GLY A 344 11.158 -19.754 -1.727 0.84 82.53 A C
ANISOU 2940 CA GLY A 344 11167 12505 7684 2128 38 -3851 A C
ATOM 2941 C GLY A 344 11.847 -21.093 -1.927 0.84 81.18 A C
ANISOU 2941 C GLY A 344 11046 12182 7617 1901 -140 -3740 A C
ATOM 2942 O GLY A 344 11.406 -22.112 -1.388 0.84 88.60 A O
ANISOU 2942 O GLY A 344 11865 12960 8838 1441 -14 -3900 A O
ATOM 2943 N HIS A 345 12.929 -21.115 -2.705 1.00 80.41 A N
ANISOU 2943 N HIS A 345 11122 12125 7305 2199 -438 -3497 A N
ATOM 2944 CA HIS A 345 13.638 -22.372 -2.933 1.00 86.91 A C
ANISOU 2944 CA HIS A 345 11947 12804 8272 2052 -676 -3476 A C
ATOM 2945 C HIS A 345 14.315 -22.861 -1.658 1.00 86.61 A C
ANISOU 2945 C HIS A 345 12339 12328 8242 1471 -561 -3135 A C
ATOM 2946 O HIS A 345 14.312 -24.062 -1.365 1.00 84.72 A O
ANISOU 2946 O HIS A 345 12096 11832 8261 1134 -691 -3217 A O
ATOM 2947 CB HIS A 345 14.666 -22.198 -4.051 1.00 85.30 A C
ANISOU 2947 CB HIS A 345 11788 12801 7822 2496 -961 -3373 A C
ATOM 2948 N TYR A 346 14.895 -21.941 -0.887 1.00 76.28 A N
ANISOU 2948 N TYR A 346 11449 10883 6649 1355 -374 -2753 A N
ATOM 2949 CA TYR A 346 15.553 -22.316 0.360 1.00 80.21 A C
ANISOU 2949 CA TYR A 346 12444 10931 7102 839 -325 -2426 A C
ATOM 2950 C TYR A 346 14.549 -22.871 1.361 1.00 87.82 A C
ANISOU 2950 C TYR A 346 13473 11702 8194 272 -31 -2539 A C
ATOM 2951 O TYR A 346 14.785 -23.913 1.984 1.00 85.38 A O
ANISOU 2951 O TYR A 346 13451 11004 7988 -186 -149 -2439 A O
ATOM 2952 CB TYR A 346 16.277 -21.095 0.934 1.00 84.31 A C
ANISOU 2952 CB TYR A 346 13362 11374 7299 883 -191 -2050 A C
ATOM 2953 CG TYR A 346 16.928 -21.302 2.281 1.00 80.17 A C
ANISOU 2953 CG TYR A 346 13416 10371 6674 401 -173 -1720 A C
ATOM 2954 CD1 TYR A 346 16.210 -21.162 3.465 1.00 78.77 A C
ANISOU 2954 CD1 TYR A 346 13516 10033 6381 -56 181 -1672 A C
ATOM 2955 CD2 TYR A 346 18.275 -21.628 2.365 1.00 68.15 A C
ANISOU 2955 CD2 TYR A 346 12170 8560 5164 409 -525 -1502 A C
ATOM 2956 CE1 TYR A 346 16.827 -21.346 4.697 1.00 81.23 A C
ANISOU 2956 CE1 TYR A 346 14465 9880 6517 -494 153 -1352 A C
ATOM 2957 CE2 TYR A 346 18.892 -21.816 3.563 1.00 65.65 A C
ANISOU 2957 CE2 TYR A 346 12426 7757 4761 25 -620 -1227 A C
ATOM 2958 CZ TYR A 346 18.172 -21.674 4.739 1.00 71.36 A C
ANISOU 2958 CZ TYR A 346 13524 8297 5294 -429 -294 -1118 A C
ATOM 2959 OH TYR A 346 18.813 -21.867 5.939 1.00 68.66 A O
ANISOU 2959 OH TYR A 346 13859 7439 4790 -810 -436 -827 A O
ATOM 2960 N LEU A 347 13.414 -22.190 1.524 1.00 90.53 A N
ANISOU 2960 N LEU A 347 13562 12298 8537 272 345 -2777 A N
ATOM 2961 CA LEU A 347 12.441 -22.595 2.531 1.00 96.98 A C
ANISOU 2961 CA LEU A 347 14412 12995 9440 -338 757 -2931 A C
ATOM 2962 C LEU A 347 11.663 -23.836 2.109 1.00 97.13 A C
ANISOU 2962 C LEU A 347 14026 13017 9862 -546 694 -3303 A C
ATOM 2963 O LEU A 347 11.197 -24.592 2.968 1.00 95.53 A O
ANISOU 2963 O LEU A 347 14006 12563 9728 -1218 950 -3315 A O
ATOM 2964 CB LEU A 347 11.485 -21.438 2.820 1.00100.55 A C
ANISOU 2964 CB LEU A 347 14622 13754 9830 -238 1178 -3188 A C
ATOM 2965 CG LEU A 347 12.119 -20.251 3.555 1.00 94.65 A C
ANISOU 2965 CG LEU A 347 14343 12923 8697 -185 1304 -2830 A C
ATOM 2966 CD1 LEU A 347 11.090 -19.141 3.759 1.00 85.19 A C
ANISOU 2966 CD1 LEU A 347 12826 12029 7513 -22 1648 -3196 A C
ATOM 2967 CD2 LEU A 347 12.743 -20.684 4.886 1.00 78.00 A C
ANISOU 2967 CD2 LEU A 347 12936 10375 6325 -823 1443 -2429 A C
ATOM 2968 N GLU A 348 11.512 -24.064 0.804 0.93 98.43 A N
ANISOU 2968 N GLU A 348 13683 13444 10273 -11 355 -3606 A N
ATOM 2969 CA GLU A 348 10.891 -25.302 0.344 0.93107.60 A C
ANISOU 2969 CA GLU A 348 14460 14565 11858 -166 200 -3966 A C
ATOM 2970 C GLU A 348 11.671 -26.525 0.810 0.93109.45 A C
ANISOU 2970 C GLU A 348 15146 14299 12141 -618 -75 -3675 A C
ATOM 2971 O GLU A 348 11.083 -27.597 1.000 0.93112.87 A O
ANISOU 2971 O GLU A 348 15481 14521 12884 -1068 -72 -3860 A O
ATOM 2972 CB GLU A 348 10.784 -25.291 -1.184 0.93101.42 A C
ANISOU 2972 CB GLU A 348 13147 14135 11252 566 -207 -4314 A C
ATOM 2973 CG GLU A 348 10.192 -26.554 -1.832 0.93119.41 A C
ANISOU 2973 CG GLU A 348 14973 16390 14007 530 -470 -4742 A C
ATOM 2974 CD GLU A 348 8.780 -26.897 -1.375 0.93122.30 A C
ANISOU 2974 CD GLU A 348 14931 16775 14760 77 -91 -5175 A C
ATOM 2975 OE1 GLU A 348 8.024 -27.464 -2.193 0.93120.18 A O
ANISOU 2975 OE1 GLU A 348 14086 16656 14919 288 -299 -5685 A O
ATOM 2976 OE2 GLU A 348 8.420 -26.619 -0.213 0.93132.76 A O
ANISOU 2976 OE2 GLU A 348 16490 17980 15974 -503 424 -5050 A O
ATOM 2977 N ARG A 349 12.982 -26.387 1.014 0.88108.64 A N
ANISOU 2977 N ARG A 349 15541 13964 11774 -516 -349 -3251 A N
ATOM 2978 CA ARG A 349 13.860 -27.525 1.249 0.88108.30 A C
ANISOU 2978 CA ARG A 349 15881 13429 11839 -762 -806 -3057 A C
ATOM 2979 C ARG A 349 14.255 -27.712 2.710 0.88116.35 A C
ANISOU 2979 C ARG A 349 17691 13905 12611 -1428 -703 -2622 A C
ATOM 2980 O ARG A 349 14.939 -28.691 3.025 0.88126.21 A O
ANISOU 2980 O ARG A 349 19355 14641 13958 -1673 -1159 -2459 A O
ATOM 2981 CB ARG A 349 15.126 -27.389 0.392 0.88101.91 A C
ANISOU 2981 CB ARG A 349 15024 12709 10988 -165 -1278 -3000 A C
ATOM 2982 N VAL A 350 13.856 -26.809 3.605 1.00109.68 A N
ANISOU 2982 N VAL A 350 17101 13134 11441 -1706 -173 -2457 A N
ATOM 2983 CA VAL A 350 14.089 -27.011 5.035 1.00109.18 A C
ANISOU 2983 CA VAL A 350 17849 12566 11067 -2394 -33 -2070 A C
ATOM 2984 C VAL A 350 12.793 -27.473 5.697 1.00114.98 A C
ANISOU 2984 C VAL A 350 18581 13277 11827 -3119 511 -2237 A C
ATOM 2985 O VAL A 350 12.519 -28.670 5.782 1.00116.83 A O
ANISOU 2985 O VAL A 350 18935 13172 12282 -3574 347 -2276 A O
ATOM 2986 CB VAL A 350 14.626 -25.740 5.732 1.00106.14 A C
ANISOU 2986 CB VAL A 350 17851 12230 10248 -2286 190 -1770 A C
ATOM 2987 CG1 VAL A 350 15.706 -25.071 4.890 1.00102.03 A C
ANISOU 2987 CG1 VAL A 350 17131 11885 9751 -1552 -194 -1705 A C
ATOM 2988 CG2 VAL A 350 13.490 -24.768 6.037 1.00103.89 A C
ANISOU 2988 CG2 VAL A 350 17267 12386 9822 -2378 891 -1991 A C
TER
HETATM 2989 P FMN A 401 29.908 -1.125 48.728 1.00 80.16 B P
HETATM 2990 O1P FMN A 401 30.328 -0.295 49.919 1.00 66.02 B O
HETATM 2991 O2P FMN A 401 30.159 -2.587 48.992 1.00 77.71 B O
HETATM 2992 O3P FMN A 401 30.634 -0.685 47.479 1.00 66.14 B O
HETATM 2993 C5' FMN A 401 27.812 -1.182 47.198 1.00 62.58 B C
HETATM 2994 O5' FMN A 401 28.304 -0.895 48.468 1.00 79.20 B O
HETATM 2995 C4' FMN A 401 26.315 -0.898 47.238 1.00 55.44 B C
HETATM 2996 O4' FMN A 401 26.105 0.484 47.216 1.00 56.43 B O
HETATM 2997 C3' FMN A 401 25.665 -1.580 46.036 1.00 52.72 B C
HETATM 2998 O3' FMN A 401 25.606 -2.940 46.371 1.00 47.86 B O
HETATM 2999 C2' FMN A 401 24.265 -1.031 45.756 1.00 51.18 B C
HETATM 3000 O2' FMN A 401 23.718 -1.606 44.600 1.00 50.49 B O
HETATM 3001 C1' FMN A 401 23.375 -1.465 46.892 1.00 48.63 B C
HETATM 3002 N1 FMN A 401 23.391 1.112 48.009 1.00 51.27 B N
HETATM 3003 C2 FMN A 401 23.458 2.445 48.616 1.00 56.74 B C
HETATM 3004 O2 FMN A 401 24.507 2.896 48.926 1.00 59.82 B O
HETATM 3005 N3 FMN A 401 22.211 3.215 48.829 1.00 50.59 B N
HETATM 3006 C4 FMN A 401 20.926 2.654 48.445 1.00 48.53 B C
HETATM 3007 C4A FMN A 401 20.884 1.282 47.815 1.00 47.46 B C
HETATM 3008 O4 FMN A 401 19.937 3.283 48.640 1.00 49.76 B O
HETATM 3009 C5A FMN A 401 19.624 -0.661 46.796 1.00 49.02 B C
HETATM 3010 N5 FMN A 401 19.638 0.686 47.414 1.00 46.03 B N
HETATM 3011 C6 FMN A 401 18.393 -1.204 46.413 1.00 44.22 B C
HETATM 3012 C7 FMN A 401 18.373 -2.470 45.841 1.00 47.67 B C
HETATM 3013 C7M FMN A 401 16.909 -2.766 45.545 1.00 46.58 B C
HETATM 3014 C8 FMN A 401 19.558 -3.185 45.646 1.00 47.22 B C
HETATM 3015 C8M FMN A 401 19.412 -4.555 45.004 1.00 44.84 B C
HETATM 3016 C9 FMN A 401 20.779 -2.644 46.030 1.00 47.73 B C
HETATM 3017 C9A FMN A 401 20.814 -1.375 46.604 1.00 46.46 B C
HETATM 3018 C10 FMN A 401 22.112 0.546 47.613 1.00 46.06 B C
HETATM 3019 N10 FMN A 401 22.107 -0.760 47.022 1.00 44.08 B N
HETATM 3020 PA AATP A 402 3.895 -7.915 2.546 0.58 39.31 C P
HETATM 3021 PA BATP A 402 3.798 -7.650 2.584 0.42 39.37 C P
HETATM 3022 PB AATP A 402 5.886 -9.876 1.598 0.58 39.28 C P
HETATM 3023 PB BATP A 402 5.640 -9.691 1.531 0.42 39.25 C P
HETATM 3024 PG AATP A 402 7.385 -7.849 0.094 0.58 37.87 C P
HETATM 3025 PG BATP A 402 7.142 -7.762 -0.148 0.42 39.30 C P
HETATM 3026 C5'AATP A 402 3.474 -9.154 4.837 0.58 41.05 C C
HETATM 3027 C5'BATP A 402 3.779 -9.393 4.565 0.42 41.35 C C
HETATM 3028 O5'AATP A 402 2.945 -8.582 3.620 0.58 41.65 C O
HETATM 3029 O5'BATP A 402 3.159 -8.281 3.884 0.42 42.78 C O
HETATM 3030 C4'AATP A 402 2.539 -8.949 6.011 0.58 39.22 C C
HETATM 3031 C4'BATP A 402 2.745 -9.988 5.489 0.42 41.52 C C
HETATM 3032 O4'AATP A 402 2.355 -7.533 6.171 0.58 37.58 C O
HETATM 3033 O4'BATP A 402 2.329 -8.936 6.385 0.42 38.46 C O
HETATM 3034 C3'AATP A 402 1.137 -9.432 5.688 0.58 39.51 C C
HETATM 3035 C3'BATP A 402 1.504 -10.339 4.666 0.42 40.08 C C
HETATM 3036 O3'AATP A 402 1.070 -10.753 6.216 0.58 41.54 C O
HETATM 3037 O3'BATP A 402 0.874 -11.446 5.300 0.42 40.98 C O
HETATM 3038 C2'AATP A 402 0.281 -8.579 6.616 0.58 38.98 C C
HETATM 3039 C2'BATP A 402 0.585 -9.154 4.930 0.42 40.35 C C
HETATM 3040 O2'AATP A 402 0.467 -9.042 7.952 0.58 37.38 C O
HETATM 3041 O2'BATP A 402 -0.749 -9.654 4.980 0.42 41.34 C O
HETATM 3042 C1'AATP A 402 1.037 -7.249 6.607 0.58 40.09 C C
HETATM 3043 C1'BATP A 402 0.925 -8.895 6.382 0.42 39.37 C C
HETATM 3044 N1 AATP A 402 -1.632 -2.918 5.858 0.58 36.62 C N
HETATM 3045 N1 BATP A 402 -1.110 -6.072 10.120 0.42 37.86 C N
HETATM 3046 O1AAATP A 402 3.156 -7.025 1.627 0.58 39.45 C O
HETATM 3047 O1ABATP A 402 2.809 -6.892 1.791 0.42 42.40 C O
HETATM 3048 O1BAATP A 402 6.711 -9.622 2.800 0.58 39.42 C O
HETATM 3049 O1BBATP A 402 6.563 -9.493 2.669 0.42 39.01 C O
HETATM 3050 O1GAATP A 402 8.769 -8.263 -0.300 0.58 36.44 C O
HETATM 3051 O1GBATP A 402 8.421 -8.286 -0.724 0.42 39.27 C O
HETATM 3052 C2 AATP A 402 -1.265 -3.557 6.969 0.58 41.75 C C
HETATM 3053 C2 BATP A 402 -0.783 -7.364 10.042 0.42 27.87 C C
HETATM 3054 O2AAATP A 402 5.075 -7.253 3.279 0.58 35.90 C O
HETATM 3055 O2ABATP A 402 5.052 -6.873 2.998 0.42 35.52 C O
HETATM 3056 O2BAATP A 402 5.650 -11.327 1.211 0.58 41.87 C O
HETATM 3057 O2BBATP A 402 5.304 -11.133 1.174 0.42 41.14 C O
HETATM 3058 O2GAATP A 402 7.314 -7.049 1.393 0.58 38.50 C O
HETATM 3059 O2GBATP A 402 7.328 -6.993 1.151 0.42 38.00 C O
HETATM 3060 N3 AATP A 402 -0.570 -4.690 7.089 0.58 39.36 C N
HETATM 3061 N3 BATP A 402 -0.256 -8.035 9.022 0.42 38.52 C N
HETATM 3062 O3AAATP A 402 4.481 -9.147 1.730 0.58 42.33 C O
HETATM 3063 O3ABATP A 402 4.274 -8.919 1.771 0.42 41.48 C O
HETATM 3064 O3BAATP A 402 6.513 -9.140 0.382 0.58 40.56 C O
HETATM 3065 O3BBATP A 402 6.181 -8.971 0.244 0.42 38.75 C O
HETATM 3066 O3GAATP A 402 6.620 -7.108 -1.004 0.58 38.25 C O
HETATM 3067 O3GBATP A 402 6.329 -6.921 -1.129 0.42 38.58 C O
HETATM 3068 C4 AATP A 402 -0.248 -5.187 5.891 0.58 40.40 C C
HETATM 3069 C4 BATP A 402 -0.048 -7.228 7.982 0.42 41.04 C C
HETATM 3070 C5 AATP A 402 -0.563 -4.648 4.655 0.58 46.36 C C
HETATM 3071 C5 BATP A 402 -0.327 -5.874 7.909 0.42 39.12 C C
HETATM 3072 C6 AATP A 402 -1.309 -3.453 4.659 0.58 48.47 C C
HETATM 3073 C6 BATP A 402 -0.892 -5.282 9.053 0.42 37.75 C C
HETATM 3074 N6 AATP A 402 -1.688 -2.806 3.552 0.58 50.77 C N
HETATM 3075 N6 BATP A 402 -1.219 -3.991 9.145 0.42 43.00 C N
HETATM 3076 N7 AATP A 402 -0.080 -5.452 3.630 0.58 44.58 C N
HETATM 3077 N7 BATP A 402 0.021 -5.369 6.665 0.42 43.16 C N
HETATM 3078 C8 AATP A 402 0.538 -6.419 4.262 0.58 41.49 C C
HETATM 3079 C8 BATP A 402 0.498 -6.412 6.031 0.42 40.44 C C
HETATM 3080 N9 AATP A 402 0.465 -6.330 5.628 0.58 40.01 C N
HETATM 3081 N9 BATP A 402 0.504 -7.563 6.776 0.42 37.32 C N
HETATM 3082 MG MG A 403 7.209 -7.599 3.370 1.00 35.90 D MG
ATOM 3083 N MET B 1 -16.805 -19.958 45.596 1.00 78.68 D000 N
ANISOU 3083 N MET B 1 11789 6426 11679 -920 -3273 -53 D000 N
ATOM 3084 CA MET B 1 -16.751 -18.519 45.959 1.00 75.46 D000 C
ANISOU 3084 CA MET B 1 11096 6663 10914 -779 -2837 -203 D000 C
ATOM 3085 C MET B 1 -16.075 -17.728 44.854 1.00 73.85 D000 C
ANISOU 3085 C MET B 1 10797 6798 10464 -700 -2528 42 D000 C
ATOM 3086 O MET B 1 -15.232 -18.251 44.127 1.00 71.64 D000 O
ANISOU 3086 O MET B 1 10683 6301 10234 -568 -2664 160 D000 O
ATOM 3087 CB MET B 1 -15.998 -18.314 47.273 1.00 72.49 D000 C
ANISOU 3087 CB MET B 1 10737 6387 10418 -335 -2858 -755 D000 C
ATOM 3088 CG MET B 1 -16.455 -17.099 48.065 1.00 82.02 D000 C
ANISOU 3088 CG MET B 1 11702 8107 11358 -328 -2560 -901 D000 C
ATOM 3089 SD MET B 1 -16.103 -17.117 49.845 1.00 95.84 D000 S
ANISOU 3089 SD MET B 1 13515 9940 12961 38 -2666 -1496 D000 S
ATOM 3090 CE MET B 1 -15.790 -18.846 50.197 1.00 85.33 D000 C
ANISOU 3090 CE MET B 1 12535 7923 11962 198 -3198 -1795 D000 C
ATOM 3091 N LYS B 2 -16.444 -16.459 44.748 1.00 68.68 D000 N
ANISOU 3091 N LYS B 2 9887 6656 9553 -763 -2153 97 D000 N
ATOM 3092 CA LYS B 2 -15.884 -15.547 43.762 1.00 61.36 D000 C
ANISOU 3092 CA LYS B 2 8862 6079 8371 -692 -1867 269 D000 C
ATOM 3093 C LYS B 2 -15.291 -14.346 44.484 1.00 58.49 D000 C
ANISOU 3093 C LYS B 2 8330 6102 7793 -411 -1629 -37 D000 C
ATOM 3094 O LYS B 2 -15.794 -13.923 45.529 1.00 58.82 D000 O
ANISOU 3094 O LYS B 2 8266 6276 7809 -400 -1574 -241 D000 O
ATOM 3095 CB LYS B 2 -16.967 -15.112 42.773 1.00 69.53 D000 C
ANISOU 3095 CB LYS B 2 9756 7356 9308 -1061 -1643 658 D000 C
ATOM 3096 CG LYS B 2 -16.474 -14.332 41.577 1.00 70.47 D000 C
ANISOU 3096 CG LYS B 2 9837 7791 9148 -1010 -1405 843 D000 C
ATOM 3097 CD LYS B 2 -17.632 -14.022 40.639 1.00 73.65 D000 C
ANISOU 3097 CD LYS B 2 10098 8460 9426 -1353 -1171 1193 D000 C
ATOM 3098 CE LYS B 2 -17.152 -13.459 39.313 1.00 80.88 D000 C
ANISOU 3098 CE LYS B 2 11050 9654 10028 -1308 -990 1382 D000 C
ATOM 3099 NZ LYS B 2 -18.223 -13.476 38.281 1.00 69.03 D000 N
ANISOU 3099 NZ LYS B 2 9457 8396 8373 -1644 -782 1763 D000 N
ATOM 3100 N ARG B 3 -14.206 -13.802 43.938 1.00 57.21 D000 N
ANISOU 3100 N ARG B 3 8143 6111 7481 -200 -1516 -47 D000 N
ATOM 3101 CA ARG B 3 -13.616 -12.594 44.500 1.00 50.94 D000 C
ANISOU 3101 CA ARG B 3 7174 5679 6503 -0 -1287 -261 D000 C
ATOM 3102 C ARG B 3 -13.247 -11.636 43.376 1.00 55.44 D000 C
ANISOU 3102 C ARG B 3 7658 6511 6895 -24 -1097 -87 D000 C
ATOM 3103 O ARG B 3 -12.552 -12.012 42.425 1.00 56.61 D000 O
ANISOU 3103 O ARG B 3 7904 6568 7036 30 -1199 43 D000 O
ATOM 3104 CB ARG B 3 -12.389 -12.922 45.363 1.00 53.22 D000 C
ANISOU 3104 CB ARG B 3 7481 5916 6825 352 -1385 -583 D000 C
ATOM 3105 CG ARG B 3 -11.739 -11.700 46.011 1.00 53.93 D000 C
ANISOU 3105 CG ARG B 3 7369 6395 6728 506 -1138 -750 D000 C
ATOM 3106 CD ARG B 3 -10.905 -12.097 47.220 1.00 61.42 D000 C
ANISOU 3106 CD ARG B 3 8299 7368 7670 810 -1184 -1092 D000 C
ATOM 3107 NE ARG B 3 -9.931 -13.121 46.864 1.00 66.41 D000 N
ANISOU 3107 NE ARG B 3 9014 7760 8459 1056 -1394 -1189 D000 N
ATOM 3108 CZ ARG B 3 -9.774 -14.279 47.493 1.00 71.33 D000 C
ANISOU 3108 CZ ARG B 3 9783 8099 9221 1263 -1629 -1441 D000 C
ATOM 3109 NH1 ARG B 3 -10.462 -14.579 48.583 1.00 74.62 D000 N
ANISOU 3109 NH1 ARG B 3 10284 8464 9606 1256 -1683 -1654 D000 N
ATOM 3110 NH2 ARG B 3 -8.898 -15.158 47.016 1.00 71.03 D000 N
ANISOU 3110 NH2 ARG B 3 9819 7806 9362 1506 -1851 -1503 D000 N
ATOM 3111 N LEU B 4 -13.723 -10.397 43.504 1.00 52.11 D000 N
ANISOU 3111 N LEU B 4 7074 6393 6333 -89 -861 -100 D000 N
ATOM 3112 CA LEU B 4 -13.534 -9.338 42.526 1.00 52.98 D000 C
ANISOU 3112 CA LEU B 4 7110 6747 6272 -109 -692 1 D000 C
ATOM 3113 C LEU B 4 -12.698 -8.209 43.113 1.00 50.38 D000 C
ANISOU 3113 C LEU B 4 6650 6615 5878 57 -586 -188 D000 C
ATOM 3114 O LEU B 4 -12.908 -7.790 44.256 1.00 48.44 D000 O
ANISOU 3114 O LEU B 4 6320 6441 5643 90 -523 -322 D000 O
ATOM 3115 CB LEU B 4 -14.882 -8.768 42.078 1.00 51.89 D000 C
ANISOU 3115 CB LEU B 4 6885 6777 6056 -319 -520 141 D000 C
ATOM 3116 CG LEU B 4 -15.324 -9.031 40.643 1.00 69.77 D000 C
ANISOU 3116 CG LEU B 4 9213 9099 8197 -479 -471 406 D000 C
ATOM 3117 CD1 LEU B 4 -15.351 -10.514 40.340 1.00 78.19 D000 C
ANISOU 3117 CD1 LEU B 4 10453 9870 9385 -602 -678 610 D000 C
ATOM 3118 CD2 LEU B 4 -16.693 -8.396 40.423 1.00 70.16 D000 C
ANISOU 3118 CD2 LEU B 4 9092 9386 8178 -637 -253 477 D000 C
ATOM 3119 N THR B 5 -11.766 -7.703 42.315 1.00 46.49 D000 N
ANISOU 3119 N THR B 5 6141 6213 5311 134 -584 -172 D000 N
ATOM 3120 CA THR B 5 -10.938 -6.560 42.684 1.00 45.48 D000 C
ANISOU 3120 CA THR B 5 5870 6259 5151 225 -500 -296 D000 C
ATOM 3121 C THR B 5 -11.049 -5.531 41.570 1.00 48.66 D000 C
ANISOU 3121 C THR B 5 6270 6786 5432 155 -441 -232 D000 C
ATOM 3122 O THR B 5 -10.761 -5.848 40.411 1.00 48.05 D000 O
ANISOU 3122 O THR B 5 6291 6693 5272 154 -531 -143 D000 O
ATOM 3123 CB THR B 5 -9.471 -6.963 42.877 1.00 49.50 D000 C
ANISOU 3123 CB THR B 5 6315 6752 5738 410 -611 -396 D000 C
ATOM 3124 CG2 THR B 5 -8.670 -5.792 43.404 1.00 51.72 D000 C
ANISOU 3124 CG2 THR B 5 6401 7235 6015 437 -504 -482 D000 C
ATOM 3125 OG1 THR B 5 -9.370 -8.059 43.793 1.00 48.85 D000 O
ANISOU 3125 OG1 THR B 5 6268 6539 5755 533 -688 -507 D000 O
ATOM 3126 N TYR B 6 -11.461 -4.308 41.903 1.00 46.53 D000 N
ANISOU 3126 N TYR B 6 5915 6627 5139 113 -320 -287 D000 N
ATOM 3127 CA TYR B 6 -11.544 -3.263 40.891 1.00 44.48 D000 C
ANISOU 3127 CA TYR B 6 5671 6455 4776 90 -293 -300 D000 C
ATOM 3128 C TYR B 6 -11.045 -1.939 41.458 1.00 43.90 D000 C
ANISOU 3128 C TYR B 6 5492 6410 4778 98 -280 -394 D000 C
ATOM 3129 O TYR B 6 -10.894 -1.766 42.668 1.00 43.46 D000 O
ANISOU 3129 O TYR B 6 5348 6354 4811 94 -239 -403 D000 O
ATOM 3130 CB TYR B 6 -12.980 -3.116 40.337 1.00 46.98 D000 C
ANISOU 3130 CB TYR B 6 6022 6843 4985 21 -171 -250 D000 C
ATOM 3131 CG TYR B 6 -13.947 -2.420 41.269 1.00 42.38 D000 C
ANISOU 3131 CG TYR B 6 5334 6282 4486 6 -70 -300 D000 C
ATOM 3132 CD1 TYR B 6 -14.029 -1.036 41.308 1.00 42.66 D000 C
ANISOU 3132 CD1 TYR B 6 5327 6343 4541 57 -49 -405 D000 C
ATOM 3133 CD2 TYR B 6 -14.768 -3.150 42.126 1.00 49.05 D000 C
ANISOU 3133 CD2 TYR B 6 6135 7091 5410 -53 -47 -247 D000 C
ATOM 3134 CE1 TYR B 6 -14.896 -0.392 42.174 1.00 52.06 D000 C
ANISOU 3134 CE1 TYR B 6 6433 7525 5823 68 -5 -430 D000 C
ATOM 3135 CE2 TYR B 6 -15.647 -2.514 42.989 1.00 46.95 D000 C
ANISOU 3135 CE2 TYR B 6 5769 6853 5216 -53 -2 -286 D000 C
ATOM 3136 CZ TYR B 6 -15.705 -1.136 43.007 1.00 49.06 D000 C
ANISOU 3136 CZ TYR B 6 5996 7150 5496 17 21 -365 D000 C
ATOM 3137 OH TYR B 6 -16.562 -0.501 43.874 1.00 49.90 D000 O
ANISOU 3137 OH TYR B 6 6015 7258 5687 41 20 -382 D000 O
ATOM 3138 N ILE B 7 -10.761 -1.014 40.543 1.00 45.02 D000 N
ANISOU 3138 N ILE B 7 5664 6572 4868 100 -335 -456 D000 N
ATOM 3139 CA ILE B 7 -10.437 0.370 40.866 1.00 45.77 D000 C
ANISOU 3139 CA ILE B 7 5697 6627 5065 71 -368 -530 D000 C
ATOM 3140 C ILE B 7 -11.366 1.283 40.079 1.00 49.38 D000 C
ANISOU 3140 C ILE B 7 6244 7078 5441 108 -351 -634 D000 C
ATOM 3141 O ILE B 7 -11.850 0.933 38.998 1.00 46.31 D000 O
ANISOU 3141 O ILE B 7 5950 6781 4865 156 -321 -666 D000 O
ATOM 3142 CB ILE B 7 -8.940 0.682 40.582 1.00 46.92 D000 C
ANISOU 3142 CB ILE B 7 5769 6763 5297 43 -525 -558 D000 C
ATOM 3143 CG1 ILE B 7 -8.667 0.873 39.089 1.00 51.88 D000 C
ANISOU 3143 CG1 ILE B 7 6515 7401 5796 79 -676 -650 D000 C
ATOM 3144 CG2 ILE B 7 -8.058 -0.403 41.185 1.00 57.75 D000 C
ANISOU 3144 CG2 ILE B 7 7022 8192 6728 78 -526 -494 D000 C
ATOM 3145 CD1 ILE B 7 -7.345 1.584 38.812 1.00 60.84 D000 C
ANISOU 3145 CD1 ILE B 7 7556 8497 7065 19 -885 -712 D000 C
ATOM 3146 N SER B 8 -11.634 2.459 40.638 1.00 43.95 D000 N
ANISOU 3146 N SER B 8 5528 6290 4883 100 -368 -684 D000 N
ATOM 3147 CA SER B 8 -12.483 3.429 39.963 1.00 44.97 D000 C
ANISOU 3147 CA SER B 8 5731 6382 4975 196 -378 -842 D000 C
ATOM 3148 C SER B 8 -12.055 4.829 40.371 1.00 48.24 D000 C
ANISOU 3148 C SER B 8 6154 6576 5599 163 -538 -900 D000 C
ATOM 3149 O SER B 8 -11.265 5.014 41.297 1.00 46.99 D000 O
ANISOU 3149 O SER B 8 5919 6339 5596 28 -590 -759 D000 O
ATOM 3150 CB SER B 8 -13.966 3.204 40.287 1.00 47.36 D000 C
ANISOU 3150 CB SER B 8 5983 6769 5244 268 -214 -826 D000 C
ATOM 3151 OG SER B 8 -14.222 3.470 41.659 1.00 50.17 D000 O
ANISOU 3151 OG SER B 8 6262 7030 5768 226 -218 -722 D000 O
ATOM 3152 N LYS B 9 -12.591 5.819 39.662 1.00 50.26 D000 N
ANISOU 3152 N LYS B 9 6506 6736 5856 288 -618 -1108 D000 N
ATOM 3153 CA LYS B 9 -12.298 7.225 39.896 1.00 50.03 D000 C
ANISOU 3153 CA LYS B 9 6534 6413 6063 268 -831 -1187 D000 C
ATOM 3154 C LYS B 9 -13.532 7.926 40.449 1.00 53.85 D000 C
ANISOU 3154 C LYS B 9 7020 6781 6660 410 -808 -1227 D000 C
ATOM 3155 O LYS B 9 -14.654 7.661 40.003 1.00 54.01 D000 O
ANISOU 3155 O LYS B 9 7014 6965 6541 599 -661 -1354 D000 O
ATOM 3156 CB LYS B 9 -11.854 7.904 38.592 1.00 57.80 D000 C
ANISOU 3156 CB LYS B 9 7663 7307 6992 343 -1030 -1467 D000 C
ATOM 3157 CG LYS B 9 -11.291 9.305 38.780 1.00 69.92 D000 C
ANISOU 3157 CG LYS B 9 9275 8462 8830 262 -1331 -1542 D000 C
ATOM 3158 CD LYS B 9 -11.089 10.060 37.456 1.00 83.29 D000 C
ANISOU 3158 CD LYS B 9 11153 10032 10461 392 -1571 -1912 D000 C
ATOM 3159 CE LYS B 9 -12.300 10.895 37.040 1.00114.69 D000 C
ANISOU 3159 CE LYS B 9 15258 13898 14422 702 -1590 -2228 D000 C
ATOM 3160 NZ LYS B 9 -12.011 12.359 37.086 1.00109.77 D000 N
ANISOU 3160 NZ LYS B 9 14785 12785 14138 699 -1964 -2402 D000 N
ATOM 3161 N PHE B 10 -13.327 8.815 41.425 1.00 54.89 D000 N
ANISOU 3161 N PHE B 10 7161 6644 7049 314 -959 -1091 D000 N
ATOM 3162 CA PHE B 10 -14.413 9.675 41.888 1.00 51.78 D000 C
ANISOU 3162 CA PHE B 10 6798 6065 6811 479 -1032 -1138 D000 C
ATOM 3163 C PHE B 10 -15.001 10.443 40.704 1.00 58.21 D000 C
ANISOU 3163 C PHE B 10 7719 6779 7620 755 -1130 -1523 D000 C
ATOM 3164 O PHE B 10 -14.272 11.099 39.956 1.00 57.02 D000 O
ANISOU 3164 O PHE B 10 7703 6437 7524 739 -1334 -1706 D000 O
ATOM 3165 CB PHE B 10 -13.911 10.684 42.932 1.00 61.98 D000 C
ANISOU 3165 CB PHE B 10 8148 7015 8387 307 -1255 -911 D000 C
ATOM 3166 CG PHE B 10 -13.580 10.101 44.299 1.00 55.27 D000 C
ANISOU 3166 CG PHE B 10 7197 6304 7500 91 -1137 -539 D000 C
ATOM 3167 CD1 PHE B 10 -13.357 8.748 44.487 1.00 52.33 D000 C
ANISOU 3167 CD1 PHE B 10 6704 6281 6900 31 -898 -462 D000 C
ATOM 3168 CD2 PHE B 10 -13.463 10.948 45.397 1.00 63.26 D000 C
ANISOU 3168 CD2 PHE B 10 8260 7080 8696 -45 -1291 -269 D000 C
ATOM 3169 CE1 PHE B 10 -13.038 8.247 45.746 1.00 53.05 D000 C
ANISOU 3169 CE1 PHE B 10 6720 6511 6926 -121 -800 -188 D000 C
ATOM 3170 CE2 PHE B 10 -13.146 10.453 46.654 1.00 63.54 D000 C
ANISOU 3170 CE2 PHE B 10 8220 7298 8625 -228 -1169 58 D000 C
ATOM 3171 CZ PHE B 10 -12.931 9.105 46.828 1.00 61.18 D000 C
ANISOU 3171 CZ PHE B 10 7794 7374 8078 -248 -917 67 D000 C
ATOM 3172 N ASER B 11 -16.324 10.365 40.533 0.70 58.65 D000 N
ANISOU 3172 N ASER B 11 7694 6983 7607 1019 -994 -1671 D000 N
ATOM 3173 N BSER B 11 -16.325 10.362 40.539 0.30 58.72 D000 N
ANISOU 3173 N BSER B 11 7702 6992 7616 1018 -993 -1669 D000 N
ATOM 3174 CA ASER B 11 -16.975 11.198 39.528 0.70 61.15 D000 C
ANISOU 3174 CA ASER B 11 8086 7230 7918 1345 -1069 -2075 D000 C
ATOM 3175 CA BSER B 11 -16.997 11.192 39.546 0.30 61.20 D000 C
ANISOU 3175 CA BSER B 11 8089 7239 7926 1347 -1066 -2072 D000 C
ATOM 3176 C ASER B 11 -17.005 12.659 39.951 0.70 61.19 D000 C
ANISOU 3176 C ASER B 11 8233 6728 8290 1450 -1417 -2165 D000 C
ATOM 3177 C BSER B 11 -17.041 12.653 39.970 0.30 61.39 D000 C
ANISOU 3177 C BSER B 11 8253 6757 8316 1455 -1412 -2163 D000 C
ATOM 3178 O ASER B 11 -17.116 13.545 39.097 0.70 66.98 D000 O
ANISOU 3178 O ASER B 11 9106 7266 9076 1691 -1594 -2544 D000 O
ATOM 3179 O BSER B 11 -17.176 13.535 39.114 0.30 67.01 D000 O
ANISOU 3179 O BSER B 11 9103 7279 9080 1702 -1585 -2545 D000 O
ATOM 3180 CB ASER B 11 -18.400 10.708 39.274 0.70 62.14 D000 C
ANISOU 3180 CB ASER B 11 8012 7709 7890 1600 -797 -2193 D000 C
ATOM 3181 CB BSER B 11 -18.421 10.687 39.306 0.30 62.20 D000 C
ANISOU 3181 CB BSER B 11 8013 7721 7898 1597 -792 -2184 D000 C
ATOM 3182 OG ASER B 11 -19.251 11.063 40.351 0.70 67.01 D000 O
ANISOU 3182 OG ASER B 11 8510 8196 8754 1687 -859 -2067 D000 O
ATOM 3183 OG BSER B 11 -18.429 9.539 38.479 0.30 63.44 D000 O
ANISOU 3183 OG BSER B 11 8098 8308 7699 1538 -510 -2181 D000 O
ATOM 3184 N AARG B 12 -16.901 12.919 41.249 0.70 64.25 D000 N
ANISOU 3184 N AARG B 12 8608 6889 8916 1276 -1537 -1823 D000 N
ATOM 3185 N BARG B 12 -16.927 12.922 41.266 0.30 64.34 D000 N
ANISOU 3185 N BARG B 12 8617 6901 8930 1280 -1536 -1822 D000 N
ATOM 3186 CA AARG B 12 -16.953 14.264 41.799 0.70 71.50 D000 C
ANISOU 3186 CA AARG B 12 9678 7283 10206 1330 -1897 -1802 D000 C
ATOM 3187 CA BARG B 12 -16.978 14.274 41.802 0.30 71.46 D000 C
ANISOU 3187 CA BARG B 12 9671 7277 10204 1337 -1898 -1805 D000 C
ATOM 3188 C AARG B 12 -16.277 14.245 43.161 0.70 68.49 D000 C
ANISOU 3188 C AARG B 12 9302 6767 9953 962 -1972 -1298 D000 C
ATOM 3189 C BARG B 12 -16.350 14.255 43.188 0.30 68.58 D000 C
ANISOU 3189 C BARG B 12 9310 6778 9968 978 -1972 -1299 D000 C
ATOM 3190 O AARG B 12 -16.056 13.171 43.732 0.70 63.38 D000 O
ANISOU 3190 O AARG B 12 8515 6470 9095 768 -1720 -1041 D000 O
ATOM 3191 O BARG B 12 -16.223 13.187 43.799 0.30 64.00 D000 O
ANISOU 3191 O BARG B 12 8586 6550 9181 800 -1719 -1042 D000 O
ATOM 3192 CB AARG B 12 -18.404 14.759 41.922 0.70 72.89 D000 C
ANISOU 3192 CB AARG B 12 9781 7406 10509 1739 -1936 -1995 D000 C
ATOM 3193 CB BARG B 12 -18.425 14.795 41.859 0.30 72.90 D000 C
ANISOU 3193 CB BARG B 12 9787 7401 10511 1758 -1941 -2021 D000 C
ATOM 3194 CG AARG B 12 -19.172 14.165 43.102 0.70 77.27 D000 C
ANISOU 3194 CG AARG B 12 10147 8161 11051 1702 -1806 -1669 D000 C
ATOM 3195 CG BARG B 12 -19.062 14.813 43.246 0.30 79.52 D000 C
ANISOU 3195 CG BARG B 12 10535 8177 11502 1725 -1996 -1667 D000 C
ATOM 3196 CD AARG B 12 -20.665 14.478 43.014 0.70 85.31 D000 C
ANISOU 3196 CD AARG B 12 11002 9240 12170 2138 -1808 -1913 D000 C
ATOM 3197 CD BARG B 12 -20.542 15.191 43.168 0.30 82.81 D000 C
ANISOU 3197 CD BARG B 12 10808 8618 12038 2181 -2024 -1921 D000 C
ATOM 3198 NE AARG B 12 -21.475 13.564 43.813 0.70 88.12 D000 N
ANISOU 3198 NE AARG B 12 11107 9949 12426 2101 -1615 -1685 D000 N
ATOM 3199 NE BARG B 12 -21.391 14.338 43.995 0.30 87.89 D000 N
ANISOU 3199 NE BARG B 12 11200 9610 12584 2168 -1837 -1693 D000 N
ATOM 3200 CZ AARG B 12 -21.527 13.568 45.139 0.70 90.62 D000 C
ANISOU 3200 CZ AARG B 12 11440 10151 12843 1941 -1758 -1310 D000 C
ATOM 3201 CZ BARG B 12 -21.884 13.165 43.618 0.30 87.28 D000 C
ANISOU 3201 CZ BARG B 12 10874 10055 12234 2165 -1477 -1749 D000 C
ATOM 3202 NH1AARG B 12 -20.824 14.430 45.857 0.70 90.10 D000 N
ANISOU 3202 NH1AARG B 12 11616 9646 12970 1780 -2062 -1060 D000 N
ATOM 3203 NH1BARG B 12 -21.626 12.656 42.424 0.30 82.06 D000 N
ANISOU 3203 NH1BARG B 12 10187 9670 11324 2177 -1231 -1990 D000 N
ATOM 3204 NH2AARG B 12 -22.305 12.686 45.761 0.70 88.58 D000 N
ANISOU 3204 NH2AARG B 12 10952 10230 12475 1924 -1608 -1171 D000 N
ATOM 3205 NH2BARG B 12 -22.660 12.487 44.460 0.30 86.22 D000 N
ANISOU 3205 NH2BARG B 12 10525 10159 12075 2131 -1391 -1543 D000 N
ATOM 3206 N PRO B 13 -15.920 15.408 43.697 1.00 74.22 D000 N
ANISOU 3206 N PRO B 13 10199 6993 11010 856 -2318 -1144 D000 N
ATOM 3207 CA PRO B 13 -15.407 15.452 45.071 1.00 72.40 D000 C
ANISOU 3207 CA PRO B 13 9969 6686 10853 513 -2363 -618 D000 C
ATOM 3208 C PRO B 13 -16.385 14.813 46.047 1.00 77.10 D000 C
ANISOU 3208 C PRO B 13 10434 7561 11298 618 -2192 -425 D000 C
ATOM 3209 O PRO B 13 -17.579 15.126 46.056 1.00 79.87 D000 O
ANISOU 3209 O PRO B 13 10764 7840 11741 953 -2276 -587 D000 O
ATOM 3210 CB PRO B 13 -15.235 16.951 45.348 1.00 80.89 D000 C
ANISOU 3210 CB PRO B 13 11276 7115 12342 463 -2812 -518 D000 C
ATOM 3211 CG PRO B 13 -15.480 17.665 44.048 1.00 85.68 D000 C
ANISOU 3211 CG PRO B 13 12016 7430 13109 775 -3025 -1054 D000 C
ATOM 3212 CD PRO B 13 -15.663 16.659 42.964 1.00 86.50 D000 C
ANISOU 3212 CD PRO B 13 11974 8037 12855 962 -2690 -1429 D000 C
ATOM 3213 N LEU B 14 -15.868 13.904 46.867 1.00 74.15 D000 N
ANISOU 3213 N LEU B 14 9957 7520 10695 348 -1969 -106 D000 N
ATOM 3214 CA LEU B 14 -16.627 13.269 47.935 1.00 65.35 D000 C
ANISOU 3214 CA LEU B 14 8749 6664 9415 387 -1852 102 D000 C
ATOM 3215 C LEU B 14 -15.973 13.613 49.264 1.00 72.43 D000 C
ANISOU 3215 C LEU B 14 9736 7480 10303 76 -1945 590 D000 C
ATOM 3216 O LEU B 14 -14.750 13.494 49.407 1.00 69.66 D000 O
ANISOU 3216 O LEU B 14 9375 7200 9892 -239 -1855 780 D000 O
ATOM 3217 CB LEU B 14 -16.680 11.750 47.756 1.00 61.09 D000 C
ANISOU 3217 CB LEU B 14 8025 6629 8557 376 -1501 7 D000 C
ATOM 3218 CG LEU B 14 -17.162 11.207 46.414 1.00 59.93 D000 C
ANISOU 3218 CG LEU B 14 7777 6659 8335 597 -1342 -390 D000 C
ATOM 3219 CD1 LEU B 14 -17.110 9.687 46.418 1.00 63.03 D000 C
ANISOU 3219 CD1 LEU B 14 8025 7479 8447 512 -1046 -376 D000 C
ATOM 3220 CD2 LEU B 14 -18.572 11.688 46.113 1.00 74.85 D000 C
ANISOU 3220 CD2 LEU B 14 9608 8475 10356 952 -1430 -621 D000 C
ATOM 3221 N SER B 15 -16.780 14.033 50.232 1.00 66.14 D000 N
ANISOU 3221 N SER B 15 9010 6571 9550 165 -2121 803 D000 N
ATOM 3222 CA SER B 15 -16.246 14.325 51.551 1.00 73.53 D000 C
ANISOU 3222 CA SER B 15 10050 7495 10393 -128 -2191 1307 D000 C
ATOM 3223 C SER B 15 -15.999 13.026 52.312 1.00 67.72 D000 C
ANISOU 3223 C SER B 15 9184 7307 9240 -252 -1870 1423 D000 C
ATOM 3224 O SER B 15 -16.476 11.952 51.940 1.00 59.65 D000 O
ANISOU 3224 O SER B 15 8014 6593 8059 -89 -1667 1139 D000 O
ATOM 3225 CB SER B 15 -17.199 15.218 52.340 1.00 74.93 D000 C
ANISOU 3225 CB SER B 15 10380 7359 10729 24 -2538 1519 D000 C
ATOM 3226 OG SER B 15 -18.543 14.817 52.151 1.00 81.22 D000 O
ANISOU 3226 OG SER B 15 11055 8278 11527 406 -2553 1223 D000 O
ATOM 3227 N GLY B 16 -15.239 13.133 53.399 1.00 66.09 D000 N
ANISOU 3227 N GLY B 16 9038 7221 8851 -548 -1829 1847 D000 N
ATOM 3228 CA GLY B 16 -15.011 11.965 54.229 1.00 70.84 D000 C
ANISOU 3228 CA GLY B 16 9545 8340 9032 -621 -1549 1923 D000 C
ATOM 3229 C GLY B 16 -16.306 11.364 54.740 1.00 66.85 D000 C
ANISOU 3229 C GLY B 16 9034 7994 8371 -362 -1608 1804 D000 C
ATOM 3230 O GLY B 16 -16.444 10.141 54.829 1.00 60.85 D000 O
ANISOU 3230 O GLY B 16 8160 7593 7368 -296 -1399 1607 D000 O
ATOM 3231 N AASP B 17 -17.285 12.213 55.059 0.53 64.96 D000 N
ANISOU 3231 N AASP B 17 8913 7462 8308 -206 -1932 1908 D000 N
ATOM 3232 N BASP B 17 -17.273 12.216 55.088 0.47 64.99 D000 N
ANISOU 3232 N BASP B 17 8919 7469 8306 -212 -1932 1918 D000 N
ATOM 3233 CA AASP B 17 -18.531 11.700 55.620 0.53 67.95 D000 C
ANISOU 3233 CA AASP B 17 9251 8002 8566 24 -2038 1820 D000 C
ATOM 3234 CA BASP B 17 -18.539 11.710 55.607 0.47 67.96 D000 C
ANISOU 3234 CA BASP B 17 9252 7997 8572 26 -2041 1817 D000 C
ATOM 3235 C AASP B 17 -19.344 10.946 54.574 0.53 64.84 D000 C
ANISOU 3235 C AASP B 17 8639 7694 8302 273 -1931 1352 D000 C
ATOM 3236 C BASP B 17 -19.269 10.887 54.555 0.47 64.83 D000 C
ANISOU 3236 C BASP B 17 8635 7712 8287 259 -1909 1348 D000 C
ATOM 3237 O AASP B 17 -20.044 9.986 54.914 0.53 61.40 D000 O
ANISOU 3237 O AASP B 17 8090 7540 7700 362 -1880 1224 D000 O
ATOM 3238 O BASP B 17 -19.833 9.830 54.862 0.47 61.03 D000 O
ANISOU 3238 O BASP B 17 8039 7535 7613 323 -1819 1214 D000 O
ATOM 3239 CB AASP B 17 -19.345 12.842 56.243 0.53 69.49 D000 C
ANISOU 3239 CB AASP B 17 9607 7856 8942 147 -2453 2073 D000 C
ATOM 3240 CB BASP B 17 -19.419 12.866 56.081 0.47 69.55 D000 C
ANISOU 3240 CB BASP B 17 9597 7832 8997 179 -2458 2022 D000 C
ATOM 3241 CG AASP B 17 -19.790 13.884 55.231 0.53 73.91 D000 C
ANISOU 3241 CG AASP B 17 10174 7922 9985 364 -2685 1884 D000 C
ATOM 3242 CG BASP B 17 -18.970 13.434 57.412 0.47 75.18 D000 C
ANISOU 3242 CG BASP B 17 10545 8540 9482 -55 -2608 2564 D000 C
ATOM 3243 OD1AASP B 17 -18.921 14.548 54.628 0.53 75.99 D000 O
ANISOU 3243 OD1AASP B 17 10524 7907 10443 215 -2684 1917 D000 O
ATOM 3244 OD1BASP B 17 -18.131 12.797 58.085 0.47 79.60 D000 O
ANISOU 3244 OD1BASP B 17 11119 9485 9642 -299 -2350 2739 D000 O
ATOM 3245 OD2AASP B 17 -21.018 14.061 55.065 0.53 77.98 D000 O
ANISOU 3245 OD2AASP B 17 10600 8333 10696 696 -2890 1687 D000 O
ATOM 3246 OD2BASP B 17 -19.466 14.517 57.793 0.47 85.93 D000 O
ANISOU 3246 OD2BASP B 17 12077 9523 11050 20 -2987 2819 D000 O
ATOM 3247 N GLU B 18 -19.246 11.341 53.300 1.00 61.23 D000 N
ANISOU 3247 N GLU B 18 8124 7018 8122 368 -1899 1100 D000 N
ATOM 3248 CA GLU B 18 -19.945 10.615 52.245 1.00 66.45 D000 C
ANISOU 3248 CA GLU B 18 8573 7825 8848 571 -1745 698 D000 C
ATOM 3249 C GLU B 18 -19.318 9.246 52.025 1.00 57.32 D000 C
ANISOU 3249 C GLU B 18 7323 7023 7430 417 -1423 596 D000 C
ATOM 3250 O GLU B 18 -20.026 8.266 51.766 1.00 58.40 D000 O
ANISOU 3250 O GLU B 18 7300 7385 7505 504 -1312 402 D000 O
ATOM 3251 CB GLU B 18 -19.933 11.414 50.943 1.00 65.01 D000 C
ANISOU 3251 CB GLU B 18 8389 7358 8953 726 -1788 443 D000 C
ATOM 3252 CG GLU B 18 -20.659 12.750 51.023 1.00 73.89 D000 C
ANISOU 3252 CG GLU B 18 9601 8076 10399 963 -2141 454 D000 C
ATOM 3253 CD GLU B 18 -20.597 13.516 49.713 1.00 91.17 D000 C
ANISOU 3253 CD GLU B 18 11813 9983 12843 1150 -2193 125 D000 C
ATOM 3254 OE1 GLU B 18 -21.489 13.305 48.862 1.00 87.76 D000 O
ANISOU 3254 OE1 GLU B 18 11193 9684 12468 1445 -2100 -234 D000 O
ATOM 3255 OE2 GLU B 18 -19.647 14.311 49.527 1.00 77.11 D000 O
ANISOU 3255 OE2 GLU B 18 10231 7873 11194 992 -2323 219 D000 O
ATOM 3256 N ILE B 19 -17.987 9.162 52.114 1.00 57.00 D000 N
ANISOU 3256 N ILE B 19 7365 7026 7267 183 -1290 731 D000 N
ATOM 3257 CA ILE B 19 -17.315 7.876 51.960 1.00 56.99 D000 C
ANISOU 3257 CA ILE B 19 7281 7332 7042 77 -1021 630 D000 C
ATOM 3258 C ILE B 19 -17.696 6.944 53.102 1.00 54.44 D000 C
ANISOU 3258 C ILE B 19 6952 7283 6452 65 -996 694 D000 C
ATOM 3259 O ILE B 19 -17.932 5.747 52.893 1.00 52.28 D000 O
ANISOU 3259 O ILE B 19 6585 7199 6079 99 -873 504 D000 O
ATOM 3260 CB ILE B 19 -15.790 8.075 51.872 1.00 65.54 D000 C
ANISOU 3260 CB ILE B 19 8401 8420 8082 -145 -905 761 D000 C
ATOM 3261 CG1 ILE B 19 -15.414 8.718 50.532 1.00 63.02 D000 C
ANISOU 3261 CG1 ILE B 19 8077 7855 8012 -126 -944 597 D000 C
ATOM 3262 CG2 ILE B 19 -15.054 6.742 52.041 1.00 53.92 D000 C
ANISOU 3262 CG2 ILE B 19 6843 7282 6361 -216 -661 690 D000 C
ATOM 3263 CD1 ILE B 19 -14.301 9.748 50.642 1.00 71.68 D000 C
ANISOU 3263 CD1 ILE B 19 9249 8744 9242 -350 -1039 821 D000 C
ATOM 3264 N AGLU B 20 -17.747 7.473 54.328 0.65 56.94 D000 N
ANISOU 3264 N AGLU B 20 7390 7608 6636 8 -1140 969 D000 N
ATOM 3265 N BGLU B 20 -17.779 7.474 54.322 0.35 57.04 D000 N
ANISOU 3265 N BGLU B 20 7401 7618 6652 13 -1144 966 D000 N
ATOM 3266 CA AGLU B 20 -18.184 6.670 55.465 0.65 60.29 D000 C
ANISOU 3266 CA AGLU B 20 7844 8297 6768 23 -1170 1000 D000 C
ATOM 3267 CA BGLU B 20 -18.165 6.641 55.454 0.35 60.26 D000 C
ANISOU 3267 CA BGLU B 20 7838 8298 6760 21 -1163 995 D000 C
ATOM 3268 C AGLU B 20 -19.596 6.149 55.250 0.65 57.29 D000 C
ANISOU 3268 C AGLU B 20 7340 7918 6509 201 -1304 782 D000 C
ATOM 3269 C BGLU B 20 -19.619 6.190 55.348 0.35 57.30 D000 C
ANISOU 3269 C BGLU B 20 7352 7921 6499 200 -1321 801 D000 C
ATOM 3270 O AGLU B 20 -19.900 4.994 55.574 0.65 52.45 D000 O
ANISOU 3270 O AGLU B 20 6678 7510 5739 205 -1267 633 D000 O
ATOM 3271 O BGLU B 20 -19.968 5.113 55.843 0.35 53.32 D000 O
ANISOU 3271 O BGLU B 20 6817 7629 5815 207 -1313 680 D000 O
ATOM 3272 CB AGLU B 20 -18.129 7.493 56.755 0.65 58.83 D000 C
ANISOU 3272 CB AGLU B 20 7836 8117 6398 -54 -1345 1365 D000 C
ATOM 3273 CB BGLU B 20 -17.937 7.395 56.765 0.35 59.65 D000 C
ANISOU 3273 CB BGLU B 20 7940 8258 6468 -78 -1301 1365 D000 C
ATOM 3274 CG AGLU B 20 -16.889 7.258 57.607 0.65 66.38 D000 C
ANISOU 3274 CG AGLU B 20 8875 9361 6987 -251 -1141 1571 D000 C
ATOM 3275 CG BGLU B 20 -16.468 7.538 57.182 0.35 64.78 D000 C
ANISOU 3275 CG BGLU B 20 8645 9071 6899 -307 -1084 1593 D000 C
ATOM 3276 CD AGLU B 20 -16.800 5.840 58.142 0.65 76.12 D000 C
ANISOU 3276 CD AGLU B 20 10079 10963 7882 -200 -990 1347 D000 C
ATOM 3277 CD BGLU B 20 -15.694 6.230 57.137 0.35 69.28 D000 C
ANISOU 3277 CD BGLU B 20 9113 9973 7238 -322 -791 1366 D000 C
ATOM 3278 OE1AGLU B 20 -17.701 5.425 58.904 0.65 67.31 D000 O
ANISOU 3278 OE1AGLU B 20 9028 9952 6594 -97 -1169 1293 D000 O
ATOM 3279 OE1BGLU B 20 -16.093 5.274 57.835 0.35 71.88 D000 O
ANISOU 3279 OE1BGLU B 20 9470 10542 7299 -231 -791 1224 D000 O
ATOM 3280 OE2AGLU B 20 -15.824 5.137 57.798 0.65 71.85 D000 O
ANISOU 3280 OE2AGLU B 20 9449 10584 7265 -247 -728 1206 D000 O
ATOM 3281 OE2BGLU B 20 -14.679 6.161 56.411 0.35 70.46 D000 O
ANISOU 3281 OE2BGLU B 20 9158 10122 7492 -412 -598 1314 D000 O
ATOM 3282 N ALA B 21 -20.478 6.992 54.713 1.00 51.54 D000 N
ANISOU 3282 N ALA B 21 6543 6959 6082 352 -1475 749 D000 N
ATOM 3283 CA ALA B 21 -21.867 6.579 54.534 1.00 52.79 D000 C
ANISOU 3283 CA ALA B 21 6509 7165 6384 517 -1595 565 D000 C
ATOM 3284 C ALA B 21 -21.972 5.466 53.500 1.00 50.17 D000 C
ANISOU 3284 C ALA B 21 5996 6968 6099 496 -1359 298 D000 C
ATOM 3285 O ALA B 21 -22.796 4.555 53.643 1.00 52.06 D000 O
ANISOU 3285 O ALA B 21 6089 7355 6336 500 -1394 184 D000 O
ATOM 3286 CB ALA B 21 -22.728 7.775 54.132 1.00 63.28 D000 C
ANISOU 3286 CB ALA B 21 7764 8240 8038 734 -1807 558 D000 C
ATOM 3287 N ILE B 22 -21.136 5.515 52.459 1.00 51.99 D000 N
ANISOU 3287 N ILE B 22 6241 7138 6373 450 -1147 219 D000 N
ATOM 3288 CA ILE B 22 -21.074 4.413 51.502 1.00 51.34 D000 C
ANISOU 3288 CA ILE B 22 6041 7184 6282 401 -931 30 D000 C
ATOM 3289 C ILE B 22 -20.666 3.129 52.207 1.00 56.50 D000 C
ANISOU 3289 C ILE B 22 6752 8002 6714 269 -882 28 D000 C
ATOM 3290 O ILE B 22 -21.242 2.060 51.967 1.00 51.22 D000 O
ANISOU 3290 O ILE B 22 5972 7422 6067 234 -856 -90 D000 O
ATOM 3291 CB ILE B 22 -20.113 4.753 50.348 1.00 55.19 D000 C
ANISOU 3291 CB ILE B 22 6579 7581 6810 380 -764 -33 D000 C
ATOM 3292 CG1 ILE B 22 -20.727 5.828 49.445 1.00 56.52 D000 C
ANISOU 3292 CG1 ILE B 22 6677 7599 7199 562 -815 -145 D000 C
ATOM 3293 CG2 ILE B 22 -19.763 3.490 49.545 1.00 57.03 D000 C
ANISOU 3293 CG2 ILE B 22 6760 7951 6957 294 -565 -153 D000 C
ATOM 3294 CD1 ILE B 22 -19.721 6.525 48.556 1.00 59.43 D000 C
ANISOU 3294 CD1 ILE B 22 7161 7809 7609 548 -763 -198 D000 C
ATOM 3295 N GLY B 23 -19.680 3.215 53.101 1.00 51.25 D000 N
ANISOU 3295 N GLY B 23 6257 7381 5836 194 -875 155 D000 N
ATOM 3296 CA GLY B 23 -19.253 2.035 53.831 1.00 51.21 D000 C
ANISOU 3296 CA GLY B 23 6319 7544 5595 131 -834 93 D000 C
ATOM 3297 C GLY B 23 -20.316 1.507 54.775 1.00 49.00 D000 C
ANISOU 3297 C GLY B 23 6029 7344 5244 159 -1048 48 D000 C
ATOM 3298 O GLY B 23 -20.461 0.292 54.938 1.00 51.31 D000 O
ANISOU 3298 O GLY B 23 6319 7701 5476 126 -1065 -111 D000 O
ATOM 3299 N ARG B 24 -21.055 2.409 55.431 1.00 51.58 D000 N
ANISOU 3299 N ARG B 24 6366 7643 5591 222 -1258 186 D000 N
ATOM 3300 CA ARG B 24 -22.128 1.984 56.324 1.00 52.74 D000 C
ANISOU 3300 CA ARG B 24 6484 7870 5684 254 -1522 143 D000 C
ATOM 3301 C ARG B 24 -23.196 1.210 55.565 1.00 56.11 D000 C
ANISOU 3301 C ARG B 24 6664 8272 6384 242 -1560 -37 D000 C
ATOM 3302 O ARG B 24 -23.603 0.118 55.978 1.00 52.95 D000 O
ANISOU 3302 O ARG B 24 6246 7936 5938 174 -1676 -170 D000 O
ATOM 3303 CB ARG B 24 -22.773 3.190 57.014 1.00 67.42 D000 C
ANISOU 3303 CB ARG B 24 8376 9673 7567 351 -1779 348 D000 C
ATOM 3304 CG ARG B 24 -22.040 3.691 58.230 1.00 68.00 D000 C
ANISOU 3304 CG ARG B 24 8714 9845 7277 314 -1840 579 D000 C
ATOM 3305 CD ARG B 24 -22.965 4.401 59.213 1.00 63.12 D000 C
ANISOU 3305 CD ARG B 24 8157 9216 6610 404 -2209 761 D000 C
ATOM 3306 NE ARG B 24 -23.734 5.503 58.636 1.00 56.02 D000 N
ANISOU 3306 NE ARG B 24 7125 8066 6093 539 -2369 847 D000 N
ATOM 3307 CZ ARG B 24 -23.206 6.639 58.197 1.00 64.56 D000 C
ANISOU 3307 CZ ARG B 24 8282 8925 7322 551 -2315 1025 D000 C
ATOM 3308 NH1 ARG B 24 -21.899 6.837 58.193 1.00 54.89 D000 N
ANISOU 3308 NH1 ARG B 24 7222 7710 5923 394 -2085 1166 D000 N
ATOM 3309 NH2 ARG B 24 -24.012 7.601 57.756 1.00 62.92 D000 N
ANISOU 3309 NH2 ARG B 24 7967 8471 7469 733 -2517 1046 D000 N
ATOM 3310 N ILE B 25 -23.701 1.786 54.471 1.00 47.01 D000 N
ANISOU 3310 N ILE B 25 5310 7033 5517 304 -1476 -43 D000 N
ATOM 3311 CA ILE B 25 -24.759 1.112 53.726 1.00 53.93 D000 C
ANISOU 3311 CA ILE B 25 5901 7954 6637 268 -1467 -167 D000 C
ATOM 3312 C ILE B 25 -24.223 -0.181 53.132 1.00 49.20 D000 C
ANISOU 3312 C ILE B 25 5335 7365 5995 105 -1287 -263 D000 C
ATOM 3313 O ILE B 25 -24.916 -1.207 53.111 1.00 50.38 D000 O
ANISOU 3313 O ILE B 25 5352 7542 6247 -19 -1370 -334 D000 O
ATOM 3314 CB ILE B 25 -25.329 2.039 52.640 1.00 55.42 D000 C
ANISOU 3314 CB ILE B 25 5866 8112 7078 408 -1362 -180 D000 C
ATOM 3315 CG1 ILE B 25 -26.214 3.113 53.269 1.00 62.77 D000 C
ANISOU 3315 CG1 ILE B 25 6700 9005 8143 601 -1631 -118 D000 C
ATOM 3316 CG2 ILE B 25 -26.123 1.242 51.613 1.00 57.80 D000 C
ANISOU 3316 CG2 ILE B 25 5866 8535 7562 325 -1214 -279 D000 C
ATOM 3317 CD1 ILE B 25 -26.343 4.357 52.419 1.00 70.30 D000 C
ANISOU 3317 CD1 ILE B 25 7574 9846 9289 816 -1561 -148 D000 C
ATOM 3318 N SER B 26 -22.985 -0.150 52.642 1.00 48.87 D000 N
ANISOU 3318 N SER B 26 5463 7276 5831 95 -1074 -252 D000 N
ATOM 3319 CA ASER B 26 -22.369 -1.349 52.079 0.82 52.73 D000 C
ANISOU 3319 CA ASER B 26 6011 7739 6286 -23 -941 -329 D000 C
ATOM 3320 CA BSER B 26 -22.403 -1.356 52.073 0.18 52.71 D000 C
ANISOU 3320 CA BSER B 26 6003 7737 6288 -24 -943 -329 D000 C
ATOM 3321 C SER B 26 -22.271 -2.454 53.121 1.00 52.06 D000 C
ANISOU 3321 C SER B 26 6059 7652 6071 -85 -1112 -426 D000 C
ATOM 3322 O SER B 26 -22.532 -3.626 52.829 1.00 50.88 D000 O
ANISOU 3322 O SER B 26 5881 7432 6020 -204 -1156 -505 D000 O
ATOM 3323 CB ASER B 26 -20.973 -1.029 51.537 0.82 49.32 D000 C
ANISOU 3323 CB ASER B 26 5727 7270 5740 9 -737 -304 D000 C
ATOM 3324 CB BSER B 26 -21.046 -1.043 51.454 0.18 49.58 D000 C
ANISOU 3324 CB BSER B 26 5745 7302 5790 6 -734 -306 D000 C
ATOM 3325 OG ASER B 26 -21.015 -0.132 50.446 0.82 47.02 D000 O
ANISOU 3325 OG ASER B 26 5347 6954 5564 65 -606 -270 D000 O
ATOM 3326 OG BSER B 26 -20.396 -2.248 51.117 0.18 51.16 D000 O
ANISOU 3326 OG BSER B 26 6027 7462 5949 -70 -669 -378 D000 O
ATOM 3327 N SER B 27 -21.871 -2.094 54.345 1.00 52.61 D000 N
ANISOU 3327 N SER B 27 6294 7793 5902 -7 -1220 -420 D000 N
ATOM 3328 CA ASER B 27 -21.789 -3.073 55.422 0.56 58.27 D000 C
ANISOU 3328 CA ASER B 27 7164 8543 6432 -17 -1398 -571 D000 C
ATOM 3329 CA BSER B 27 -21.788 -3.076 55.419 0.44 58.26 D000 C
ANISOU 3329 CA BSER B 27 7163 8542 6431 -17 -1398 -571 D000 C
ATOM 3330 C SER B 27 -23.144 -3.720 55.676 1.00 57.19 D000 C
ANISOU 3330 C SER B 27 6892 8362 6477 -112 -1679 -651 D000 C
ATOM 3331 O SER B 27 -23.248 -4.945 55.810 1.00 60.07 D000 O
ANISOU 3331 O SER B 27 7312 8628 6884 -199 -1810 -813 D000 O
ATOM 3332 CB ASER B 27 -21.276 -2.403 56.698 0.56 60.82 D000 C
ANISOU 3332 CB ASER B 27 7671 9031 6408 85 -1452 -513 D000 C
ATOM 3333 CB BSER B 27 -21.264 -2.410 56.692 0.44 60.83 D000 C
ANISOU 3333 CB BSER B 27 7673 9032 6409 85 -1449 -514 D000 C
ATOM 3334 OG ASER B 27 -21.067 -3.360 57.718 0.56 72.20 D000 O
ANISOU 3334 OG ASER B 27 9287 10550 7594 120 -1593 -713 D000 O
ATOM 3335 OG BSER B 27 -20.808 -3.378 57.618 0.44 71.88 D000 O
ANISOU 3335 OG BSER B 27 9259 10512 7539 127 -1534 -715 D000 O
ATOM 3336 N GLN B 28 -24.198 -2.904 55.754 1.00 53.64 D000 N
ANISOU 3336 N GLN B 28 6251 7964 6168 -94 -1806 -544 D000 N
ATOM 3337 CA GLN B 28 -25.519 -3.422 56.078 1.00 53.39 D000 C
ANISOU 3337 CA GLN B 28 6026 7929 6330 -190 -2103 -607 D000 C
ATOM 3338 C GLN B 28 -26.011 -4.402 55.026 1.00 58.07 D000 C
ANISOU 3338 C GLN B 28 6412 8421 7233 -391 -2033 -635 D000 C
ATOM 3339 O GLN B 28 -26.573 -5.451 55.359 1.00 59.65 D000 O
ANISOU 3339 O GLN B 28 6579 8537 7549 -550 -2275 -742 D000 O
ATOM 3340 CB GLN B 28 -26.507 -2.265 56.217 1.00 54.06 D000 C
ANISOU 3340 CB GLN B 28 5888 8102 6552 -88 -2231 -479 D000 C
ATOM 3341 CG GLN B 28 -26.268 -1.404 57.446 1.00 61.92 D000 C
ANISOU 3341 CG GLN B 28 7102 9173 7250 66 -2416 -399 D000 C
ATOM 3342 CD GLN B 28 -27.007 -0.078 57.387 1.00 67.68 D000 C
ANISOU 3342 CD GLN B 28 7653 9914 8147 217 -2517 -238 D000 C
ATOM 3343 NE2 GLN B 28 -26.476 0.926 58.079 1.00 65.12 D000 N
ANISOU 3343 NE2 GLN B 28 7561 9593 7589 340 -2568 -73 D000 N
ATOM 3344 OE1 GLN B 28 -28.045 0.039 56.735 1.00 64.22 D000 O
ANISOU 3344 OE1 GLN B 28 6864 9483 8052 228 -2552 -256 D000 O
ATOM 3345 N ALYS B 29 -25.821 -4.074 53.747 0.45 51.27 D000 N
ANISOU 3345 N ALYS B 29 5418 7562 6500 -402 -1723 -528 D000 N
ATOM 3346 N BLYS B 29 -25.822 -4.073 53.748 0.55 51.20 D000 N
ANISOU 3346 N BLYS B 29 5410 7554 6491 -402 -1724 -528 D000 N
ATOM 3347 CA ALYS B 29 -26.320 -4.937 52.681 0.45 57.81 D000 C
ANISOU 3347 CA ALYS B 29 6045 8342 7579 -616 -1625 -485 D000 C
ATOM 3348 CA BLYS B 29 -26.319 -4.938 52.682 0.55 57.81 D000 C
ANISOU 3348 CA BLYS B 29 6044 8342 7578 -616 -1626 -485 D000 C
ATOM 3349 C ALYS B 29 -25.456 -6.184 52.530 0.45 57.72 D000 C
ANISOU 3349 C ALYS B 29 6287 8132 7511 -731 -1621 -553 D000 C
ATOM 3350 C BLYS B 29 -25.456 -6.186 52.536 0.55 57.74 D000 C
ANISOU 3350 C BLYS B 29 6290 8134 7513 -731 -1623 -554 D000 C
ATOM 3351 O ALYS B 29 -25.979 -7.294 52.367 0.45 56.34 D000 O
ANISOU 3351 O ALYS B 29 6049 7824 7535 -959 -1767 -556 D000 O
ATOM 3352 O BLYS B 29 -25.978 -7.298 52.390 0.55 56.30 D000 O
ANISOU 3352 O BLYS B 29 6046 7817 7528 -958 -1773 -559 D000 O
ATOM 3353 CB ALYS B 29 -26.379 -4.151 51.370 0.45 59.49 D000 C
ANISOU 3353 CB ALYS B 29 6065 8671 7868 -559 -1296 -366 D000 C
ATOM 3354 CB BLYS B 29 -26.377 -4.152 51.372 0.55 59.49 D000 C
ANISOU 3354 CB BLYS B 29 6066 8670 7867 -559 -1296 -366 D000 C
ATOM 3355 CG ALYS B 29 -27.403 -3.016 51.398 0.45 60.61 D000 C
ANISOU 3355 CG ALYS B 29 5903 8983 8144 -415 -1323 -338 D000 C
ATOM 3356 CG BLYS B 29 -27.420 -3.032 51.401 0.55 60.61 D000 C
ANISOU 3356 CG BLYS B 29 5898 8983 8146 -418 -1326 -337 D000 C
ATOM 3357 CD ALYS B 29 -27.494 -2.282 50.068 0.45 63.06 D000 C
ANISOU 3357 CD ALYS B 29 6032 9420 8508 -317 -999 -292 D000 C
ATOM 3358 CD BLYS B 29 -27.398 -2.174 50.142 0.55 63.00 D000 C
ANISOU 3358 CD BLYS B 29 6056 9401 8481 -291 -1006 -297 D000 C
ATOM 3359 CE ALYS B 29 -28.369 -3.028 49.076 0.45 66.17 D000 C
ANISOU 3359 CE ALYS B 29 6089 9965 9087 -531 -844 -215 D000 C
ATOM 3360 CE BLYS B 29 -28.173 -2.818 49.004 0.55 66.28 D000 C
ANISOU 3360 CE BLYS B 29 6151 9973 9060 -478 -809 -225 D000 C
ATOM 3361 NZ ALYS B 29 -28.061 -2.645 47.669 0.45 65.05 D000 N
ANISOU 3361 NZ ALYS B 29 5907 9950 8857 -466 -482 -183 D000 N
ATOM 3362 NZ BLYS B 29 -29.593 -3.093 49.362 0.55 69.04 D000 N
ANISOU 3362 NZ BLYS B 29 6090 10465 9676 -592 -980 -205 D000 N
ATOM 3363 N ASN B 30 -24.135 -6.027 52.602 1.00 54.11 D000 N
ANISOU 3363 N ASN B 30 6106 7637 6815 -578 -1482 -604 D000 N
ATOM 3364 CA ASN B 30 -23.244 -7.169 52.421 1.00 56.01 D000 C
ANISOU 3364 CA ASN B 30 6574 7685 7024 -620 -1487 -691 D000 C
ATOM 3365 C ASN B 30 -23.461 -8.219 53.505 1.00 56.19 D000 C
ANISOU 3365 C ASN B 30 6748 7557 7045 -665 -1830 -897 D000 C
ATOM 3366 O ASN B 30 -23.459 -9.423 53.225 1.00 57.46 D000 O
ANISOU 3366 O ASN B 30 6989 7471 7372 -807 -1964 -949 D000 O
ATOM 3367 CB ASN B 30 -21.790 -6.700 52.416 1.00 50.98 D000 C
ANISOU 3367 CB ASN B 30 6137 7094 6139 -416 -1285 -726 D000 C
ATOM 3368 CG ASN B 30 -21.414 -5.942 51.152 1.00 53.48 D000 C
ANISOU 3368 CG ASN B 30 6358 7477 6485 -398 -997 -565 D000 C
ATOM 3369 ND2 ASN B 30 -20.158 -5.516 51.080 1.00 50.07 D000 N
ANISOU 3369 ND2 ASN B 30 6056 7080 5886 -258 -848 -582 D000 N
ATOM 3370 OD1 ASN B 30 -22.236 -5.738 50.255 1.00 50.02 D000 O
ANISOU 3370 OD1 ASN B 30 5716 7084 6207 -506 -912 -441 D000 O
ATOM 3371 N GLN B 31 -23.654 -7.781 54.753 1.00 55.83 D000 N
ANISOU 3371 N GLN B 31 6769 7639 6806 -545 -2007 -1017 D000 N
ATOM 3372 CA GLN B 31 -23.906 -8.725 55.836 1.00 56.36 D000 C
ANISOU 3372 CA GLN B 31 7002 7589 6823 -563 -2369 -1265 D000 C
ATOM 3373 C GLN B 31 -25.069 -9.649 55.503 1.00 63.51 D000 C
ANISOU 3373 C GLN B 31 7731 8286 8112 -858 -2634 -1246 D000 C
ATOM 3374 O GLN B 31 -25.008 -10.858 55.755 1.00 67.39 D000 O
ANISOU 3374 O GLN B 31 8394 8505 8707 -947 -2891 -1430 D000 O
ATOM 3375 CB GLN B 31 -24.190 -7.961 57.130 1.00 63.07 D000 C
ANISOU 3375 CB GLN B 31 7908 8667 7388 -419 -2536 -1334 D000 C
ATOM 3376 CG GLN B 31 -24.326 -8.842 58.360 1.00 83.28 D000 C
ANISOU 3376 CG GLN B 31 10697 11164 9783 -381 -2918 -1645 D000 C
ATOM 3377 CD GLN B 31 -23.754 -8.188 59.602 1.00 98.37 D000 C
ANISOU 3377 CD GLN B 31 12832 13357 11188 -137 -2923 -1736 D000 C
ATOM 3378 NE2 GLN B 31 -22.750 -8.823 60.197 1.00113.30 D000 N
ANISOU 3378 NE2 GLN B 31 15007 15269 12774 41 -2898 -2005 D000 N
ATOM 3379 OE1 GLN B 31 -24.200 -7.114 60.012 1.00 93.25 D000 O
ANISOU 3379 OE1 GLN B 31 12097 12917 10417 -99 -2944 -1555 D000 O
ATOM 3380 N GLN B 32 -26.147 -9.094 54.943 1.00 61.37 D000 N
ANISOU 3380 N GLN B 32 7102 8139 8077 -1014 -2585 -1031 D000 N
ATOM 3381 CA GLN B 32 -27.306 -9.912 54.611 1.00 65.29 D000 C
ANISOU 3381 CA GLN B 32 7348 8498 8960 -1343 -2807 -962 D000 C
ATOM 3382 C GLN B 32 -26.991 -10.911 53.507 1.00 69.31 D000 C
ANISOU 3382 C GLN B 32 7899 8754 9680 -1560 -2691 -837 D000 C
ATOM 3383 O GLN B 32 -27.573 -12.004 53.480 1.00 70.48 D000 O
ANISOU 3383 O GLN B 32 8014 8646 10121 -1851 -2969 -835 D000 O
ATOM 3384 CB GLN B 32 -28.473 -9.027 54.179 1.00 75.69 D000 C
ANISOU 3384 CB GLN B 32 8206 10080 10471 -1421 -2712 -758 D000 C
ATOM 3385 CG GLN B 32 -28.970 -8.084 55.241 1.00 73.10 D000 C
ANISOU 3385 CG GLN B 32 7810 9957 10006 -1228 -2911 -838 D000 C
ATOM 3386 CD GLN B 32 -30.165 -7.287 54.770 1.00 61.84 D000 C
ANISOU 3386 CD GLN B 32 5891 8769 8837 -1266 -2849 -668 D000 C
ATOM 3387 NE2 GLN B 32 -29.927 -6.041 54.385 1.00 76.69 D000 N
ANISOU 3387 NE2 GLN B 32 7710 10829 10598 -1018 -2567 -575 D000 N
ATOM 3388 OE1 GLN B 32 -31.282 -7.796 54.720 1.00 70.58 D000 O
ANISOU 3388 OE1 GLN B 32 6655 9891 10270 -1514 -3055 -629 D000 O
ATOM 3389 N ALA B 33 -26.094 -10.549 52.590 1.00 67.61 D000 N
ANISOU 3389 N ALA B 33 7762 8590 9335 -1442 -2321 -712 D000 N
ATOM 3390 CA ALA B 33 -25.762 -11.374 51.439 1.00 67.89 D000 C
ANISOU 3390 CA ALA B 33 7848 8421 9525 -1627 -2198 -536 D000 C
ATOM 3391 C ALA B 33 -24.565 -12.280 51.687 1.00 72.57 D000 C
ANISOU 3391 C ALA B 33 8849 8695 10030 -1493 -2326 -724 D000 C
ATOM 3392 O ALA B 33 -24.112 -12.958 50.757 1.00 72.20 D000 O
ANISOU 3392 O ALA B 33 8902 8441 10089 -1594 -2258 -575 D000 O
ATOM 3393 CB ALA B 33 -25.488 -10.487 50.222 1.00 65.18 D000 C
ANISOU 3393 CB ALA B 33 7359 8328 9077 -1561 -1761 -308 D000 C
ATOM 3394 N AASN B 34 -24.051 -12.319 52.915 0.46 67.36 D000 N
ANISOU 3394 N AASN B 34 8420 8008 9164 -1248 -2515 -1047 D000 N
ATOM 3395 N BASN B 34 -24.047 -12.311 52.914 0.54 67.34 D000 N
ANISOU 3395 N BASN B 34 8418 8009 9161 -1247 -2513 -1047 D000 N
ATOM 3396 CA AASN B 34 -22.861 -13.106 53.233 0.46 66.95 D000 C
ANISOU 3396 CA AASN B 34 8721 7714 9002 -1035 -2610 -1293 D000 C
ATOM 3397 CA BASN B 34 -22.862 -13.100 53.235 0.54 66.93 D000 C
ANISOU 3397 CA BASN B 34 8718 7714 8999 -1034 -2609 -1293 D000 C
ATOM 3398 C AASN B 34 -21.715 -12.738 52.296 0.46 66.42 D000 C
ANISOU 3398 C AASN B 34 8704 7722 8811 -873 -2259 -1159 D000 C
ATOM 3399 C BASN B 34 -21.717 -12.738 52.295 0.54 66.41 D000 C
ANISOU 3399 C BASN B 34 8703 7721 8810 -874 -2259 -1159 D000 C
ATOM 3400 O AASN B 34 -21.014 -13.601 51.763 0.46 67.82 D000 O
ANISOU 3400 O AASN B 34 9058 7620 9092 -847 -2310 -1167 D000 O
ATOM 3401 O BASN B 34 -21.023 -13.604 51.758 0.54 67.84 D000 O
ANISOU 3401 O BASN B 34 9058 7620 9096 -850 -2311 -1165 D000 O
ATOM 3402 CB AASN B 34 -23.158 -14.605 53.172 0.46 70.34 D000 C
ANISOU 3402 CB AASN B 34 9306 7661 9760 -1247 -2991 -1367 D000 C
ATOM 3403 CB BASN B 34 -23.167 -14.597 53.184 0.54 70.34 D000 C
ANISOU 3403 CB BASN B 34 9303 7663 9758 -1247 -2992 -1368 D000 C
ATOM 3404 CG AASN B 34 -24.066 -15.067 54.297 0.46 73.75 D000 C
ANISOU 3404 CG AASN B 34 9758 7975 10288 -1357 -3424 -1609 D000 C
ATOM 3405 CG BASN B 34 -22.176 -15.421 53.986 0.54 74.53 D000 C
ANISOU 3405 CG BASN B 34 10205 7942 10172 -949 -3220 -1777 D000 C
ATOM 3406 ND2AASN B 34 -24.948 -16.012 53.994 0.46 77.59 D000 N
ANISOU 3406 ND2AASN B 34 10178 8119 11182 -1734 -3733 -1498 D000 N
ATOM 3407 ND2BASN B 34 -21.985 -16.674 53.585 0.54 75.61 D000 N
ANISOU 3407 ND2BASN B 34 10538 7591 10601 -1044 -3481 -1809 D000 N
ATOM 3408 OD1AASN B 34 -23.971 -14.586 55.426 0.46 76.11 D000 O
ANISOU 3408 OD1AASN B 34 10136 8493 10290 -1124 -3499 -1876 D000 O
ATOM 3409 OD1BASN B 34 -21.593 -14.940 54.957 0.54 76.65 D000 O
ANISOU 3409 OD1BASN B 34 10581 8456 10086 -628 -3164 -2056 D000 O
ATOM 3410 N VAL B 35 -21.540 -11.437 52.081 1.00 59.58 D000 N
ANISOU 3410 N VAL B 35 7683 7209 7745 -765 -1942 -1035 D000 N
ATOM 3411 CA VAL B 35 -20.455 -10.891 51.278 1.00 60.27 D000 C
ANISOU 3411 CA VAL B 35 7794 7408 7696 -611 -1633 -932 D000 C
ATOM 3412 C VAL B 35 -19.500 -10.176 52.222 1.00 54.33 D000 C
ANISOU 3412 C VAL B 35 7135 6877 6630 -315 -1530 -1124 D000 C
ATOM 3413 O VAL B 35 -19.929 -9.568 53.206 1.00 54.38 D000 O
ANISOU 3413 O VAL B 35 7109 7068 6485 -267 -1582 -1199 D000 O
ATOM 3414 CB VAL B 35 -21.001 -9.934 50.200 1.00 52.84 D000 C
ANISOU 3414 CB VAL B 35 6606 6677 6792 -739 -1368 -645 D000 C
ATOM 3415 CG1 VAL B 35 -19.892 -9.084 49.616 1.00 52.76 D000 C
ANISOU 3415 CG1 VAL B 35 6625 6825 6598 -552 -1094 -598 D000 C
ATOM 3416 CG2 VAL B 35 -21.735 -10.726 49.115 1.00 61.29 D000 C
ANISOU 3416 CG2 VAL B 35 7583 7591 8113 -1038 -1395 -410 D000 C
ATOM 3417 N THR B 36 -18.203 -10.275 51.945 1.00 52.87 D000 N
ANISOU 3417 N THR B 36 7052 6689 6345 -125 -1395 -1183 D000 N
ATOM 3418 CA THR B 36 -17.196 -9.590 52.742 1.00 48.23 D000 C
ANISOU 3418 CA THR B 36 6497 6361 5465 119 -1242 -1315 D000 C
ATOM 3419 C THR B 36 -16.253 -8.858 51.801 1.00 53.65 D000 C
ANISOU 3419 C THR B 36 7092 7165 6126 170 -975 -1150 D000 C
ATOM 3420 O THR B 36 -16.213 -9.130 50.598 1.00 53.38 D000 O
ANISOU 3420 O THR B 36 7036 6986 6261 78 -947 -1004 D000 O
ATOM 3421 CB THR B 36 -16.397 -10.555 53.625 1.00 55.17 D000 C
ANISOU 3421 CB THR B 36 7563 7170 6229 357 -1375 -1651 D000 C
ATOM 3422 CG2 THR B 36 -17.271 -11.145 54.702 1.00 60.67 D000 C
ANISOU 3422 CG2 THR B 36 8380 7782 6891 332 -1671 -1870 D000 C
ATOM 3423 OG1 THR B 36 -15.848 -11.611 52.823 1.00 57.02 D000 O
ANISOU 3423 OG1 THR B 36 7886 7096 6682 402 -1469 -1694 D000 O
ATOM 3424 N GLY B 37 -15.485 -7.926 52.348 1.00 49.64 D000 N
ANISOU 3424 N GLY B 37 6537 6927 5397 298 -796 -1158 D000 N
ATOM 3425 CA GLY B 37 -14.549 -7.201 51.515 1.00 53.89 D000 C
ANISOU 3425 CA GLY B 37 6976 7562 5937 324 -589 -1021 D000 C
ATOM 3426 C GLY B 37 -14.015 -5.959 52.198 1.00 53.93 D000 C
ANISOU 3426 C GLY B 37 6901 7852 5737 363 -417 -950 D000 C
ATOM 3427 O GLY B 37 -14.233 -5.723 53.388 1.00 50.73 D000 O
ANISOU 3427 O GLY B 37 6539 7606 5132 402 -437 -1004 D000 O
ATOM 3428 N VAL B 38 -13.310 -5.164 51.396 1.00 51.03 D000 N
ANISOU 3428 N VAL B 38 6431 7538 5420 333 -273 -809 D000 N
ATOM 3429 CA AVAL B 38 -12.649 -3.959 51.873 0.77 49.05 D000 C
ANISOU 3429 CA AVAL B 38 6093 7506 5039 318 -123 -689 D000 C
ATOM 3430 CA BVAL B 38 -12.620 -3.967 51.859 0.23 49.36 D000 C
ANISOU 3430 CA BVAL B 38 6131 7546 5079 319 -121 -690 D000 C
ATOM 3431 C VAL B 38 -12.771 -2.885 50.801 1.00 53.16 D000 C
ANISOU 3431 C VAL B 38 6545 7945 5708 196 -86 -511 D000 C
ATOM 3432 O VAL B 38 -12.784 -3.172 49.600 1.00 48.75 D000 O
ANISOU 3432 O VAL B 38 5982 7251 5291 178 -110 -513 D000 O
ATOM 3433 CB AVAL B 38 -11.175 -4.261 52.234 0.77 55.67 D000 C
ANISOU 3433 CB AVAL B 38 6845 8534 5774 453 5 -785 D000 C
ATOM 3434 CB BVAL B 38 -11.128 -4.240 52.143 0.23 55.79 D000 C
ANISOU 3434 CB BVAL B 38 6852 8542 5802 450 8 -779 D000 C
ATOM 3435 CG1AVAL B 38 -10.365 -4.526 50.978 0.77 53.89 D000 C
ANISOU 3435 CG1AVAL B 38 6538 8199 5741 481 8 -787 D000 C
ATOM 3436 CG1BVAL B 38 -10.444 -2.987 52.670 0.23 59.30 D000 C
ANISOU 3436 CG1BVAL B 38 7176 9230 6126 364 172 -596 D000 C
ATOM 3437 CG2AVAL B 38 -10.583 -3.136 53.053 0.77 59.00 D000 C
ANISOU 3437 CG2AVAL B 38 7169 9231 6017 391 166 -629 D000 C
ATOM 3438 CG2BVAL B 38 -10.980 -5.389 53.118 0.23 58.44 D000 C
ANISOU 3438 CG2BVAL B 38 7268 8952 5984 640 -35 -1036 D000 C
ATOM 3439 N LEU B 39 -12.890 -1.638 51.251 1.00 48.06 D000 N
ANISOU 3439 N LEU B 39 5873 7374 5014 119 -49 -359 D000 N
ATOM 3440 CA LEU B 39 -13.024 -0.478 50.380 1.00 44.52 D000 C
ANISOU 3440 CA LEU B 39 5387 6816 4712 33 -53 -233 D000 C
ATOM 3441 C LEU B 39 -11.983 0.543 50.805 1.00 49.73 D000 C
ANISOU 3441 C LEU B 39 5982 7575 5336 -46 21 -84 D000 C
ATOM 3442 O LEU B 39 -11.993 0.998 51.951 1.00 49.28 D000 O
ANISOU 3442 O LEU B 39 5947 7643 5134 -85 42 37 D000 O
ATOM 3443 CB LEU B 39 -14.432 0.115 50.465 1.00 45.46 D000 C
ANISOU 3443 CB LEU B 39 5541 6840 4890 14 -153 -181 D000 C
ATOM 3444 CG LEU B 39 -14.695 1.406 49.688 1.00 53.41 D000 C
ANISOU 3444 CG LEU B 39 6530 7714 6049 -14 -185 -105 D000 C
ATOM 3445 CD1 LEU B 39 -14.428 1.189 48.210 1.00 49.44 D000 C
ANISOU 3445 CD1 LEU B 39 6004 7143 5637 -1 -145 -200 D000 C
ATOM 3446 CD2 LEU B 39 -16.125 1.907 49.919 1.00 60.54 D000 C
ANISOU 3446 CD2 LEU B 39 7428 8551 7024 31 -293 -86 D000 C
ATOM 3447 N LEU B 40 -11.079 0.891 49.898 1.00 49.40 D000 N
ANISOU 3447 N LEU B 40 5860 7491 5419 -91 45 -73 D000 N
ATOM 3448 CA LEU B 40 -10.052 1.883 50.175 1.00 47.44 D000 C
ANISOU 3448 CA LEU B 40 5511 7311 5202 -224 92 92 D000 C
ATOM 3449 C LEU B 40 -10.240 3.065 49.242 1.00 50.67 D000 C
ANISOU 3449 C LEU B 40 5957 7476 5817 -316 -35 148 D000 C
ATOM 3450 O LEU B 40 -10.698 2.912 48.109 1.00 49.93 D000 O
ANISOU 3450 O LEU B 40 5917 7244 5808 -244 -105 8 D000 O
ATOM 3451 CB LEU B 40 -8.651 1.306 49.988 1.00 54.15 D000 C
ANISOU 3451 CB LEU B 40 6184 8333 6056 -204 188 33 D000 C
ATOM 3452 CG LEU B 40 -8.329 0.149 50.923 1.00 66.96 D000 C
ANISOU 3452 CG LEU B 40 7761 10202 7479 -55 310 -84 D000 C
ATOM 3453 CD1 LEU B 40 -8.168 -1.095 50.121 1.00 69.45 D000 C
ANISOU 3453 CD1 LEU B 40 8084 10439 7865 116 252 -301 D000 C
ATOM 3454 CD2 LEU B 40 -7.054 0.447 51.678 1.00 69.91 D000 C
ANISOU 3454 CD2 LEU B 40 7911 10886 7766 -118 485 23 D000 C
ATOM 3455 N CYS B 41 -9.890 4.249 49.718 1.00 47.90 D000 N
ANISOU 3455 N CYS B 41 5594 7073 5535 -477 -72 354 D000 N
ATOM 3456 CA CYS B 41 -9.820 5.390 48.825 1.00 51.88 D000 C
ANISOU 3456 CA CYS B 41 6137 7303 6271 -563 -234 370 D000 C
ATOM 3457 C CYS B 41 -8.520 6.142 49.060 1.00 52.46 D000 C
ANISOU 3457 C CYS B 41 6073 7400 6458 -801 -239 568 D000 C
ATOM 3458 O CYS B 41 -7.962 6.160 50.161 1.00 54.55 D000 O
ANISOU 3458 O CYS B 41 6237 7886 6606 -926 -107 784 D000 O
ATOM 3459 CB CYS B 41 -11.022 6.320 48.976 1.00 55.46 D000 C
ANISOU 3459 CB CYS B 41 6752 7513 6809 -522 -382 417 D000 C
ATOM 3460 SG CYS B 41 -11.133 7.181 50.519 1.00 61.43 D000 S
ANISOU 3460 SG CYS B 41 7567 8264 7511 -670 -420 769 D000 S
ATOM 3461 N LEU B 42 -8.033 6.737 47.984 1.00 51.08 D000 N
ANISOU 3461 N LEU B 42 5884 7025 6498 -871 -394 487 D000 N
ATOM 3462 CA LEU B 42 -6.780 7.478 48.027 1.00 54.40 D000 C
ANISOU 3462 CA LEU B 42 6140 7429 7099 -1139 -452 664 D000 C
ATOM 3463 C LEU B 42 -6.821 8.487 46.898 1.00 55.81 D000 C
ANISOU 3463 C LEU B 42 6438 7227 7540 -1190 -740 542 D000 C
ATOM 3464 O LEU B 42 -6.889 8.095 45.726 1.00 53.82 D000 O
ANISOU 3464 O LEU B 42 6232 6935 7282 -1034 -818 264 D000 O
ATOM 3465 CB LEU B 42 -5.585 6.535 47.881 1.00 53.44 D000 C
ANISOU 3465 CB LEU B 42 5748 7629 6927 -1139 -310 605 D000 C
ATOM 3466 CG LEU B 42 -4.199 7.177 47.974 1.00 61.06 D000 C
ANISOU 3466 CG LEU B 42 6438 8668 8093 -1436 -340 798 D000 C
ATOM 3467 CD1 LEU B 42 -3.981 7.862 49.319 1.00 68.57 D000 C
ANISOU 3467 CD1 LEU B 42 7311 9738 9005 -1693 -210 1181 D000 C
ATOM 3468 CD2 LEU B 42 -3.138 6.118 47.724 1.00 64.91 D000 C
ANISOU 3468 CD2 LEU B 42 6631 9488 8544 -1342 -219 673 D000 C
ATOM 3469 N ASP B 43 -6.798 9.767 47.244 1.00 59.33 D000 N
ANISOU 3469 N ASP B 43 6961 7385 8198 -1398 -916 746 D000 N
ATOM 3470 CA ASP B 43 -6.681 10.855 46.283 1.00 67.45 D000 C
ANISOU 3470 CA ASP B 43 8110 7997 9520 -1474 -1243 622 D000 C
ATOM 3471 C ASP B 43 -7.580 10.633 45.067 1.00 67.24 D000 C
ANISOU 3471 C ASP B 43 8273 7850 9424 -1146 -1335 211 D000 C
ATOM 3472 O ASP B 43 -7.136 10.611 43.921 1.00 63.38 D000 O
ANISOU 3472 O ASP B 43 7790 7310 8980 -1108 -1474 -34 D000 O
ATOM 3473 CB ASP B 43 -5.231 11.033 45.834 1.00 76.09 D000 C
ANISOU 3473 CB ASP B 43 8976 9129 10806 -1740 -1343 665 D000 C
ATOM 3474 CG ASP B 43 -5.010 12.344 45.107 1.00 86.87 D000 C
ANISOU 3474 CG ASP B 43 10477 10008 12523 -1904 -1741 595 D000 C
ATOM 3475 OD1 ASP B 43 -5.618 13.356 45.517 1.00 79.90 D000 O
ANISOU 3475 OD1 ASP B 43 9800 8755 11805 -1963 -1913 723 D000 O
ATOM 3476 OD2 ASP B 43 -4.253 12.360 44.113 1.00 78.51 D000 O
ANISOU 3476 OD2 ASP B 43 9338 8910 11581 -1955 -1923 392 D000 O
ATOM 3477 N GLY B 44 -8.868 10.455 45.346 1.00 58.21 D000 N
ANISOU 3477 N GLY B 44 7268 6702 8148 -911 -1253 150 D000 N
ATOM 3478 CA GLY B 44 -9.863 10.408 44.291 1.00 59.44 D000 C
ANISOU 3478 CA GLY B 44 7575 6770 8240 -610 -1308 -202 D000 C
ATOM 3479 C GLY B 44 -9.983 9.088 43.574 1.00 54.20 D000 C
ANISOU 3479 C GLY B 44 6849 6435 7308 -444 -1110 -389 D000 C
ATOM 3480 O GLY B 44 -10.658 9.027 42.536 1.00 52.83 D000 O
ANISOU 3480 O | 
