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-rwxr-xr-xDocking/Target/6LU7.pdb2535
-rwxr-xr-xDocking/Target/6y84.cif7803
-rwxr-xr-xDocking/Target/6y84.pdb5934
3 files changed, 16272 insertions, 0 deletions
diff --git a/Docking/Target/6LU7.pdb b/Docking/Target/6LU7.pdb
new file mode 100755
index 0000000..52c93b7
--- /dev/null
+++ b/Docking/Target/6LU7.pdb
@@ -0,0 +1,2535 @@
+ATOM 1 N SER A 1 -32.073 9.085 33.695 1.00 38.90 A N
+ATOM 2 CA SER A 1 -32.156 8.073 34.741 1.00 37.44 A C
+ATOM 3 C SER A 1 -30.857 8.000 35.536 1.00 34.96 A C
+ATOM 4 O SER A 1 -30.047 8.926 35.507 1.00 33.29 A O
+ATOM 5 CB SER A 1 -32.483 6.704 34.140 1.00 44.07 A C
+ATOM 6 OG SER A 1 -31.312 6.067 33.660 1.00 47.56 A O
+ATOM 7 N GLY A 2 -30.665 6.892 36.240 1.00 36.02 A N
+ATOM 8 CA GLY A 2 -29.510 6.712 37.092 1.00 34.67 A C
+ATOM 9 C GLY A 2 -29.828 6.998 38.551 1.00 38.34 A C
+ATOM 10 O GLY A 2 -30.810 7.663 38.892 1.00 45.40 A O
+ATOM 11 N PHE A 3 -28.974 6.479 39.430 1.00 38.38 A N
+ATOM 12 CA PHE A 3 -29.155 6.661 40.866 1.00 36.10 A C
+ATOM 13 C PHE A 3 -27.790 6.744 41.527 1.00 44.18 A C
+ATOM 14 O PHE A 3 -26.981 5.820 41.399 1.00 40.82 A O
+ATOM 15 CB PHE A 3 -29.978 5.522 41.468 1.00 38.52 A C
+ATOM 16 CG PHE A 3 -30.635 5.875 42.770 1.00 40.78 A C
+ATOM 17 CD1 PHE A 3 -31.642 6.824 42.816 1.00 43.38 A C
+ATOM 18 CD2 PHE A 3 -30.247 5.261 43.949 1.00 40.00 A C
+ATOM 19 CE1 PHE A 3 -32.251 7.155 44.012 1.00 42.94 A C
+ATOM 20 CE2 PHE A 3 -30.851 5.586 45.148 1.00 40.35 A C
+ATOM 21 CZ PHE A 3 -31.854 6.534 45.179 1.00 43.94 A C
+ATOM 22 N ARG A 4 -27.541 7.844 42.233 1.00 39.42 A N
+ATOM 23 CA ARG A 4 -26.277 8.066 42.915 1.00 38.88 A C
+ATOM 24 C ARG A 4 -26.545 8.642 44.296 1.00 40.55 A C
+ATOM 25 O ARG A 4 -27.552 9.320 44.517 1.00 36.11 A O
+ATOM 26 CB ARG A 4 -25.367 9.020 42.127 1.00 36.87 A C
+ATOM 27 CG ARG A 4 -24.669 8.388 40.936 1.00 42.81 A C
+ATOM 28 CD ARG A 4 -23.342 7.771 41.340 1.00 42.72 A C
+ATOM 29 NE ARG A 4 -22.460 7.579 40.193 1.00 47.79 A N
+ATOM 30 CZ ARG A 4 -21.235 7.068 40.270 1.00 53.27 A C
+ATOM 31 NH1 ARG A 4 -20.744 6.693 41.443 1.00 47.42 A N1+
+ATOM 32 NH2 ARG A 4 -20.502 6.930 39.173 1.00 49.36 A N
+ATOM 33 N LYS A 5 -25.636 8.362 45.227 1.00 34.78 A N
+ATOM 34 CA LYS A 5 -25.667 9.020 46.528 1.00 36.92 A C
+ATOM 35 C LYS A 5 -25.399 10.504 46.317 1.00 32.31 A C
+ATOM 36 O LYS A 5 -24.261 10.908 46.053 1.00 37.11 A O
+ATOM 37 CB LYS A 5 -24.643 8.396 47.471 1.00 39.24 A C
+ATOM 38 CG LYS A 5 -25.062 8.413 48.934 1.00 39.96 A C
+ATOM 39 CD LYS A 5 -24.326 7.353 49.740 1.00 43.24 A C
+ATOM 40 CE LYS A 5 -24.965 5.984 49.571 1.00 48.83 A C
+ATOM 41 NZ LYS A 5 -24.162 4.914 50.226 1.00 58.11 A N1+
+ATOM 42 N MET A 6 -26.446 11.316 46.414 1.00 25.57 A N
+ATOM 43 CA MET A 6 -26.400 12.716 46.023 1.00 36.94 A C
+ATOM 44 C MET A 6 -26.467 13.607 47.255 1.00 30.91 A C
+ATOM 45 O MET A 6 -27.368 13.459 48.088 1.00 28.98 A O
+ATOM 46 CB MET A 6 -27.548 13.047 45.068 1.00 32.35 A C
+ATOM 47 CG MET A 6 -27.370 14.341 44.297 1.00 41.91 A C
+ATOM 48 SD MET A 6 -28.586 14.521 42.977 1.00 50.06 A S
+ATOM 49 CE MET A 6 -28.245 13.061 41.999 1.00 42.04 A C
+ATOM 50 N ALA A 7 -25.516 14.525 47.363 1.00 24.70 A N
+ATOM 51 CA ALA A 7 -25.496 15.526 48.417 1.00 31.84 A C
+ATOM 52 C ALA A 7 -26.118 16.824 47.917 1.00 39.13 A C
+ATOM 53 O ALA A 7 -26.143 17.108 46.717 1.00 30.67 A O
+ATOM 54 CB ALA A 7 -24.065 15.781 48.898 1.00 31.91 A C
+ATOM 55 N PHE A 8 -26.629 17.612 48.859 1.00 35.53 A N
+ATOM 56 CA PHE A 8 -27.182 18.909 48.513 1.00 34.19 A C
+ATOM 57 C PHE A 8 -26.060 19.874 48.132 1.00 35.86 A C
+ATOM 58 O PHE A 8 -24.929 19.740 48.607 1.00 37.71 A O
+ATOM 59 CB PHE A 8 -27.983 19.479 49.680 1.00 31.88 A C
+ATOM 60 CG PHE A 8 -29.339 18.855 49.850 1.00 34.04 A C
+ATOM 61 CD1 PHE A 8 -30.396 19.234 49.041 1.00 37.68 A C
+ATOM 62 CD2 PHE A 8 -29.557 17.893 50.822 1.00 32.78 A C
+ATOM 63 CE1 PHE A 8 -31.646 18.663 49.196 1.00 38.75 A C
+ATOM 64 CE2 PHE A 8 -30.804 17.319 50.982 1.00 35.47 A C
+ATOM 65 CZ PHE A 8 -31.849 17.705 50.168 1.00 40.42 A C
+ATOM 66 N PRO A 9 -26.342 20.843 47.261 1.00 35.98 A N
+ATOM 67 CA PRO A 9 -25.340 21.872 46.956 1.00 37.27 A C
+ATOM 68 C PRO A 9 -24.923 22.612 48.219 1.00 33.84 A C
+ATOM 69 O PRO A 9 -25.761 23.012 49.030 1.00 38.14 A O
+ATOM 70 CB PRO A 9 -26.066 22.790 45.966 1.00 38.03 A C
+ATOM 71 CG PRO A 9 -27.105 21.918 45.343 1.00 42.20 A C
+ATOM 72 CD PRO A 9 -27.551 20.986 46.433 1.00 40.32 A C
+ATOM 73 N SER A 10 -23.613 22.787 48.383 1.00 35.35 A N
+ATOM 74 CA SER A 10 -23.037 23.278 49.626 1.00 38.41 A C
+ATOM 75 C SER A 10 -22.730 24.770 49.600 1.00 37.76 A C
+ATOM 76 O SER A 10 -22.106 25.275 50.538 1.00 34.95 A O
+ATOM 77 CB SER A 10 -21.762 22.498 49.953 1.00 33.59 A C
+ATOM 78 OG SER A 10 -20.780 22.691 48.950 1.00 36.17 A O
+ATOM 79 N GLY A 11 -23.156 25.485 48.556 1.00 41.13 A N
+ATOM 80 CA GLY A 11 -22.802 26.892 48.440 1.00 38.60 A C
+ATOM 81 C GLY A 11 -23.316 27.735 49.592 1.00 38.39 A C
+ATOM 82 O GLY A 11 -22.598 28.590 50.117 1.00 46.36 A O
+ATOM 83 N LYS A 12 -24.564 27.505 50.005 1.00 38.09 A N
+ATOM 84 CA LYS A 12 -25.146 28.293 51.086 1.00 36.59 A C
+ATOM 85 C LYS A 12 -24.552 27.946 52.445 1.00 39.48 A C
+ATOM 86 O LYS A 12 -24.652 28.754 53.375 1.00 40.17 A O
+ATOM 87 CB LYS A 12 -26.663 28.106 51.107 1.00 42.83 A C
+ATOM 88 CG LYS A 12 -27.354 28.626 49.856 1.00 42.78 A C
+ATOM 89 CD LYS A 12 -28.638 27.867 49.562 1.00 57.42 A C
+ATOM 90 CE LYS A 12 -29.857 28.610 50.085 1.00 57.45 A C
+ATOM 91 NZ LYS A 12 -30.058 28.392 51.544 1.00 55.48 A N1+
+ATOM 92 N VAL A 13 -23.940 26.773 52.582 1.00 38.78 A N
+ATOM 93 CA VAL A 13 -23.264 26.421 53.825 1.00 36.52 A C
+ATOM 94 C VAL A 13 -21.793 26.832 53.796 1.00 35.77 A C
+ATOM 95 O VAL A 13 -21.223 27.157 54.843 1.00 39.87 A O
+ATOM 96 CB VAL A 13 -23.418 24.915 54.103 1.00 33.81 A C
+ATOM 97 CG1 VAL A 13 -22.767 24.538 55.426 1.00 35.72 A C
+ATOM 98 CG2 VAL A 13 -24.889 24.527 54.104 1.00 33.49 A C
+ATOM 99 N GLU A 14 -21.172 26.840 52.613 1.00 31.88 A N
+ATOM 100 CA GLU A 14 -19.769 27.233 52.505 1.00 38.31 A C
+ATOM 101 C GLU A 14 -19.544 28.649 53.024 1.00 39.80 A C
+ATOM 102 O GLU A 14 -18.514 28.932 53.648 1.00 36.53 A O
+ATOM 103 CB GLU A 14 -19.305 27.122 51.052 1.00 41.13 A C
+ATOM 104 CG GLU A 14 -18.957 25.712 50.607 1.00 41.37 A C
+ATOM 105 CD GLU A 14 -18.897 25.579 49.098 1.00 41.45 A C
+ATOM 106 OE1 GLU A 14 -19.869 25.067 48.504 1.00 37.79 A O
+ATOM 107 OE2 GLU A 14 -17.877 25.989 48.505 1.00 40.99 A O1-
+ATOM 108 N GLY A 15 -20.495 29.549 52.781 1.00 34.24 A N
+ATOM 109 CA GLY A 15 -20.362 30.928 53.211 1.00 40.10 A C
+ATOM 110 C GLY A 15 -20.501 31.162 54.700 1.00 43.58 A C
+ATOM 111 O GLY A 15 -20.387 32.309 55.140 1.00 42.28 A O
+ATOM 112 N CYS A 16 -20.739 30.114 55.488 1.00 36.43 A N
+ATOM 113 CA CYS A 16 -20.917 30.244 56.927 1.00 35.87 A C
+ATOM 114 C CYS A 16 -19.815 29.573 57.732 1.00 33.79 A C
+ATOM 115 O CYS A 16 -19.841 29.644 58.965 1.00 36.56 A O
+ATOM 116 CB CYS A 16 -22.275 29.667 57.345 1.00 36.64 A C
+ATOM 117 SG CYS A 16 -23.654 30.190 56.312 1.00 50.68 A S
+ATOM 118 N MET A 17 -18.852 28.928 57.079 1.00 30.44 A N
+ATOM 119 CA MET A 17 -17.799 28.220 57.794 1.00 32.33 A C
+ATOM 120 C MET A 17 -16.675 29.177 58.171 1.00 39.30 A C
+ATOM 121 O MET A 17 -16.188 29.942 57.332 1.00 39.57 A O
+ATOM 122 CB MET A 17 -17.256 27.071 56.946 1.00 35.47 A C
+ATOM 123 CG MET A 17 -18.289 26.004 56.621 1.00 34.34 A C
+ATOM 124 SD MET A 17 -19.267 25.517 58.058 1.00 44.04 A S
+ATOM 125 CE MET A 17 -17.998 24.861 59.141 1.00 32.95 A C
+ATOM 126 N VAL A 18 -16.269 29.134 59.440 1.00 30.96 A N
+ATOM 127 CA VAL A 18 -15.179 29.950 59.953 1.00 35.69 A C
+ATOM 128 C VAL A 18 -14.221 29.049 60.721 1.00 36.49 A C
+ATOM 129 O VAL A 18 -14.511 27.885 60.999 1.00 32.93 A O
+ATOM 130 CB VAL A 18 -15.676 31.100 60.854 1.00 33.25 A C
+ATOM 131 CG1 VAL A 18 -16.514 32.083 60.052 1.00 34.40 A C
+ATOM 132 CG2 VAL A 18 -16.465 30.548 62.031 1.00 32.86 A C
+ATOM 133 N GLN A 19 -13.064 29.608 61.058 1.00 35.39 A N
+ATOM 134 CA GLN A 19 -12.057 28.923 61.855 1.00 36.84 A C
+ATOM 135 C GLN A 19 -12.040 29.523 63.253 1.00 40.23 A C
+ATOM 136 O GLN A 19 -11.925 30.743 63.408 1.00 37.54 A O
+ATOM 137 CB GLN A 19 -10.673 29.035 61.211 1.00 40.75 A C
+ATOM 138 CG GLN A 19 -9.561 28.393 62.024 1.00 44.72 A C
+ATOM 139 CD GLN A 19 -8.189 28.636 61.429 1.00 52.55 A C
+ATOM 140 NE2 GLN A 19 -7.693 29.860 61.566 1.00 57.38 A N
+ATOM 141 OE1 GLN A 19 -7.581 27.734 60.852 1.00 53.65 A O
+ATOM 142 N VAL A 20 -12.162 28.667 64.263 1.00 37.22 A N
+ATOM 143 CA VAL A 20 -12.179 29.083 65.661 1.00 37.75 A C
+ATOM 144 C VAL A 20 -10.928 28.533 66.329 1.00 39.41 A C
+ATOM 145 O VAL A 20 -10.678 27.322 66.294 1.00 40.62 A O
+ATOM 146 CB VAL A 20 -13.447 28.601 66.381 1.00 35.93 A C
+ATOM 147 CG1 VAL A 20 -13.469 29.112 67.814 1.00 35.66 A C
+ATOM 148 CG2 VAL A 20 -14.688 29.051 65.627 1.00 29.32 A C
+ATOM 149 N THR A 21 -10.144 29.419 66.937 1.00 42.33 A N
+ATOM 150 CA THR A 21 -8.913 29.045 67.619 1.00 39.43 A C
+ATOM 151 C THR A 21 -8.969 29.519 69.064 1.00 42.16 A C
+ATOM 152 O THR A 21 -9.258 30.691 69.327 1.00 39.79 A O
+ATOM 153 CB THR A 21 -7.684 29.636 66.921 1.00 43.87 A C
+ATOM 154 CG2 THR A 21 -6.406 29.187 67.616 1.00 46.67 A C
+ATOM 155 OG1 THR A 21 -7.653 29.201 65.555 1.00 49.18 A O
+ATOM 156 N CYS A 22 -8.699 28.605 69.992 1.00 46.16 A N
+ATOM 157 CA CYS A 22 -8.591 28.916 71.416 1.00 42.65 A C
+ATOM 158 C CYS A 22 -7.289 28.291 71.905 1.00 47.48 A C
+ATOM 159 O CYS A 22 -7.209 27.073 72.087 1.00 47.27 A O
+ATOM 160 CB CYS A 22 -9.794 28.394 72.196 1.00 35.21 A C
+ATOM 161 SG CYS A 22 -9.850 28.921 73.924 1.00 57.47 A S
+ATOM 162 N GLY A 23 -6.271 29.123 72.106 1.00 43.57 A N
+ATOM 163 CA GLY A 23 -4.951 28.628 72.441 1.00 48.54 A C
+ATOM 164 C GLY A 23 -4.291 27.961 71.253 1.00 48.65 A C
+ATOM 165 O GLY A 23 -4.089 28.592 70.211 1.00 58.32 A O
+ATOM 166 N THR A 24 -3.956 26.681 71.392 1.00 46.27 A N
+ATOM 167 CA THR A 24 -3.402 25.902 70.294 1.00 54.16 A C
+ATOM 168 C THR A 24 -4.429 24.989 69.640 1.00 51.12 A C
+ATOM 169 O THR A 24 -4.066 24.193 68.768 1.00 57.86 A O
+ATOM 170 CB THR A 24 -2.213 25.067 70.778 1.00 52.71 A C
+ATOM 171 CG2 THR A 24 -1.016 25.962 71.073 1.00 54.72 A C
+ATOM 172 OG1 THR A 24 -2.574 24.354 71.966 1.00 57.38 A O
+ATOM 173 N THR A 25 -5.695 25.080 70.036 1.00 50.73 A N
+ATOM 174 CA THR A 25 -6.750 24.247 69.473 1.00 48.80 A C
+ATOM 175 C THR A 25 -7.468 25.013 68.371 1.00 45.57 A C
+ATOM 176 O THR A 25 -7.907 26.147 68.585 1.00 42.11 A O
+ATOM 177 CB THR A 25 -7.747 23.818 70.551 1.00 45.82 A C
+ATOM 178 CG2 THR A 25 -8.709 22.779 70.002 1.00 44.98 A C
+ATOM 179 OG1 THR A 25 -7.040 23.274 71.673 1.00 52.62 A O
+ATOM 180 N THR A 26 -7.589 24.392 67.200 1.00 46.56 A N
+ATOM 181 CA THR A 26 -8.224 25.031 66.060 1.00 43.98 A C
+ATOM 182 C THR A 26 -9.218 24.075 65.426 1.00 39.56 A C
+ATOM 183 O THR A 26 -8.883 22.919 65.137 1.00 42.53 A O
+ATOM 184 CB THR A 26 -7.184 25.490 65.034 1.00 45.90 A C
+ATOM 185 CG2 THR A 26 -6.155 24.392 64.757 1.00 47.20 A C
+ATOM 186 OG1 THR A 26 -7.836 25.859 63.814 1.00 50.51 A O
+ATOM 187 N LEU A 27 -10.433 24.568 65.192 1.00 36.95 A N
+ATOM 188 CA LEU A 27 -11.471 23.771 64.549 1.00 37.04 A C
+ATOM 189 C LEU A 27 -12.390 24.710 63.786 1.00 38.51 A C
+ATOM 190 O LEU A 27 -12.154 25.920 63.720 1.00 29.66 A O
+ATOM 191 CB LEU A 27 -12.225 22.902 65.570 1.00 37.70 A C
+ATOM 192 CG LEU A 27 -12.639 23.447 66.937 1.00 36.32 A C
+ATOM 193 CD1 LEU A 27 -13.847 24.364 66.831 1.00 32.79 A C
+ATOM 194 CD2 LEU A 27 -12.936 22.285 67.873 1.00 31.17 A C
+ATOM 195 N ASN A 28 -13.448 24.141 63.222 1.00 30.29 A N
+ATOM 196 CA ASN A 28 -14.372 24.876 62.380 1.00 32.66 A C
+ATOM 197 C ASN A 28 -15.551 25.393 63.193 1.00 27.62 A C
+ATOM 198 O ASN A 28 -15.959 24.793 64.189 1.00 31.18 A O
+ATOM 199 CB ASN A 28 -14.877 23.989 61.240 1.00 30.89 A C
+ATOM 200 CG ASN A 28 -13.749 23.365 60.446 1.00 32.19 A C
+ATOM 201 ND2 ASN A 28 -13.426 22.114 60.755 1.00 35.87 A N
+ATOM 202 OD1 ASN A 28 -13.172 24.000 59.565 1.00 33.71 A O
+ATOM 203 N GLY A 29 -16.098 26.525 62.749 1.00 28.97 A N
+ATOM 204 CA GLY A 29 -17.267 27.095 63.375 1.00 29.43 A C
+ATOM 205 C GLY A 29 -18.309 27.457 62.335 1.00 29.30 A C
+ATOM 206 O GLY A 29 -18.006 27.655 61.159 1.00 30.37 A O
+ATOM 207 N LEU A 30 -19.555 27.536 62.795 1.00 30.94 A N
+ATOM 208 CA LEU A 30 -20.692 27.883 61.949 1.00 31.77 A C
+ATOM 209 C LEU A 30 -21.108 29.312 62.273 1.00 31.91 A C
+ATOM 210 O LEU A 30 -21.612 29.586 63.367 1.00 32.56 A O
+ATOM 211 CB LEU A 30 -21.848 26.907 62.161 1.00 31.92 A C
+ATOM 212 CG LEU A 30 -22.986 26.989 61.143 1.00 31.71 A C
+ATOM 213 CD1 LEU A 30 -22.489 26.629 59.750 1.00 32.72 A C
+ATOM 214 CD2 LEU A 30 -24.140 26.089 61.552 1.00 30.45 A C
+ATOM 215 N TRP A 31 -20.902 30.218 61.319 1.00 33.46 A N
+ATOM 216 CA TRP A 31 -21.166 31.644 61.503 1.00 31.27 A C
+ATOM 217 C TRP A 31 -22.534 31.965 60.907 1.00 34.76 A C
+ATOM 218 O TRP A 31 -22.679 32.092 59.688 1.00 31.78 A O
+ATOM 219 CB TRP A 31 -20.062 32.478 60.860 1.00 34.28 A C
+ATOM 220 CG TRP A 31 -20.199 33.957 61.074 1.00 38.48 A C
+ATOM 221 CD1 TRP A 31 -20.963 34.587 62.015 1.00 35.41 A C
+ATOM 222 CD2 TRP A 31 -19.548 34.993 60.329 1.00 37.93 A C
+ATOM 223 CE2 TRP A 31 -19.965 36.225 60.871 1.00 41.14 A C
+ATOM 224 CE3 TRP A 31 -18.654 34.998 59.254 1.00 40.41 A C
+ATOM 225 NE1 TRP A 31 -20.829 35.949 61.899 1.00 38.91 A N
+ATOM 226 CZ2 TRP A 31 -19.519 37.448 60.376 1.00 40.49 A C
+ATOM 227 CZ3 TRP A 31 -18.212 36.214 58.763 1.00 47.09 A C
+ATOM 228 CH2 TRP A 31 -18.645 37.421 59.324 1.00 42.02 A C
+ATOM 229 N LEU A 32 -23.535 32.098 61.773 1.00 29.78 A N
+ATOM 230 CA LEU A 32 -24.892 32.456 61.377 1.00 31.50 A C
+ATOM 231 C LEU A 32 -25.290 33.722 62.120 1.00 39.34 A C
+ATOM 232 O LEU A 32 -25.246 33.758 63.355 1.00 36.42 A O
+ATOM 233 CB LEU A 32 -25.874 31.323 61.679 1.00 38.19 A C
+ATOM 234 CG LEU A 32 -25.647 30.004 60.938 1.00 34.57 A C
+ATOM 235 CD1 LEU A 32 -26.558 28.924 61.493 1.00 33.34 A C
+ATOM 236 CD2 LEU A 32 -25.868 30.181 59.445 1.00 32.67 A C
+ATOM 237 N ASP A 33 -25.681 34.750 61.369 1.00 39.86 A N
+ATOM 238 CA ASP A 33 -26.000 36.076 61.916 1.00 40.96 A C
+ATOM 239 C ASP A 33 -24.764 36.546 62.682 1.00 39.17 A C
+ATOM 240 O ASP A 33 -23.659 36.526 62.117 1.00 41.90 A O
+ATOM 241 CB ASP A 33 -27.293 36.008 62.721 1.00 41.67 A C
+ATOM 242 CG ASP A 33 -28.466 35.509 61.898 1.00 50.38 A C
+ATOM 243 OD1 ASP A 33 -28.621 35.962 60.745 1.00 52.37 A O
+ATOM 244 OD2 ASP A 33 -29.231 34.661 62.404 1.00 53.30 A O1-
+ATOM 245 N ASP A 34 -24.885 36.953 63.945 1.00 36.41 A N
+ATOM 246 CA ASP A 34 -23.749 37.410 64.736 1.00 40.57 A C
+ATOM 247 C ASP A 34 -23.337 36.386 65.790 1.00 40.01 A C
+ATOM 248 O ASP A 34 -22.807 36.750 66.843 1.00 37.93 A O
+ATOM 249 CB ASP A 34 -24.063 38.754 65.393 1.00 42.76 A C
+ATOM 250 CG ASP A 34 -25.304 38.701 66.263 1.00 51.09 A C
+ATOM 251 OD1 ASP A 34 -26.354 38.231 65.777 1.00 57.36 A O
+ATOM 252 OD2 ASP A 34 -25.229 39.131 67.434 1.00 52.82 A O1-
+ATOM 253 N VAL A 35 -23.574 35.103 65.523 1.00 35.15 A N
+ATOM 254 CA VAL A 35 -23.243 34.028 66.449 1.00 34.04 A C
+ATOM 255 C VAL A 35 -22.415 32.985 65.712 1.00 35.49 A C
+ATOM 256 O VAL A 35 -22.720 32.631 64.568 1.00 32.04 A O
+ATOM 257 CB VAL A 35 -24.510 33.385 67.055 1.00 33.33 A C
+ATOM 258 CG1 VAL A 35 -24.134 32.278 68.031 1.00 31.88 A C
+ATOM 259 CG2 VAL A 35 -25.366 34.437 67.745 1.00 32.07 A C
+ATOM 260 N VAL A 36 -21.366 32.496 66.369 1.00 31.67 A N
+ATOM 261 CA VAL A 36 -20.511 31.442 65.835 1.00 34.48 A C
+ATOM 262 C VAL A 36 -20.680 30.210 66.712 1.00 34.24 A C
+ATOM 263 O VAL A 36 -20.465 30.269 67.929 1.00 34.29 A O
+ATOM 264 CB VAL A 36 -19.039 31.878 65.775 1.00 31.91 A C
+ATOM 265 CG1 VAL A 36 -18.153 30.695 65.414 1.00 30.09 A C
+ATOM 266 CG2 VAL A 36 -18.862 33.006 64.773 1.00 31.39 A C
+ATOM 267 N TYR A 37 -21.067 29.096 66.097 1.00 30.91 A N
+ATOM 268 CA TYR A 37 -21.262 27.834 66.796 1.00 25.81 A C
+ATOM 269 C TYR A 37 -20.089 26.911 66.499 1.00 33.31 A C
+ATOM 270 O TYR A 37 -19.680 26.776 65.342 1.00 33.64 A O
+ATOM 271 CB TYR A 37 -22.573 27.166 66.374 1.00 31.93 A C
+ATOM 272 CG TYR A 37 -23.799 28.049 66.479 1.00 28.04 A C
+ATOM 273 CD1 TYR A 37 -24.106 28.970 65.485 1.00 30.82 A C
+ATOM 274 CD2 TYR A 37 -24.657 27.951 67.567 1.00 29.93 A C
+ATOM 275 CE1 TYR A 37 -25.225 29.775 65.576 1.00 24.79 A C
+ATOM 276 CE2 TYR A 37 -25.780 28.750 67.665 1.00 28.93 A C
+ATOM 277 CZ TYR A 37 -26.059 29.660 66.667 1.00 30.20 A C
+ATOM 278 OH TYR A 37 -27.174 30.458 66.762 1.00 32.62 A O
+ATOM 279 N CYS A 38 -19.555 26.277 67.537 1.00 28.03 A N
+ATOM 280 CA CYS A 38 -18.419 25.382 67.383 1.00 29.55 A C
+ATOM 281 C CYS A 38 -18.436 24.379 68.527 1.00 30.64 A C
+ATOM 282 O CYS A 38 -19.055 24.631 69.566 1.00 29.00 A O
+ATOM 283 CB CYS A 38 -17.094 26.158 67.362 1.00 33.99 A C
+ATOM 284 SG CYS A 38 -16.612 26.882 68.946 1.00 39.36 A S
+ATOM 285 N PRO A 39 -17.786 23.226 68.357 1.00 28.03 A N
+ATOM 286 CA PRO A 39 -17.701 22.266 69.465 1.00 30.12 A C
+ATOM 287 C PRO A 39 -16.998 22.878 70.667 1.00 30.67 A C
+ATOM 288 O PRO A 39 -16.035 23.635 70.530 1.00 33.30 A O
+ATOM 289 CB PRO A 39 -16.894 21.107 68.869 1.00 27.83 A C
+ATOM 290 CG PRO A 39 -17.094 21.224 67.394 1.00 32.19 A C
+ATOM 291 CD PRO A 39 -17.189 22.695 67.120 1.00 32.72 A C
+ATOM 292 N ARG A 40 -17.494 22.542 71.859 1.00 30.74 A N
+ATOM 293 CA ARG A 40 -16.988 23.157 73.078 1.00 37.68 A C
+ATOM 294 C ARG A 40 -15.606 22.656 73.474 1.00 35.98 A C
+ATOM 295 O ARG A 40 -14.947 23.300 74.296 1.00 38.97 A O
+ATOM 296 CB ARG A 40 -17.967 22.928 74.233 1.00 36.25 A C
+ATOM 297 CG ARG A 40 -18.007 21.502 74.755 1.00 35.21 A C
+ATOM 298 CD ARG A 40 -18.840 21.416 76.025 1.00 38.69 A C
+ATOM 299 NE ARG A 40 -19.094 20.034 76.424 1.00 38.85 A N
+ATOM 300 CZ ARG A 40 -19.794 19.685 77.498 1.00 36.84 A C
+ATOM 301 NH1 ARG A 40 -20.308 20.617 78.289 1.00 37.14 A N1+
+ATOM 302 NH2 ARG A 40 -19.975 18.403 77.785 1.00 35.64 A N
+ATOM 303 N HIS A 41 -15.145 21.538 72.916 1.00 35.84 A N
+ATOM 304 CA HIS A 41 -13.820 21.037 73.265 1.00 38.89 A C
+ATOM 305 C HIS A 41 -12.697 21.814 72.589 1.00 37.13 A C
+ATOM 306 O HIS A 41 -11.539 21.391 72.668 1.00 39.19 A O
+ATOM 307 CB HIS A 41 -13.705 19.545 72.937 1.00 42.38 A C
+ATOM 308 CG HIS A 41 -13.826 19.231 71.479 1.00 37.90 A C
+ATOM 309 CD2 HIS A 41 -12.964 19.414 70.451 1.00 37.33 A C
+ATOM 310 ND1 HIS A 41 -14.947 18.638 70.939 1.00 36.57 A N
+ATOM 311 CE1 HIS A 41 -14.774 18.477 69.640 1.00 41.55 A C
+ATOM 312 NE2 HIS A 41 -13.579 18.940 69.318 1.00 41.88 A N
+ATOM 313 N VAL A 42 -13.011 22.932 71.930 1.00 35.20 A N
+ATOM 314 CA VAL A 42 -11.972 23.826 71.436 1.00 39.75 A C
+ATOM 315 C VAL A 42 -11.252 24.518 72.587 1.00 40.51 A C
+ATOM 316 O VAL A 42 -10.132 25.010 72.411 1.00 45.18 A O
+ATOM 317 CB VAL A 42 -12.576 24.854 70.458 1.00 34.88 A C
+ATOM 318 CG1 VAL A 42 -13.447 25.854 71.200 1.00 28.67 A C
+ATOM 319 CG2 VAL A 42 -11.482 25.565 69.669 1.00 37.02 A C
+ATOM 320 N ILE A 43 -11.866 24.557 73.776 1.00 39.40 A N
+ATOM 321 CA ILE A 43 -11.235 25.160 74.945 1.00 45.41 A C
+ATOM 322 C ILE A 43 -10.322 24.190 75.681 1.00 44.13 A C
+ATOM 323 O ILE A 43 -9.723 24.569 76.697 1.00 53.91 A O
+ATOM 324 CB ILE A 43 -12.293 25.705 75.927 1.00 38.96 A C
+ATOM 325 CG1 ILE A 43 -13.044 24.551 76.594 1.00 39.31 A C
+ATOM 326 CG2 ILE A 43 -13.257 26.636 75.211 1.00 39.80 A C
+ATOM 327 CD1 ILE A 43 -14.181 24.995 77.490 1.00 37.22 A C
+ATOM 328 N CYS A 44 -10.196 22.955 75.208 1.00 49.20 A N
+ATOM 329 CA CYS A 44 -9.356 21.954 75.847 1.00 50.36 A C
+ATOM 330 C CYS A 44 -8.022 21.818 75.124 1.00 56.74 A C
+ATOM 331 O CYS A 44 -7.859 22.241 73.976 1.00 54.23 A O
+ATOM 332 CB CYS A 44 -10.057 20.592 75.883 1.00 52.03 A C
+ATOM 333 SG CYS A 44 -11.790 20.639 76.366 1.00 57.89 A S
+ATOM 334 N THR A 45 -7.064 21.219 75.820 1.00 61.24 A N
+ATOM 335 CA THR A 45 -5.783 20.824 75.253 1.00 65.40 A C
+ATOM 336 C THR A 45 -5.623 19.313 75.424 1.00 65.43 A C
+ATOM 337 O THR A 45 -6.547 18.617 75.855 1.00 65.90 A O
+ATOM 338 CB THR A 45 -4.635 21.607 75.896 1.00 69.65 A C
+ATOM 339 CG2 THR A 45 -4.399 21.145 77.328 1.00 66.61 A C
+ATOM 340 OG1 THR A 45 -3.438 21.416 75.131 1.00 75.39 A O
+ATOM 341 N SER A 46 -4.437 18.804 75.082 1.00 68.52 A N
+ATOM 342 CA SER A 46 -4.225 17.360 75.096 1.00 68.51 A C
+ATOM 343 C SER A 46 -4.359 16.773 76.496 1.00 69.36 A C
+ATOM 344 O SER A 46 -4.830 15.640 76.649 1.00 71.42 A O
+ATOM 345 CB SER A 46 -2.855 17.028 74.504 1.00 67.95 A C
+ATOM 346 OG SER A 46 -2.750 17.507 73.174 1.00 67.72 A O
+ATOM 347 N GLU A 47 -3.965 17.521 77.527 1.00 70.96 A N
+ATOM 348 CA GLU A 47 -4.049 17.023 78.895 1.00 70.54 A C
+ATOM 349 C GLU A 47 -5.452 17.117 79.482 1.00 69.09 A C
+ATOM 350 O GLU A 47 -5.693 16.560 80.559 1.00 69.43 A O
+ATOM 351 CB GLU A 47 -3.065 17.782 79.791 1.00 71.46 A C
+ATOM 352 CG GLU A 47 -2.573 16.982 80.987 1.00 79.64 A C
+ATOM 353 CD GLU A 47 -1.180 17.384 81.429 1.00 85.00 A C
+ATOM 354 OE1 GLU A 47 -1.058 18.045 82.481 1.00 85.44 A O
+ATOM 355 OE2 GLU A 47 -0.209 17.036 80.725 1.00 82.68 A O1-
+ATOM 356 N ASP A 48 -6.379 17.796 78.807 1.00 67.45 A N
+ATOM 357 CA ASP A 48 -7.738 17.946 79.309 1.00 66.01 A C
+ATOM 358 C ASP A 48 -8.702 16.904 78.758 1.00 61.87 A C
+ATOM 359 O ASP A 48 -9.706 16.606 79.414 1.00 57.55 A O
+ATOM 360 CB ASP A 48 -8.281 19.339 78.967 1.00 67.91 A C
+ATOM 361 CG ASP A 48 -7.577 20.447 79.727 1.00 70.82 A C
+ATOM 362 OD1 ASP A 48 -7.511 20.368 80.972 1.00 74.63 A O
+ATOM 363 OD2 ASP A 48 -7.100 21.402 79.079 1.00 65.47 A O1-
+ATOM 364 N MET A 49 -8.413 16.332 77.588 1.00 64.80 A N
+ATOM 365 CA MET A 49 -9.418 15.600 76.823 1.00 61.58 A C
+ATOM 366 C MET A 49 -9.793 14.249 77.421 1.00 54.59 A C
+ATOM 367 O MET A 49 -10.736 13.623 76.925 1.00 50.82 A O
+ATOM 368 CB MET A 49 -8.930 15.410 75.386 1.00 62.15 A C
+ATOM 369 CG MET A 49 -8.934 16.691 74.567 1.00 60.24 A C
+ATOM 370 SD MET A 49 -8.229 16.487 72.920 1.00 77.15 A S
+ATOM 371 CE MET A 49 -8.703 18.038 72.158 1.00 60.34 A C
+ATOM 372 N LEU A 50 -9.098 13.777 78.459 1.00 55.58 A N
+ATOM 373 CA LEU A 50 -9.472 12.497 79.056 1.00 50.20 A C
+ATOM 374 C LEU A 50 -10.771 12.620 79.843 1.00 50.23 A C
+ATOM 375 O LEU A 50 -11.702 11.828 79.656 1.00 53.98 A O
+ATOM 376 CB LEU A 50 -8.348 11.972 79.949 1.00 56.38 A C
+ATOM 377 CG LEU A 50 -8.686 10.683 80.706 1.00 56.22 A C
+ATOM 378 CD1 LEU A 50 -9.083 9.574 79.738 1.00 54.68 A C
+ATOM 379 CD2 LEU A 50 -7.524 10.242 81.582 1.00 61.06 A C
+ATOM 380 N ASN A 51 -10.852 13.606 80.734 1.00 54.23 A N
+ATOM 381 CA ASN A 51 -12.073 13.874 81.495 1.00 56.71 A C
+ATOM 382 C ASN A 51 -12.099 15.344 81.875 1.00 53.53 A C
+ATOM 383 O ASN A 51 -11.754 15.724 83.001 1.00 59.55 A O
+ATOM 384 CB ASN A 51 -12.165 12.987 82.737 1.00 60.04 A C
+ATOM 385 CG ASN A 51 -13.429 13.238 83.538 1.00 66.55 A C
+ATOM 386 ND2 ASN A 51 -13.266 13.713 84.768 1.00 64.37 A N
+ATOM 387 OD1 ASN A 51 -14.540 13.012 83.056 1.00 68.23 A O
+ATOM 388 N PRO A 52 -12.498 16.214 80.948 1.00 51.24 A N
+ATOM 389 CA PRO A 52 -12.552 17.645 81.255 1.00 51.92 A C
+ATOM 390 C PRO A 52 -13.895 18.065 81.828 1.00 44.57 A C
+ATOM 391 O PRO A 52 -14.959 17.609 81.403 1.00 48.93 A O
+ATOM 392 CB PRO A 52 -12.320 18.290 79.883 1.00 53.34 A C
+ATOM 393 CG PRO A 52 -12.940 17.322 78.923 1.00 53.26 A C
+ATOM 394 CD PRO A 52 -12.813 15.939 79.534 1.00 52.84 A C
+ATOM 395 N ASN A 53 -13.837 18.944 82.824 1.00 42.70 A N
+ATOM 396 CA ASN A 53 -15.027 19.629 83.318 1.00 41.54 A C
+ATOM 397 C ASN A 53 -15.147 20.918 82.518 1.00 45.98 A C
+ATOM 398 O ASN A 53 -14.410 21.880 82.750 1.00 43.49 A O
+ATOM 399 CB ASN A 53 -14.935 19.889 84.817 1.00 47.59 A C
+ATOM 400 CG ASN A 53 -16.245 20.385 85.400 1.00 50.78 A C
+ATOM 401 ND2 ASN A 53 -16.830 19.598 86.295 1.00 58.51 A N
+ATOM 402 OD1 ASN A 53 -16.730 21.458 85.043 1.00 49.11 A O
+ATOM 403 N TYR A 54 -16.074 20.929 81.559 1.00 41.02 A N
+ATOM 404 CA TYR A 54 -16.130 22.020 80.594 1.00 37.74 A C
+ATOM 405 C TYR A 54 -16.556 23.333 81.234 1.00 36.00 A C
+ATOM 406 O TYR A 54 -16.115 24.400 80.794 1.00 38.89 A O
+ATOM 407 CB TYR A 54 -17.070 21.652 79.448 1.00 36.00 A C
+ATOM 408 CG TYR A 54 -16.478 20.641 78.495 1.00 32.02 A C
+ATOM 409 CD1 TYR A 54 -15.662 21.044 77.448 1.00 36.25 A C
+ATOM 410 CD2 TYR A 54 -16.725 19.284 78.648 1.00 36.73 A C
+ATOM 411 CE1 TYR A 54 -15.118 20.125 76.574 1.00 40.78 A C
+ATOM 412 CE2 TYR A 54 -16.184 18.357 77.779 1.00 37.10 A C
+ATOM 413 CZ TYR A 54 -15.380 18.784 76.744 1.00 36.90 A C
+ATOM 414 OH TYR A 54 -14.835 17.868 75.874 1.00 37.87 A O
+ATOM 415 N GLU A 55 -17.407 23.288 82.262 1.00 37.41 A N
+ATOM 416 CA GLU A 55 -17.793 24.529 82.925 1.00 46.21 A C
+ATOM 417 C GLU A 55 -16.624 25.125 83.697 1.00 40.08 A C
+ATOM 418 O GLU A 55 -16.481 26.352 83.769 1.00 45.60 A O
+ATOM 419 CB GLU A 55 -18.986 24.296 83.851 1.00 47.59 A C
+ATOM 420 CG GLU A 55 -20.340 24.679 83.246 1.00 53.59 A C
+ATOM 421 CD GLU A 55 -20.351 26.046 82.565 1.00 58.43 A C
+ATOM 422 OE1 GLU A 55 -19.654 26.974 83.035 1.00 62.86 A O
+ATOM 423 OE2 GLU A 55 -21.061 26.193 81.549 1.00 60.77 A O1-
+ATOM 424 N ASP A 56 -15.777 24.274 84.281 1.00 40.14 A N
+ATOM 425 CA ASP A 56 -14.560 24.768 84.913 1.00 46.72 A C
+ATOM 426 C ASP A 56 -13.630 25.396 83.885 1.00 46.75 A C
+ATOM 427 O ASP A 56 -13.065 26.470 84.120 1.00 41.56 A O
+ATOM 428 CB ASP A 56 -13.852 23.632 85.650 1.00 47.88 A C
+ATOM 429 CG ASP A 56 -14.054 23.692 87.150 1.00 55.58 A C
+ATOM 430 OD1 ASP A 56 -14.694 24.652 87.627 1.00 58.88 A O
+ATOM 431 OD2 ASP A 56 -13.573 22.778 87.852 1.00 63.71 A O1-
+ATOM 432 N LEU A 57 -13.470 24.746 82.729 1.00 42.40 A N
+ATOM 433 CA LEU A 57 -12.561 25.256 81.710 1.00 39.63 A C
+ATOM 434 C LEU A 57 -13.090 26.528 81.064 1.00 40.16 A C
+ATOM 435 O LEU A 57 -12.300 27.389 80.662 1.00 40.96 A O
+ATOM 436 CB LEU A 57 -12.313 24.186 80.646 1.00 42.67 A C
+ATOM 437 CG LEU A 57 -11.561 22.936 81.105 1.00 50.37 A C
+ATOM 438 CD1 LEU A 57 -11.538 21.886 80.006 1.00 49.87 A C
+ATOM 439 CD2 LEU A 57 -10.148 23.290 81.543 1.00 49.56 A C
+ATOM 440 N LEU A 58 -14.413 26.670 80.954 1.00 38.25 A N
+ATOM 441 CA LEU A 58 -14.972 27.838 80.281 1.00 40.40 A C
+ATOM 442 C LEU A 58 -14.925 29.078 81.165 1.00 39.95 A C
+ATOM 443 O LEU A 58 -14.673 30.183 80.671 1.00 35.67 A O
+ATOM 444 CB LEU A 58 -16.408 27.563 79.840 1.00 36.53 A C
+ATOM 445 CG LEU A 58 -17.019 28.704 79.024 1.00 40.35 A C
+ATOM 446 CD1 LEU A 58 -16.204 28.953 77.763 1.00 39.04 A C
+ATOM 447 CD2 LEU A 58 -18.469 28.424 78.686 1.00 45.58 A C
+ATOM 448 N ILE A 59 -15.171 28.920 82.469 1.00 42.81 A N
+ATOM 449 CA ILE A 59 -15.132 30.065 83.370 1.00 40.37 A C
+ATOM 450 C ILE A 59 -13.727 30.640 83.487 1.00 35.67 A C
+ATOM 451 O ILE A 59 -13.564 31.788 83.915 1.00 46.91 A O
+ATOM 452 CB ILE A 59 -15.689 29.679 84.755 1.00 42.33 A C
+ATOM 453 CG1 ILE A 59 -16.261 30.909 85.466 1.00 48.47 A C
+ATOM 454 CG2 ILE A 59 -14.614 29.017 85.607 1.00 37.96 A C
+ATOM 455 CD1 ILE A 59 -17.496 31.479 84.802 1.00 52.04 A C
+ATOM 456 N ARG A 60 -12.704 29.876 83.107 1.00 37.38 A N
+ATOM 457 CA ARG A 60 -11.325 30.345 83.122 1.00 39.45 A C
+ATOM 458 C ARG A 60 -10.927 31.042 81.829 1.00 40.28 A C
+ATOM 459 O ARG A 60 -9.770 31.449 81.690 1.00 42.72 A O
+ATOM 460 CB ARG A 60 -10.372 29.178 83.392 1.00 37.15 A C
+ATOM 461 CG ARG A 60 -10.613 28.483 84.719 1.00 36.47 A C
+ATOM 462 CD ARG A 60 -9.772 27.226 84.842 1.00 36.22 A C
+ATOM 463 NE ARG A 60 -10.147 26.436 86.010 1.00 42.15 A N
+ATOM 464 CZ ARG A 60 -9.663 25.229 86.281 1.00 54.61 A C
+ATOM 465 NH1 ARG A 60 -8.779 24.669 85.466 1.00 54.73 A N1+
+ATOM 466 NH2 ARG A 60 -10.061 24.583 87.368 1.00 53.63 A N
+ATOM 467 N LYS A 61 -11.851 31.186 80.886 1.00 38.95 A N
+ATOM 468 CA LYS A 61 -11.614 31.878 79.631 1.00 39.80 A C
+ATOM 469 C LYS A 61 -12.501 33.114 79.543 1.00 39.96 A C
+ATOM 470 O LYS A 61 -13.520 33.229 80.229 1.00 41.63 A O
+ATOM 471 CB LYS A 61 -11.880 30.960 78.431 1.00 42.50 A C
+ATOM 472 CG LYS A 61 -11.268 29.575 78.554 1.00 40.30 A C
+ATOM 473 CD LYS A 61 -10.068 29.419 77.632 1.00 43.28 A C
+ATOM 474 CE LYS A 61 -9.474 28.023 77.733 1.00 50.52 A C
+ATOM 475 NZ LYS A 61 -9.547 27.496 79.124 1.00 57.16 A N1+
+ATOM 476 N SER A 62 -12.092 34.048 78.691 1.00 36.02 A N
+ATOM 477 CA SER A 62 -12.873 35.239 78.389 1.00 45.54 A C
+ATOM 478 C SER A 62 -12.968 35.395 76.875 1.00 46.47 A C
+ATOM 479 O SER A 62 -12.510 34.540 76.110 1.00 42.97 A O
+ATOM 480 CB SER A 62 -12.264 36.486 79.042 1.00 50.61 A C
+ATOM 481 OG SER A 62 -10.909 36.647 78.674 1.00 52.06 A O
+ATOM 482 N ASN A 63 -13.570 36.504 76.440 1.00 45.75 A N
+ATOM 483 CA ASN A 63 -13.822 36.700 75.016 1.00 46.75 A C
+ATOM 484 C ASN A 63 -12.531 36.844 74.220 1.00 48.42 A C
+ATOM 485 O ASN A 63 -12.477 36.432 73.056 1.00 43.99 A O
+ATOM 486 CB ASN A 63 -14.714 37.922 74.809 1.00 48.34 A C
+ATOM 487 CG ASN A 63 -16.120 37.707 75.325 1.00 48.12 A C
+ATOM 488 ND2 ASN A 63 -16.859 38.794 75.499 1.00 52.25 A N
+ATOM 489 OD1 ASN A 63 -16.538 36.575 75.568 1.00 47.86 A O
+ATOM 490 N HIS A 64 -11.487 37.413 74.824 1.00 42.81 A N
+ATOM 491 CA HIS A 64 -10.226 37.603 74.116 1.00 47.58 A C
+ATOM 492 C HIS A 64 -9.485 36.297 73.861 1.00 45.70 A C
+ATOM 493 O HIS A 64 -8.532 36.293 73.074 1.00 44.67 A O
+ATOM 494 CB HIS A 64 -9.326 38.562 74.897 1.00 55.48 A C
+ATOM 495 CG HIS A 64 -8.487 37.890 75.939 1.00 57.45 A C
+ATOM 496 CD2 HIS A 64 -7.155 37.652 75.995 1.00 62.77 A C
+ATOM 497 ND1 HIS A 64 -9.018 37.366 77.098 1.00 65.64 A N
+ATOM 498 CE1 HIS A 64 -8.049 36.837 77.824 1.00 67.36 A C
+ATOM 499 NE2 HIS A 64 -6.909 36.998 77.177 1.00 70.85 A N
+ATOM 500 N ASN A 65 -9.891 35.199 74.500 1.00 46.87 A N
+ATOM 501 CA ASN A 65 -9.232 33.913 74.312 1.00 42.60 A C
+ATOM 502 C ASN A 65 -9.683 33.191 73.049 1.00 43.44 A C
+ATOM 503 O ASN A 65 -9.116 32.144 72.720 1.00 45.20 A O
+ATOM 504 CB ASN A 65 -9.479 33.014 75.528 1.00 43.59 A C
+ATOM 505 CG ASN A 65 -8.871 33.572 76.800 1.00 48.45 A C
+ATOM 506 ND2 ASN A 65 -7.579 33.875 76.756 1.00 48.19 A N
+ATOM 507 OD1 ASN A 65 -9.554 33.725 77.813 1.00 45.49 A O
+ATOM 508 N PHE A 66 -10.676 33.718 72.338 1.00 38.08 A N
+ATOM 509 CA PHE A 66 -11.234 33.076 71.155 1.00 40.63 A C
+ATOM 510 C PHE A 66 -10.905 33.913 69.926 1.00 41.32 A C
+ATOM 511 O PHE A 66 -11.373 35.049 69.799 1.00 44.74 A O
+ATOM 512 CB PHE A 66 -12.747 32.898 71.288 1.00 38.85 A C
+ATOM 513 CG PHE A 66 -13.155 31.991 72.414 1.00 39.29 A C
+ATOM 514 CD1 PHE A 66 -13.187 30.616 72.245 1.00 37.23 A C
+ATOM 515 CD2 PHE A 66 -13.506 32.517 73.646 1.00 37.37 A C
+ATOM 516 CE1 PHE A 66 -13.564 29.783 73.286 1.00 36.49 A C
+ATOM 517 CE2 PHE A 66 -13.883 31.691 74.689 1.00 35.33 A C
+ATOM 518 CZ PHE A 66 -13.912 30.323 74.509 1.00 43.59 A C
+ATOM 519 N LEU A 67 -10.106 33.350 69.026 1.00 37.46 A N
+ATOM 520 CA LEU A 67 -9.759 33.989 67.760 1.00 39.60 A C
+ATOM 521 C LEU A 67 -10.605 33.356 66.658 1.00 45.47 A C
+ATOM 522 O LEU A 67 -10.447 32.170 66.353 1.00 47.86 A O
+ATOM 523 CB LEU A 67 -8.267 33.836 67.459 1.00 41.67 A C
+ATOM 524 CG LEU A 67 -7.852 34.306 66.063 1.00 50.78 A C
+ATOM 525 CD1 LEU A 67 -7.697 35.811 66.075 1.00 54.65 A C
+ATOM 526 CD2 LEU A 67 -6.565 33.632 65.596 1.00 53.28 A C
+ATOM 527 N VAL A 68 -11.503 34.139 66.068 1.00 41.73 A N
+ATOM 528 CA VAL A 68 -12.392 33.669 65.012 1.00 41.94 A C
+ATOM 529 C VAL A 68 -11.961 34.319 63.703 1.00 48.24 A C
+ATOM 530 O VAL A 68 -11.912 35.551 63.596 1.00 48.40 A O
+ATOM 531 CB VAL A 68 -13.860 33.983 65.332 1.00 43.81 A C
+ATOM 532 CG1 VAL A 68 -14.762 33.503 64.202 1.00 38.39 A C
+ATOM 533 CG2 VAL A 68 -14.269 33.341 66.650 1.00 37.29 A C
+ATOM 534 N GLN A 69 -11.657 33.492 62.708 1.00 42.65 A N
+ATOM 535 CA GLN A 69 -11.207 33.957 61.403 1.00 40.20 A C
+ATOM 536 C GLN A 69 -12.207 33.536 60.335 1.00 45.19 A C
+ATOM 537 O GLN A 69 -12.541 32.352 60.222 1.00 41.18 A O
+ATOM 538 CB GLN A 69 -9.818 33.404 61.068 1.00 42.53 A C
+ATOM 539 CG GLN A 69 -8.666 34.243 61.596 1.00 48.54 A C
+ATOM 540 CD GLN A 69 -7.348 33.493 61.584 1.00 53.50 A C
+ATOM 541 NE2 GLN A 69 -6.378 34.008 60.836 1.00 54.98 A N
+ATOM 542 OE1 GLN A 69 -7.203 32.459 62.237 1.00 58.04 A O
+ATOM 543 N ALA A 70 -12.681 34.506 59.560 1.00 47.87 A N
+ATOM 544 CA ALA A 70 -13.549 34.265 58.410 1.00 48.51 A C
+ATOM 545 C ALA A 70 -12.748 34.645 57.168 1.00 53.00 A C
+ATOM 546 O ALA A 70 -12.752 35.799 56.736 1.00 57.30 A O
+ATOM 547 CB ALA A 70 -14.847 35.058 58.519 1.00 42.49 A C
+ATOM 548 N GLY A 71 -12.057 33.663 56.597 1.00 51.17 A N
+ATOM 549 CA GLY A 71 -11.104 33.933 55.542 1.00 53.14 A C
+ATOM 550 C GLY A 71 -9.906 34.691 56.072 1.00 60.48 A C
+ATOM 551 O GLY A 71 -9.224 34.222 56.987 1.00 64.43 A O
+ATOM 552 N ASN A 72 -9.640 35.867 55.512 1.00 64.84 A N
+ATOM 553 CA ASN A 72 -8.597 36.742 56.027 1.00 65.70 A C
+ATOM 554 C ASN A 72 -9.132 37.775 57.010 1.00 67.64 A C
+ATOM 555 O ASN A 72 -8.343 38.534 57.581 1.00 70.47 A O
+ATOM 556 CB ASN A 72 -7.880 37.452 54.873 1.00 67.25 A C
+ATOM 557 CG ASN A 72 -6.610 36.741 54.452 1.00 69.63 A C
+ATOM 558 ND2 ASN A 72 -5.498 37.089 55.090 1.00 66.84 A N
+ATOM 559 OD1 ASN A 72 -6.627 35.888 53.564 1.00 69.66 A O
+ATOM 560 N VAL A 73 -10.444 37.816 57.223 1.00 62.71 A N
+ATOM 561 CA VAL A 73 -11.062 38.773 58.132 1.00 57.40 A C
+ATOM 562 C VAL A 73 -11.174 38.141 59.513 1.00 57.48 A C
+ATOM 563 O VAL A 73 -11.630 36.999 59.649 1.00 52.71 A O
+ATOM 564 CB VAL A 73 -12.442 39.212 57.614 1.00 56.38 A C
+ATOM 565 CG1 VAL A 73 -13.041 40.275 58.524 1.00 55.15 A C
+ATOM 566 CG2 VAL A 73 -12.335 39.721 56.185 1.00 57.14 A C
+ATOM 567 N GLN A 74 -10.758 38.880 60.536 1.00 55.65 A N
+ATOM 568 CA GLN A 74 -10.859 38.437 61.918 1.00 54.17 A C
+ATOM 569 C GLN A 74 -12.094 39.047 62.567 1.00 52.79 A C
+ATOM 570 O GLN A 74 -12.364 40.241 62.413 1.00 57.72 A O
+ATOM 571 CB GLN A 74 -9.607 38.823 62.709 1.00 51.64 A C
+ATOM 572 CG GLN A 74 -9.667 38.459 64.183 1.00 59.47 A C
+ATOM 573 CD GLN A 74 -8.486 39.001 64.964 1.00 65.67 A C
+ATOM 574 NE2 GLN A 74 -8.624 39.053 66.284 1.00 60.42 A N
+ATOM 575 OE1 GLN A 74 -7.464 39.373 64.387 1.00 68.08 A O
+ATOM 576 N LEU A 75 -12.844 38.219 63.287 1.00 49.98 A N
+ATOM 577 CA LEU A 75 -14.034 38.661 64.001 1.00 45.97 A C
+ATOM 578 C LEU A 75 -13.722 38.758 65.487 1.00 51.19 A C
+ATOM 579 O LEU A 75 -13.122 37.842 66.061 1.00 51.25 A O
+ATOM 580 CB LEU A 75 -15.203 37.701 63.771 1.00 45.98 A C
+ATOM 581 CG LEU A 75 -15.397 37.124 62.366 1.00 46.40 A C
+ATOM 582 CD1 LEU A 75 -16.637 36.245 62.327 1.00 43.70 A C
+ATOM 583 CD2 LEU A 75 -15.490 38.228 61.323 1.00 46.98 A C
+ATOM 584 N ARG A 76 -14.125 39.864 66.105 1.00 47.70 A N
+ATOM 585 CA ARG A 76 -13.924 40.058 67.533 1.00 48.38 A C
+ATOM 586 C ARG A 76 -15.060 39.403 68.306 1.00 39.67 A C
+ATOM 587 O ARG A 76 -16.236 39.687 68.055 1.00 42.34 A O
+ATOM 588 CB ARG A 76 -13.840 41.545 67.879 1.00 50.15 A C
+ATOM 589 CG ARG A 76 -13.612 41.813 69.360 1.00 52.87 A C
+ATOM 590 CD ARG A 76 -13.416 43.294 69.645 1.00 55.14 A C
+ATOM 591 NE ARG A 76 -14.581 44.088 69.265 1.00 64.31 A N
+ATOM 592 CZ ARG A 76 -14.626 44.888 68.204 1.00 67.73 A C
+ATOM 593 NH1 ARG A 76 -13.568 45.003 67.413 1.00 66.74 A N1+
+ATOM 594 NH2 ARG A 76 -15.728 45.573 67.934 1.00 66.20 A N
+ATOM 595 N VAL A 77 -14.705 38.525 69.239 1.00 40.40 A N
+ATOM 596 CA VAL A 77 -15.688 37.865 70.092 1.00 41.40 A C
+ATOM 597 C VAL A 77 -16.126 38.862 71.160 1.00 42.42 A C
+ATOM 598 O VAL A 77 -15.323 39.286 71.994 1.00 41.41 A O
+ATOM 599 CB VAL A 77 -15.122 36.588 70.720 1.00 42.39 A C
+ATOM 600 CG1 VAL A 77 -16.166 35.927 71.607 1.00 42.45 A C
+ATOM 601 CG2 VAL A 77 -14.650 35.629 69.637 1.00 45.27 A C
+ATOM 602 N ILE A 78 -17.404 39.247 71.130 1.00 45.11 A N
+ATOM 603 CA ILE A 78 -17.956 40.173 72.111 1.00 47.98 A C
+ATOM 604 C ILE A 78 -18.777 39.464 73.176 1.00 45.95 A C
+ATOM 605 O ILE A 78 -19.370 40.129 74.037 1.00 46.80 A O
+ATOM 606 CB ILE A 78 -18.805 41.263 71.426 1.00 45.44 A C
+ATOM 607 CG1 ILE A 78 -19.998 40.633 70.705 1.00 46.53 A C
+ATOM 608 CG2 ILE A 78 -17.953 42.068 70.458 1.00 49.79 A C
+ATOM 609 CD1 ILE A 78 -21.254 41.473 70.759 1.00 46.96 A C
+ATOM 610 N GLY A 79 -18.825 38.136 73.148 1.00 44.35 A N
+ATOM 611 CA GLY A 79 -19.570 37.368 74.125 1.00 40.60 A C
+ATOM 612 C GLY A 79 -19.483 35.882 73.851 1.00 41.13 A C
+ATOM 613 O GLY A 79 -19.364 35.467 72.694 1.00 40.70 A O
+ATOM 614 N HIS A 80 -19.532 35.067 74.901 1.00 38.25 A N
+ATOM 615 CA HIS A 80 -19.459 33.623 74.754 1.00 43.22 A C
+ATOM 616 C HIS A 80 -20.447 32.967 75.705 1.00 45.13 A C
+ATOM 617 O HIS A 80 -20.775 33.515 76.761 1.00 41.76 A O
+ATOM 618 CB HIS A 80 -18.040 33.094 75.012 1.00 41.39 A C
+ATOM 619 CG HIS A 80 -17.537 33.357 76.396 1.00 48.48 A C
+ATOM 620 CD2 HIS A 80 -17.684 32.660 77.547 1.00 46.89 A C
+ATOM 621 ND1 HIS A 80 -16.769 34.457 76.711 1.00 51.98 A N
+ATOM 622 CE1 HIS A 80 -16.469 34.429 77.998 1.00 48.92 A C
+ATOM 623 NE2 HIS A 80 -17.012 33.348 78.528 1.00 50.90 A N
+ATOM 624 N SER A 81 -20.917 31.785 75.316 1.00 38.75 A N
+ATOM 625 CA SER A 81 -21.886 31.042 76.106 1.00 41.79 A C
+ATOM 626 C SER A 81 -21.831 29.580 75.694 1.00 40.92 A C
+ATOM 627 O SER A 81 -21.705 29.270 74.506 1.00 45.55 A O
+ATOM 628 CB SER A 81 -23.301 31.598 75.918 1.00 43.04 A C
+ATOM 629 OG SER A 81 -24.271 30.573 76.035 1.00 52.68 A O
+ATOM 630 N MET A 82 -21.922 28.691 76.677 1.00 35.70 A N
+ATOM 631 CA MET A 82 -21.948 27.257 76.429 1.00 40.92 A C
+ATOM 632 C MET A 82 -23.390 26.778 76.399 1.00 37.18 A C
+ATOM 633 O MET A 82 -24.151 27.020 77.342 1.00 43.24 A O
+ATOM 634 CB MET A 82 -21.159 26.492 77.492 1.00 35.75 A C
+ATOM 635 CG MET A 82 -21.076 24.998 77.240 1.00 31.49 A C
+ATOM 636 SD MET A 82 -19.971 24.146 78.382 1.00 52.99 A S
+ATOM 637 CE MET A 82 -18.380 24.771 77.848 1.00 46.40 A C
+ATOM 638 N GLN A 83 -23.763 26.115 75.310 1.00 36.53 A N
+ATOM 639 CA GLN A 83 -25.081 25.506 75.169 1.00 38.76 A C
+ATOM 640 C GLN A 83 -24.859 24.008 75.017 1.00 35.47 A C
+ATOM 641 O GLN A 83 -24.610 23.522 73.909 1.00 38.88 A O
+ATOM 642 CB GLN A 83 -25.835 26.093 73.985 1.00 42.05 A C
+ATOM 643 CG GLN A 83 -27.334 26.150 74.186 1.00 49.29 A C
+ATOM 644 CD GLN A 83 -28.094 25.956 72.894 1.00 56.32 A C
+ATOM 645 NE2 GLN A 83 -29.407 25.796 73.002 1.00 59.16 A N
+ATOM 646 OE1 GLN A 83 -27.511 25.956 71.809 1.00 59.39 A O
+ATOM 647 N ASN A 84 -24.943 23.286 76.135 1.00 35.48 A N
+ATOM 648 CA ASN A 84 -24.667 21.854 76.163 1.00 28.78 A C
+ATOM 649 C ASN A 84 -23.255 21.576 75.665 1.00 32.51 A C
+ATOM 650 O ASN A 84 -22.282 21.926 76.339 1.00 37.59 A O
+ATOM 651 CB ASN A 84 -25.704 21.085 75.339 1.00 33.36 A C
+ATOM 652 CG ASN A 84 -27.120 21.394 75.766 1.00 31.17 A C
+ATOM 653 ND2 ASN A 84 -27.944 21.838 74.824 1.00 32.50 A N
+ATOM 654 OD1 ASN A 84 -27.467 21.251 76.939 1.00 37.19 A O
+ATOM 655 N CYS A 85 -23.115 20.964 74.490 1.00 31.33 A N
+ATOM 656 CA CYS A 85 -21.798 20.585 73.993 1.00 29.75 A C
+ATOM 657 C CYS A 85 -21.272 21.497 72.891 1.00 27.93 A C
+ATOM 658 O CYS A 85 -20.211 21.212 72.327 1.00 30.14 A O
+ATOM 659 CB CYS A 85 -21.806 19.130 73.517 1.00 30.66 A C
+ATOM 660 SG CYS A 85 -22.241 17.929 74.804 1.00 41.25 A S
+ATOM 661 N VAL A 86 -21.956 22.597 72.589 1.00 26.22 A N
+ATOM 662 CA VAL A 86 -21.462 23.546 71.599 1.00 31.73 A C
+ATOM 663 C VAL A 86 -21.217 24.889 72.270 1.00 35.24 A C
+ATOM 664 O VAL A 86 -21.880 25.253 73.248 1.00 34.26 A O
+ATOM 665 CB VAL A 86 -22.422 23.712 70.400 1.00 34.22 A C
+ATOM 666 CG1 VAL A 86 -22.536 22.411 69.618 1.00 32.41 A C
+ATOM 667 CG2 VAL A 86 -23.786 24.197 70.866 1.00 37.90 A C
+ATOM 668 N LEU A 87 -20.248 25.624 71.735 1.00 34.20 A N
+ATOM 669 CA LEU A 87 -19.981 26.989 72.159 1.00 38.10 A C
+ATOM 670 C LEU A 87 -20.746 27.959 71.272 1.00 37.42 A C
+ATOM 671 O LEU A 87 -20.863 27.752 70.060 1.00 39.21 A O
+ATOM 672 CB LEU A 87 -18.483 27.293 72.093 1.00 39.41 A C
+ATOM 673 CG LEU A 87 -17.705 27.345 73.407 1.00 41.24 A C
+ATOM 674 CD1 LEU A 87 -16.210 27.344 73.135 1.00 39.84 A C
+ATOM 675 CD2 LEU A 87 -18.101 28.566 74.221 1.00 45.07 A C
+ATOM 676 N LYS A 88 -21.273 29.017 71.882 1.00 35.57 A N
+ATOM 677 CA LYS A 88 -21.956 30.086 71.160 1.00 35.57 A C
+ATOM 678 C LYS A 88 -21.167 31.370 71.373 1.00 42.07 A C
+ATOM 679 O LYS A 88 -21.201 31.953 72.462 1.00 39.09 A O
+ATOM 680 CB LYS A 88 -23.403 30.235 71.629 1.00 39.36 A C
+ATOM 681 CG LYS A 88 -24.281 29.038 71.296 1.00 41.29 A C
+ATOM 682 CD LYS A 88 -25.665 29.167 71.909 1.00 46.58 A C
+ATOM 683 CE LYS A 88 -26.601 29.951 71.005 1.00 43.72 A C
+ATOM 684 NZ LYS A 88 -27.998 29.944 71.521 1.00 51.46 A N1+
+ATOM 685 N LEU A 89 -20.451 31.801 70.337 1.00 35.18 A N
+ATOM 686 CA LEU A 89 -19.587 32.974 70.406 1.00 35.95 A C
+ATOM 687 C LEU A 89 -20.274 34.136 69.697 1.00 39.94 A C
+ATOM 688 O LEU A 89 -20.422 34.124 68.471 1.00 37.92 A O
+ATOM 689 CB LEU A 89 -18.225 32.683 69.778 1.00 35.83 A C
+ATOM 690 CG LEU A 89 -17.443 31.484 70.316 1.00 34.70 A C
+ATOM 691 CD1 LEU A 89 -16.114 31.346 69.590 1.00 35.27 A C
+ATOM 692 CD2 LEU A 89 -17.225 31.612 71.813 1.00 34.21 A C
+ATOM 693 N LYS A 90 -20.694 35.133 70.470 1.00 37.44 A N
+ATOM 694 CA LYS A 90 -21.231 36.355 69.888 1.00 37.63 A C
+ATOM 695 C LYS A 90 -20.093 37.183 69.306 1.00 44.75 A C
+ATOM 696 O LYS A 90 -19.088 37.432 69.979 1.00 43.60 A O
+ATOM 697 CB LYS A 90 -21.990 37.156 70.944 1.00 45.52 A C
+ATOM 698 CG LYS A 90 -23.177 37.940 70.409 1.00 47.69 A C
+ATOM 699 CD LYS A 90 -24.005 38.518 71.547 1.00 55.70 A C
+ATOM 700 CE LYS A 90 -25.345 39.037 71.053 1.00 59.25 A C
+ATOM 701 NZ LYS A 90 -26.228 39.447 72.181 1.00 57.77 A N1+
+ATOM 702 N VAL A 91 -20.244 37.605 68.052 1.00 39.26 A N
+ATOM 703 CA VAL A 91 -19.193 38.332 67.355 1.00 38.65 A C
+ATOM 704 C VAL A 91 -19.715 39.699 66.932 1.00 46.65 A C
+ATOM 705 O VAL A 91 -20.920 39.964 66.930 1.00 44.94 A O
+ATOM 706 CB VAL A 91 -18.655 37.554 66.137 1.00 43.56 A C
+ATOM 707 CG1 VAL A 91 -17.792 36.387 66.598 1.00 41.53 A C
+ATOM 708 CG2 VAL A 91 -19.802 37.068 65.267 1.00 38.87 A C
+ATOM 709 N ASP A 92 -18.775 40.571 66.563 1.00 47.50 A N
+ATOM 710 CA ASP A 92 -19.097 41.962 66.265 1.00 55.99 A C
+ATOM 711 C ASP A 92 -19.813 42.133 64.931 1.00 55.99 A C
+ATOM 712 O ASP A 92 -20.446 43.172 64.713 1.00 51.50 A O
+ATOM 713 CB ASP A 92 -17.816 42.800 66.282 1.00 56.73 A C
+ATOM 714 CG ASP A 92 -18.082 44.282 66.104 1.00 71.09 A C
+ATOM 715 OD1 ASP A 92 -18.456 44.945 67.094 1.00 74.54 A O
+ATOM 716 OD2 ASP A 92 -17.917 44.784 64.971 1.00 72.25 A O1-
+ATOM 717 N THR A 93 -19.741 41.146 64.042 1.00 53.36 A N
+ATOM 718 CA THR A 93 -20.267 41.272 62.689 1.00 50.11 A C
+ATOM 719 C THR A 93 -21.298 40.186 62.421 1.00 48.58 A C
+ATOM 720 O THR A 93 -21.081 39.019 62.764 1.00 44.46 A O
+ATOM 721 CB THR A 93 -19.142 41.188 61.653 1.00 51.85 A C
+ATOM 722 CG2 THR A 93 -19.574 41.829 60.342 1.00 53.12 A C
+ATOM 723 OG1 THR A 93 -17.981 41.863 62.151 1.00 61.92 A O
+ATOM 724 N ALA A 94 -22.416 40.574 61.812 1.00 44.58 A N
+ATOM 725 CA ALA A 94 -23.384 39.608 61.318 1.00 45.34 A C
+ATOM 726 C ALA A 94 -22.932 39.095 59.958 1.00 41.83 A C
+ATOM 727 O ALA A 94 -22.536 39.880 59.092 1.00 44.83 A O
+ATOM 728 CB ALA A 94 -24.773 40.237 61.218 1.00 37.38 A C
+ATOM 729 N ASN A 95 -22.978 37.777 59.777 1.00 42.65 A N
+ATOM 730 CA ASN A 95 -22.552 37.160 58.527 1.00 40.38 A C
+ATOM 731 C ASN A 95 -23.452 37.626 57.389 1.00 40.35 A C
+ATOM 732 O ASN A 95 -24.653 37.326 57.383 1.00 39.89 A O
+ATOM 733 CB ASN A 95 -22.572 35.634 58.650 1.00 42.27 A C
+ATOM 734 CG ASN A 95 -21.926 34.936 57.464 1.00 43.20 A C
+ATOM 735 ND2 ASN A 95 -21.754 33.625 57.578 1.00 42.09 A N
+ATOM 736 OD1 ASN A 95 -21.591 35.563 56.459 1.00 44.92 A O
+ATOM 737 N PRO A 96 -22.914 38.362 56.412 1.00 42.52 A N
+ATOM 738 CA PRO A 96 -23.755 38.820 55.295 1.00 43.84 A C
+ATOM 739 C PRO A 96 -24.223 37.695 54.392 1.00 43.73 A C
+ATOM 740 O PRO A 96 -25.225 37.868 53.687 1.00 44.92 A O
+ATOM 741 CB PRO A 96 -22.840 39.796 54.544 1.00 41.66 A C
+ATOM 742 CG PRO A 96 -21.459 39.322 54.857 1.00 41.64 A C
+ATOM 743 CD PRO A 96 -21.512 38.793 56.265 1.00 39.46 A C
+ATOM 744 N LYS A 97 -23.537 36.555 54.387 1.00 45.99 A N
+ATOM 745 CA LYS A 97 -23.938 35.402 53.596 1.00 45.32 A C
+ATOM 746 C LYS A 97 -24.868 34.462 54.351 1.00 44.01 A C
+ATOM 747 O LYS A 97 -25.065 33.325 53.911 1.00 46.12 A O
+ATOM 748 CB LYS A 97 -22.704 34.628 53.123 1.00 43.79 A C
+ATOM 749 CG LYS A 97 -21.662 35.472 52.411 1.00 48.51 A C
+ATOM 750 CD LYS A 97 -20.651 34.588 51.697 1.00 47.89 A C
+ATOM 751 CE LYS A 97 -19.319 35.297 51.519 1.00 51.57 A C
+ATOM 752 NZ LYS A 97 -18.351 34.464 50.753 1.00 64.60 A N1+
+ATOM 753 N THR A 98 -25.435 34.903 55.468 1.00 42.46 A N
+ATOM 754 CA THR A 98 -26.312 34.054 56.263 1.00 39.45 A C
+ATOM 755 C THR A 98 -27.555 33.682 55.465 1.00 38.73 A C
+ATOM 756 O THR A 98 -28.349 34.570 55.120 1.00 41.52 A O
+ATOM 757 CB THR A 98 -26.728 34.751 57.556 1.00 43.49 A C
+ATOM 758 CG2 THR A 98 -27.706 33.882 58.333 1.00 38.44 A C
+ATOM 759 OG1 THR A 98 -25.574 34.995 58.365 1.00 42.89 A O
+ATOM 760 N PRO A 99 -27.766 32.410 55.155 1.00 38.95 A N
+ATOM 761 CA PRO A 99 -29.005 32.004 54.492 1.00 38.09 A C
+ATOM 762 C PRO A 99 -30.127 31.867 55.511 1.00 41.90 A C
+ATOM 763 O PRO A 99 -29.914 31.905 56.724 1.00 39.74 A O
+ATOM 764 CB PRO A 99 -28.640 30.650 53.883 1.00 40.27 A C
+ATOM 765 CG PRO A 99 -27.665 30.080 54.873 1.00 44.92 A C
+ATOM 766 CD PRO A 99 -26.901 31.254 55.452 1.00 39.70 A C
+ATOM 767 N LYS A 100 -31.343 31.718 54.996 1.00 36.74 A N
+ATOM 768 CA LYS A 100 -32.447 31.325 55.856 1.00 42.54 A C
+ATOM 769 C LYS A 100 -32.197 29.902 56.336 1.00 42.21 A C
+ATOM 770 O LYS A 100 -31.913 29.008 55.533 1.00 40.24 A O
+ATOM 771 CB LYS A 100 -33.777 31.423 55.113 1.00 40.57 A C
+ATOM 772 CG LYS A 100 -34.989 31.181 55.998 1.00 49.85 A C
+ATOM 773 CD LYS A 100 -36.118 30.512 55.235 1.00 57.75 A C
+ATOM 774 CE LYS A 100 -37.472 30.904 55.803 1.00 58.16 A C
+ATOM 775 NZ LYS A 100 -38.084 29.783 56.571 1.00 62.23 A N1+
+ATOM 776 N TYR A 101 -32.267 29.692 57.647 1.00 37.56 A N
+ATOM 777 CA TYR A 101 -31.842 28.424 58.217 1.00 37.16 A C
+ATOM 778 C TYR A 101 -32.766 28.016 59.353 1.00 37.23 A C
+ATOM 779 O TYR A 101 -33.559 28.809 59.867 1.00 36.86 A O
+ATOM 780 CB TYR A 101 -30.390 28.492 58.709 1.00 33.76 A C
+ATOM 781 CG TYR A 101 -30.181 29.414 59.891 1.00 39.07 A C
+ATOM 782 CD1 TYR A 101 -29.935 30.768 59.704 1.00 33.22 A C
+ATOM 783 CD2 TYR A 101 -30.223 28.929 61.193 1.00 36.68 A C
+ATOM 784 CE1 TYR A 101 -29.742 31.614 60.779 1.00 38.66 A C
+ATOM 785 CE2 TYR A 101 -30.032 29.768 62.274 1.00 35.64 A C
+ATOM 786 CZ TYR A 101 -29.791 31.108 62.062 1.00 42.74 A C
+ATOM 787 OH TYR A 101 -29.599 31.947 63.136 1.00 44.17 A O
+ATOM 788 N LYS A 102 -32.647 26.746 59.734 1.00 34.77 A N
+ATOM 789 CA LYS A 102 -33.343 26.180 60.877 1.00 35.68 A C
+ATOM 790 C LYS A 102 -32.405 25.213 61.582 1.00 36.28 A C
+ATOM 791 O LYS A 102 -31.485 24.664 60.972 1.00 34.40 A O
+ATOM 792 CB LYS A 102 -34.628 25.446 60.464 1.00 40.86 A C
+ATOM 793 CG LYS A 102 -35.760 26.352 60.011 1.00 49.31 A C
+ATOM 794 CD LYS A 102 -37.092 25.614 60.025 1.00 49.25 A C
+ATOM 795 CE LYS A 102 -37.465 25.108 58.640 1.00 61.49 A C
+ATOM 796 NZ LYS A 102 -36.684 23.899 58.253 1.00 62.18 A N1+
+ATOM 797 N PHE A 103 -32.639 25.016 62.876 1.00 31.56 A N
+ATOM 798 CA PHE A 103 -31.916 24.031 63.672 1.00 34.73 A C
+ATOM 799 C PHE A 103 -32.868 22.876 63.951 1.00 31.35 A C
+ATOM 800 O PHE A 103 -33.804 23.015 64.745 1.00 32.98 A O
+ATOM 801 CB PHE A 103 -31.397 24.641 64.973 1.00 34.30 A C
+ATOM 802 CG PHE A 103 -30.156 25.473 64.804 1.00 32.28 A C
+ATOM 803 CD1 PHE A 103 -29.508 25.539 63.583 1.00 30.49 A C
+ATOM 804 CD2 PHE A 103 -29.635 26.186 65.873 1.00 35.60 A C
+ATOM 805 CE1 PHE A 103 -28.366 26.303 63.428 1.00 30.40 A C
+ATOM 806 CE2 PHE A 103 -28.494 26.951 65.725 1.00 31.28 A C
+ATOM 807 CZ PHE A 103 -27.858 27.010 64.501 1.00 32.20 A C
+ATOM 808 N VAL A 104 -32.639 21.743 63.295 1.00 28.64 A N
+ATOM 809 CA VAL A 104 -33.501 20.580 63.455 1.00 32.71 A C
+ATOM 810 C VAL A 104 -32.669 19.403 63.943 1.00 37.01 A C
+ATOM 811 O VAL A 104 -31.476 19.285 63.645 1.00 37.44 A O
+ATOM 812 CB VAL A 104 -34.243 20.218 62.148 1.00 35.46 A C
+ATOM 813 CG1 VAL A 104 -34.967 21.437 61.592 1.00 38.21 A C
+ATOM 814 CG2 VAL A 104 -33.279 19.645 61.119 1.00 38.51 A C
+ATOM 815 N ARG A 105 -33.310 18.537 64.720 1.00 27.53 A N
+ATOM 816 CA ARG A 105 -32.716 17.283 65.158 1.00 30.16 A C
+ATOM 817 C ARG A 105 -33.377 16.153 64.381 1.00 31.64 A C
+ATOM 818 O ARG A 105 -34.589 15.941 64.495 1.00 36.99 A O
+ATOM 819 CB ARG A 105 -32.889 17.086 66.664 1.00 29.60 A C
+ATOM 820 CG ARG A 105 -32.252 15.817 67.206 1.00 31.99 A C
+ATOM 821 CD ARG A 105 -32.393 15.729 68.718 1.00 31.57 A C
+ATOM 822 NE ARG A 105 -31.731 14.547 69.267 1.00 29.72 A N
+ATOM 823 CZ ARG A 105 -30.480 14.532 69.716 1.00 30.68 A C
+ATOM 824 NH1 ARG A 105 -29.748 15.638 69.683 1.00 28.54 A N1+
+ATOM 825 NH2 ARG A 105 -29.959 13.412 70.199 1.00 29.69 A N
+ATOM 826 N ILE A 106 -32.584 15.441 63.587 1.00 25.77 A N
+ATOM 827 CA ILE A 106 -33.120 14.410 62.707 1.00 29.24 A C
+ATOM 828 C ILE A 106 -33.326 13.118 63.484 1.00 33.97 A C
+ATOM 829 O ILE A 106 -32.914 13.000 64.644 1.00 37.23 A O
+ATOM 830 CB ILE A 106 -32.201 14.192 61.492 1.00 33.86 A C
+ATOM 831 CG1 ILE A 106 -30.825 13.704 61.946 1.00 28.97 A C
+ATOM 832 CG2 ILE A 106 -32.072 15.474 60.686 1.00 41.61 A C
+ATOM 833 CD1 ILE A 106 -30.830 12.308 62.499 1.00 40.69 A C
+ATOM 834 N GLN A 107 -33.961 12.151 62.849 1.00 29.20 A N
+ATOM 835 CA GLN A 107 -34.263 10.844 63.402 1.00 31.86 A C
+ATOM 836 C GLN A 107 -33.318 9.796 62.837 1.00 35.06 A C
+ATOM 837 O GLN A 107 -32.727 9.986 61.770 1.00 32.68 A O
+ATOM 838 CB GLN A 107 -35.711 10.456 63.080 1.00 34.98 A C
+ATOM 839 CG GLN A 107 -36.752 11.168 63.925 1.00 33.40 A C
+ATOM 840 CD GLN A 107 -36.793 10.647 65.347 1.00 40.18 A C
+ATOM 841 NE2 GLN A 107 -37.030 11.542 66.299 1.00 39.77 A N
+ATOM 842 OE1 GLN A 107 -36.614 9.454 65.587 1.00 42.80 A O
+ATOM 843 N PRO A 108 -33.136 8.678 63.540 1.00 32.40 A N
+ATOM 844 CA PRO A 108 -32.407 7.553 62.945 1.00 33.04 A C
+ATOM 845 C PRO A 108 -33.084 7.093 61.663 1.00 31.54 A C
+ATOM 846 O PRO A 108 -34.312 7.033 61.573 1.00 30.44 A O
+ATOM 847 CB PRO A 108 -32.466 6.477 64.034 1.00 33.49 A C
+ATOM 848 CG PRO A 108 -32.630 7.241 65.303 1.00 35.33 A C
+ATOM 849 CD PRO A 108 -33.472 8.435 64.954 1.00 38.44 A C
+ATOM 850 N GLY A 109 -32.267 6.778 60.660 1.00 30.37 A N
+ATOM 851 CA GLY A 109 -32.757 6.413 59.353 1.00 31.93 A C
+ATOM 852 C GLY A 109 -32.860 7.561 58.373 1.00 36.89 A C
+ATOM 853 O GLY A 109 -32.925 7.320 57.161 1.00 34.94 A O
+ATOM 854 N GLN A 110 -32.882 8.799 58.858 1.00 34.68 A N
+ATOM 855 CA GLN A 110 -32.911 9.958 57.984 1.00 28.85 A C
+ATOM 856 C GLN A 110 -31.503 10.294 57.503 1.00 33.18 A C
+ATOM 857 O GLN A 110 -30.500 9.919 58.116 1.00 31.04 A O
+ATOM 858 CB GLN A 110 -33.526 11.160 58.700 1.00 32.11 A C
+ATOM 859 CG GLN A 110 -35.021 11.034 58.939 1.00 34.62 A C
+ATOM 860 CD GLN A 110 -35.781 10.671 57.679 1.00 48.98 A C
+ATOM 861 NE2 GLN A 110 -35.857 11.610 56.743 1.00 47.85 A N
+ATOM 862 OE1 GLN A 110 -36.293 9.559 57.548 1.00 50.45 A O
+ATOM 863 N THR A 111 -31.438 11.013 56.388 1.00 30.03 A N
+ATOM 864 CA THR A 111 -30.174 11.341 55.749 1.00 31.68 A C
+ATOM 865 C THR A 111 -29.918 12.841 55.794 1.00 26.77 A C
+ATOM 866 O THR A 111 -30.797 13.645 56.118 1.00 28.89 A O
+ATOM 867 CB THR A 111 -30.151 10.848 54.298 1.00 33.24 A C
+ATOM 868 CG2 THR A 111 -30.191 9.330 54.253 1.00 30.08 A C
+ATOM 869 OG1 THR A 111 -31.279 11.377 53.591 1.00 31.13 A O
+ATOM 870 N PHE A 112 -28.683 13.202 55.458 1.00 25.75 A N
+ATOM 871 CA PHE A 112 -28.249 14.590 55.396 1.00 24.19 A C
+ATOM 872 C PHE A 112 -26.898 14.635 54.701 1.00 25.60 A C
+ATOM 873 O PHE A 112 -26.188 13.628 54.618 1.00 29.54 A O
+ATOM 874 CB PHE A 112 -28.162 15.227 56.788 1.00 25.66 A C
+ATOM 875 CG PHE A 112 -27.238 14.509 57.732 1.00 31.15 A C
+ATOM 876 CD1 PHE A 112 -27.672 13.402 58.442 1.00 33.13 A C
+ATOM 877 CD2 PHE A 112 -25.937 14.949 57.918 1.00 28.12 A C
+ATOM 878 CE1 PHE A 112 -26.826 12.742 59.313 1.00 35.25 A C
+ATOM 879 CE2 PHE A 112 -25.087 14.293 58.788 1.00 33.87 A C
+ATOM 880 CZ PHE A 112 -25.532 13.188 59.486 1.00 32.49 A C
+ATOM 881 N SER A 113 -26.554 15.817 54.203 1.00 27.87 A N
+ATOM 882 CA SER A 113 -25.286 16.046 53.527 1.00 26.39 A C
+ATOM 883 C SER A 113 -24.273 16.620 54.508 1.00 31.32 A C
+ATOM 884 O SER A 113 -24.619 17.427 55.374 1.00 23.80 A O
+ATOM 885 CB SER A 113 -25.460 16.995 52.340 1.00 29.74 A C
+ATOM 886 OG SER A 113 -26.449 16.512 51.449 1.00 31.08 A O
+ATOM 887 N VAL A 114 -23.020 16.198 54.367 1.00 29.58 A N
+ATOM 888 CA VAL A 114 -21.937 16.611 55.249 1.00 29.24 A C
+ATOM 889 C VAL A 114 -20.945 17.436 54.444 1.00 29.20 A C
+ATOM 890 O VAL A 114 -20.467 16.992 53.395 1.00 29.25 A O
+ATOM 891 CB VAL A 114 -21.241 15.399 55.891 1.00 26.68 A C
+ATOM 892 CG1 VAL A 114 -19.953 15.834 56.583 1.00 30.26 A C
+ATOM 893 CG2 VAL A 114 -22.173 14.711 56.873 1.00 26.58 A C
+ATOM 894 N LEU A 115 -20.638 18.631 54.934 1.00 26.73 A N
+ATOM 895 CA LEU A 115 -19.599 19.477 54.354 1.00 28.06 A C
+ATOM 896 C LEU A 115 -18.365 19.348 55.243 1.00 31.91 A C
+ATOM 897 O LEU A 115 -18.268 19.997 56.286 1.00 33.35 A O
+ATOM 898 CB LEU A 115 -20.062 20.926 54.246 1.00 31.46 A C
+ATOM 899 CG LEU A 115 -18.982 21.877 53.731 1.00 34.58 A C
+ATOM 900 CD1 LEU A 115 -18.587 21.434 52.340 1.00 38.33 A C
+ATOM 901 CD2 LEU A 115 -19.451 23.325 53.720 1.00 37.35 A C
+ATOM 902 N ALA A 116 -17.429 18.494 54.841 1.00 28.72 A N
+ATOM 903 CA ALA A 116 -16.209 18.305 55.616 1.00 36.61 A C
+ATOM 904 C ALA A 116 -15.293 19.509 55.429 1.00 36.10 A C
+ATOM 905 O ALA A 116 -14.879 19.816 54.306 1.00 36.85 A O
+ATOM 906 CB ALA A 116 -15.506 17.018 55.194 1.00 35.24 A C
+ATOM 907 N CYS A 117 -14.976 20.189 56.527 1.00 31.42 A N
+ATOM 908 CA CYS A 117 -14.143 21.380 56.496 1.00 35.33 A C
+ATOM 909 C CYS A 117 -12.897 21.176 57.345 1.00 37.63 A C
+ATOM 910 O CYS A 117 -12.895 20.398 58.304 1.00 33.01 A O
+ATOM 911 CB CYS A 117 -14.908 22.610 56.999 1.00 36.22 A C
+ATOM 912 SG CYS A 117 -16.563 22.801 56.305 1.00 50.70 A S
+ATOM 913 N TYR A 118 -11.833 21.886 56.978 1.00 41.48 A N
+ATOM 914 CA TYR A 118 -10.576 21.862 57.717 1.00 38.25 A C
+ATOM 915 C TYR A 118 -10.033 23.280 57.770 1.00 41.43 A C
+ATOM 916 O TYR A 118 -9.813 23.898 56.723 1.00 40.83 A O
+ATOM 917 CB TYR A 118 -9.566 20.912 57.064 1.00 32.92 A C
+ATOM 918 CG TYR A 118 -9.998 19.462 57.089 1.00 37.18 A C
+ATOM 919 CD1 TYR A 118 -10.765 18.928 56.060 1.00 37.78 A C
+ATOM 920 CD2 TYR A 118 -9.644 18.629 58.142 1.00 35.64 A C
+ATOM 921 CE1 TYR A 118 -11.166 17.606 56.080 1.00 35.34 A C
+ATOM 922 CE2 TYR A 118 -10.039 17.304 58.170 1.00 37.65 A C
+ATOM 923 CZ TYR A 118 -10.800 16.798 57.136 1.00 37.82 A C
+ATOM 924 OH TYR A 118 -11.196 15.481 57.160 1.00 39.89 A O
+ATOM 925 N ASN A 119 -9.826 23.791 58.986 1.00 44.86 A N
+ATOM 926 CA ASN A 119 -9.350 25.159 59.202 1.00 42.76 A C
+ATOM 927 C ASN A 119 -10.291 26.181 58.567 1.00 41.56 A C
+ATOM 928 O ASN A 119 -9.857 27.147 57.936 1.00 39.63 A O
+ATOM 929 CB ASN A 119 -7.920 25.337 58.687 1.00 49.38 A C
+ATOM 930 CG ASN A 119 -6.915 24.506 59.460 1.00 51.44 A C
+ATOM 931 ND2 ASN A 119 -6.392 25.069 60.544 1.00 48.44 A N
+ATOM 932 OD1 ASN A 119 -6.614 23.372 59.090 1.00 56.00 A O
+ATOM 933 N GLY A 120 -11.594 25.964 58.736 1.00 39.01 A N
+ATOM 934 CA GLY A 120 -12.598 26.855 58.194 1.00 36.10 A C
+ATOM 935 C GLY A 120 -12.758 26.823 56.691 1.00 42.88 A C
+ATOM 936 O GLY A 120 -13.523 27.632 56.153 1.00 41.11 A O
+ATOM 937 N SER A 121 -12.073 25.920 55.994 1.00 37.25 A N
+ATOM 938 CA SER A 121 -12.134 25.844 54.539 1.00 41.19 A C
+ATOM 939 C SER A 121 -12.780 24.531 54.120 1.00 42.94 A C
+ATOM 940 O SER A 121 -12.235 23.454 54.418 1.00 38.68 A O
+ATOM 941 CB SER A 121 -10.737 25.972 53.929 1.00 39.49 A C
+ATOM 942 OG SER A 121 -10.804 26.471 52.605 1.00 58.46 A O
+ATOM 943 N PRO A 122 -13.928 24.561 53.445 1.00 45.78 A N
+ATOM 944 CA PRO A 122 -14.554 23.310 52.997 1.00 41.91 A C
+ATOM 945 C PRO A 122 -13.688 22.585 51.977 1.00 41.77 A C
+ATOM 946 O PRO A 122 -13.072 23.202 51.104 1.00 44.19 A O
+ATOM 947 CB PRO A 122 -15.877 23.779 52.379 1.00 45.61 A C
+ATOM 948 CG PRO A 122 -16.126 25.132 52.974 1.00 48.15 A C
+ATOM 949 CD PRO A 122 -14.771 25.736 53.169 1.00 44.74 A C
+ATOM 950 N SER A 123 -13.646 21.256 52.093 1.00 40.84 A N
+ATOM 951 CA SER A 123 -12.852 20.428 51.199 1.00 40.73 A C
+ATOM 952 C SER A 123 -13.640 19.332 50.498 1.00 39.49 A C
+ATOM 953 O SER A 123 -13.140 18.779 49.512 1.00 37.35 A O
+ATOM 954 CB SER A 123 -11.685 19.777 51.960 1.00 42.66 A C
+ATOM 955 OG SER A 123 -12.107 18.608 52.639 1.00 40.82 A O
+ATOM 956 N GLY A 124 -14.838 19.001 50.965 1.00 34.94 A N
+ATOM 957 CA GLY A 124 -15.622 17.959 50.331 1.00 36.97 A C
+ATOM 958 C GLY A 124 -17.024 17.915 50.891 1.00 35.80 A C
+ATOM 959 O GLY A 124 -17.290 18.400 51.996 1.00 34.45 A O
+ATOM 960 N VAL A 125 -17.922 17.321 50.108 1.00 28.17 A N
+ATOM 961 CA VAL A 125 -19.322 17.178 50.492 1.00 28.26 A C
+ATOM 962 C VAL A 125 -19.792 15.780 50.111 1.00 31.29 A C
+ATOM 963 O VAL A 125 -19.449 15.266 49.041 1.00 30.39 A O
+ATOM 964 CB VAL A 125 -20.205 18.269 49.846 1.00 34.00 A C
+ATOM 965 CG1 VAL A 125 -20.116 18.216 48.329 1.00 34.39 A C
+ATOM 966 CG2 VAL A 125 -21.649 18.144 50.315 1.00 32.78 A C
+ATOM 967 N TYR A 126 -20.561 15.155 51.001 1.00 29.87 A N
+ATOM 968 CA TYR A 126 -21.078 13.816 50.757 1.00 27.60 A C
+ATOM 969 C TYR A 126 -22.326 13.610 51.601 1.00 30.08 A C
+ATOM 970 O TYR A 126 -22.582 14.348 52.557 1.00 29.92 A O
+ATOM 971 CB TYR A 126 -20.029 12.739 51.064 1.00 29.36 A C
+ATOM 972 CG TYR A 126 -19.484 12.790 52.475 1.00 31.82 A C
+ATOM 973 CD1 TYR A 126 -18.368 13.557 52.782 1.00 36.26 A C
+ATOM 974 CD2 TYR A 126 -20.084 12.070 53.500 1.00 33.37 A C
+ATOM 975 CE1 TYR A 126 -17.866 13.607 54.069 1.00 33.14 A C
+ATOM 976 CE2 TYR A 126 -19.589 12.115 54.789 1.00 33.73 A C
+ATOM 977 CZ TYR A 126 -18.481 12.884 55.068 1.00 32.44 A C
+ATOM 978 OH TYR A 126 -17.986 12.931 56.351 1.00 34.56 A O
+ATOM 979 N GLN A 127 -23.097 12.590 51.236 1.00 26.24 A N
+ATOM 980 CA GLN A 127 -24.341 12.272 51.923 1.00 29.01 A C
+ATOM 981 C GLN A 127 -24.090 11.281 53.053 1.00 36.22 A C
+ATOM 982 O GLN A 127 -23.270 10.367 52.926 1.00 34.05 A O
+ATOM 983 CB GLN A 127 -25.365 11.701 50.940 1.00 35.77 A C
+ATOM 984 CG GLN A 127 -26.783 11.617 51.485 1.00 35.54 A C
+ATOM 985 CD GLN A 127 -27.555 12.914 51.326 1.00 36.56 A C
+ATOM 986 NE2 GLN A 127 -28.879 12.813 51.296 1.00 39.16 A N
+ATOM 987 OE1 GLN A 127 -26.970 13.994 51.231 1.00 39.37 A O
+ATOM 988 N CYS A 128 -24.805 11.471 54.160 1.00 34.64 A N
+ATOM 989 CA CYS A 128 -24.686 10.612 55.328 1.00 36.77 A C
+ATOM 990 C CYS A 128 -26.075 10.273 55.846 1.00 37.19 A C
+ATOM 991 O CYS A 128 -27.039 11.008 55.624 1.00 34.84 A O
+ATOM 992 CB CYS A 128 -23.862 11.274 56.441 1.00 38.70 A C
+ATOM 993 SG CYS A 128 -22.145 10.732 56.529 1.00 50.17 A S
+ATOM 994 N ALA A 129 -26.166 9.147 56.549 1.00 36.72 A N
+ATOM 995 CA ALA A 129 -27.407 8.712 57.171 1.00 34.50 A C
+ATOM 996 C ALA A 129 -27.171 8.455 58.650 1.00 38.35 A C
+ATOM 997 O ALA A 129 -26.155 7.867 59.034 1.00 35.86 A O
+ATOM 998 CB ALA A 129 -27.959 7.447 56.504 1.00 35.38 A C
+ATOM 999 N MET A 130 -28.110 8.903 59.478 1.00 31.95 A N
+ATOM 1000 CA MET A 130 -28.039 8.638 60.908 1.00 34.80 A C
+ATOM 1001 C MET A 130 -28.416 7.185 61.173 1.00 34.79 A C
+ATOM 1002 O MET A 130 -29.550 6.772 60.908 1.00 32.27 A O
+ATOM 1003 CB MET A 130 -28.963 9.587 61.667 1.00 34.04 A C
+ATOM 1004 CG MET A 130 -28.954 9.416 63.181 1.00 37.20 A C
+ATOM 1005 SD MET A 130 -27.369 9.810 63.951 1.00 39.63 A S
+ATOM 1006 CE MET A 130 -27.092 11.482 63.378 1.00 29.75 A C
+ATOM 1007 N ARG A 131 -27.462 6.409 61.682 1.00 31.26 A N
+ATOM 1008 CA ARG A 131 -27.706 5.007 61.960 1.00 27.15 A C
+ATOM 1009 C ARG A 131 -28.658 4.859 63.146 1.00 31.08 A C
+ATOM 1010 O ARG A 131 -28.791 5.770 63.966 1.00 31.54 A O
+ATOM 1011 CB ARG A 131 -26.390 4.285 62.245 1.00 29.07 A C
+ATOM 1012 CG ARG A 131 -25.361 4.385 61.129 1.00 34.50 A C
+ATOM 1013 CD ARG A 131 -25.937 3.938 59.800 1.00 31.99 A C
+ATOM 1014 NE ARG A 131 -26.509 2.598 59.876 1.00 34.57 A N
+ATOM 1015 CZ ARG A 131 -27.092 1.978 58.856 1.00 40.72 A C
+ATOM 1016 NH1 ARG A 131 -27.182 2.579 57.677 1.00 35.13 A N1+
+ATOM 1017 NH2 ARG A 131 -27.587 0.758 59.013 1.00 34.74 A N
+ATOM 1018 N PRO A 132 -29.344 3.717 63.248 1.00 31.94 A N
+ATOM 1019 CA PRO A 132 -30.232 3.495 64.402 1.00 32.67 A C
+ATOM 1020 C PRO A 132 -29.533 3.587 65.749 1.00 30.17 A C
+ATOM 1021 O PRO A 132 -30.204 3.849 66.755 1.00 34.15 A O
+ATOM 1022 CB PRO A 132 -30.783 2.086 64.151 1.00 35.36 A C
+ATOM 1023 CG PRO A 132 -30.727 1.929 62.669 1.00 30.83 A C
+ATOM 1024 CD PRO A 132 -29.499 2.670 62.222 1.00 31.83 A C
+ATOM 1025 N ASN A 133 -28.217 3.378 65.809 1.00 28.62 A N
+ATOM 1026 CA ASN A 133 -27.464 3.550 67.044 1.00 32.37 A C
+ATOM 1027 C ASN A 133 -26.894 4.959 67.189 1.00 31.42 A C
+ATOM 1028 O ASN A 133 -25.970 5.166 67.985 1.00 32.54 A O
+ATOM 1029 CB ASN A 133 -26.348 2.504 67.139 1.00 31.04 A C
+ATOM 1030 CG ASN A 133 -25.351 2.592 65.996 1.00 34.72 A C
+ATOM 1031 ND2 ASN A 133 -24.429 1.638 65.948 1.00 34.83 A N
+ATOM 1032 OD1 ASN A 133 -25.406 3.501 65.169 1.00 33.90 A O
+ATOM 1033 N PHE A 134 -27.417 5.918 66.422 1.00 26.93 A N
+ATOM 1034 CA PHE A 134 -27.065 7.335 66.535 1.00 30.85 A C
+ATOM 1035 C PHE A 134 -25.603 7.605 66.190 1.00 30.75 A C
+ATOM 1036 O PHE A 134 -24.990 8.534 66.723 1.00 37.79 A O
+ATOM 1037 CB PHE A 134 -27.390 7.880 67.927 1.00 30.04 A C
+ATOM 1038 CG PHE A 134 -28.851 7.841 68.270 1.00 28.50 A C
+ATOM 1039 CD1 PHE A 134 -29.719 8.797 67.770 1.00 32.28 A C
+ATOM 1040 CD2 PHE A 134 -29.356 6.849 69.094 1.00 31.25 A C
+ATOM 1041 CE1 PHE A 134 -31.064 8.766 68.084 1.00 30.50 A C
+ATOM 1042 CE2 PHE A 134 -30.701 6.812 69.413 1.00 34.66 A C
+ATOM 1043 CZ PHE A 134 -31.556 7.772 68.906 1.00 39.29 A C
+ATOM 1044 N THR A 135 -25.031 6.806 65.298 1.00 29.58 A N
+ATOM 1045 CA THR A 135 -23.727 7.085 64.718 1.00 28.22 A C
+ATOM 1046 C THR A 135 -23.886 7.364 63.230 1.00 32.13 A C
+ATOM 1047 O THR A 135 -24.944 7.136 62.639 1.00 31.70 A O
+ATOM 1048 CB THR A 135 -22.756 5.918 64.938 1.00 32.25 A C
+ATOM 1049 CG2 THR A 135 -22.584 5.641 66.420 1.00 30.07 A C
+ATOM 1050 OG1 THR A 135 -23.259 4.744 64.289 1.00 31.33 A O
+ATOM 1051 N ILE A 136 -22.820 7.880 62.625 1.00 28.12 A N
+ATOM 1052 CA ILE A 136 -22.771 8.078 61.184 1.00 32.40 A C
+ATOM 1053 C ILE A 136 -21.455 7.521 60.664 1.00 33.86 A C
+ATOM 1054 O ILE A 136 -20.433 7.535 61.358 1.00 29.44 A O
+ATOM 1055 CB ILE A 136 -22.935 9.563 60.777 1.00 30.33 A C
+ATOM 1056 CG1 ILE A 136 -21.760 10.402 61.281 1.00 31.67 A C
+ATOM 1057 CG2 ILE A 136 -24.257 10.122 61.286 1.00 31.37 A C
+ATOM 1058 CD1 ILE A 136 -21.685 11.774 60.648 1.00 32.53 A C
+ATOM 1059 N LYS A 137 -21.491 7.011 59.436 1.00 33.03 A N
+ATOM 1060 CA LYS A 137 -20.306 6.485 58.764 1.00 34.40 A C
+ATOM 1061 C LYS A 137 -19.824 7.561 57.797 1.00 36.09 A C
+ATOM 1062 O LYS A 137 -20.184 7.575 56.620 1.00 37.73 A O
+ATOM 1063 CB LYS A 137 -20.615 5.173 58.052 1.00 39.92 A C
+ATOM 1064 CG LYS A 137 -20.622 3.960 58.968 1.00 42.67 A C
+ATOM 1065 CD LYS A 137 -21.819 3.065 58.694 1.00 48.77 A C
+ATOM 1066 CE LYS A 137 -21.664 1.713 59.370 1.00 47.32 A C
+ATOM 1067 NZ LYS A 137 -22.790 0.796 59.040 1.00 54.99 A N1+
+ATOM 1068 N GLY A 138 -19.006 8.480 58.310 1.00 38.65 A N
+ATOM 1069 CA GLY A 138 -18.490 9.579 57.540 1.00 31.62 A C
+ATOM 1070 C GLY A 138 -17.015 9.433 57.225 1.00 32.08 A C
+ATOM 1071 O GLY A 138 -16.431 8.347 57.314 1.00 36.03 A O
+ATOM 1072 N SER A 139 -16.406 10.554 56.841 1.00 30.94 A N
+ATOM 1073 CA SER A 139 -14.974 10.612 56.546 1.00 34.67 A C
+ATOM 1074 C SER A 139 -14.441 11.890 57.186 1.00 35.77 A C
+ATOM 1075 O SER A 139 -14.612 12.983 56.638 1.00 34.43 A O
+ATOM 1076 CB SER A 139 -14.714 10.584 55.045 1.00 32.16 A C
+ATOM 1077 OG SER A 139 -13.436 11.114 54.738 1.00 38.59 A O
+ATOM 1078 N PHE A 140 -13.801 11.748 58.344 1.00 35.40 A N
+ATOM 1079 CA PHE A 140 -13.339 12.882 59.131 1.00 32.87 A C
+ATOM 1080 C PHE A 140 -11.914 12.636 59.601 1.00 35.47 A C
+ATOM 1081 O PHE A 140 -11.601 11.554 60.109 1.00 36.85 A O
+ATOM 1082 CB PHE A 140 -14.252 13.122 60.337 1.00 30.41 A C
+ATOM 1083 CG PHE A 140 -15.641 13.561 59.972 1.00 31.56 A C
+ATOM 1084 CD1 PHE A 140 -15.874 14.835 59.480 1.00 31.97 A C
+ATOM 1085 CD2 PHE A 140 -16.716 12.702 60.129 1.00 29.36 A C
+ATOM 1086 CE1 PHE A 140 -17.153 15.243 59.148 1.00 27.22 A C
+ATOM 1087 CE2 PHE A 140 -17.997 13.103 59.798 1.00 31.61 A C
+ATOM 1088 CZ PHE A 140 -18.215 14.376 59.308 1.00 31.05 A C
+ATOM 1089 N LEU A 141 -11.059 13.638 59.435 1.00 34.91 A N
+ATOM 1090 CA LEU A 141 -9.684 13.609 59.906 1.00 39.01 A C
+ATOM 1091 C LEU A 141 -9.519 14.591 61.062 1.00 40.38 A C
+ATOM 1092 O LEU A 141 -10.482 15.206 61.530 1.00 36.02 A O
+ATOM 1093 CB LEU A 141 -8.716 13.934 58.766 1.00 41.14 A C
+ATOM 1094 CG LEU A 141 -8.832 13.083 57.500 1.00 46.39 A C
+ATOM 1095 CD1 LEU A 141 -7.882 13.589 56.425 1.00 48.33 A C
+ATOM 1096 CD2 LEU A 141 -8.563 11.619 57.811 1.00 44.19 A C
+ATOM 1097 N ASN A 142 -8.278 14.733 61.524 1.00 43.31 A N
+ATOM 1098 CA ASN A 142 -7.978 15.712 62.559 1.00 43.18 A C
+ATOM 1099 C ASN A 142 -8.280 17.118 62.054 1.00 38.14 A C
+ATOM 1100 O ASN A 142 -7.951 17.473 60.919 1.00 41.06 A O
+ATOM 1101 CB ASN A 142 -6.512 15.609 62.983 1.00 38.76 A C
+ATOM 1102 CG ASN A 142 -6.236 14.393 63.847 1.00 50.71 A C
+ATOM 1103 ND2 ASN A 142 -5.048 14.345 64.438 1.00 55.08 A N
+ATOM 1104 OD1 ASN A 142 -7.080 13.508 63.983 1.00 51.97 A O
+ATOM 1105 N GLY A 143 -8.918 17.918 62.905 1.00 39.21 A N
+ATOM 1106 CA GLY A 143 -9.293 19.269 62.548 1.00 38.72 A C
+ATOM 1107 C GLY A 143 -10.611 19.402 61.819 1.00 37.47 A C
+ATOM 1108 O GLY A 143 -10.969 20.518 61.421 1.00 38.50 A O
+ATOM 1109 N SER A 144 -11.343 18.306 61.628 1.00 35.11 A N
+ATOM 1110 CA SER A 144 -12.628 18.343 60.945 1.00 32.51 A C
+ATOM 1111 C SER A 144 -13.788 18.683 61.871 1.00 31.55 A C
+ATOM 1112 O SER A 144 -14.921 18.811 61.394 1.00 30.39 A O
+ATOM 1113 CB SER A 144 -12.901 16.998 60.267 1.00 30.85 A C
+ATOM 1114 OG SER A 144 -13.231 16.013 61.229 1.00 30.21 A O
+ATOM 1115 N CYS A 145 -13.539 18.826 63.171 1.00 31.83 A N
+ATOM 1116 CA CYS A 145 -14.607 19.162 64.101 1.00 29.71 A C
+ATOM 1117 C CYS A 145 -15.167 20.542 63.788 1.00 30.11 A C
+ATOM 1118 O CYS A 145 -14.451 21.446 63.350 1.00 29.28 A O
+ATOM 1119 CB CYS A 145 -14.100 19.110 65.541 1.00 31.75 A C
+ATOM 1120 SG CYS A 145 -14.043 17.445 66.228 1.00 39.68 A S
+ATOM 1121 N GLY A 146 -16.467 20.699 64.023 1.00 24.04 A N
+ATOM 1122 CA GLY A 146 -17.189 21.858 63.556 1.00 27.34 A C
+ATOM 1123 C GLY A 146 -17.833 21.683 62.200 1.00 29.22 A C
+ATOM 1124 O GLY A 146 -18.678 22.506 61.824 1.00 31.51 A O
+ATOM 1125 N SER A 147 -17.454 20.646 61.454 1.00 31.09 A N
+ATOM 1126 CA SER A 147 -18.140 20.326 60.210 1.00 29.06 A C
+ATOM 1127 C SER A 147 -19.613 20.069 60.492 1.00 28.41 A C
+ATOM 1128 O SER A 147 -19.968 19.419 61.478 1.00 29.87 A O
+ATOM 1129 CB SER A 147 -17.507 19.098 59.554 1.00 26.05 A C
+ATOM 1130 OG SER A 147 -16.269 19.423 58.945 1.00 30.42 A O
+ATOM 1131 N VAL A 148 -20.476 20.592 59.628 1.00 25.32 A N
+ATOM 1132 CA VAL A 148 -21.911 20.554 59.865 1.00 26.26 A C
+ATOM 1133 C VAL A 148 -22.584 19.656 58.838 1.00 30.06 A C
+ATOM 1134 O VAL A 148 -22.147 19.544 57.686 1.00 28.78 A O
+ATOM 1135 CB VAL A 148 -22.529 21.969 59.846 1.00 28.80 A C
+ATOM 1136 CG1 VAL A 148 -21.922 22.824 60.950 1.00 30.53 A C
+ATOM 1137 CG2 VAL A 148 -22.327 22.622 58.490 1.00 29.80 A C
+ATOM 1138 N GLY A 149 -23.650 18.994 59.276 1.00 27.96 A N
+ATOM 1139 CA GLY A 149 -24.540 18.274 58.391 1.00 28.23 A C
+ATOM 1140 C GLY A 149 -25.803 19.086 58.180 1.00 31.16 A C
+ATOM 1141 O GLY A 149 -26.241 19.814 59.068 1.00 26.13 A O
+ATOM 1142 N PHE A 150 -26.389 18.963 56.992 1.00 23.38 A N
+ATOM 1143 CA PHE A 150 -27.490 19.848 56.642 1.00 31.49 A C
+ATOM 1144 C PHE A 150 -28.366 19.206 55.578 1.00 30.93 A C
+ATOM 1145 O PHE A 150 -27.928 18.340 54.816 1.00 27.90 A O
+ATOM 1146 CB PHE A 150 -26.972 21.204 56.149 1.00 27.04 A C
+ATOM 1147 CG PHE A 150 -26.192 21.125 54.865 1.00 30.67 A C
+ATOM 1148 CD1 PHE A 150 -24.842 20.814 54.876 1.00 30.93 A C
+ATOM 1149 CD2 PHE A 150 -26.810 21.359 53.646 1.00 32.96 A C
+ATOM 1150 CE1 PHE A 150 -24.122 20.737 53.698 1.00 31.18 A C
+ATOM 1151 CE2 PHE A 150 -26.096 21.284 52.464 1.00 33.04 A C
+ATOM 1152 CZ PHE A 150 -24.750 20.973 52.491 1.00 36.84 A C
+ATOM 1153 N ASN A 151 -29.619 19.653 55.547 1.00 30.01 A N
+ATOM 1154 CA ASN A 151 -30.535 19.417 54.444 1.00 35.52 A C
+ATOM 1155 C ASN A 151 -31.061 20.760 53.956 1.00 36.96 A C
+ATOM 1156 O ASN A 151 -31.091 21.740 54.707 1.00 32.38 A O
+ATOM 1157 CB ASN A 151 -31.705 18.512 54.857 1.00 28.64 A C
+ATOM 1158 CG ASN A 151 -31.300 17.057 54.989 1.00 32.83 A C
+ATOM 1159 ND2 ASN A 151 -31.273 16.559 56.220 1.00 29.52 A N
+ATOM 1160 OD1 ASN A 151 -31.020 16.385 53.996 1.00 34.81 A O
+ATOM 1161 N ILE A 152 -31.466 20.808 52.691 1.00 34.85 A N
+ATOM 1162 CA ILE A 152 -31.988 22.025 52.078 1.00 41.87 A C
+ATOM 1163 C ILE A 152 -33.430 21.754 51.677 1.00 46.04 A C
+ATOM 1164 O ILE A 152 -33.688 21.003 50.728 1.00 52.68 A O
+ATOM 1165 CB ILE A 152 -31.150 22.471 50.873 1.00 40.85 A C
+ATOM 1166 CG1 ILE A 152 -29.720 22.793 51.311 1.00 39.00 A C
+ATOM 1167 CG2 ILE A 152 -31.784 23.682 50.206 1.00 50.84 A C
+ATOM 1168 CD1 ILE A 152 -28.825 23.255 50.183 1.00 43.80 A C
+ATOM 1169 N ASP A 153 -34.371 22.360 52.401 1.00 52.69 A N
+ATOM 1170 CA ASP A 153 -35.790 22.190 52.117 1.00 60.52 A C
+ATOM 1171 C ASP A 153 -36.142 22.824 50.778 1.00 67.41 A C
+ATOM 1172 O ASP A 153 -36.488 22.124 49.821 1.00 75.21 A O
+ATOM 1173 CB ASP A 153 -36.634 22.799 53.240 1.00 65.02 A C
+ATOM 1174 CG ASP A 153 -37.904 22.015 53.504 1.00 75.87 A C
+ATOM 1175 OD1 ASP A 153 -38.568 21.610 52.527 1.00 79.94 A O
+ATOM 1176 OD2 ASP A 153 -38.237 21.804 54.689 1.00 77.44 A O1-
+ATOM 1177 N TYR A 154 -36.061 24.151 50.708 1.00 64.25 A N
+ATOM 1178 CA TYR A 154 -36.246 24.881 49.460 1.00 62.43 A C
+ATOM 1179 C TYR A 154 -35.086 25.848 49.280 1.00 62.70 A C
+ATOM 1180 O TYR A 154 -34.151 25.583 48.517 1.00 64.83 A O
+ATOM 1181 CB TYR A 154 -37.580 25.629 49.462 1.00 64.26 A C
+ATOM 1182 CG TYR A 154 -38.651 24.978 48.620 1.00 76.60 A C
+ATOM 1183 CD1 TYR A 154 -39.239 23.783 49.011 1.00 76.32 A C
+ATOM 1184 CD2 TYR A 154 -39.078 25.561 47.434 1.00 76.70 A C
+ATOM 1185 CE1 TYR A 154 -40.222 23.184 48.244 1.00 81.64 A C
+ATOM 1186 CE2 TYR A 154 -40.060 24.971 46.661 1.00 80.18 A C
+ATOM 1187 CZ TYR A 154 -40.628 23.783 47.070 1.00 86.72 A C
+ATOM 1188 OH TYR A 154 -41.606 23.193 46.302 1.00 86.80 A O
+ATOM 1189 N ASP A 155 -35.146 26.976 49.984 1.00 60.02 A N
+ATOM 1190 CA ASP A 155 -34.013 27.876 50.141 1.00 63.44 A C
+ATOM 1191 C ASP A 155 -33.515 27.902 51.580 1.00 54.86 A C
+ATOM 1192 O ASP A 155 -32.618 28.687 51.905 1.00 53.92 A O
+ATOM 1193 CB ASP A 155 -34.386 29.289 49.689 1.00 63.17 A C
+ATOM 1194 CG ASP A 155 -35.485 29.899 50.537 1.00 67.12 A C
+ATOM 1195 OD1 ASP A 155 -36.403 29.158 50.949 1.00 65.31 A O
+ATOM 1196 OD2 ASP A 155 -35.432 31.120 50.794 1.00 67.10 A O1-
+ATOM 1197 N CYS A 156 -34.076 27.059 52.443 1.00 51.88 A N
+ATOM 1198 CA CYS A 156 -33.808 27.088 53.873 1.00 47.11 A C
+ATOM 1199 C CYS A 156 -32.890 25.929 54.241 1.00 40.27 A C
+ATOM 1200 O CYS A 156 -33.222 24.765 53.995 1.00 40.45 A O
+ATOM 1201 CB CYS A 156 -35.112 27.015 54.665 1.00 48.72 A C
+ATOM 1202 SG CYS A 156 -34.916 26.550 56.396 1.00 55.79 A S
+ATOM 1203 N VAL A 157 -31.744 26.248 54.832 1.00 37.71 A N
+ATOM 1204 CA VAL A 157 -30.794 25.228 55.263 1.00 40.48 A C
+ATOM 1205 C VAL A 157 -31.224 24.697 56.622 1.00 37.91 A C
+ATOM 1206 O VAL A 157 -31.343 25.457 57.591 1.00 37.72 A O
+ATOM 1207 CB VAL A 157 -29.365 25.786 55.319 1.00 39.56 A C
+ATOM 1208 CG1 VAL A 157 -28.378 24.675 55.644 1.00 27.46 A C
+ATOM 1209 CG2 VAL A 157 -29.003 26.458 54.006 1.00 42.10 A C
+ATOM 1210 N SER A 158 -31.451 23.391 56.703 1.00 37.64 A N
+ATOM 1211 CA SER A 158 -31.802 22.730 57.956 1.00 35.25 A C
+ATOM 1212 C SER A 158 -30.540 22.086 58.517 1.00 34.22 A C
+ATOM 1213 O SER A 158 -30.177 20.971 58.135 1.00 33.58 A O
+ATOM 1214 CB SER A 158 -32.911 21.706 57.742 1.00 39.56 A C
+ATOM 1215 OG SER A 158 -34.152 22.344 57.498 1.00 46.93 A O
+ATOM 1216 N PHE A 159 -29.865 22.797 59.418 1.00 30.35 A N
+ATOM 1217 CA PHE A 159 -28.686 22.252 60.075 1.00 28.89 A C
+ATOM 1218 C PHE A 159 -29.103 21.192 61.086 1.00 30.48 A C
+ATOM 1219 O PHE A 159 -29.973 21.431 61.929 1.00 31.69 A O
+ATOM 1220 CB PHE A 159 -27.896 23.363 60.765 1.00 29.95 A C
+ATOM 1221 CG PHE A 159 -27.286 24.355 59.817 1.00 27.12 A C
+ATOM 1222 CD1 PHE A 159 -26.139 24.041 59.107 1.00 23.30 A C
+ATOM 1223 CD2 PHE A 159 -27.857 25.606 59.642 1.00 27.13 A C
+ATOM 1224 CE1 PHE A 159 -25.574 24.954 58.236 1.00 22.49 A C
+ATOM 1225 CE2 PHE A 159 -27.298 26.523 58.772 1.00 21.46 A C
+ATOM 1226 CZ PHE A 159 -26.154 26.197 58.069 1.00 25.42 A C
+ATOM 1227 N CYS A 160 -28.477 20.018 61.007 1.00 27.59 A N
+ATOM 1228 CA CYS A 160 -28.876 18.893 61.837 1.00 29.38 A C
+ATOM 1229 C CYS A 160 -27.729 18.182 62.538 1.00 27.74 A C
+ATOM 1230 O CYS A 160 -27.997 17.319 63.381 1.00 32.03 A O
+ATOM 1231 CB CYS A 160 -29.647 17.861 61.000 1.00 31.79 A C
+ATOM 1232 SG CYS A 160 -28.664 17.112 59.689 1.00 35.39 A S
+ATOM 1233 N TYR A 161 -26.476 18.509 62.235 1.00 29.51 A N
+ATOM 1234 CA TYR A 161 -25.358 17.750 62.774 1.00 24.96 A C
+ATOM 1235 C TYR A 161 -24.121 18.631 62.848 1.00 27.16 A C
+ATOM 1236 O TYR A 161 -23.894 19.470 61.974 1.00 25.90 A O
+ATOM 1237 CB TYR A 161 -25.074 16.515 61.911 1.00 27.30 A C
+ATOM 1238 CG TYR A 161 -23.908 15.673 62.380 1.00 27.33 A C
+ATOM 1239 CD1 TYR A 161 -24.061 14.756 63.411 1.00 24.56 A C
+ATOM 1240 CD2 TYR A 161 -22.659 15.785 61.783 1.00 27.43 A C
+ATOM 1241 CE1 TYR A 161 -23.004 13.980 63.839 1.00 23.21 A C
+ATOM 1242 CE2 TYR A 161 -21.594 15.013 62.205 1.00 21.74 A C
+ATOM 1243 CZ TYR A 161 -21.772 14.113 63.234 1.00 26.15 A C
+ATOM 1244 OH TYR A 161 -20.715 13.340 63.658 1.00 24.39 A O
+ATOM 1245 N MET A 162 -23.334 18.436 63.904 1.00 25.59 A N
+ATOM 1246 CA MET A 162 -22.006 19.022 64.028 1.00 26.04 A C
+ATOM 1247 C MET A 162 -21.066 17.931 64.516 1.00 23.77 A C
+ATOM 1248 O MET A 162 -21.362 17.252 65.504 1.00 23.47 A O
+ATOM 1249 CB MET A 162 -22.000 20.218 64.990 1.00 24.61 A C
+ATOM 1250 CG MET A 162 -20.620 20.824 65.217 1.00 25.23 A C
+ATOM 1251 SD MET A 162 -20.661 22.392 66.114 1.00 33.95 A S
+ATOM 1252 CE MET A 162 -21.109 23.529 64.803 1.00 28.77 A C
+ATOM 1253 N HIS A 163 -19.947 17.753 63.819 1.00 22.67 A N
+ATOM 1254 CA HIS A 163 -19.055 16.637 64.100 1.00 27.27 A C
+ATOM 1255 C HIS A 163 -18.229 16.896 65.353 1.00 26.21 A C
+ATOM 1256 O HIS A 163 -17.765 18.016 65.590 1.00 27.47 A O
+ATOM 1257 CB HIS A 163 -18.129 16.377 62.914 1.00 26.00 A C
+ATOM 1258 CG HIS A 163 -17.215 15.210 63.116 1.00 26.66 A C
+ATOM 1259 CD2 HIS A 163 -15.868 15.106 63.030 1.00 29.24 A C
+ATOM 1260 ND1 HIS A 163 -17.675 13.959 63.466 1.00 26.97 A N
+ATOM 1261 CE1 HIS A 163 -16.651 13.132 63.581 1.00 30.44 A C
+ATOM 1262 NE2 HIS A 163 -15.543 13.804 63.323 1.00 30.00 A N
+ATOM 1263 N HIS A 164 -18.035 15.849 66.145 1.00 26.00 A N
+ATOM 1264 CA HIS A 164 -17.329 15.988 67.414 1.00 34.12 A C
+ATOM 1265 C HIS A 164 -16.213 14.974 67.613 1.00 31.14 A C
+ATOM 1266 O HIS A 164 -15.161 15.336 68.144 1.00 36.46 A O
+ATOM 1267 CB HIS A 164 -18.324 15.889 68.582 1.00 28.25 A C
+ATOM 1268 CG HIS A 164 -19.098 17.148 68.820 1.00 33.09 A C
+ATOM 1269 CD2 HIS A 164 -20.086 17.737 68.106 1.00 29.37 A C
+ATOM 1270 ND1 HIS A 164 -18.888 17.954 69.918 1.00 29.04 A N
+ATOM 1271 CE1 HIS A 164 -19.711 18.985 69.869 1.00 28.86 A C
+ATOM 1272 NE2 HIS A 164 -20.448 18.878 68.777 1.00 31.33 A N
+ATOM 1273 N MET A 165 -16.406 13.719 67.212 1.00 28.31 A N
+ATOM 1274 CA MET A 165 -15.411 12.702 67.535 1.00 34.30 A C
+ATOM 1275 C MET A 165 -15.651 11.445 66.709 1.00 31.53 A C
+ATOM 1276 O MET A 165 -16.653 11.315 66.000 1.00 29.92 A O
+ATOM 1277 CB MET A 165 -15.435 12.364 69.027 1.00 39.09 A C
+ATOM 1278 CG MET A 165 -16.781 11.878 69.510 1.00 36.67 A C
+ATOM 1279 SD MET A 165 -16.725 11.270 71.202 1.00 60.86 A S
+ATOM 1280 CE MET A 165 -18.459 10.934 71.465 1.00 42.06 A C
+ATOM 1281 N GLU A 166 -14.706 10.515 66.826 1.00 29.94 A N
+ATOM 1282 CA GLU A 166 -14.746 9.219 66.167 1.00 28.52 A C
+ATOM 1283 C GLU A 166 -14.686 8.122 67.218 1.00 33.40 A C
+ATOM 1284 O GLU A 166 -13.884 8.192 68.156 1.00 30.18 A O
+ATOM 1285 CB GLU A 166 -13.578 9.064 65.189 1.00 29.90 A C
+ATOM 1286 CG GLU A 166 -13.555 7.770 64.398 1.00 36.08 A C
+ATOM 1287 CD GLU A 166 -12.432 7.748 63.378 1.00 45.17 A C
+ATOM 1288 OE1 GLU A 166 -11.440 7.019 63.595 1.00 50.70 A O
+ATOM 1289 OE2 GLU A 166 -12.536 8.469 62.363 1.00 40.54 A O1-
+ATOM 1290 N LEU A 167 -15.536 7.116 67.061 1.00 31.24 A N
+ATOM 1291 CA LEU A 167 -15.557 5.995 67.983 1.00 31.34 A C
+ATOM 1292 C LEU A 167 -14.508 4.960 67.582 1.00 37.94 A C
+ATOM 1293 O LEU A 167 -14.042 4.948 66.439 1.00 38.96 A O
+ATOM 1294 CB LEU A 167 -16.951 5.377 68.012 1.00 30.02 A C
+ATOM 1295 CG LEU A 167 -18.065 6.349 68.410 1.00 32.99 A C
+ATOM 1296 CD1 LEU A 167 -19.406 5.641 68.485 1.00 35.09 A C
+ATOM 1297 CD2 LEU A 167 -17.742 7.034 69.731 1.00 38.72 A C
+ATOM 1298 N PRO A 168 -14.101 4.090 68.515 1.00 40.04 A N
+ATOM 1299 CA PRO A 168 -13.058 3.099 68.191 1.00 37.38 A C
+ATOM 1300 C PRO A 168 -13.368 2.232 66.981 1.00 42.32 A C
+ATOM 1301 O PRO A 168 -12.436 1.774 66.307 1.00 43.53 A O
+ATOM 1302 CB PRO A 168 -12.975 2.260 69.473 1.00 41.24 A C
+ATOM 1303 CG PRO A 168 -13.394 3.190 70.551 1.00 45.84 A C
+ATOM 1304 CD PRO A 168 -14.451 4.071 69.947 1.00 33.25 A C
+ATOM 1305 N THR A 169 -14.643 1.994 66.680 1.00 40.94 A N
+ATOM 1306 CA THR A 169 -15.014 1.178 65.531 1.00 38.12 A C
+ATOM 1307 C THR A 169 -14.893 1.920 64.206 1.00 39.50 A C
+ATOM 1308 O THR A 169 -15.177 1.330 63.158 1.00 39.33 A O
+ATOM 1309 CB THR A 169 -16.446 0.658 65.692 1.00 43.58 A C
+ATOM 1310 CG2 THR A 169 -16.511 -0.390 66.795 1.00 42.72 A C
+ATOM 1311 OG1 THR A 169 -17.318 1.747 66.019 1.00 42.26 A O
+ATOM 1312 N GLY A 170 -14.482 3.187 64.220 1.00 39.12 A N
+ATOM 1313 CA GLY A 170 -14.354 3.965 63.009 1.00 38.41 A C
+ATOM 1314 C GLY A 170 -15.560 4.807 62.656 1.00 36.73 A C
+ATOM 1315 O GLY A 170 -15.482 5.605 61.713 1.00 39.19 A O
+ATOM 1316 N VAL A 171 -16.673 4.654 63.372 1.00 32.47 A N
+ATOM 1317 CA VAL A 171 -17.859 5.467 63.130 1.00 29.31 A C
+ATOM 1318 C VAL A 171 -17.684 6.804 63.837 1.00 37.09 A C
+ATOM 1319 O VAL A 171 -16.757 6.980 64.635 1.00 30.46 A O
+ATOM 1320 CB VAL A 171 -19.140 4.752 63.594 1.00 31.56 A C
+ATOM 1321 CG1 VAL A 171 -19.397 3.520 62.739 1.00 42.63 A C
+ATOM 1322 CG2 VAL A 171 -19.039 4.380 65.062 1.00 35.89 A C
+ATOM 1323 N HIS A 172 -18.573 7.750 63.554 1.00 33.02 A N
+ATOM 1324 CA HIS A 172 -18.444 9.111 64.049 1.00 29.85 A C
+ATOM 1325 C HIS A 172 -19.693 9.516 64.819 1.00 28.73 A C
+ATOM 1326 O HIS A 172 -20.794 9.023 64.557 1.00 28.16 A O
+ATOM 1327 CB HIS A 172 -18.188 10.085 62.898 1.00 26.76 A C
+ATOM 1328 CG HIS A 172 -16.989 9.734 62.074 1.00 28.76 A C
+ATOM 1329 CD2 HIS A 172 -15.678 10.030 62.237 1.00 29.36 A C
+ATOM 1330 ND1 HIS A 172 -17.070 8.967 60.931 1.00 29.32 A N
+ATOM 1331 CE1 HIS A 172 -15.861 8.814 60.420 1.00 32.44 A C
+ATOM 1332 NE2 HIS A 172 -14.998 9.449 61.194 1.00 33.77 A N
+ATOM 1333 N ALA A 173 -19.507 10.418 65.779 1.00 29.16 A N
+ATOM 1334 CA ALA A 173 -20.584 10.891 66.630 1.00 26.75 A C
+ATOM 1335 C ALA A 173 -20.528 12.406 66.731 1.00 26.43 A C
+ATOM 1336 O ALA A 173 -19.460 13.014 66.626 1.00 28.60 A O
+ATOM 1337 CB ALA A 173 -20.510 10.272 68.034 1.00 32.55 A C
+ATOM 1338 N GLY A 174 -21.691 13.009 66.934 1.00 26.18 A N
+ATOM 1339 CA GLY A 174 -21.774 14.443 67.066 1.00 26.05 A C
+ATOM 1340 C GLY A 174 -23.081 14.855 67.700 1.00 24.76 A C
+ATOM 1341 O GLY A 174 -23.815 14.031 68.247 1.00 24.68 A O
+ATOM 1342 N THR A 175 -23.363 16.149 67.615 1.00 16.91 A N
+ATOM 1343 CA THR A 175 -24.546 16.742 68.216 1.00 19.69 A C
+ATOM 1344 C THR A 175 -25.379 17.433 67.146 1.00 24.03 A C
+ATOM 1345 O THR A 175 -24.942 17.622 66.008 1.00 25.67 A O
+ATOM 1346 CB THR A 175 -24.167 17.756 69.306 1.00 24.54 A C
+ATOM 1347 CG2 THR A 175 -23.072 17.203 70.202 1.00 20.58 A C
+ATOM 1348 OG1 THR A 175 -23.698 18.964 68.692 1.00 26.54 A O
+ATOM 1349 N ASP A 176 -26.597 17.810 67.524 1.00 25.13 A N
+ATOM 1350 CA ASP A 176 -27.340 18.787 66.746 1.00 29.00 A C
+ATOM 1351 C ASP A 176 -26.767 20.177 67.025 1.00 33.50 A C
+ATOM 1352 O ASP A 176 -25.829 20.342 67.810 1.00 30.82 A O
+ATOM 1353 CB ASP A 176 -28.833 18.706 67.062 1.00 27.46 A C
+ATOM 1354 CG ASP A 176 -29.127 18.779 68.551 1.00 37.54 A C
+ATOM 1355 OD1 ASP A 176 -28.308 19.340 69.309 1.00 34.75 A O
+ATOM 1356 OD2 ASP A 176 -30.193 18.278 68.967 1.00 40.56 A O1-
+ATOM 1357 N LEU A 177 -27.336 21.196 66.384 1.00 31.64 A N
+ATOM 1358 CA LEU A 177 -26.765 22.531 66.521 1.00 33.12 A C
+ATOM 1359 C LEU A 177 -27.097 23.194 67.852 1.00 32.72 A C
+ATOM 1360 O LEU A 177 -26.627 24.310 68.094 1.00 33.84 A O
+ATOM 1361 CB LEU A 177 -27.213 23.423 65.359 1.00 27.51 A C
+ATOM 1362 CG LEU A 177 -26.192 23.530 64.223 1.00 33.83 A C
+ATOM 1363 CD1 LEU A 177 -24.893 24.130 64.742 1.00 35.02 A C
+ATOM 1364 CD2 LEU A 177 -25.936 22.174 63.580 1.00 35.14 A C
+ATOM 1365 N GLU A 178 -27.881 22.545 68.708 1.00 36.73 A N
+ATOM 1366 CA GLU A 178 -28.137 23.000 70.069 1.00 36.85 A C
+ATOM 1367 C GLU A 178 -27.211 22.346 71.086 1.00 38.02 A C
+ATOM 1368 O GLU A 178 -27.408 22.527 72.293 1.00 34.89 A O
+ATOM 1369 CB GLU A 178 -29.596 22.728 70.455 1.00 41.16 A C
+ATOM 1370 CG GLU A 178 -30.603 22.994 69.339 1.00 47.87 A C
+ATOM 1371 CD GLU A 178 -31.132 24.411 69.373 1.00 55.20 A C
+ATOM 1372 OE1 GLU A 178 -30.472 25.274 69.991 1.00 59.22 A O
+ATOM 1373 OE2 GLU A 178 -32.202 24.659 68.777 1.00 54.25 A O1-
+ATOM 1374 N GLY A 179 -26.234 21.562 70.630 1.00 30.25 A N
+ATOM 1375 CA GLY A 179 -25.243 20.969 71.502 1.00 31.66 A C
+ATOM 1376 C GLY A 179 -25.615 19.635 72.107 1.00 32.94 A C
+ATOM 1377 O GLY A 179 -24.836 19.097 72.903 1.00 31.20 A O
+ATOM 1378 N ASN A 180 -26.770 19.079 71.762 1.00 30.48 A N
+ATOM 1379 CA ASN A 180 -27.215 17.821 72.345 1.00 28.25 A C
+ATOM 1380 C ASN A 180 -26.740 16.665 71.474 1.00 30.27 A C
+ATOM 1381 O ASN A 180 -27.064 16.602 70.282 1.00 27.11 A O
+ATOM 1382 CB ASN A 180 -28.734 17.811 72.497 1.00 33.31 A C
+ATOM 1383 CG ASN A 180 -29.230 18.923 73.398 1.00 35.42 A C
+ATOM 1384 ND2 ASN A 180 -29.981 19.855 72.827 1.00 37.17 A N
+ATOM 1385 OD1 ASN A 180 -28.937 18.946 74.594 1.00 31.56 A O
+ATOM 1386 N PHE A 181 -25.981 15.753 72.077 1.00 24.02 A N
+ATOM 1387 CA PHE A 181 -25.398 14.642 71.338 1.00 28.64 A C
+ATOM 1388 C PHE A 181 -26.479 13.740 70.757 1.00 27.74 A C
+ATOM 1389 O PHE A 181 -27.564 13.582 71.323 1.00 27.75 A O
+ATOM 1390 CB PHE A 181 -24.481 13.819 72.247 1.00 26.92 A C
+ATOM 1391 CG PHE A 181 -23.017 14.038 71.995 1.00 26.64 A C
+ATOM 1392 CD1 PHE A 181 -22.363 13.354 70.983 1.00 25.04 A C
+ATOM 1393 CD2 PHE A 181 -22.293 14.923 72.777 1.00 26.06 A C
+ATOM 1394 CE1 PHE A 181 -21.015 13.554 70.752 1.00 27.50 A C
+ATOM 1395 CE2 PHE A 181 -20.946 15.127 72.550 1.00 29.98 A C
+ATOM 1396 CZ PHE A 181 -20.306 14.442 71.537 1.00 29.14 A C
+ATOM 1397 N TYR A 182 -26.172 13.150 69.604 1.00 29.30 A N
+ATOM 1398 CA TYR A 182 -26.962 12.046 69.071 1.00 25.62 A C
+ATOM 1399 C TYR A 182 -26.467 10.762 69.725 1.00 24.04 A C
+ATOM 1400 O TYR A 182 -25.329 10.342 69.494 1.00 28.52 A O
+ATOM 1401 CB TYR A 182 -26.837 11.965 67.552 1.00 26.72 A C
+ATOM 1402 CG TYR A 182 -27.578 13.040 66.788 1.00 25.22 A C
+ATOM 1403 CD1 TYR A 182 -28.946 12.945 66.566 1.00 23.72 A C
+ATOM 1404 CD2 TYR A 182 -26.905 14.139 66.271 1.00 23.16 A C
+ATOM 1405 CE1 TYR A 182 -29.624 13.923 65.860 1.00 28.59 A C
+ATOM 1406 CE2 TYR A 182 -27.575 15.121 65.564 1.00 22.77 A C
+ATOM 1407 CZ TYR A 182 -28.934 15.008 65.362 1.00 24.08 A C
+ATOM 1408 OH TYR A 182 -29.603 15.983 64.659 1.00 27.97 A O
+ATOM 1409 N GLY A 183 -27.305 10.147 70.556 1.00 25.88 A N
+ATOM 1410 CA GLY A 183 -26.962 8.895 71.186 1.00 27.44 A C
+ATOM 1411 C GLY A 183 -26.318 9.060 72.547 1.00 28.90 A C
+ATOM 1412 O GLY A 183 -26.182 10.171 73.068 1.00 29.68 A O
+ATOM 1413 N PRO A 184 -25.898 7.935 73.152 1.00 30.61 A N
+ATOM 1414 CA PRO A 184 -25.339 7.951 74.509 1.00 35.89 A C
+ATOM 1415 C PRO A 184 -23.844 8.253 74.541 1.00 36.43 A C
+ATOM 1416 O PRO A 184 -23.060 7.562 75.201 1.00 45.10 A O
+ATOM 1417 CB PRO A 184 -25.635 6.528 75.004 1.00 24.72 A C
+ATOM 1418 CG PRO A 184 -25.508 5.698 73.760 1.00 30.83 A C
+ATOM 1419 CD PRO A 184 -25.977 6.568 72.606 1.00 30.89 A C
+ATOM 1420 N PHE A 185 -23.436 9.298 73.830 1.00 27.29 A N
+ATOM 1421 CA PHE A 185 -22.032 9.643 73.683 1.00 32.30 A C
+ATOM 1422 C PHE A 185 -21.727 10.963 74.380 1.00 36.71 A C
+ATOM 1423 O PHE A 185 -22.596 11.829 74.517 1.00 31.19 A O
+ATOM 1424 CB PHE A 185 -21.649 9.727 72.203 1.00 32.57 A C
+ATOM 1425 CG PHE A 185 -22.037 8.512 71.409 1.00 36.05 A C
+ATOM 1426 CD1 PHE A 185 -21.517 7.268 71.722 1.00 34.58 A C
+ATOM 1427 CD2 PHE A 185 -22.924 8.614 70.350 1.00 26.99 A C
+ATOM 1428 CE1 PHE A 185 -21.874 6.148 70.995 1.00 34.92 A C
+ATOM 1429 CE2 PHE A 185 -23.284 7.499 69.618 1.00 32.50 A C
+ATOM 1430 CZ PHE A 185 -22.759 6.264 69.942 1.00 30.45 A C
+ATOM 1431 N VAL A 186 -20.479 11.103 74.826 1.00 36.48 A N
+ATOM 1432 CA VAL A 186 -20.018 12.289 75.535 1.00 34.53 A C
+ATOM 1433 C VAL A 186 -18.704 12.748 74.921 1.00 37.15 A C
+ATOM 1434 O VAL A 186 -17.918 11.941 74.414 1.00 33.71 A O
+ATOM 1435 CB VAL A 186 -19.850 12.026 77.049 1.00 41.23 A C
+ATOM 1436 CG1 VAL A 186 -21.209 11.867 77.714 1.00 34.01 A C
+ATOM 1437 CG2 VAL A 186 -18.990 10.794 77.281 1.00 36.94 A C
+ATOM 1438 N ASP A 187 -18.462 14.058 74.974 1.00 35.60 A N
+ATOM 1439 CA ASP A 187 -17.285 14.649 74.335 1.00 38.81 A C
+ATOM 1440 C ASP A 187 -16.080 14.562 75.275 1.00 37.16 A C
+ATOM 1441 O ASP A 187 -15.610 15.547 75.849 1.00 38.69 A O
+ATOM 1442 CB ASP A 187 -17.570 16.085 73.910 1.00 37.81 A C
+ATOM 1443 CG ASP A 187 -18.234 16.899 75.003 1.00 33.44 A C
+ATOM 1444 OD1 ASP A 187 -18.687 16.304 76.002 1.00 35.30 A O
+ATOM 1445 OD2 ASP A 187 -18.304 18.138 74.859 1.00 36.30 A O1-
+ATOM 1446 N ARG A 188 -15.579 13.337 75.418 1.00 41.07 A N
+ATOM 1447 CA ARG A 188 -14.355 13.079 76.161 1.00 45.49 A C
+ATOM 1448 C ARG A 188 -13.724 11.804 75.623 1.00 43.19 A C
+ATOM 1449 O ARG A 188 -14.419 10.908 75.136 1.00 36.57 A O
+ATOM 1450 CB ARG A 188 -14.612 12.971 77.671 1.00 44.09 A C
+ATOM 1451 CG ARG A 188 -15.279 11.681 78.112 1.00 47.40 A C
+ATOM 1452 CD ARG A 188 -15.488 11.659 79.620 1.00 57.54 A C
+ATOM 1453 NE ARG A 188 -16.780 12.223 80.002 1.00 56.65 A N
+ATOM 1454 CZ ARG A 188 -16.946 13.445 80.498 1.00 62.33 A C
+ATOM 1455 NH1 ARG A 188 -15.900 14.242 80.676 1.00 58.47 A N1+
+ATOM 1456 NH2 ARG A 188 -18.161 13.872 80.816 1.00 62.46 A N
+ATOM 1457 N GLN A 189 -12.396 11.733 75.709 1.00 40.15 A N
+ATOM 1458 CA GLN A 189 -11.641 10.633 75.105 1.00 38.41 A C
+ATOM 1459 C GLN A 189 -11.563 9.455 76.078 1.00 45.05 A C
+ATOM 1460 O GLN A 189 -10.526 9.149 76.671 1.00 49.99 A O
+ATOM 1461 CB GLN A 189 -10.259 11.109 74.679 1.00 37.59 A C
+ATOM 1462 CG GLN A 189 -10.292 12.189 73.610 1.00 45.60 A C
+ATOM 1463 CD GLN A 189 -9.031 12.221 72.770 1.00 47.27 A C
+ATOM 1464 NE2 GLN A 189 -7.950 11.661 73.302 1.00 44.45 A N
+ATOM 1465 OE1 GLN A 189 -9.029 12.743 71.655 1.00 41.09 A O
+ATOM 1466 N THR A 190 -12.702 8.787 76.228 1.00 41.89 A N
+ATOM 1467 CA THR A 190 -12.814 7.564 77.007 1.00 42.08 A C
+ATOM 1468 C THR A 190 -13.344 6.446 76.119 1.00 49.27 A C
+ATOM 1469 O THR A 190 -13.749 6.665 74.974 1.00 47.54 A O
+ATOM 1470 CB THR A 190 -13.733 7.754 78.222 1.00 45.73 A C
+ATOM 1471 CG2 THR A 190 -13.185 8.833 79.143 1.00 45.44 A C
+ATOM 1472 OG1 THR A 190 -15.045 8.123 77.779 1.00 46.25 A O
+ATOM 1473 N ALA A 191 -13.336 5.232 76.664 1.00 45.12 A N
+ATOM 1474 CA ALA A 191 -13.843 4.070 75.942 1.00 47.47 A C
+ATOM 1475 C ALA A 191 -15.358 4.175 75.817 1.00 44.46 A C
+ATOM 1476 O ALA A 191 -16.083 4.018 76.804 1.00 47.06 A O
+ATOM 1477 CB ALA A 191 -13.439 2.785 76.657 1.00 48.89 A C
+ATOM 1478 N GLN A 192 -15.837 4.449 74.607 1.00 42.30 A N
+ATOM 1479 CA GLN A 192 -17.263 4.548 74.333 1.00 42.18 A C
+ATOM 1480 C GLN A 192 -17.611 3.644 73.162 1.00 43.69 A C
+ATOM 1481 O GLN A 192 -16.900 3.617 72.153 1.00 41.21 A O
+ATOM 1482 CB GLN A 192 -17.677 5.991 74.025 1.00 38.85 A C
+ATOM 1483 CG GLN A 192 -17.435 6.959 75.168 1.00 39.81 A C
+ATOM 1484 CD GLN A 192 -17.848 8.375 74.827 1.00 39.03 A C
+ATOM 1485 NE2 GLN A 192 -16.869 9.262 74.699 1.00 37.82 A N
+ATOM 1486 OE1 GLN A 192 -19.034 8.669 74.678 1.00 40.68 A O
+ATOM 1487 N ALA A 193 -18.708 2.907 73.301 1.00 43.81 A N
+ATOM 1488 CA ALA A 193 -19.155 1.967 72.287 1.00 46.29 A C
+ATOM 1489 C ALA A 193 -20.565 2.321 71.839 1.00 38.09 A C
+ATOM 1490 O ALA A 193 -21.434 2.620 72.664 1.00 36.20 A O
+ATOM 1491 CB ALA A 193 -19.121 0.528 72.810 1.00 40.37 A C
+ATOM 1492 N ALA A 194 -20.782 2.292 70.530 1.00 44.33 A N
+ATOM 1493 CA ALA A 194 -22.125 2.458 70.000 1.00 41.14 A C
+ATOM 1494 C ALA A 194 -22.943 1.195 70.236 1.00 38.55 A C
+ATOM 1495 O ALA A 194 -22.406 0.087 70.320 1.00 41.94 A O
+ATOM 1496 CB ALA A 194 -22.075 2.776 68.507 1.00 40.77 A C
+ATOM 1497 N GLY A 195 -24.253 1.373 70.352 1.00 45.01 A N
+ATOM 1498 CA GLY A 195 -25.147 0.237 70.444 1.00 44.26 A C
+ATOM 1499 C GLY A 195 -25.122 -0.599 69.179 1.00 40.94 A C
+ATOM 1500 O GLY A 195 -24.599 -0.208 68.136 1.00 36.27 A O
+ATOM 1501 N THR A 196 -25.699 -1.793 69.288 1.00 46.36 A N
+ATOM 1502 CA THR A 196 -25.764 -2.699 68.149 1.00 43.74 A C
+ATOM 1503 C THR A 196 -26.551 -2.055 67.016 1.00 40.82 A C
+ATOM 1504 O THR A 196 -27.701 -1.644 67.201 1.00 43.52 A O
+ATOM 1505 CB THR A 196 -26.405 -4.025 68.560 1.00 47.36 A C
+ATOM 1506 CG2 THR A 196 -25.527 -4.749 69.572 1.00 46.11 A C
+ATOM 1507 OG1 THR A 196 -27.692 -3.777 69.141 1.00 56.08 A O
+ATOM 1508 N ASP A 197 -25.925 -1.955 65.848 1.00 38.21 A N
+ATOM 1509 CA ASP A 197 -26.566 -1.321 64.709 1.00 43.61 A C
+ATOM 1510 C ASP A 197 -27.552 -2.279 64.046 1.00 46.04 A C
+ATOM 1511 O ASP A 197 -27.460 -3.503 64.178 1.00 42.52 A O
+ATOM 1512 CB ASP A 197 -25.524 -0.854 63.692 1.00 42.39 A C
+ATOM 1513 CG ASP A 197 -26.014 0.305 62.848 1.00 48.19 A C
+ATOM 1514 OD1 ASP A 197 -27.002 0.957 63.247 1.00 43.28 A O
+ATOM 1515 OD2 ASP A 197 -25.414 0.563 61.783 1.00 52.59 A O1-
+ATOM 1516 N THR A 198 -28.512 -1.699 63.331 1.00 44.88 A N
+ATOM 1517 CA THR A 198 -29.509 -2.459 62.593 1.00 42.59 A C
+ATOM 1518 C THR A 198 -29.668 -1.846 61.209 1.00 41.18 A C
+ATOM 1519 O THR A 198 -29.206 -0.734 60.940 1.00 40.92 A O
+ATOM 1520 CB THR A 198 -30.858 -2.491 63.326 1.00 45.63 A C
+ATOM 1521 CG2 THR A 198 -30.774 -3.365 64.569 1.00 43.99 A C
+ATOM 1522 OG1 THR A 198 -31.228 -1.160 63.707 1.00 45.23 A O
+ATOM 1523 N THR A 199 -30.329 -2.587 60.324 1.00 36.67 A N
+ATOM 1524 CA THR A 199 -30.578 -2.128 58.965 1.00 31.64 A C
+ATOM 1525 C THR A 199 -31.920 -1.410 58.905 1.00 34.02 A C
+ATOM 1526 O THR A 199 -32.924 -1.914 59.418 1.00 36.37 A O
+ATOM 1527 CB THR A 199 -30.558 -3.300 57.984 1.00 36.63 A C
+ATOM 1528 CG2 THR A 199 -30.819 -2.814 56.567 1.00 31.73 A C
+ATOM 1529 OG1 THR A 199 -29.278 -3.942 58.029 1.00 37.11 A O
+ATOM 1530 N ILE A 200 -31.932 -0.232 58.283 1.00 31.92 A N
+ATOM 1531 CA ILE A 200 -33.151 0.562 58.139 1.00 27.61 A C
+ATOM 1532 C ILE A 200 -33.977 -0.076 57.025 1.00 32.15 A C
+ATOM 1533 O ILE A 200 -33.675 0.083 55.841 1.00 31.56 A O
+ATOM 1534 CB ILE A 200 -32.842 2.032 57.850 1.00 30.51 A C
+ATOM 1535 CG1 ILE A 200 -31.835 2.567 58.872 1.00 34.99 A C
+ATOM 1536 CG2 ILE A 200 -34.118 2.857 57.879 1.00 32.45 A C
+ATOM 1537 CD1 ILE A 200 -30.780 3.474 58.276 1.00 32.07 A C
+ATOM 1538 N THR A 201 -35.034 -0.798 57.407 1.00 32.97 A N
+ATOM 1539 CA THR A 201 -35.790 -1.590 56.441 1.00 28.43 A C
+ATOM 1540 C THR A 201 -36.511 -0.710 55.427 1.00 28.55 A C
+ATOM 1541 O THR A 201 -36.513 -1.014 54.228 1.00 28.53 A O
+ATOM 1542 CB THR A 201 -36.789 -2.490 57.167 1.00 33.11 A C
+ATOM 1543 CG2 THR A 201 -37.429 -3.469 56.193 1.00 33.05 A C
+ATOM 1544 OG1 THR A 201 -36.114 -3.221 58.198 1.00 38.48 A O
+ATOM 1545 N VAL A 202 -37.131 0.382 55.885 1.00 24.18 A N
+ATOM 1546 CA VAL A 202 -37.892 1.234 54.974 1.00 28.40 A C
+ATOM 1547 C VAL A 202 -36.980 1.869 53.933 1.00 29.17 A C
+ATOM 1548 O VAL A 202 -37.407 2.141 52.804 1.00 29.13 A O
+ATOM 1549 CB VAL A 202 -38.685 2.294 55.768 1.00 28.41 A C
+ATOM 1550 CG1 VAL A 202 -37.748 3.308 56.412 1.00 35.77 A C
+ATOM 1551 CG2 VAL A 202 -39.700 2.988 54.868 1.00 38.10 A C
+ATOM 1552 N ASN A 203 -35.710 2.096 54.280 1.00 25.67 A N
+ATOM 1553 CA ASN A 203 -34.771 2.653 53.312 1.00 26.61 A C
+ATOM 1554 C ASN A 203 -34.387 1.620 52.260 1.00 26.96 A C
+ATOM 1555 O ASN A 203 -34.223 1.958 51.082 1.00 25.39 A O
+ATOM 1556 CB ASN A 203 -33.528 3.176 54.031 1.00 26.02 A C
+ATOM 1557 CG ASN A 203 -33.765 4.514 54.705 1.00 29.29 A C
+ATOM 1558 ND2 ASN A 203 -32.683 5.179 55.095 1.00 27.49 A N
+ATOM 1559 OD1 ASN A 203 -34.905 4.945 54.874 1.00 27.39 A O
+ATOM 1560 N VAL A 204 -34.234 0.358 52.667 1.00 26.81 A N
+ATOM 1561 CA VAL A 204 -33.919 -0.700 51.711 1.00 32.26 A C
+ATOM 1562 C VAL A 204 -35.050 -0.858 50.704 1.00 28.76 A C
+ATOM 1563 O VAL A 204 -34.814 -1.000 49.497 1.00 28.91 A O
+ATOM 1564 CB VAL A 204 -33.630 -2.020 52.449 1.00 31.36 A C
+ATOM 1565 CG1 VAL A 204 -33.509 -3.170 51.460 1.00 31.24 A C
+ATOM 1566 CG2 VAL A 204 -32.367 -1.898 53.286 1.00 25.72 A C
+ATOM 1567 N LEU A 205 -36.297 -0.825 51.181 1.00 23.97 A N
+ATOM 1568 CA LEU A 205 -37.438 -0.964 50.284 1.00 29.72 A C
+ATOM 1569 C LEU A 205 -37.516 0.199 49.305 1.00 31.96 A C
+ATOM 1570 O LEU A 205 -37.776 -0.001 48.113 1.00 29.24 A O
+ATOM 1571 CB LEU A 205 -38.729 -1.076 51.094 1.00 28.11 A C
+ATOM 1572 CG LEU A 205 -38.919 -2.390 51.854 1.00 31.29 A C
+ATOM 1573 CD1 LEU A 205 -40.077 -2.286 52.833 1.00 32.67 A C
+ATOM 1574 CD2 LEU A 205 -39.133 -3.543 50.885 1.00 33.54 A C
+ATOM 1575 N ALA A 206 -37.290 1.424 49.789 1.00 23.26 A N
+ATOM 1576 CA ALA A 206 -37.275 2.578 48.896 1.00 27.13 A C
+ATOM 1577 C ALA A 206 -36.149 2.464 47.877 1.00 28.64 A C
+ATOM 1578 O ALA A 206 -36.312 2.848 46.713 1.00 33.46 A O
+ATOM 1579 CB ALA A 206 -37.142 3.867 49.707 1.00 28.39 A C
+ATOM 1580 N TRP A 207 -34.999 1.934 48.298 1.00 27.23 A N
+ATOM 1581 CA TRP A 207 -33.892 1.717 47.375 1.00 29.46 A C
+ATOM 1582 C TRP A 207 -34.220 0.636 46.352 1.00 30.50 A C
+ATOM 1583 O TRP A 207 -33.796 0.732 45.194 1.00 27.71 A O
+ATOM 1584 CB TRP A 207 -32.633 1.360 48.164 1.00 25.98 A C
+ATOM 1585 CG TRP A 207 -31.469 0.929 47.333 1.00 33.09 A C
+ATOM 1586 CD1 TRP A 207 -30.689 1.718 46.539 1.00 34.56 A C
+ATOM 1587 CD2 TRP A 207 -30.935 -0.396 47.230 1.00 35.87 A C
+ATOM 1588 CE2 TRP A 207 -29.839 -0.337 46.348 1.00 37.47 A C
+ATOM 1589 CE3 TRP A 207 -31.282 -1.628 47.794 1.00 33.55 A C
+ATOM 1590 NE1 TRP A 207 -29.709 0.964 45.940 1.00 33.32 A N
+ATOM 1591 CZ2 TRP A 207 -29.087 -1.462 46.017 1.00 41.96 A C
+ATOM 1592 CZ3 TRP A 207 -30.535 -2.743 47.463 1.00 41.15 A C
+ATOM 1593 CH2 TRP A 207 -29.449 -2.652 46.585 1.00 41.36 A C
+ATOM 1594 N LEU A 208 -34.974 -0.391 46.754 1.00 24.10 A N
+ATOM 1595 CA LEU A 208 -35.429 -1.392 45.794 1.00 32.57 A C
+ATOM 1596 C LEU A 208 -36.387 -0.781 44.781 1.00 30.65 A C
+ATOM 1597 O LEU A 208 -36.365 -1.144 43.599 1.00 34.37 A O
+ATOM 1598 CB LEU A 208 -36.095 -2.559 46.522 1.00 30.22 A C
+ATOM 1599 CG LEU A 208 -35.190 -3.465 47.360 1.00 29.05 A C
+ATOM 1600 CD1 LEU A 208 -35.997 -4.582 48.006 1.00 32.79 A C
+ATOM 1601 CD2 LEU A 208 -34.061 -4.033 46.516 1.00 31.48 A C
+ATOM 1602 N TYR A 209 -37.239 0.145 45.226 1.00 29.01 A N
+ATOM 1603 CA TYR A 209 -38.120 0.845 44.298 1.00 31.92 A C
+ATOM 1604 C TYR A 209 -37.319 1.679 43.309 1.00 35.92 A C
+ATOM 1605 O TYR A 209 -37.668 1.753 42.125 1.00 32.34 A O
+ATOM 1606 CB TYR A 209 -39.105 1.723 45.069 1.00 31.20 A C
+ATOM 1607 CG TYR A 209 -40.334 0.986 45.545 1.00 37.03 A C
+ATOM 1608 CD1 TYR A 209 -41.285 0.526 44.643 1.00 40.06 A C
+ATOM 1609 CD2 TYR A 209 -40.544 0.748 46.896 1.00 28.79 A C
+ATOM 1610 CE1 TYR A 209 -42.410 -0.151 45.073 1.00 40.63 A C
+ATOM 1611 CE2 TYR A 209 -41.666 0.072 47.337 1.00 34.89 A C
+ATOM 1612 CZ TYR A 209 -42.595 -0.374 46.421 1.00 39.51 A C
+ATOM 1613 OH TYR A 209 -43.714 -1.047 46.852 1.00 40.05 A O
+ATOM 1614 N ALA A 210 -36.238 2.311 43.774 1.00 32.32 A N
+ATOM 1615 CA ALA A 210 -35.374 3.062 42.869 1.00 33.39 A C
+ATOM 1616 C ALA A 210 -34.761 2.159 41.808 1.00 33.08 A C
+ATOM 1617 O ALA A 210 -34.537 2.597 40.674 1.00 31.00 A O
+ATOM 1618 CB ALA A 210 -34.276 3.774 43.659 1.00 38.63 A C
+ATOM 1619 N ALA A 211 -34.482 0.901 42.156 1.00 29.95 A N
+ATOM 1620 CA ALA A 211 -33.960 -0.041 41.173 1.00 38.71 A C
+ATOM 1621 C ALA A 211 -34.998 -0.357 40.104 1.00 38.27 A C
+ATOM 1622 O ALA A 211 -34.666 -0.448 38.917 1.00 39.96 A O
+ATOM 1623 CB ALA A 211 -33.500 -1.321 41.868 1.00 37.27 A C
+ATOM 1624 N VAL A 212 -36.259 -0.530 40.507 1.00 37.46 A N
+ATOM 1625 CA VAL A 212 -37.313 -0.821 39.540 1.00 41.82 A C
+ATOM 1626 C VAL A 212 -37.554 0.381 38.635 1.00 43.94 A C
+ATOM 1627 O VAL A 212 -37.760 0.232 37.424 1.00 43.74 A O
+ATOM 1628 CB VAL A 212 -38.600 -1.251 40.268 1.00 36.71 A C
+ATOM 1629 CG1 VAL A 212 -39.731 -1.458 39.272 1.00 41.97 A C
+ATOM 1630 CG2 VAL A 212 -38.353 -2.518 41.074 1.00 31.36 A C
+ATOM 1631 N ILE A 213 -37.528 1.589 39.205 1.00 38.15 A N
+ATOM 1632 CA ILE A 213 -37.674 2.796 38.398 1.00 39.62 A C
+ATOM 1633 C ILE A 213 -36.529 2.914 37.400 1.00 44.72 A C
+ATOM 1634 O ILE A 213 -36.690 3.498 36.321 1.00 51.05 A O
+ATOM 1635 CB ILE A 213 -37.774 4.035 39.312 1.00 44.90 A C
+ATOM 1636 CG1 ILE A 213 -38.956 3.896 40.273 1.00 44.60 A C
+ATOM 1637 CG2 ILE A 213 -37.941 5.297 38.496 1.00 50.73 A C
+ATOM 1638 CD1 ILE A 213 -39.157 5.095 41.178 1.00 40.25 A C
+ATOM 1639 N ASN A 214 -35.368 2.346 37.726 1.00 41.68 A N
+ATOM 1640 CA ASN A 214 -34.215 2.350 36.837 1.00 47.03 A C
+ATOM 1641 C ASN A 214 -34.057 1.051 36.055 1.00 49.42 A C
+ATOM 1642 O ASN A 214 -33.087 0.912 35.304 1.00 48.17 A O
+ATOM 1643 CB ASN A 214 -32.938 2.638 37.632 1.00 43.76 A C
+ATOM 1644 CG ASN A 214 -32.853 4.080 38.091 1.00 45.61 A C
+ATOM 1645 ND2 ASN A 214 -33.549 4.398 39.177 1.00 48.13 A N
+ATOM 1646 OD1 ASN A 214 -32.174 4.900 37.474 1.00 45.51 A O
+ATOM 1647 N GLY A 215 -34.972 0.100 36.216 1.00 55.59 A N
+ATOM 1648 CA GLY A 215 -34.999 -1.067 35.358 1.00 50.39 A C
+ATOM 1649 C GLY A 215 -34.272 -2.290 35.860 1.00 50.72 A C
+ATOM 1650 O GLY A 215 -34.046 -3.218 35.076 1.00 55.25 A O
+ATOM 1651 N ASP A 216 -33.883 -2.324 37.129 1.00 46.39 A N
+ATOM 1652 CA ASP A 216 -33.368 -3.546 37.740 1.00 49.22 A C
+ATOM 1653 C ASP A 216 -34.560 -4.257 38.365 1.00 52.58 A C
+ATOM 1654 O ASP A 216 -35.069 -3.844 39.409 1.00 51.20 A O
+ATOM 1655 CB ASP A 216 -32.280 -3.237 38.763 1.00 53.88 A C
+ATOM 1656 CG ASP A 216 -30.882 -3.415 38.197 1.00 60.12 A C
+ATOM 1657 OD1 ASP A 216 -30.761 -3.766 37.004 1.00 63.39 A O
+ATOM 1658 OD2 ASP A 216 -29.903 -3.208 38.946 1.00 58.15 A O1-
+ATOM 1659 N ARG A 217 -35.026 -5.318 37.708 1.00 48.18 A N
+ATOM 1660 CA ARG A 217 -36.243 -6.010 38.114 1.00 43.89 A C
+ATOM 1661 C ARG A 217 -36.021 -7.493 38.384 1.00 40.80 A C
+ATOM 1662 O ARG A 217 -36.995 -8.217 38.627 1.00 41.42 A O
+ATOM 1663 CB ARG A 217 -37.330 -5.845 37.047 1.00 40.56 A C
+ATOM 1664 CG ARG A 217 -37.746 -4.408 36.784 1.00 43.72 A C
+ATOM 1665 CD ARG A 217 -38.826 -4.346 35.714 1.00 42.23 A C
+ATOM 1666 NE ARG A 217 -40.026 -5.077 36.111 1.00 41.31 A N
+ATOM 1667 CZ ARG A 217 -41.128 -4.504 36.583 1.00 43.64 A C
+ATOM 1668 NH1 ARG A 217 -41.187 -3.186 36.717 1.00 45.45 A N1+
+ATOM 1669 NH2 ARG A 217 -42.172 -5.248 36.921 1.00 41.32 A N
+ATOM 1670 N TRP A 218 -34.774 -7.966 38.352 1.00 36.38 A N
+ATOM 1671 CA TRP A 218 -34.523 -9.396 38.493 1.00 41.06 A C
+ATOM 1672 C TRP A 218 -34.910 -9.926 39.868 1.00 44.70 A C
+ATOM 1673 O TRP A 218 -35.140 -11.132 40.009 1.00 40.75 A O
+ATOM 1674 CB TRP A 218 -33.050 -9.704 38.209 1.00 43.64 A C
+ATOM 1675 CG TRP A 218 -32.097 -9.108 39.201 1.00 47.86 A C
+ATOM 1676 CD1 TRP A 218 -31.435 -7.920 39.089 1.00 43.05 A C
+ATOM 1677 CD2 TRP A 218 -31.690 -9.678 40.451 1.00 43.40 A C
+ATOM 1678 CE2 TRP A 218 -30.784 -8.778 41.045 1.00 44.70 A C
+ATOM 1679 CE3 TRP A 218 -32.005 -10.862 41.127 1.00 46.52 A C
+ATOM 1680 NE1 TRP A 218 -30.645 -7.713 40.194 1.00 48.32 A N
+ATOM 1681 CZ2 TRP A 218 -30.191 -9.023 42.281 1.00 49.87 A C
+ATOM 1682 CZ3 TRP A 218 -31.417 -11.102 42.354 1.00 49.27 A C
+ATOM 1683 CH2 TRP A 218 -30.519 -10.187 42.918 1.00 54.03 A C
+ATOM 1684 N PHE A 219 -34.991 -9.062 40.879 1.00 39.97 A N
+ATOM 1685 CA PHE A 219 -35.325 -9.491 42.230 1.00 38.29 A C
+ATOM 1686 C PHE A 219 -36.825 -9.558 42.488 1.00 34.23 A C
+ATOM 1687 O PHE A 219 -37.232 -10.074 43.535 1.00 41.36 A O
+ATOM 1688 CB PHE A 219 -34.677 -8.557 43.261 1.00 35.64 A C
+ATOM 1689 CG PHE A 219 -34.950 -7.100 43.018 1.00 34.08 A C
+ATOM 1690 CD1 PHE A 219 -36.108 -6.507 43.495 1.00 33.57 A C
+ATOM 1691 CD2 PHE A 219 -34.047 -6.322 42.315 1.00 35.98 A C
+ATOM 1692 CE1 PHE A 219 -36.361 -5.167 43.273 1.00 36.10 A C
+ATOM 1693 CE2 PHE A 219 -34.292 -4.982 42.092 1.00 41.53 A C
+ATOM 1694 CZ PHE A 219 -35.452 -4.404 42.569 1.00 38.37 A C
+ATOM 1695 N LEU A 220 -37.649 -9.047 41.578 1.00 34.04 A N
+ATOM 1696 CA LEU A 220 -39.092 -9.102 41.762 1.00 34.67 A C
+ATOM 1697 C LEU A 220 -39.590 -10.539 41.667 1.00 42.10 A C
+ATOM 1698 O LEU A 220 -38.970 -11.395 41.030 1.00 37.53 A O
+ATOM 1699 CB LEU A 220 -39.798 -8.235 40.721 1.00 37.23 A C
+ATOM 1700 CG LEU A 220 -39.579 -6.726 40.837 1.00 34.79 A C
+ATOM 1701 CD1 LEU A 220 -40.188 -6.006 39.647 1.00 39.78 A C
+ATOM 1702 CD2 LEU A 220 -40.157 -6.201 42.141 1.00 38.56 A C
+ATOM 1703 N ASN A 221 -40.724 -10.802 42.312 1.00 41.05 A N
+ATOM 1704 CA ASN A 221 -41.298 -12.138 42.314 1.00 49.57 A C
+ATOM 1705 C ASN A 221 -42.815 -12.038 42.374 1.00 50.99 A C
+ATOM 1706 O ASN A 221 -43.382 -10.984 42.674 1.00 47.82 A O
+ATOM 1707 CB ASN A 221 -40.759 -12.979 43.479 1.00 46.91 A C
+ATOM 1708 CG ASN A 221 -40.893 -12.282 44.824 1.00 52.27 A C
+ATOM 1709 ND2 ASN A 221 -39.917 -12.500 45.697 1.00 52.91 A N
+ATOM 1710 OD1 ASN A 221 -41.860 -11.564 45.079 1.00 56.83 A O
+ATOM 1711 N ARG A 222 -43.469 -13.164 42.084 1.00 55.29 A N
+ATOM 1712 CA ARG A 222 -44.923 -13.232 42.155 1.00 55.44 A C
+ATOM 1713 C ARG A 222 -45.430 -13.272 43.590 1.00 58.31 A C
+ATOM 1714 O ARG A 222 -46.604 -12.969 43.826 1.00 60.54 A O
+ATOM 1715 CB ARG A 222 -45.425 -14.465 41.404 1.00 59.44 A C
+ATOM 1716 CG ARG A 222 -44.941 -15.773 42.010 1.00 64.22 A C
+ATOM 1717 CD ARG A 222 -45.221 -16.957 41.105 1.00 63.67 A C
+ATOM 1718 NE ARG A 222 -44.228 -18.013 41.282 1.00 64.36 A N
+ATOM 1719 CZ ARG A 222 -44.288 -18.945 42.228 1.00 68.65 A C
+ATOM 1720 NH1 ARG A 222 -45.296 -18.954 43.090 1.00 70.23 A N1+
+ATOM 1721 NH2 ARG A 222 -43.338 -19.866 42.315 1.00 66.89 A N
+ATOM 1722 N PHE A 223 -44.577 -13.636 44.545 1.00 55.79 A N
+ATOM 1723 CA PHE A 223 -45.010 -13.794 45.923 1.00 57.06 A C
+ATOM 1724 C PHE A 223 -45.434 -12.459 46.527 1.00 54.34 A C
+ATOM 1725 O PHE A 223 -45.062 -11.379 46.060 1.00 54.33 A O
+ATOM 1726 CB PHE A 223 -43.897 -14.390 46.789 1.00 54.56 A C
+ATOM 1727 CG PHE A 223 -43.201 -15.568 46.175 1.00 61.54 A C
+ATOM 1728 CD1 PHE A 223 -43.776 -16.828 46.208 1.00 67.27 A C
+ATOM 1729 CD2 PHE A 223 -41.957 -15.421 45.587 1.00 62.61 A C
+ATOM 1730 CE1 PHE A 223 -43.128 -17.914 45.650 1.00 63.74 A C
+ATOM 1731 CE2 PHE A 223 -41.305 -16.501 45.027 1.00 67.45 A C
+ATOM 1732 CZ PHE A 223 -41.891 -17.750 45.059 1.00 63.58 A C
+ATOM 1733 N THR A 224 -46.234 -12.555 47.585 1.00 53.15 A N
+ATOM 1734 CA THR A 224 -46.495 -11.455 48.498 1.00 54.87 A C
+ATOM 1735 C THR A 224 -46.470 -12.025 49.909 1.00 57.84 A C
+ATOM 1736 O THR A 224 -46.354 -13.238 50.107 1.00 57.11 A O
+ATOM 1737 CB THR A 224 -47.827 -10.759 48.195 1.00 58.32 A C
+ATOM 1738 CG2 THR A 224 -48.995 -11.653 48.574 1.00 59.49 A C
+ATOM 1739 OG1 THR A 224 -47.906 -9.536 48.940 1.00 55.79 A O
+ATOM 1740 N THR A 225 -46.568 -11.146 50.901 1.00 54.55 A N
+ATOM 1741 CA THR A 225 -46.491 -11.579 52.287 1.00 52.09 A C
+ATOM 1742 C THR A 225 -47.276 -10.614 53.160 1.00 52.22 A C
+ATOM 1743 O THR A 225 -47.565 -9.480 52.767 1.00 51.74 A O
+ATOM 1744 CB THR A 225 -45.037 -11.668 52.770 1.00 52.66 A C
+ATOM 1745 CG2 THR A 225 -44.384 -10.294 52.751 1.00 48.22 A C
+ATOM 1746 OG1 THR A 225 -45.002 -12.191 54.104 1.00 57.56 A O
+ATOM 1747 N THR A 226 -47.630 -11.086 54.350 1.00 48.89 A N
+ATOM 1748 CA THR A 226 -48.220 -10.218 55.351 1.00 49.18 A C
+ATOM 1749 C THR A 226 -47.131 -9.399 56.035 1.00 47.11 A C
+ATOM 1750 O THR A 226 -45.949 -9.757 56.027 1.00 49.91 A O
+ATOM 1751 CB THR A 226 -48.995 -11.034 56.387 1.00 52.38 A C
+ATOM 1752 CG2 THR A 226 -50.048 -11.896 55.705 1.00 52.43 A C
+ATOM 1753 OG1 THR A 226 -48.089 -11.880 57.105 1.00 53.45 A O
+ATOM 1754 N LEU A 227 -47.543 -8.276 56.626 1.00 44.28 A N
+ATOM 1755 CA LEU A 227 -46.585 -7.415 57.310 1.00 46.11 A C
+ATOM 1756 C LEU A 227 -45.959 -8.114 58.510 1.00 48.45 A C
+ATOM 1757 O LEU A 227 -44.781 -7.892 58.814 1.00 47.38 A O
+ATOM 1758 CB LEU A 227 -47.265 -6.116 57.743 1.00 48.35 A C
+ATOM 1759 CG LEU A 227 -46.384 -5.090 58.458 1.00 53.13 A C
+ATOM 1760 CD1 LEU A 227 -45.169 -4.753 57.611 1.00 51.92 A C
+ATOM 1761 CD2 LEU A 227 -47.177 -3.836 58.787 1.00 50.91 A C
+ATOM 1762 N ASN A 228 -46.723 -8.969 59.194 1.00 48.68 A N
+ATOM 1763 CA ASN A 228 -46.198 -9.644 60.376 1.00 50.79 A C
+ATOM 1764 C ASN A 228 -45.209 -10.740 60.000 1.00 49.09 A C
+ATOM 1765 O ASN A 228 -44.176 -10.902 60.659 1.00 51.86 A O
+ATOM 1766 CB ASN A 228 -47.347 -10.217 61.205 1.00 52.01 A C
+ATOM 1767 CG ASN A 228 -48.001 -9.176 62.089 1.00 58.59 A C
+ATOM 1768 ND2 ASN A 228 -47.236 -8.631 63.028 1.00 64.61 A N
+ATOM 1769 OD1 ASN A 228 -49.181 -8.861 61.930 1.00 63.31 A O
+ATOM 1770 N ASP A 229 -45.508 -11.504 58.946 1.00 51.91 A N
+ATOM 1771 CA ASP A 229 -44.587 -12.553 58.521 1.00 54.27 A C
+ATOM 1772 C ASP A 229 -43.296 -11.972 57.962 1.00 50.38 A C
+ATOM 1773 O ASP A 229 -42.241 -12.611 58.052 1.00 48.25 A O
+ATOM 1774 CB ASP A 229 -45.259 -13.460 57.491 1.00 52.46 A C
+ATOM 1775 CG ASP A 229 -46.033 -14.594 58.134 1.00 63.17 A C
+ATOM 1776 OD1 ASP A 229 -47.225 -14.397 58.453 1.00 67.92 A O
+ATOM 1777 OD2 ASP A 229 -45.449 -15.682 58.325 1.00 71.71 A O1-
+ATOM 1778 N PHE A 230 -43.355 -10.770 57.384 1.00 45.69 A N
+ATOM 1779 CA PHE A 230 -42.130 -10.100 56.962 1.00 47.77 A C
+ATOM 1780 C PHE A 230 -41.323 -9.630 58.165 1.00 44.56 A C
+ATOM 1781 O PHE A 230 -40.097 -9.789 58.198 1.00 47.05 A O
+ATOM 1782 CB PHE A 230 -42.459 -8.923 56.045 1.00 44.71 A C
+ATOM 1783 CG PHE A 230 -41.269 -8.073 55.703 1.00 46.06 A C
+ATOM 1784 CD1 PHE A 230 -40.377 -8.472 54.721 1.00 39.89 A C
+ATOM 1785 CD2 PHE A 230 -41.040 -6.877 56.364 1.00 46.70 A C
+ATOM 1786 CE1 PHE A 230 -39.280 -7.695 54.405 1.00 44.09 A C
+ATOM 1787 CE2 PHE A 230 -39.944 -6.095 56.053 1.00 43.17 A C
+ATOM 1788 CZ PHE A 230 -39.063 -6.504 55.072 1.00 46.40 A C
+ATOM 1789 N ASN A 231 -41.994 -9.049 59.163 1.00 47.09 A N
+ATOM 1790 CA ASN A 231 -41.304 -8.588 60.362 1.00 48.54 A C
+ATOM 1791 C ASN A 231 -40.692 -9.738 61.151 1.00 46.93 A C
+ATOM 1792 O ASN A 231 -39.744 -9.517 61.913 1.00 51.54 A O
+ATOM 1793 CB ASN A 231 -42.265 -7.794 61.248 1.00 44.45 A C
+ATOM 1794 CG ASN A 231 -42.510 -6.390 60.729 1.00 46.53 A C
+ATOM 1795 ND2 ASN A 231 -43.741 -5.912 60.872 1.00 48.18 A N
+ATOM 1796 OD1 ASN A 231 -41.604 -5.743 60.206 1.00 49.46 A O
+ATOM 1797 N LEU A 232 -41.212 -10.957 60.990 1.00 49.26 A N
+ATOM 1798 CA LEU A 232 -40.596 -12.111 61.635 1.00 48.59 A C
+ATOM 1799 C LEU A 232 -39.250 -12.439 61.000 1.00 50.95 A C
+ATOM 1800 O LEU A 232 -38.296 -12.796 61.702 1.00 54.89 A O
+ATOM 1801 CB LEU A 232 -41.534 -13.316 61.561 1.00 51.33 A C
+ATOM 1802 CG LEU A 232 -42.569 -13.440 62.681 1.00 54.42 A C
+ATOM 1803 CD1 LEU A 232 -43.539 -14.575 62.391 1.00 56.04 A C
+ATOM 1804 CD2 LEU A 232 -41.886 -13.644 64.024 1.00 48.57 A C
+ATOM 1805 N VAL A 233 -39.155 -12.323 59.675 1.00 46.36 A N
+ATOM 1806 CA VAL A 233 -37.884 -12.556 59.000 1.00 48.55 A C
+ATOM 1807 C VAL A 233 -36.952 -11.363 59.172 1.00 48.47 A C
+ATOM 1808 O VAL A 233 -35.728 -11.531 59.241 1.00 48.19 A O
+ATOM 1809 CB VAL A 233 -38.124 -12.874 57.514 1.00 51.22 A C
+ATOM 1810 CG1 VAL A 233 -36.822 -13.265 56.829 1.00 47.79 A C
+ATOM 1811 CG2 VAL A 233 -39.160 -13.978 57.369 1.00 51.84 A C
+ATOM 1812 N ALA A 234 -37.504 -10.150 59.254 1.00 49.48 A N
+ATOM 1813 CA ALA A 234 -36.671 -8.965 59.431 1.00 48.29 A C
+ATOM 1814 C ALA A 234 -35.930 -9.001 60.762 1.00 47.50 A C
+ATOM 1815 O ALA A 234 -34.783 -8.550 60.855 1.00 46.36 A O
+ATOM 1816 CB ALA A 234 -37.527 -7.703 59.325 1.00 46.76 A C
+ATOM 1817 N MET A 235 -36.570 -9.538 61.803 1.00 52.01 A N
+ATOM 1818 CA MET A 235 -35.920 -9.622 63.107 1.00 49.80 A C
+ATOM 1819 C MET A 235 -34.730 -10.573 63.074 1.00 52.99 A C
+ATOM 1820 O MET A 235 -33.694 -10.302 63.693 1.00 54.42 A O
+ATOM 1821 CB MET A 235 -36.929 -10.066 64.166 1.00 54.15 A C
+ATOM 1822 CG MET A 235 -37.574 -8.925 64.933 1.00 63.16 A C
+ATOM 1823 SD MET A 235 -38.598 -9.508 66.297 1.00 89.99 A S
+ATOM 1824 CE MET A 235 -40.140 -8.666 65.948 1.00 71.61 A C
+ATOM 1825 N LYS A 236 -34.859 -11.692 62.356 1.00 53.54 A N
+ATOM 1826 CA LYS A 236 -33.779 -12.672 62.308 1.00 53.13 A C
+ATOM 1827 C LYS A 236 -32.551 -12.125 61.592 1.00 54.14 A C
+ATOM 1828 O LYS A 236 -31.424 -12.529 61.901 1.00 56.65 A O
+ATOM 1829 CB LYS A 236 -34.269 -13.953 61.630 1.00 52.75 A C
+ATOM 1830 CG LYS A 236 -33.263 -15.094 61.637 1.00 64.88 A C
+ATOM 1831 CD LYS A 236 -33.221 -15.801 60.290 1.00 62.89 A C
+ATOM 1832 CE LYS A 236 -32.220 -16.946 60.292 1.00 68.06 A C
+ATOM 1833 NZ LYS A 236 -30.849 -16.487 59.928 1.00 65.62 A N1+
+ATOM 1834 N TYR A 237 -32.741 -11.203 60.647 1.00 51.24 A N
+ATOM 1835 CA TYR A 237 -31.645 -10.635 59.874 1.00 48.39 A C
+ATOM 1836 C TYR A 237 -31.255 -9.239 60.351 1.00 44.17 A C
+ATOM 1837 O TYR A 237 -30.624 -8.489 59.598 1.00 45.24 A O
+ATOM 1838 CB TYR A 237 -32.009 -10.612 58.390 1.00 46.67 A C
+ATOM 1839 CG TYR A 237 -32.051 -11.987 57.763 1.00 47.83 A C
+ATOM 1840 CD1 TYR A 237 -33.224 -12.730 57.749 1.00 49.26 A C
+ATOM 1841 CD2 TYR A 237 -30.915 -12.545 57.192 1.00 45.38 A C
+ATOM 1842 CE1 TYR A 237 -33.266 -13.989 57.180 1.00 52.16 A C
+ATOM 1843 CE2 TYR A 237 -30.947 -13.803 56.621 1.00 54.25 A C
+ATOM 1844 CZ TYR A 237 -32.125 -14.520 56.618 1.00 53.00 A C
+ATOM 1845 OH TYR A 237 -32.160 -15.773 56.050 1.00 56.94 A O
+ATOM 1846 N ASN A 238 -31.619 -8.883 61.584 1.00 41.18 A N
+ATOM 1847 CA ASN A 238 -31.241 -7.606 62.194 1.00 43.30 A C
+ATOM 1848 C ASN A 238 -31.773 -6.418 61.394 1.00 42.30 A C
+ATOM 1849 O ASN A 238 -31.087 -5.410 61.210 1.00 39.45 A O
+ATOM 1850 CB ASN A 238 -29.725 -7.504 62.376 1.00 43.06 A C
+ATOM 1851 CG ASN A 238 -29.339 -6.684 63.590 1.00 55.19 A C
+ATOM 1852 ND2 ASN A 238 -28.160 -6.076 63.544 1.00 54.07 A N
+ATOM 1853 OD1 ASN A 238 -30.093 -6.598 64.559 1.00 61.37 A O
+ATOM 1854 N TYR A 239 -33.005 -6.538 60.914 1.00 38.35 A N
+ATOM 1855 CA TYR A 239 -33.696 -5.443 60.254 1.00 38.80 A C
+ATOM 1856 C TYR A 239 -34.716 -4.833 61.206 1.00 37.82 A C
+ATOM 1857 O TYR A 239 -35.311 -5.527 62.035 1.00 36.96 A O
+ATOM 1858 CB TYR A 239 -34.400 -5.920 58.980 1.00 31.71 A C
+ATOM 1859 CG TYR A 239 -33.530 -5.922 57.744 1.00 32.97 A C
+ATOM 1860 CD1 TYR A 239 -32.316 -6.593 57.728 1.00 35.06 A C
+ATOM 1861 CD2 TYR A 239 -33.928 -5.258 56.590 1.00 30.21 A C
+ATOM 1862 CE1 TYR A 239 -31.519 -6.601 56.600 1.00 32.54 A C
+ATOM 1863 CE2 TYR A 239 -33.139 -5.261 55.456 1.00 29.91 A C
+ATOM 1864 CZ TYR A 239 -31.935 -5.934 55.466 1.00 37.95 A C
+ATOM 1865 OH TYR A 239 -31.143 -5.940 54.341 1.00 37.23 A O
+ATOM 1866 N GLU A 240 -34.907 -3.523 61.084 1.00 38.44 A N
+ATOM 1867 CA GLU A 240 -35.923 -2.854 61.876 1.00 42.23 A C
+ATOM 1868 C GLU A 240 -37.312 -3.344 61.467 1.00 40.61 A C
+ATOM 1869 O GLU A 240 -37.544 -3.674 60.302 1.00 44.38 A O
+ATOM 1870 CB GLU A 240 -35.836 -1.342 61.700 1.00 43.45 A C
+ATOM 1871 CG GLU A 240 -34.515 -0.739 62.137 1.00 46.13 A C
+ATOM 1872 CD GLU A 240 -34.532 0.776 62.102 1.00 53.52 A C
+ATOM 1873 OE1 GLU A 240 -33.846 1.398 62.939 1.00 59.47 A O
+ATOM 1874 OE2 GLU A 240 -35.234 1.346 61.239 1.00 57.69 A O1-
+ATOM 1875 N PRO A 241 -38.249 -3.410 62.410 1.00 47.91 A N
+ATOM 1876 CA PRO A 241 -39.607 -3.838 62.060 1.00 45.17 A C
+ATOM 1877 C PRO A 241 -40.286 -2.823 61.155 1.00 44.29 A C
+ATOM 1878 O PRO A 241 -40.181 -1.611 61.358 1.00 49.06 A O
+ATOM 1879 CB PRO A 241 -40.311 -3.939 63.418 1.00 48.34 A C
+ATOM 1880 CG PRO A 241 -39.537 -3.023 64.311 1.00 49.80 A C
+ATOM 1881 CD PRO A 241 -38.112 -3.119 63.848 1.00 43.55 A C
+ATOM 1882 N LEU A 242 -40.980 -3.330 60.141 1.00 49.39 A N
+ATOM 1883 CA LEU A 242 -41.715 -2.484 59.213 1.00 48.40 A C
+ATOM 1884 C LEU A 242 -43.097 -2.190 59.782 1.00 47.01 A C
+ATOM 1885 O LEU A 242 -43.827 -3.110 60.164 1.00 49.95 A O
+ATOM 1886 CB LEU A 242 -41.834 -3.149 57.842 1.00 47.22 A C
+ATOM 1887 CG LEU A 242 -42.174 -2.196 56.695 1.00 47.45 A C
+ATOM 1888 CD1 LEU A 242 -40.953 -1.385 56.295 1.00 40.14 A C
+ATOM 1889 CD2 LEU A 242 -42.730 -2.957 55.505 1.00 45.10 A C
+ATOM 1890 N THR A 243 -43.447 -0.912 59.839 1.00 48.07 A N
+ATOM 1891 CA THR A 243 -44.722 -0.472 60.381 1.00 49.82 A C
+ATOM 1892 C THR A 243 -45.686 -0.117 59.255 1.00 49.20 A C
+ATOM 1893 O THR A 243 -45.311 -0.016 58.084 1.00 48.55 A O
+ATOM 1894 CB THR A 243 -44.526 0.731 61.309 1.00 48.03 A C
+ATOM 1895 CG2 THR A 243 -43.562 0.385 62.433 1.00 47.32 A C
+ATOM 1896 OG1 THR A 243 -43.999 1.833 60.558 1.00 53.04 A O
+ATOM 1897 N GLN A 244 -46.955 0.068 59.629 1.00 51.96 A N
+ATOM 1898 CA GLN A 244 -47.948 0.513 58.657 1.00 52.08 A C
+ATOM 1899 C GLN A 244 -47.639 1.916 58.154 1.00 51.01 A C
+ATOM 1900 O GLN A 244 -47.957 2.249 57.006 1.00 47.96 A O
+ATOM 1901 CB GLN A 244 -49.347 0.460 59.273 1.00 51.18 A C
+ATOM 1902 CG GLN A 244 -50.475 0.670 58.275 1.00 54.26 A C
+ATOM 1903 CD GLN A 244 -50.549 -0.432 57.237 1.00 54.72 A C
+ATOM 1904 NE2 GLN A 244 -50.878 -0.062 56.005 1.00 57.47 A N
+ATOM 1905 OE1 GLN A 244 -50.313 -1.602 57.538 1.00 57.20 A O
+ATOM 1906 N ASP A 245 -47.015 2.748 58.993 1.00 45.99 A N
+ATOM 1907 CA ASP A 245 -46.618 4.082 58.558 1.00 47.89 A C
+ATOM 1908 C ASP A 245 -45.512 4.024 57.512 1.00 47.57 A C
+ATOM 1909 O ASP A 245 -45.474 4.865 56.606 1.00 46.82 A O
+ATOM 1910 CB ASP A 245 -46.171 4.915 59.759 1.00 51.97 A C
+ATOM 1911 CG ASP A 245 -45.823 6.340 59.382 1.00 57.42 A C
+ATOM 1912 OD1 ASP A 245 -46.503 6.902 58.497 1.00 55.98 A O
+ATOM 1913 OD2 ASP A 245 -44.871 6.900 59.966 1.00 65.93 A O1-
+ATOM 1914 N HIS A 246 -44.607 3.048 57.621 1.00 45.42 A N
+ATOM 1915 CA HIS A 246 -43.579 2.876 56.600 1.00 43.93 A C
+ATOM 1916 C HIS A 246 -44.199 2.517 55.255 1.00 48.62 A C
+ATOM 1917 O HIS A 246 -43.751 2.998 54.207 1.00 45.31 A O
+ATOM 1918 CB HIS A 246 -42.583 1.798 57.030 1.00 44.30 A C
+ATOM 1919 CG HIS A 246 -41.765 2.170 58.227 1.00 47.71 A C
+ATOM 1920 CD2 HIS A 246 -41.312 3.370 58.662 1.00 45.28 A C
+ATOM 1921 ND1 HIS A 246 -41.313 1.238 59.137 1.00 46.96 A N
+ATOM 1922 CE1 HIS A 246 -40.619 1.847 60.081 1.00 47.59 A C
+ATOM 1923 NE2 HIS A 246 -40.604 3.142 59.817 1.00 49.38 A N
+ATOM 1924 N VAL A 247 -45.230 1.670 55.267 1.00 47.35 A N
+ATOM 1925 CA VAL A 247 -45.919 1.311 54.031 1.00 48.04 A C
+ATOM 1926 C VAL A 247 -46.585 2.538 53.421 1.00 47.65 A C
+ATOM 1927 O VAL A 247 -46.571 2.728 52.198 1.00 46.30 A O
+ATOM 1928 CB VAL A 247 -46.935 0.185 54.298 1.00 46.32 A C
+ATOM 1929 CG1 VAL A 247 -47.749 -0.111 53.048 1.00 51.18 A C
+ATOM 1930 CG2 VAL A 247 -46.221 -1.067 54.786 1.00 48.81 A C
+ATOM 1931 N ASP A 248 -47.170 3.393 54.262 1.00 47.34 A N
+ATOM 1932 CA ASP A 248 -47.792 4.615 53.763 1.00 51.44 A C
+ATOM 1933 C ASP A 248 -46.756 5.559 53.164 1.00 50.16 A C
+ATOM 1934 O ASP A 248 -47.027 6.229 52.161 1.00 46.82 A O
+ATOM 1935 CB ASP A 248 -48.562 5.308 54.888 1.00 55.15 A C
+ATOM 1936 CG ASP A 248 -49.762 4.508 55.353 1.00 58.06 A C
+ATOM 1937 OD1 ASP A 248 -50.023 3.433 54.774 1.00 59.26 A O
+ATOM 1938 OD2 ASP A 248 -50.445 4.954 56.299 1.00 63.30 A O1-
+ATOM 1939 N ILE A 249 -45.566 5.625 53.765 1.00 45.19 A N
+ATOM 1940 CA ILE A 249 -44.513 6.485 53.235 1.00 44.04 A C
+ATOM 1941 C ILE A 249 -44.048 5.981 51.873 1.00 39.55 A C
+ATOM 1942 O ILE A 249 -43.749 6.772 50.971 1.00 41.30 A O
+ATOM 1943 CB ILE A 249 -43.350 6.582 54.240 1.00 46.18 A C
+ATOM 1944 CG1 ILE A 249 -43.793 7.338 55.494 1.00 49.70 A C
+ATOM 1945 CG2 ILE A 249 -42.148 7.270 53.614 1.00 42.94 A C
+ATOM 1946 CD1 ILE A 249 -42.780 7.304 56.619 1.00 50.92 A C
+ATOM 1947 N LEU A 250 -43.996 4.661 51.697 1.00 42.25 A N
+ATOM 1948 CA LEU A 250 -43.636 4.068 50.415 1.00 39.38 A C
+ATOM 1949 C LEU A 250 -44.776 4.105 49.404 1.00 43.67 A C
+ATOM 1950 O LEU A 250 -44.617 3.573 48.299 1.00 39.75 A O
+ATOM 1951 CB LEU A 250 -43.175 2.623 50.618 1.00 38.35 A C
+ATOM 1952 CG LEU A 250 -41.896 2.426 51.436 1.00 37.43 A C
+ATOM 1953 CD1 LEU A 250 -41.737 0.968 51.836 1.00 34.63 A C
+ATOM 1954 CD2 LEU A 250 -40.681 2.908 50.659 1.00 33.70 A C
+ATOM 1955 N GLY A 251 -45.907 4.714 49.754 1.00 45.30 A N
+ATOM 1956 CA GLY A 251 -47.060 4.795 48.888 1.00 43.60 A C
+ATOM 1957 C GLY A 251 -46.779 5.379 47.516 1.00 44.79 A C
+ATOM 1958 O GLY A 251 -47.056 4.750 46.489 1.00 45.76 A O
+ATOM 1959 N PRO A 252 -46.246 6.607 47.468 1.00 41.67 A N
+ATOM 1960 CA PRO A 252 -45.926 7.211 46.161 1.00 42.38 A C
+ATOM 1961 C PRO A 252 -45.035 6.345 45.286 1.00 45.83 A C
+ATOM 1962 O PRO A 252 -45.278 6.240 44.078 1.00 45.57 A O
+ATOM 1963 CB PRO A 252 -45.236 8.524 46.554 1.00 39.06 A C
+ATOM 1964 CG PRO A 252 -45.842 8.874 47.864 1.00 43.74 A C
+ATOM 1965 CD PRO A 252 -46.072 7.568 48.573 1.00 43.29 A C
+ATOM 1966 N LEU A 253 -44.007 5.717 45.862 1.00 43.10 A N
+ATOM 1967 CA LEU A 253 -43.181 4.803 45.081 1.00 42.15 A C
+ATOM 1968 C LEU A 253 -43.956 3.555 44.678 1.00 44.40 A C
+ATOM 1969 O LEU A 253 -43.698 2.984 43.612 1.00 40.00 A O
+ATOM 1970 CB LEU A 253 -41.928 4.420 45.869 1.00 40.83 A C
+ATOM 1971 CG LEU A 253 -40.964 5.563 46.185 1.00 39.67 A C
+ATOM 1972 CD1 LEU A 253 -39.773 5.057 46.981 1.00 35.17 A C
+ATOM 1973 CD2 LEU A 253 -40.508 6.244 44.904 1.00 41.25 A C
+ATOM 1974 N SER A 254 -44.904 3.120 45.510 1.00 44.93 A N
+ATOM 1975 CA SER A 254 -45.713 1.954 45.171 1.00 42.80 A C
+ATOM 1976 C SER A 254 -46.633 2.244 43.992 1.00 44.95 A C
+ATOM 1977 O SER A 254 -46.858 1.374 43.142 1.00 46.98 A O
+ATOM 1978 CB SER A 254 -46.526 1.510 46.386 1.00 42.20 A C
+ATOM 1979 OG SER A 254 -47.106 0.235 46.173 1.00 46.27 A O
+ATOM 1980 N ALA A 255 -47.174 3.463 43.925 1.00 43.76 A N
+ATOM 1981 CA ALA A 255 -48.091 3.809 42.845 1.00 51.27 A C
+ATOM 1982 C ALA A 255 -47.350 4.013 41.529 1.00 49.66 A C
+ATOM 1983 O ALA A 255 -47.828 3.589 40.471 1.00 55.93 A O
+ATOM 1984 CB ALA A 255 -48.883 5.062 43.216 1.00 41.24 A C
+ATOM 1985 N GLN A 256 -46.183 4.660 41.576 1.00 50.98 A N
+ATOM 1986 CA GLN A 256 -45.441 4.942 40.350 1.00 47.61 A C
+ATOM 1987 C GLN A 256 -44.943 3.662 39.691 1.00 48.35 A C
+ATOM 1988 O GLN A 256 -44.931 3.555 38.459 1.00 54.33 A O
+ATOM 1989 CB GLN A 256 -44.273 5.882 40.652 1.00 48.26 A C
+ATOM 1990 CG GLN A 256 -43.358 6.146 39.465 1.00 51.42 A C
+ATOM 1991 CD GLN A 256 -42.163 7.005 39.830 1.00 59.01 A C
+ATOM 1992 NE2 GLN A 256 -41.197 7.092 38.923 1.00 57.07 A N
+ATOM 1993 OE1 GLN A 256 -42.108 7.582 40.916 1.00 63.84 A O
+ATOM 1994 N THR A 257 -44.534 2.678 40.492 1.00 42.42 A N
+ATOM 1995 CA THR A 257 -43.998 1.433 39.957 1.00 44.98 A C
+ATOM 1996 C THR A 257 -45.061 0.368 39.730 1.00 40.52 A C
+ATOM 1997 O THR A 257 -44.793 -0.612 39.026 1.00 40.68 A O
+ATOM 1998 CB THR A 257 -42.927 0.869 40.895 1.00 43.73 A C
+ATOM 1999 CG2 THR A 257 -41.837 1.898 41.137 1.00 44.22 A C
+ATOM 2000 OG1 THR A 257 -43.527 0.514 42.147 1.00 41.88 A O
+ATOM 2001 N GLY A 258 -46.251 0.530 40.303 1.00 41.89 A N
+ATOM 2002 CA GLY A 258 -47.260 -0.503 40.199 1.00 42.08 A C
+ATOM 2003 C GLY A 258 -46.953 -1.753 40.989 1.00 48.21 A C
+ATOM 2004 O GLY A 258 -47.523 -2.810 40.707 1.00 49.12 A O
+ATOM 2005 N ILE A 259 -46.062 -1.663 41.972 1.00 41.66 A N
+ATOM 2006 CA ILE A 259 -45.675 -2.794 42.807 1.00 43.98 A C
+ATOM 2007 C ILE A 259 -46.094 -2.484 44.235 1.00 46.45 A C
+ATOM 2008 O ILE A 259 -45.639 -1.492 44.819 1.00 42.48 A O
+ATOM 2009 CB ILE A 259 -44.166 -3.073 42.727 1.00 45.86 A C
+ATOM 2010 CG1 ILE A 259 -43.769 -3.441 41.297 1.00 45.12 A C
+ATOM 2011 CG2 ILE A 259 -43.774 -4.177 43.698 1.00 43.52 A C
+ATOM 2012 CD1 ILE A 259 -42.287 -3.351 41.039 1.00 45.86 A C
+ATOM 2013 N ALA A 260 -46.962 -3.325 44.793 1.00 42.04 A N
+ATOM 2014 CA ALA A 260 -47.414 -3.131 46.162 1.00 45.82 A C
+ATOM 2015 C ALA A 260 -46.246 -3.260 47.133 1.00 41.51 A C
+ATOM 2016 O ALA A 260 -45.269 -3.969 46.875 1.00 42.00 A O
+ATOM 2017 CB ALA A 260 -48.506 -4.143 46.512 1.00 45.92 A C
+ATOM 2018 N VAL A 261 -46.354 -2.555 48.262 1.00 45.44 A N
+ATOM 2019 CA VAL A 261 -45.277 -2.556 49.249 1.00 40.11 A C
+ATOM 2020 C VAL A 261 -45.039 -3.962 49.781 1.00 40.40 A C
+ATOM 2021 O VAL A 261 -43.893 -4.413 49.896 1.00 40.00 A O
+ATOM 2022 CB VAL A 261 -45.592 -1.565 50.386 1.00 44.87 A C
+ATOM 2023 CG1 VAL A 261 -44.536 -1.655 51.477 1.00 37.21 A C
+ATOM 2024 CG2 VAL A 261 -45.685 -0.147 49.843 1.00 39.65 A C
+ATOM 2025 N LEU A 262 -46.116 -4.683 50.102 1.00 41.06 A N
+ATOM 2026 CA LEU A 262 -45.973 -6.045 50.600 1.00 40.25 A C
+ATOM 2027 C LEU A 262 -45.451 -6.998 49.532 1.00 41.73 A C
+ATOM 2028 O LEU A 262 -44.880 -8.039 49.875 1.00 41.71 A O
+ATOM 2029 CB LEU A 262 -47.307 -6.544 51.153 1.00 44.86 A C
+ATOM 2030 CG LEU A 262 -47.781 -5.814 52.413 1.00 45.85 A C
+ATOM 2031 CD1 LEU A 262 -49.092 -6.394 52.919 1.00 45.98 A C
+ATOM 2032 CD2 LEU A 262 -46.712 -5.864 53.497 1.00 43.73 A C
+ATOM 2033 N ASP A 263 -45.635 -6.671 48.251 1.00 40.62 A N
+ATOM 2034 CA ASP A 263 -44.984 -7.444 47.199 1.00 42.40 A C
+ATOM 2035 C ASP A 263 -43.481 -7.200 47.198 1.00 41.38 A C
+ATOM 2036 O ASP A 263 -42.693 -8.133 47.001 1.00 38.61 A O
+ATOM 2037 CB ASP A 263 -45.583 -7.096 45.836 1.00 46.15 A C
+ATOM 2038 CG ASP A 263 -47.021 -7.555 45.695 1.00 53.38 A C
+ATOM 2039 OD1 ASP A 263 -47.641 -7.900 46.722 1.00 47.26 A O
+ATOM 2040 OD2 ASP A 263 -47.531 -7.573 44.555 1.00 56.35 A O1-
+ATOM 2041 N MET A 264 -43.066 -5.950 47.419 1.00 41.82 A N
+ATOM 2042 CA MET A 264 -41.642 -5.645 47.502 1.00 42.49 A C
+ATOM 2043 C MET A 264 -41.015 -6.244 48.753 1.00 39.15 A C
+ATOM 2044 O MET A 264 -39.842 -6.633 48.732 1.00 39.74 A O
+ATOM 2045 CB MET A 264 -41.427 -4.132 47.466 1.00 38.06 A C
+ATOM 2046 CG MET A 264 -39.986 -3.717 47.231 1.00 44.12 A C
+ATOM 2047 SD MET A 264 -39.393 -4.188 45.594 1.00 43.04 A S
+ATOM 2048 CE MET A 264 -40.049 -2.855 44.595 1.00 39.43 A C
+ATOM 2049 N CYS A 265 -41.775 -6.325 49.848 1.00 37.07 A N
+ATOM 2050 CA CYS A 265 -41.266 -6.973 51.053 1.00 36.83 A C
+ATOM 2051 C CYS A 265 -41.021 -8.458 50.817 1.00 38.56 A C
+ATOM 2052 O CYS A 265 -40.050 -9.022 51.335 1.00 37.06 A O
+ATOM 2053 CB CYS A 265 -42.240 -6.766 52.212 1.00 40.31 A C
+ATOM 2054 SG CYS A 265 -42.478 -5.039 52.677 1.00 47.47 A S
+ATOM 2055 N ALA A 266 -41.892 -9.107 50.039 1.00 40.63 A N
+ATOM 2056 CA ALA A 266 -41.666 -10.505 49.688 1.00 41.15 A C
+ATOM 2057 C ALA A 266 -40.402 -10.670 48.857 1.00 39.93 A C
+ATOM 2058 O ALA A 266 -39.728 -11.702 48.951 1.00 47.79 A O
+ATOM 2059 CB ALA A 266 -42.875 -11.062 48.936 1.00 47.71 A C
+ATOM 2060 N SER A 267 -40.066 -9.670 48.040 1.00 41.06 A N
+ATOM 2061 CA SER A 267 -38.810 -9.712 47.301 1.00 43.82 A C
+ATOM 2062 C SER A 267 -37.622 -9.502 48.230 1.00 39.34 A C
+ATOM 2063 O SER A 267 -36.579 -10.147 48.070 1.00 40.48 A O
+ATOM 2064 CB SER A 267 -38.817 -8.661 46.191 1.00 38.53 A C
+ATOM 2065 OG SER A 267 -39.821 -8.940 45.232 1.00 48.72 A O
+ATOM 2066 N LEU A 268 -37.760 -8.601 49.206 1.00 38.23 A N
+ATOM 2067 CA LEU A 268 -36.692 -8.394 50.178 1.00 35.14 A C
+ATOM 2068 C LEU A 268 -36.489 -9.631 51.043 1.00 37.02 A C
+ATOM 2069 O LEU A 268 -35.353 -9.971 51.394 1.00 38.62 A O
+ATOM 2070 CB LEU A 268 -37.003 -7.174 51.045 1.00 36.68 A C
+ATOM 2071 CG LEU A 268 -36.013 -6.846 52.164 1.00 33.77 A C
+ATOM 2072 CD1 LEU A 268 -34.598 -6.756 51.616 1.00 30.10 A C
+ATOM 2073 CD2 LEU A 268 -36.402 -5.553 52.864 1.00 31.19 A C
+ATOM 2074 N LYS A 269 -37.580 -10.317 51.395 1.00 38.58 A N
+ATOM 2075 CA LYS A 269 -37.463 -11.549 52.169 1.00 40.10 A C
+ATOM 2076 C LYS A 269 -36.655 -12.597 51.415 1.00 42.05 A C
+ATOM 2077 O LYS A 269 -35.828 -13.300 52.008 1.00 41.92 A O
+ATOM 2078 CB LYS A 269 -38.852 -12.084 52.513 1.00 46.02 A C
+ATOM 2079 CG LYS A 269 -38.846 -13.426 53.224 1.00 51.23 A C
+ATOM 2080 CD LYS A 269 -40.253 -13.987 53.349 1.00 53.17 A C
+ATOM 2081 CE LYS A 269 -41.180 -13.000 54.039 1.00 51.26 A C
+ATOM 2082 NZ LYS A 269 -42.571 -13.519 54.134 1.00 56.30 A N1+
+ATOM 2083 N GLU A 270 -36.877 -12.714 50.104 1.00 43.04 A N
+ATOM 2084 CA GLU A 270 -36.107 -13.665 49.310 1.00 46.48 A C
+ATOM 2085 C GLU A 270 -34.655 -13.222 49.176 1.00 43.84 A C
+ATOM 2086 O GLU A 270 -33.743 -14.057 49.190 1.00 45.21 A O
+ATOM 2087 CB GLU A 270 -36.747 -13.842 47.933 1.00 45.69 A C
+ATOM 2088 CG GLU A 270 -38.113 -14.505 47.972 1.00 51.79 A C
+ATOM 2089 CD GLU A 270 -38.161 -15.683 48.926 1.00 60.94 A C
+ATOM 2090 OE1 GLU A 270 -38.830 -15.573 49.975 1.00 63.77 A O
+ATOM 2091 OE2 GLU A 270 -37.529 -16.718 48.627 1.00 65.14 A O1-
+ATOM 2092 N LEU A 271 -34.419 -11.914 49.046 1.00 45.19 A N
+ATOM 2093 CA LEU A 271 -33.048 -11.415 49.005 1.00 42.45 A C
+ATOM 2094 C LEU A 271 -32.335 -11.666 50.327 1.00 43.35 A C
+ATOM 2095 O LEU A 271 -31.127 -11.929 50.351 1.00 45.28 A O
+ATOM 2096 CB LEU A 271 -33.039 -9.925 48.665 1.00 41.98 A C
+ATOM 2097 CG LEU A 271 -33.507 -9.528 47.264 1.00 41.27 A C
+ATOM 2098 CD1 LEU A 271 -33.534 -8.014 47.117 1.00 37.30 A C
+ATOM 2099 CD2 LEU A 271 -32.622 -10.159 46.201 1.00 46.99 A C
+ATOM 2100 N LEU A 272 -33.068 -11.591 51.440 1.00 42.10 A N
+ATOM 2101 CA LEU A 272 -32.461 -11.854 52.740 1.00 42.09 A C
+ATOM 2102 C LEU A 272 -32.172 -13.338 52.926 1.00 48.89 A C
+ATOM 2103 O LEU A 272 -31.127 -13.710 53.472 1.00 53.66 A O
+ATOM 2104 CB LEU A 272 -33.373 -11.343 53.856 1.00 40.00 A C
+ATOM 2105 CG LEU A 272 -33.439 -9.825 54.033 1.00 41.91 A C
+ATOM 2106 CD1 LEU A 272 -34.425 -9.451 55.129 1.00 35.76 A C
+ATOM 2107 CD2 LEU A 272 -32.058 -9.269 54.332 1.00 44.46 A C
+ATOM 2108 N GLN A 273 -33.082 -14.202 52.471 1.00 52.50 A N
+ATOM 2109 CA GLN A 273 -32.925 -15.635 52.691 1.00 51.77 A C
+ATOM 2110 C GLN A 273 -31.999 -16.272 51.661 1.00 51.92 A C
+ATOM 2111 O GLN A 273 -31.243 -17.192 51.990 1.00 56.61 A O
+ATOM 2112 CB GLN A 273 -34.292 -16.321 52.672 1.00 49.12 A C
+ATOM 2113 CG GLN A 273 -35.164 -16.003 53.876 1.00 46.31 A C
+ATOM 2114 CD GLN A 273 -36.599 -16.457 53.693 1.00 52.57 A C
+ATOM 2115 NE2 GLN A 273 -37.311 -16.631 54.800 1.00 57.13 A N
+ATOM 2116 OE1 GLN A 273 -37.063 -16.649 52.569 1.00 59.44 A O
+ATOM 2117 N ASN A 274 -32.041 -15.799 50.414 1.00 50.67 A N
+ATOM 2118 CA ASN A 274 -31.258 -16.399 49.342 1.00 56.22 A C
+ATOM 2119 C ASN A 274 -29.996 -15.622 48.997 1.00 58.82 A C
+ATOM 2120 O ASN A 274 -29.052 -16.215 48.461 1.00 62.53 A O
+ATOM 2121 CB ASN A 274 -32.108 -16.537 48.071 1.00 54.86 A C
+ATOM 2122 CG ASN A 274 -33.184 -17.594 48.200 1.00 59.96 A C
+ATOM 2123 ND2 ASN A 274 -34.247 -17.272 48.928 1.00 60.96 A N
+ATOM 2124 OD1 ASN A 274 -33.065 -18.687 47.647 1.00 71.24 A O
+ATOM 2125 N GLY A 275 -29.951 -14.326 49.285 1.00 58.14 A N
+ATOM 2126 CA GLY A 275 -28.851 -13.511 48.817 1.00 56.72 A C
+ATOM 2127 C GLY A 275 -29.093 -13.035 47.395 1.00 56.27 A C
+ATOM 2128 O GLY A 275 -30.207 -13.098 46.864 1.00 59.13 A O
+ATOM 2129 N MET A 276 -28.021 -12.553 46.768 1.00 60.37 A N
+ATOM 2130 CA MET A 276 -28.094 -12.061 45.399 1.00 63.91 A C
+ATOM 2131 C MET A 276 -27.532 -13.040 44.377 1.00 67.41 A C
+ATOM 2132 O MET A 276 -27.698 -12.811 43.174 1.00 65.06 A O
+ATOM 2133 CB MET A 276 -27.361 -10.720 45.279 1.00 61.86 A C
+ATOM 2134 CG MET A 276 -27.916 -9.635 46.185 1.00 58.29 A C
+ATOM 2135 SD MET A 276 -27.474 -7.976 45.639 1.00 64.45 A S
+ATOM 2136 CE MET A 276 -28.134 -6.996 46.984 1.00 53.58 A C
+ATOM 2137 N ASN A 277 -26.874 -14.113 44.825 1.00 70.86 A N
+ATOM 2138 CA ASN A 277 -26.324 -15.145 43.943 1.00 69.91 A C
+ATOM 2139 C ASN A 277 -25.333 -14.571 42.935 1.00 69.73 A C
+ATOM 2140 O ASN A 277 -25.185 -15.093 41.827 1.00 72.21 A O
+ATOM 2141 CB ASN A 277 -27.436 -15.911 43.219 1.00 69.32 A C
+ATOM 2142 CG ASN A 277 -28.562 -16.322 44.148 1.00 71.51 A C
+ATOM 2143 ND2 ASN A 277 -28.249 -17.174 45.117 1.00 68.46 A N
+ATOM 2144 OD1 ASN A 277 -29.702 -15.881 43.995 1.00 71.38 A O
+ATOM 2145 N GLY A 278 -24.644 -13.492 43.306 1.00 69.46 A N
+ATOM 2146 CA GLY A 278 -23.637 -12.887 42.462 1.00 66.66 A C
+ATOM 2147 C GLY A 278 -24.118 -11.726 41.617 1.00 62.86 A C
+ATOM 2148 O GLY A 278 -23.292 -11.080 40.961 1.00 66.43 A O
+ATOM 2149 N ARG A 279 -25.418 -11.444 41.608 1.00 62.00 A N
+ATOM 2150 CA ARG A 279 -25.946 -10.330 40.837 1.00 58.14 A C
+ATOM 2151 C ARG A 279 -25.826 -9.033 41.636 1.00 54.97 A C
+ATOM 2152 O ARG A 279 -25.415 -9.020 42.800 1.00 57.06 A O
+ATOM 2153 CB ARG A 279 -27.394 -10.601 40.435 1.00 58.33 A C
+ATOM 2154 CG ARG A 279 -27.543 -11.605 39.305 1.00 61.48 A C
+ATOM 2155 CD ARG A 279 -28.893 -12.299 39.360 1.00 64.48 A C
+ATOM 2156 NE ARG A 279 -29.126 -12.935 40.653 1.00 68.07 A N
+ATOM 2157 CZ ARG A 279 -30.050 -13.865 40.872 1.00 66.61 A C
+ATOM 2158 NH1 ARG A 279 -30.832 -14.271 39.881 1.00 65.70 A N1+
+ATOM 2159 NH2 ARG A 279 -30.192 -14.388 42.081 1.00 64.26 A N
+ATOM 2160 N THR A 280 -26.187 -7.920 41.000 1.00 53.01 A N
+ATOM 2161 CA THR A 280 -26.103 -6.607 41.618 1.00 54.41 A C
+ATOM 2162 C THR A 280 -27.418 -5.863 41.438 1.00 47.56 A C
+ATOM 2163 O THR A 280 -28.215 -6.167 40.546 1.00 47.45 A O
+ATOM 2164 CB THR A 280 -24.955 -5.771 41.030 1.00 51.50 A C
+ATOM 2165 CG2 THR A 280 -23.611 -6.431 41.305 1.00 48.75 A C
+ATOM 2166 OG1 THR A 280 -25.136 -5.632 39.615 1.00 46.19 A O
+ATOM 2167 N ILE A 281 -27.634 -4.877 42.305 1.00 44.13 A N
+ATOM 2168 CA ILE A 281 -28.798 -4.001 42.249 1.00 42.36 A C
+ATOM 2169 C ILE A 281 -28.294 -2.566 42.272 1.00 45.61 A C
+ATOM 2170 O ILE A 281 -27.695 -2.133 43.264 1.00 43.79 A O
+ATOM 2171 CB ILE A 281 -29.770 -4.251 43.414 1.00 41.15 A C
+ATOM 2172 CG1 ILE A 281 -30.359 -5.660 43.331 1.00 44.80 A C
+ATOM 2173 CG2 ILE A 281 -30.877 -3.214 43.410 1.00 43.10 A C
+ATOM 2174 CD1 ILE A 281 -31.258 -6.012 44.497 1.00 39.65 A C
+ATOM 2175 N LEU A 282 -28.531 -1.834 41.182 1.00 43.16 A N
+ATOM 2176 CA LEU A 282 -28.071 -0.451 41.038 1.00 45.23 A C
+ATOM 2177 C LEU A 282 -26.561 -0.343 41.244 1.00 47.58 A C
+ATOM 2178 O LEU A 282 -26.058 0.635 41.801 1.00 45.25 A O
+ATOM 2179 CB LEU A 282 -28.821 0.485 41.990 1.00 41.21 A C
+ATOM 2180 CG LEU A 282 -30.264 0.819 41.604 1.00 38.59 A C
+ATOM 2181 CD1 LEU A 282 -30.929 1.671 42.675 1.00 39.34 A C
+ATOM 2182 CD2 LEU A 282 -30.310 1.518 40.254 1.00 40.02 A C
+ATOM 2183 N GLY A 283 -25.832 -1.362 40.794 1.00 47.85 A N
+ATOM 2184 CA GLY A 283 -24.388 -1.368 40.897 1.00 43.98 A C
+ATOM 2185 C GLY A 283 -23.833 -1.782 42.240 1.00 46.91 A C
+ATOM 2186 O GLY A 283 -22.619 -1.676 42.448 1.00 52.36 A O
+ATOM 2187 N SER A 284 -24.674 -2.251 43.157 1.00 46.38 A N
+ATOM 2188 CA SER A 284 -24.242 -2.652 44.488 1.00 45.39 A C
+ATOM 2189 C SER A 284 -24.530 -4.131 44.699 1.00 45.33 A C
+ATOM 2190 O SER A 284 -25.546 -4.651 44.224 1.00 44.86 A O
+ATOM 2191 CB SER A 284 -24.939 -1.822 45.570 1.00 46.80 A C
+ATOM 2192 OG SER A 284 -24.953 -2.511 46.809 1.00 52.75 A O
+ATOM 2193 N ALA A 285 -23.633 -4.806 45.416 1.00 46.95 A N
+ATOM 2194 CA ALA A 285 -23.763 -6.230 45.690 1.00 49.63 A C
+ATOM 2195 C ALA A 285 -24.365 -6.522 47.058 1.00 46.92 A C
+ATOM 2196 O ALA A 285 -24.538 -7.694 47.404 1.00 46.50 A O
+ATOM 2197 CB ALA A 285 -22.401 -6.918 45.562 1.00 45.38 A C
+ATOM 2198 N LEU A 286 -24.680 -5.496 47.844 1.00 43.38 A N
+ATOM 2199 CA LEU A 286 -25.411 -5.663 49.091 1.00 46.74 A C
+ATOM 2200 C LEU A 286 -26.575 -4.681 49.119 1.00 45.35 A C
+ATOM 2201 O LEU A 286 -26.685 -3.785 48.277 1.00 45.40 A O
+ATOM 2202 CB LEU A 286 -24.505 -5.478 50.320 1.00 44.86 A C
+ATOM 2203 CG LEU A 286 -23.537 -4.295 50.403 1.00 50.21 A C
+ATOM 2204 CD1 LEU A 286 -24.237 -3.026 50.871 1.00 52.98 A C
+ATOM 2205 CD2 LEU A 286 -22.381 -4.638 51.330 1.00 50.75 A C
+ATOM 2206 N LEU A 287 -27.454 -4.861 50.100 1.00 43.05 A N
+ATOM 2207 CA LEU A 287 -28.671 -4.065 50.194 1.00 40.31 A C
+ATOM 2208 C LEU A 287 -28.367 -2.731 50.866 1.00 40.74 A C
+ATOM 2209 O LEU A 287 -27.907 -2.696 52.013 1.00 40.08 A O
+ATOM 2210 CB LEU A 287 -29.743 -4.836 50.960 1.00 39.07 A C
+ATOM 2211 CG LEU A 287 -30.148 -6.166 50.315 1.00 45.82 A C
+ATOM 2212 CD1 LEU A 287 -30.899 -7.046 51.299 1.00 37.38 A C
+ATOM 2213 CD2 LEU A 287 -30.980 -5.927 49.065 1.00 39.23 A C
+ATOM 2214 N GLU A 288 -28.626 -1.637 50.153 1.00 43.94 A N
+ATOM 2215 CA GLU A 288 -28.346 -0.303 50.666 1.00 39.65 A C
+ATOM 2216 C GLU A 288 -29.501 0.199 51.522 1.00 35.61 A C
+ATOM 2217 O GLU A 288 -30.673 0.001 51.187 1.00 33.13 A O
+ATOM 2218 CB GLU A 288 -28.094 0.667 49.512 1.00 40.34 A C
+ATOM 2219 CG GLU A 288 -27.034 0.202 48.527 1.00 43.71 A C
+ATOM 2220 CD GLU A 288 -25.631 0.311 49.088 1.00 54.24 A C
+ATOM 2221 OE1 GLU A 288 -25.415 1.147 49.991 1.00 57.11 A O
+ATOM 2222 OE2 GLU A 288 -24.744 -0.438 48.627 1.00 55.38 A O1-
+ATOM 2223 N ASP A 289 -29.164 0.864 52.632 1.00 34.58 A N
+ATOM 2224 CA ASP A 289 -30.169 1.388 53.551 1.00 31.69 A C
+ATOM 2225 C ASP A 289 -29.940 2.860 53.881 1.00 32.60 A C
+ATOM 2226 O ASP A 289 -30.467 3.352 54.884 1.00 32.84 A O
+ATOM 2227 CB ASP A 289 -30.212 0.557 54.837 1.00 34.39 A C
+ATOM 2228 CG ASP A 289 -29.010 0.794 55.732 1.00 36.52 A C
+ATOM 2229 OD1 ASP A 289 -27.932 1.160 55.215 1.00 34.85 A O
+ATOM 2230 OD2 ASP A 289 -29.143 0.606 56.960 1.00 37.93 A O1-
+ATOM 2231 N GLU A 290 -29.171 3.577 53.060 1.00 30.06 A N
+ATOM 2232 CA GLU A 290 -28.884 4.986 53.298 1.00 37.11 A C
+ATOM 2233 C GLU A 290 -29.628 5.902 52.332 1.00 36.71 A C
+ATOM 2234 O GLU A 290 -29.228 7.055 52.144 1.00 36.45 A O
+ATOM 2235 CB GLU A 290 -27.377 5.240 53.224 1.00 42.67 A C
+ATOM 2236 CG GLU A 290 -26.565 4.420 54.218 1.00 39.72 A C
+ATOM 2237 CD GLU A 290 -25.689 5.277 55.113 1.00 49.42 A C
+ATOM 2238 OE1 GLU A 290 -25.329 6.400 54.700 1.00 46.04 A O
+ATOM 2239 OE2 GLU A 290 -25.366 4.829 56.235 1.00 45.74 A O1-
+ATOM 2240 N PHE A 291 -30.701 5.412 51.714 1.00 32.45 A N
+ATOM 2241 CA PHE A 291 -31.556 6.214 50.846 1.00 30.40 A C
+ATOM 2242 C PHE A 291 -32.960 6.229 51.430 1.00 28.93 A C
+ATOM 2243 O PHE A 291 -33.613 5.183 51.508 1.00 33.65 A O
+ATOM 2244 CB PHE A 291 -31.584 5.660 49.419 1.00 35.18 A C
+ATOM 2245 CG PHE A 291 -30.269 5.747 48.702 1.00 35.16 A C
+ATOM 2246 CD1 PHE A 291 -29.843 6.943 48.148 1.00 41.40 A C
+ATOM 2247 CD2 PHE A 291 -29.464 4.628 48.568 1.00 39.83 A C
+ATOM 2248 CE1 PHE A 291 -28.634 7.023 47.481 1.00 40.28 A C
+ATOM 2249 CE2 PHE A 291 -28.255 4.701 47.904 1.00 42.31 A C
+ATOM 2250 CZ PHE A 291 -27.839 5.900 47.359 1.00 44.36 A C
+ATOM 2251 N THR A 292 -33.421 7.405 51.836 1.00 29.18 A N
+ATOM 2252 CA THR A 292 -34.782 7.545 52.324 1.00 32.67 A C
+ATOM 2253 C THR A 292 -35.765 7.531 51.157 1.00 34.56 A C
+ATOM 2254 O THR A 292 -35.377 7.732 50.003 1.00 31.43 A O
+ATOM 2255 CB THR A 292 -34.930 8.843 53.114 1.00 34.07 A C
+ATOM 2256 CG2 THR A 292 -33.818 8.973 54.142 1.00 33.60 A C
+ATOM 2257 OG1 THR A 292 -34.881 9.960 52.217 1.00 35.62 A O
+ATOM 2258 N PRO A 293 -37.047 7.272 51.428 1.00 31.23 A N
+ATOM 2259 CA PRO A 293 -38.054 7.428 50.366 1.00 33.28 A C
+ATOM 2260 C PRO A 293 -38.059 8.815 49.749 1.00 36.53 A C
+ATOM 2261 O PRO A 293 -38.328 8.948 48.549 1.00 33.40 A O
+ATOM 2262 CB PRO A 293 -39.371 7.119 51.089 1.00 31.22 A C
+ATOM 2263 CG PRO A 293 -38.975 6.190 52.181 1.00 34.10 A C
+ATOM 2264 CD PRO A 293 -37.614 6.646 52.636 1.00 35.28 A C
+ATOM 2265 N PHE A 294 -37.763 9.854 50.535 1.00 37.82 A N
+ATOM 2266 CA PHE A 294 -37.644 11.195 49.974 1.00 37.77 A C
+ATOM 2267 C PHE A 294 -36.470 11.283 49.007 1.00 36.09 A C
+ATOM 2268 O PHE A 294 -36.580 11.898 47.939 1.00 35.93 A O
+ATOM 2269 CB PHE A 294 -37.494 12.222 51.098 1.00 39.53 A C
+ATOM 2270 CG PHE A 294 -37.046 13.579 50.629 1.00 46.89 A C
+ATOM 2271 CD1 PHE A 294 -37.962 14.491 50.131 1.00 46.71 A C
+ATOM 2272 CD2 PHE A 294 -35.710 13.946 50.694 1.00 46.02 A C
+ATOM 2273 CE1 PHE A 294 -37.555 15.740 49.699 1.00 45.80 A C
+ATOM 2274 CE2 PHE A 294 -35.297 15.193 50.263 1.00 50.10 A C
+ATOM 2275 CZ PHE A 294 -36.221 16.091 49.766 1.00 49.44 A C
+ATOM 2276 N ASP A 295 -35.335 10.677 49.366 1.00 35.46 A N
+ATOM 2277 CA ASP A 295 -34.169 10.702 48.488 1.00 36.98 A C
+ATOM 2278 C ASP A 295 -34.461 10.007 47.164 1.00 39.00 A C
+ATOM 2279 O ASP A 295 -33.961 10.422 46.112 1.00 37.31 A O
+ATOM 2280 CB ASP A 295 -32.974 10.046 49.182 1.00 35.68 A C
+ATOM 2281 CG ASP A 295 -32.512 10.817 50.404 1.00 43.97 A C
+ATOM 2282 OD1 ASP A 295 -32.531 12.065 50.364 1.00 48.13 A O
+ATOM 2283 OD2 ASP A 295 -32.130 10.174 51.406 1.00 36.81 A O1-
+ATOM 2284 N VAL A 296 -35.273 8.949 47.197 1.00 35.51 A N
+ATOM 2285 CA VAL A 296 -35.595 8.217 45.976 1.00 38.02 A C
+ATOM 2286 C VAL A 296 -36.552 9.025 45.107 1.00 40.16 A C
+ATOM 2287 O VAL A 296 -36.359 9.146 43.891 1.00 45.87 A O
+ATOM 2288 CB VAL A 296 -36.174 6.833 46.321 1.00 35.27 A C
+ATOM 2289 CG1 VAL A 296 -36.681 6.141 45.066 1.00 39.63 A C
+ATOM 2290 CG2 VAL A 296 -35.128 5.982 47.023 1.00 29.11 A C
+ATOM 2291 N VAL A 297 -37.598 9.589 45.718 1.00 38.46 A N
+ATOM 2292 CA VAL A 297 -38.575 10.374 44.966 1.00 45.90 A C
+ATOM 2293 C VAL A 297 -37.904 11.567 44.297 1.00 49.13 A C
+ATOM 2294 O VAL A 297 -38.184 11.887 43.135 1.00 52.12 A O
+ATOM 2295 CB VAL A 297 -39.724 10.819 45.892 1.00 45.77 A C
+ATOM 2296 CG1 VAL A 297 -40.575 11.887 45.220 1.00 44.51 A C
+ATOM 2297 CG2 VAL A 297 -40.577 9.627 46.294 1.00 44.40 A C
+ATOM 2298 N ARG A 298 -36.998 12.232 45.015 1.00 46.70 A N
+ATOM 2299 CA ARG A 298 -36.320 13.412 44.491 1.00 44.22 A C
+ATOM 2300 C ARG A 298 -35.428 13.088 43.296 1.00 50.73 A C
+ATOM 2301 O ARG A 298 -35.115 13.988 42.508 1.00 54.75 A O
+ATOM 2302 CB ARG A 298 -35.529 14.070 45.631 1.00 51.51 A C
+ATOM 2303 CG ARG A 298 -34.202 14.721 45.273 1.00 49.71 A C
+ATOM 2304 CD ARG A 298 -33.661 15.490 46.472 1.00 57.86 A C
+ATOM 2305 NE ARG A 298 -32.345 16.073 46.226 1.00 54.95 A N
+ATOM 2306 CZ ARG A 298 -31.228 15.674 46.826 1.00 55.85 A C
+ATOM 2307 NH1 ARG A 298 -31.264 14.684 47.709 1.00 53.66 A N1+
+ATOM 2308 NH2 ARG A 298 -30.074 16.264 46.545 1.00 43.01 A N
+ATOM 2309 N GLN A 299 -35.053 11.819 43.113 1.00 53.74 A N
+ATOM 2310 CA GLN A 299 -34.139 11.428 42.050 1.00 49.75 A C
+ATOM 2311 C GLN A 299 -34.768 10.576 40.954 1.00 52.89 A C
+ATOM 2312 O GLN A 299 -34.167 10.449 39.884 1.00 57.18 A O
+ATOM 2313 CB GLN A 299 -32.947 10.655 42.635 1.00 46.73 A C
+ATOM 2314 CG GLN A 299 -31.643 11.431 42.674 1.00 41.40 A C
+ATOM 2315 CD GLN A 299 -30.438 10.526 42.853 1.00 41.78 A C
+ATOM 2316 NE2 GLN A 299 -30.087 10.248 44.104 1.00 37.06 A N
+ATOM 2317 OE1 GLN A 299 -29.830 10.082 41.879 1.00 37.77 A O
+ATOM 2318 N CYS A 300 -35.950 9.995 41.181 1.00 53.23 A N
+ATOM 2319 CA CYS A 300 -36.463 8.962 40.288 1.00 54.39 A C
+ATOM 2320 C CYS A 300 -37.876 9.184 39.762 1.00 66.24 A C
+ATOM 2321 O CYS A 300 -38.303 8.426 38.886 1.00 64.02 A O
+ATOM 2322 CB CYS A 300 -36.423 7.591 40.983 1.00 55.59 A C
+ATOM 2323 SG CYS A 300 -34.767 7.016 41.416 1.00 58.53 A S
+ATOM 2324 N SER A 301 -38.616 10.177 40.253 1.00 63.98 A N
+ATOM 2325 CA SER A 301 -40.000 10.343 39.824 1.00 68.50 A C
+ATOM 2326 C SER A 301 -40.132 10.916 38.418 1.00 66.76 A C
+ATOM 2327 O SER A 301 -41.234 10.888 37.858 1.00 67.80 A O
+ATOM 2328 CB SER A 301 -40.761 11.225 40.816 1.00 66.83 A C
+ATOM 2329 OG SER A 301 -41.110 10.491 41.978 1.00 66.17 A O
+ATOM 2330 N GLY A 302 -39.050 11.428 37.837 1.00 66.59 A N
+ATOM 2331 CA GLY A 302 -39.082 11.879 36.459 1.00 70.74 A C
+ATOM 2332 C GLY A 302 -38.753 10.763 35.488 1.00 70.30 A C
+ATOM 2333 O GLY A 302 -38.308 11.013 34.363 1.00 72.05 A O
+ATOM 2334 N VAL A 303 -38.967 9.520 35.922 1.00 70.54 A N
+ATOM 2335 CA VAL A 303 -38.671 8.330 35.137 1.00 70.96 A C
+ATOM 2336 C VAL A 303 -39.919 7.456 35.097 1.00 71.79 A C
+ATOM 2337 O VAL A 303 -40.791 7.537 35.964 1.00 75.15 A O
+ATOM 2338 CB VAL A 303 -37.475 7.536 35.717 1.00 71.23 A C
+ATOM 2339 CG1 VAL A 303 -36.869 6.615 34.672 1.00 65.59 A C
+ATOM 2340 CG2 VAL A 303 -36.415 8.479 36.278 1.00 67.41 A C
+ATOM 2341 N THR A 304 -40.002 6.614 34.069 1.00 78.33 A N
+ATOM 2342 CA THR A 304 -41.037 5.589 34.051 1.00 83.04 A C
+ATOM 2343 C THR A 304 -40.429 4.204 33.814 1.00 78.65 A C
+ATOM 2344 O THR A 304 -40.511 3.349 34.700 1.00 79.54 A O
+ATOM 2345 CB THR A 304 -42.140 5.955 33.037 1.00 83.63 A C
+ATOM 2346 CG2 THR A 304 -41.611 6.143 31.607 1.00 79.08 A C
+ATOM 2347 OG1 THR A 304 -43.200 4.988 33.088 1.00 85.88 A O
+ATOM 2348 N PHE A 305 -39.779 3.983 32.668 1.00 77.77 A N
+ATOM 2349 CA PHE A 305 -39.123 2.709 32.349 1.00 80.32 A C
+ATOM 2350 C PHE A 305 -40.037 1.518 32.626 1.00 79.61 A C
+ATOM 2351 O PHE A 305 -39.623 0.503 33.191 1.00 76.29 A O
+ATOM 2352 CB PHE A 305 -37.799 2.567 33.104 1.00 75.88 A C
+ATOM 2353 CG PHE A 305 -36.716 1.894 32.306 1.00 75.68 A C
+ATOM 2354 CD1 PHE A 305 -36.485 2.260 30.994 1.00 79.28 A C
+ATOM 2355 CD2 PHE A 305 -35.930 0.902 32.865 1.00 71.73 A C
+ATOM 2356 CE1 PHE A 305 -35.492 1.649 30.250 1.00 79.40 A C
+ATOM 2357 CE2 PHE A 305 -34.931 0.285 32.126 1.00 73.41 A C
+ATOM 2358 CZ PHE A 305 -34.712 0.661 30.818 1.00 75.84 A C
+ATOM 2359 N GLN A 306 -41.298 1.653 32.232 1.00 80.67 A N
+ATOM 2360 CA GLN A 306 -42.296 0.612 32.439 1.00 77.22 A C
+ATOM 2361 C GLN A 306 -42.032 -0.599 31.550 1.00 70.87 A C
+ATOM 2362 O GLN A 306 -42.774 -1.581 31.583 1.00 68.39 A O
+ATOM 2363 CB GLN A 306 -43.702 1.159 32.175 1.00 77.17 A C
+ATOM 2364 CG GLN A 306 -44.077 1.275 30.699 1.00 78.18 A C
+ATOM 2365 CD GLN A 306 -43.097 2.109 29.893 1.00 78.00 A C
+ATOM 2366 NE2 GLN A 306 -42.864 1.710 28.648 1.00 71.18 A N
+ATOM 2367 OE1 GLN A 306 -42.557 3.100 30.385 1.00 83.17 A O
+TER
+HETATM 2368 O1 02J C 1 -10.048 3.755 74.575 1.00 63.01 B O
+HETATM 2369 N2 02J C 1 -10.585 4.861 74.114 1.00 56.79 B N
+HETATM 2370 C3 02J C 1 -10.848 4.738 72.810 1.00 50.26 B C
+HETATM 2371 C4 02J C 1 -10.425 3.420 72.447 1.00 54.38 B C
+HETATM 2372 C5 02J C 1 -9.924 2.857 73.642 1.00 63.03 B C
+HETATM 2373 C6 02J C 1 -9.345 1.458 73.806 1.00 64.36 B C
+HETATM 2374 C41 02J C 1 -11.475 5.798 71.891 1.00 47.56 B C
+HETATM 2375 O42 02J C 1 -11.062 5.943 70.793 1.00 47.13 B O
+ATOM 2376 N ALA C 2 -12.583 6.625 72.374 1.00 41.65 B N
+ATOM 2377 CA ALA C 2 -13.166 7.625 71.495 1.00 42.30 B C
+ATOM 2378 C ALA C 2 -12.115 8.750 71.241 1.00 41.96 B C
+ATOM 2379 O ALA C 2 -11.466 9.159 72.125 1.00 41.95 B O
+ATOM 2380 CB ALA C 2 -14.397 8.218 72.132 1.00 36.98 B C
+ATOM 2381 N VAL C 3 -11.943 9.281 69.911 1.00 34.91 B N
+ATOM 2382 CA VAL C 3 -10.955 10.336 69.666 1.00 36.29 B C
+ATOM 2383 C VAL C 3 -11.663 11.606 69.273 1.00 40.78 B C
+ATOM 2384 O VAL C 3 -12.381 11.617 68.328 1.00 36.69 B O
+ATOM 2385 CB VAL C 3 -10.004 9.895 68.515 1.00 37.53 B C
+ATOM 2386 CG1 VAL C 3 -9.130 11.086 68.012 1.00 40.26 B C
+ATOM 2387 CG2 VAL C 3 -9.116 8.687 68.955 1.00 43.10 B C
+ATOM 2388 N LEU C 4 -11.452 12.859 70.085 1.00 37.32 B N
+ATOM 2389 CA LEU C 4 -12.124 14.096 69.716 1.00 39.95 B C
+ATOM 2390 C LEU C 4 -11.582 14.561 68.334 1.00 38.38 B C
+ATOM 2391 O LEU C 4 -10.411 14.570 68.131 1.00 44.55 B O
+ATOM 2392 CB LEU C 4 -11.825 15.155 70.765 1.00 41.97 B C
+ATOM 2393 CG LEU C 4 -13.001 15.397 71.764 1.00 45.86 B C
+ATOM 2394 CD1 LEU C 4 -13.834 14.100 72.019 1.00 43.70 B C
+ATOM 2395 CD2 LEU C 4 -12.487 15.982 73.082 1.00 43.98 B C
+TER
+HETATM 2396 N5 PJE C 5 -12.524 14.987 67.260 1.00 34.60 B N
+HETATM 2397 N6 PJE C 5 -11.238 11.571 63.275 1.00 35.08 B N
+HETATM 2398 O7 PJE C 5 -10.354 17.731 67.451 1.00 57.27 B O
+HETATM 2399 O8 PJE C 5 -13.440 12.730 63.491 1.00 31.54 B O
+HETATM 2400 C19 PJE C 5 -11.993 15.425 65.951 1.00 40.54 B C
+HETATM 2401 C20 PJE C 5 -12.499 16.817 65.647 1.00 36.98 B C
+HETATM 2402 C21 PJE C 5 -11.365 17.802 65.289 1.00 45.43 B C
+HETATM 2403 C22 PJE C 5 -10.167 17.764 66.278 1.00 52.38 B C
+HETATM 2404 C25 PJE C 5 -12.456 14.464 64.858 1.00 30.76 B C
+HETATM 2405 C26 PJE C 5 -11.827 13.003 65.048 1.00 34.19 B C
+HETATM 2406 C27 PJE C 5 -10.215 13.041 64.725 1.00 40.55 B C
+HETATM 2407 C28 PJE C 5 -9.925 12.061 63.836 1.00 39.60 B C
+HETATM 2408 C29 PJE C 5 -12.383 12.148 64.256 1.00 34.70 B C
+HETATM 2409 C 010 C 6 -7.830 17.582 66.759 1.00 63.14 B C
+HETATM 2410 O 010 C 6 -8.840 17.782 65.766 1.00 52.13 B O
+HETATM 2411 C1 010 C 6 -5.739 18.930 67.322 1.00 68.45 B C
+HETATM 2412 C2 010 C 6 -5.067 20.138 67.502 1.00 70.02 B C
+HETATM 2413 C3 010 C 6 -5.744 21.347 67.320 1.00 58.91 B C
+HETATM 2414 C4 010 C 6 -7.085 21.339 66.961 1.00 57.63 B C
+HETATM 2415 C5 010 C 6 -7.760 20.134 66.778 1.00 62.65 B C
+HETATM 2416 C6 010 C 6 -7.082 18.927 66.959 1.00 66.95 B C
+HETATM 2417 O HOH A 401 -11.396 36.755 67.015 1.00 44.82 C O
+HETATM 2418 O HOH A 402 -31.222 19.553 70.556 1.00 39.23 C O
+HETATM 2419 O HOH A 403 -47.862 -5.632 43.371 1.00 42.02 C O
+HETATM 2420 O HOH A 404 -26.339 2.976 51.107 1.00 43.61 C O
+HETATM 2421 O HOH A 405 -28.990 -6.912 54.661 1.00 49.02 C O
+HETATM 2422 O HOH A 406 -35.910 6.292 56.674 1.00 35.79 C O
+HETATM 2423 O HOH A 407 -38.600 -1.119 35.531 1.00 40.87 C O
+HETATM 2424 O HOH A 408 -30.477 14.159 52.626 1.00 36.39 C O
+HETATM 2425 O HOH A 409 -24.109 6.893 58.019 1.00 33.26 C O
+HETATM 2426 O HOH A 410 -7.786 25.011 83.208 1.00 51.94 C O
+HETATM 2427 O HOH A 411 -7.908 25.459 73.866 1.00 49.73 C O
+HETATM 2428 O HOH A 412 -33.454 22.196 67.094 1.00 42.72 C O
+HETATM 2429 O HOH A 413 -11.106 11.922 55.222 1.00 43.64 C O
+HETATM 2430 O HOH A 414 -32.723 3.709 66.874 1.00 49.24 C O
+HETATM 2431 O HOH A 415 -24.947 11.967 75.516 1.00 44.74 C O
+HETATM 2432 O HOH A 416 -9.872 22.828 61.517 1.00 42.58 C O
+HETATM 2433 O HOH A 417 -36.126 20.846 58.232 1.00 54.40 C O
+HETATM 2434 O HOH A 418 -28.841 14.028 73.530 1.00 35.86 C O
+HETATM 2435 O HOH A 419 -25.942 4.008 70.311 1.00 29.32 C O
+HETATM 2436 O HOH A 420 -33.000 18.562 45.717 1.00 50.95 C O
+HETATM 2437 O HOH A 421 -18.980 22.168 57.582 1.00 30.35 C O
+HETATM 2438 O HOH A 422 -21.040 15.276 76.601 1.00 38.79 C O
+HETATM 2439 O HOH A 423 -8.936 31.124 64.275 1.00 45.45 C O
+HETATM 2440 O HOH A 424 -26.136 25.492 48.183 1.00 43.24 C O
+HETATM 2441 O HOH A 425 -23.746 11.016 67.468 1.00 27.37 C O
+HETATM 2442 O HOH A 426 -6.321 25.450 86.112 1.00 63.03 C O
+HETATM 2443 O HOH A 427 -42.521 3.816 61.535 1.00 43.86 C O
+HETATM 2444 O HOH A 428 -48.693 -1.344 48.701 1.00 48.99 C O
+HETATM 2445 O HOH A 429 -28.692 -9.242 57.896 1.00 49.31 C O
+HETATM 2446 O HOH A 430 -11.939 15.977 52.102 1.00 47.83 C O
+HETATM 2447 O HOH A 431 -36.176 -11.443 45.735 1.00 41.94 C O
+HETATM 2448 O HOH A 432 -33.951 26.668 64.570 1.00 47.43 C O
+HETATM 2449 O HOH A 433 -11.376 4.722 78.466 1.00 54.07 C O
+HETATM 2450 O HOH A 434 -21.887 9.966 45.107 1.00 41.00 C O
+HETATM 2451 O HOH A 435 -36.238 11.940 32.850 1.00 45.64 C O
+HETATM 2452 O HOH A 436 -47.189 -13.765 54.665 1.00 55.09 C O
+HETATM 2453 O HOH A 437 -29.663 21.018 64.739 1.00 34.81 C O
+HETATM 2454 O HOH A 438 -50.213 -7.644 56.288 1.00 46.21 C O
+HETATM 2455 O HOH A 439 -22.095 1.932 64.485 1.00 45.51 C O
+HETATM 2456 O HOH A 440 -33.652 13.184 56.103 1.00 44.94 C O
+HETATM 2457 O HOH A 441 -21.340 -2.148 71.596 1.00 52.72 C O
+HETATM 2458 O HOH A 442 -28.890 10.992 47.714 1.00 38.14 C O
+HETATM 2459 O HOH A 443 -26.992 -6.965 51.875 1.00 52.25 C O
+HETATM 2460 O HOH A 444 -22.766 11.524 48.675 1.00 39.36 C O
+HETATM 2461 O HOH A 445 -17.336 19.119 72.308 1.00 31.79 C O
+HETATM 2462 O HOH A 446 -34.776 9.513 33.078 1.00 45.72 C O
+HETATM 2463 O HOH A 447 -23.961 31.293 52.318 1.00 46.53 C O
+HETATM 2464 O HOH A 448 -27.427 16.910 75.823 1.00 41.86 C O
+HETATM 2465 O HOH A 449 -27.091 1.523 45.046 1.00 45.53 C O
+HETATM 2466 O HOH A 450 -23.673 13.892 76.124 1.00 39.89 C O
+HETATM 2467 O HOH A 451 -35.400 8.273 67.861 1.00 33.83 C O
+HETATM 2468 O HOH A 452 -20.247 15.161 79.391 1.00 48.26 C O
+HETATM 2469 O HOH A 453 -25.278 16.075 74.807 1.00 30.25 C O
+HETATM 2470 O HOH A 454 -26.097 1.261 53.052 1.00 42.12 C O
+HETATM 2471 O HOH A 455 -31.428 2.735 50.894 1.00 35.66 C O
+HETATM 2472 O HOH A 456 -38.302 9.890 53.337 1.00 39.24 C O
+HETATM 2473 O HOH A 457 -31.386 11.649 46.303 1.00 38.03 C O
+HETATM 2474 O HOH A 458 -20.120 1.283 65.649 1.00 48.59 C O
+HETATM 2475 O HOH A 459 -50.101 -3.677 39.790 1.00 49.35 C O
+HETATM 2476 O HOH A 460 -48.679 -3.407 49.869 1.00 45.88 C O
+HETATM 2477 O HOH A 461 -22.166 29.458 79.439 1.00 38.05 C O
+HETATM 2478 O HOH A 462 -17.937 18.744 81.787 1.00 42.38 C O
+HETATM 2479 O HOH A 463 -31.822 18.384 58.400 1.00 44.80 C O
+HETATM 2480 O HOH A 464 -29.412 9.966 50.411 1.00 39.71 C O
+HETATM 2481 O HOH A 465 -17.334 5.659 56.689 1.00 43.30 C O
+HETATM 2482 O HOH A 466 -22.985 43.446 61.307 1.00 49.15 C O
+HETATM 2483 O HOH A 467 -31.526 34.297 57.711 1.00 43.66 C O
+HETATM 2484 O HOH A 468 -38.016 0.615 58.807 1.00 36.74 C O
+HETATM 2485 O HOH A 469 -33.439 12.382 67.634 1.00 33.96 C O
+HETATM 2486 O HOH A 470 -18.865 36.012 55.044 1.00 53.31 C O
+HETATM 2487 O HOH A 471 -21.918 4.651 74.966 1.00 48.67 C O
+HETATM 2488 O HOH A 472 -33.555 32.086 59.190 1.00 40.80 C O
+HETATM 2489 O HOH A 473 -21.527 -3.206 47.118 0.50 43.20 C O
+HETATM 2490 O HOH A 474 -31.617 20.843 66.736 1.00 39.00 C O
+HETATM 2491 O HOH A 475 -23.984 4.531 39.514 1.00 49.49 C O
+HETATM 2492 O HOH A 476 -50.778 -5.153 56.973 1.00 57.15 C O
+HETATM 2493 O HOH A 477 -4.345 30.608 60.191 1.00 58.55 C O
+HETATM 2494 O HOH A 478 -4.609 28.863 58.266 1.00 60.66 C O
+HETATM 2495 O HOH A 479 -39.000 13.626 63.293 1.00 43.80 C O
+HETATM 2496 O HOH A 480 -29.483 5.661 73.412 1.00 47.54 C O
+HETATM 2497 O HOH A 481 -28.037 4.052 71.546 1.00 39.18 C O
+HETATM 2498 O HOH A 482 -27.210 -9.165 50.684 1.00 51.98 C O
+HETATM 2499 O HOH A 483 -36.053 4.725 65.510 1.00 47.25 C O
+HETATM 2500 O HOH A 484 -17.642 38.250 54.728 1.00 63.41 C O
+CONECT 1120 2401
+CONECT 2368 2369 2372
+CONECT 2369 2368 2370
+CONECT 2370 2369 2374 2371
+CONECT 2371 2370 2372
+CONECT 2372 2371 2368 2373
+CONECT 2373 2372
+CONECT 2374 2370 2375 2376
+CONECT 2375 2374
+CONECT 2376 2374
+CONECT 2390 2396
+CONECT 2396 2390 2400
+CONECT 2397 2408 2407
+CONECT 2398 2403
+CONECT 2399 2408
+CONECT 2400 2396 2401 2404
+CONECT 2401 1120 2400 2402
+CONECT 2402 2401 2403
+CONECT 2403 2402 2398 2410
+CONECT 2404 2400 2405
+CONECT 2405 2404 2406 2408
+CONECT 2406 2405 2407
+CONECT 2407 2406 2397
+CONECT 2408 2397 2405 2399
+CONECT 2409 2410 2416
+CONECT 2410 2403 2409
+CONECT 2411 2412 2416
+CONECT 2412 2411 2413
+CONECT 2413 2412 2414
+CONECT 2414 2413 2415
+CONECT 2415 2414 2416
+CONECT 2416 2409 2411 2415
+END
diff --git a/Docking/Target/6y84.cif b/Docking/Target/6y84.cif
new file mode 100755
index 0000000..3b8aa38
--- /dev/null
+++ b/Docking/Target/6y84.cif
@@ -0,0 +1,7803 @@
+data_6Y84
+#
+_entry.id 6Y84
+#
+_audit_conform.dict_name mmcif_pdbx.dic
+_audit_conform.dict_version 5.322
+_audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic
+#
+loop_
+_database_2.database_id
+_database_2.database_code
+PDB 6Y84
+WWPDB D_1292107053
+#
+_pdbx_database_status.status_code REL
+_pdbx_database_status.status_code_sf REL
+_pdbx_database_status.status_code_mr ?
+_pdbx_database_status.entry_id 6Y84
+_pdbx_database_status.recvd_initial_deposition_date 2020-03-03
+_pdbx_database_status.SG_entry N
+_pdbx_database_status.deposit_site PDBE
+_pdbx_database_status.process_site PDBE
+_pdbx_database_status.status_code_cs ?
+_pdbx_database_status.methods_development_category ?
+_pdbx_database_status.pdb_format_compatible Y
+#
+loop_
+_audit_author.name
+_audit_author.pdbx_ordinal
+_audit_author.identifier_ORCID
+'Owen, C.D.' 1 ?
+'Lukacik, P.' 2 ?
+'Strain-Damerell, C.M.' 3 ?
+'Douangamath, A.' 4 ?
+'Powell, A.J.' 5 ?
+'Fearon, D.' 6 ?
+'Brandao-Neto, J.' 7 ?
+'Crawshaw, A.D.' 8 ?
+'Aragao, D.' 9 ?
+'Williams, M.' 10 ?
+'Flaig, R.' 11 ?
+'Hall, D.' 12 ?
+'McAauley, K.' 13 ?
+'Stuart, D.I.' 14 ?
+'von Delft, F.' 15 ?
+'Walsh, M.A.' 16 ?
+#
+_citation.abstract ?
+_citation.abstract_id_CAS ?
+_citation.book_id_ISBN ?
+_citation.book_publisher ?
+_citation.book_publisher_city ?
+_citation.book_title ?
+_citation.coordinate_linkage ?
+_citation.country ?
+_citation.database_id_Medline ?
+_citation.details ?
+_citation.id primary
+_citation.journal_abbrev 'To Be Published'
+_citation.journal_id_ASTM ?
+_citation.journal_id_CSD 0353
+_citation.journal_id_ISSN ?
+_citation.journal_full ?
+_citation.journal_issue ?
+_citation.journal_volume ?
+_citation.language ?
+_citation.page_first ?
+_citation.page_last ?
+_citation.title 'COVID-19 main protease with unliganded active site'
+_citation.year ?
+_citation.database_id_CSD ?
+_citation.pdbx_database_id_DOI ?
+_citation.pdbx_database_id_PubMed ?
+_citation.unpublished_flag ?
+#
+loop_
+_citation_author.citation_id
+_citation_author.name
+_citation_author.ordinal
+_citation_author.identifier_ORCID
+primary 'Owen, C.D.' 1 ?
+primary 'Lukacik, P.' 2 ?
+primary 'Strain-Damerell, C.M.' 3 ?
+primary 'Douangamath, A.' 4 ?
+primary 'Powell, A.J.' 5 ?
+primary 'Fearon, D.' 6 ?
+primary 'Brandao-Neto, J.' 7 ?
+primary 'Crawshaw, A.D.' 8 ?
+primary 'Aragao, D.' 9 ?
+primary 'Williams, M.' 10 ?
+primary 'Flaig, R.' 11 ?
+primary 'Hall, D.' 12 ?
+primary 'McAauley, K.' 13 ?
+primary 'Stuart, D.I.' 14 ?
+primary 'von Delft, F.' 15 ?
+primary 'Walsh, M.A.' 16 ?
+#
+_cell.angle_alpha 90.000
+_cell.angle_alpha_esd ?
+_cell.angle_beta 103.160
+_cell.angle_beta_esd ?
+_cell.angle_gamma 90.000
+_cell.angle_gamma_esd ?
+_cell.entry_id 6Y84
+_cell.details ?
+_cell.formula_units_Z ?
+_cell.length_a 112.812
+_cell.length_a_esd ?
+_cell.length_b 52.949
+_cell.length_b_esd ?
+_cell.length_c 44.631
+_cell.length_c_esd ?
+_cell.volume ?
+_cell.volume_esd ?
+_cell.Z_PDB 4
+_cell.reciprocal_angle_alpha ?
+_cell.reciprocal_angle_beta ?
+_cell.reciprocal_angle_gamma ?
+_cell.reciprocal_angle_alpha_esd ?
+_cell.reciprocal_angle_beta_esd ?
+_cell.reciprocal_angle_gamma_esd ?
+_cell.reciprocal_length_a ?
+_cell.reciprocal_length_b ?
+_cell.reciprocal_length_c ?
+_cell.reciprocal_length_a_esd ?
+_cell.reciprocal_length_b_esd ?
+_cell.reciprocal_length_c_esd ?
+_cell.pdbx_unique_axis ?
+#
+_symmetry.entry_id 6Y84
+_symmetry.cell_setting ?
+_symmetry.Int_Tables_number 5
+_symmetry.space_group_name_Hall ?
+_symmetry.space_group_name_H-M 'C 1 2 1'
+_symmetry.pdbx_full_space_group_name_H-M ?
+#
+loop_
+_entity.id
+_entity.type
+_entity.src_method
+_entity.pdbx_description
+_entity.formula_weight
+_entity.pdbx_number_of_molecules
+_entity.pdbx_ec
+_entity.pdbx_mutation
+_entity.pdbx_fragment
+_entity.details
+1 polymer man 'Non-structural polyprotein 1ab' 33825.547 1 ? ? ? ?
+2 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133 4 ? ? ? ?
+3 water nat water 18.015 391 ? ? ? ?
+#
+_entity_poly.entity_id 1
+_entity_poly.type 'polypeptide(L)'
+_entity_poly.nstd_linkage no
+_entity_poly.nstd_monomer no
+_entity_poly.pdbx_seq_one_letter_code
+;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
+SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
+YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
+PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
+;
+_entity_poly.pdbx_seq_one_letter_code_can
+;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
+SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
+YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
+PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
+;
+_entity_poly.pdbx_strand_id A
+_entity_poly.pdbx_target_identifier ?
+#
+loop_
+_entity_poly_seq.entity_id
+_entity_poly_seq.num
+_entity_poly_seq.mon_id
+_entity_poly_seq.hetero
+1 1 SER n
+1 2 GLY n
+1 3 PHE n
+1 4 ARG n
+1 5 LYS n
+1 6 MET n
+1 7 ALA n
+1 8 PHE n
+1 9 PRO n
+1 10 SER n
+1 11 GLY n
+1 12 LYS n
+1 13 VAL n
+1 14 GLU n
+1 15 GLY n
+1 16 CYS n
+1 17 MET n
+1 18 VAL n
+1 19 GLN n
+1 20 VAL n
+1 21 THR n
+1 22 CYS n
+1 23 GLY n
+1 24 THR n
+1 25 THR n
+1 26 THR n
+1 27 LEU n
+1 28 ASN n
+1 29 GLY n
+1 30 LEU n
+1 31 TRP n
+1 32 LEU n
+1 33 ASP n
+1 34 ASP n
+1 35 VAL n
+1 36 VAL n
+1 37 TYR n
+1 38 CYS n
+1 39 PRO n
+1 40 ARG n
+1 41 HIS n
+1 42 VAL n
+1 43 ILE n
+1 44 CYS n
+1 45 THR n
+1 46 SER n
+1 47 GLU n
+1 48 ASP n
+1 49 MET n
+1 50 LEU n
+1 51 ASN n
+1 52 PRO n
+1 53 ASN n
+1 54 TYR n
+1 55 GLU n
+1 56 ASP n
+1 57 LEU n
+1 58 LEU n
+1 59 ILE n
+1 60 ARG n
+1 61 LYS n
+1 62 SER n
+1 63 ASN n
+1 64 HIS n
+1 65 ASN n
+1 66 PHE n
+1 67 LEU n
+1 68 VAL n
+1 69 GLN n
+1 70 ALA n
+1 71 GLY n
+1 72 ASN n
+1 73 VAL n
+1 74 GLN n
+1 75 LEU n
+1 76 ARG n
+1 77 VAL n
+1 78 ILE n
+1 79 GLY n
+1 80 HIS n
+1 81 SER n
+1 82 MET n
+1 83 GLN n
+1 84 ASN n
+1 85 CYS n
+1 86 VAL n
+1 87 LEU n
+1 88 LYS n
+1 89 LEU n
+1 90 LYS n
+1 91 VAL n
+1 92 ASP n
+1 93 THR n
+1 94 ALA n
+1 95 ASN n
+1 96 PRO n
+1 97 LYS n
+1 98 THR n
+1 99 PRO n
+1 100 LYS n
+1 101 TYR n
+1 102 LYS n
+1 103 PHE n
+1 104 VAL n
+1 105 ARG n
+1 106 ILE n
+1 107 GLN n
+1 108 PRO n
+1 109 GLY n
+1 110 GLN n
+1 111 THR n
+1 112 PHE n
+1 113 SER n
+1 114 VAL n
+1 115 LEU n
+1 116 ALA n
+1 117 CYS n
+1 118 TYR n
+1 119 ASN n
+1 120 GLY n
+1 121 SER n
+1 122 PRO n
+1 123 SER n
+1 124 GLY n
+1 125 VAL n
+1 126 TYR n
+1 127 GLN n
+1 128 CYS n
+1 129 ALA n
+1 130 MET n
+1 131 ARG n
+1 132 PRO n
+1 133 ASN n
+1 134 PHE n
+1 135 THR n
+1 136 ILE n
+1 137 LYS n
+1 138 GLY n
+1 139 SER n
+1 140 PHE n
+1 141 LEU n
+1 142 ASN n
+1 143 GLY n
+1 144 SER n
+1 145 CYS n
+1 146 GLY n
+1 147 SER n
+1 148 VAL n
+1 149 GLY n
+1 150 PHE n
+1 151 ASN n
+1 152 ILE n
+1 153 ASP n
+1 154 TYR n
+1 155 ASP n
+1 156 CYS n
+1 157 VAL n
+1 158 SER n
+1 159 PHE n
+1 160 CYS n
+1 161 TYR n
+1 162 MET n
+1 163 HIS n
+1 164 HIS n
+1 165 MET n
+1 166 GLU n
+1 167 LEU n
+1 168 PRO n
+1 169 THR n
+1 170 GLY n
+1 171 VAL n
+1 172 HIS n
+1 173 ALA n
+1 174 GLY n
+1 175 THR n
+1 176 ASP n
+1 177 LEU n
+1 178 GLU n
+1 179 GLY n
+1 180 ASN n
+1 181 PHE n
+1 182 TYR n
+1 183 GLY n
+1 184 PRO n
+1 185 PHE n
+1 186 VAL n
+1 187 ASP n
+1 188 ARG n
+1 189 GLN n
+1 190 THR n
+1 191 ALA n
+1 192 GLN n
+1 193 ALA n
+1 194 ALA n
+1 195 GLY n
+1 196 THR n
+1 197 ASP n
+1 198 THR n
+1 199 THR n
+1 200 ILE n
+1 201 THR n
+1 202 VAL n
+1 203 ASN n
+1 204 VAL n
+1 205 LEU n
+1 206 ALA n
+1 207 TRP n
+1 208 LEU n
+1 209 TYR n
+1 210 ALA n
+1 211 ALA n
+1 212 VAL n
+1 213 ILE n
+1 214 ASN n
+1 215 GLY n
+1 216 ASP n
+1 217 ARG n
+1 218 TRP n
+1 219 PHE n
+1 220 LEU n
+1 221 ASN n
+1 222 ARG n
+1 223 PHE n
+1 224 THR n
+1 225 THR n
+1 226 THR n
+1 227 LEU n
+1 228 ASN n
+1 229 ASP n
+1 230 PHE n
+1 231 ASN n
+1 232 LEU n
+1 233 VAL n
+1 234 ALA n
+1 235 MET n
+1 236 LYS n
+1 237 TYR n
+1 238 ASN n
+1 239 TYR n
+1 240 GLU n
+1 241 PRO n
+1 242 LEU n
+1 243 THR n
+1 244 GLN n
+1 245 ASP n
+1 246 HIS n
+1 247 VAL n
+1 248 ASP n
+1 249 ILE n
+1 250 LEU n
+1 251 GLY n
+1 252 PRO n
+1 253 LEU n
+1 254 SER n
+1 255 ALA n
+1 256 GLN n
+1 257 THR n
+1 258 GLY n
+1 259 ILE n
+1 260 ALA n
+1 261 VAL n
+1 262 LEU n
+1 263 ASP n
+1 264 MET n
+1 265 CYS n
+1 266 ALA n
+1 267 SER n
+1 268 LEU n
+1 269 LYS n
+1 270 GLU n
+1 271 LEU n
+1 272 LEU n
+1 273 GLN n
+1 274 ASN n
+1 275 GLY n
+1 276 MET n
+1 277 ASN n
+1 278 GLY n
+1 279 ARG n
+1 280 THR n
+1 281 ILE n
+1 282 LEU n
+1 283 GLY n
+1 284 SER n
+1 285 ALA n
+1 286 LEU n
+1 287 LEU n
+1 288 GLU n
+1 289 ASP n
+1 290 GLU n
+1 291 PHE n
+1 292 THR n
+1 293 PRO n
+1 294 PHE n
+1 295 ASP n
+1 296 VAL n
+1 297 VAL n
+1 298 ARG n
+1 299 GLN n
+1 300 CYS n
+1 301 SER n
+1 302 GLY n
+1 303 VAL n
+1 304 THR n
+1 305 PHE n
+1 306 GLN n
+#
+_entity_src_gen.entity_id 1
+_entity_src_gen.pdbx_src_id 1
+_entity_src_gen.pdbx_alt_source_flag sample
+_entity_src_gen.pdbx_seq_type 'Biological sequence'
+_entity_src_gen.pdbx_beg_seq_num 1
+_entity_src_gen.pdbx_end_seq_num 306
+_entity_src_gen.gene_src_common_name ?
+_entity_src_gen.gene_src_genus ?
+_entity_src_gen.pdbx_gene_src_gene ?
+_entity_src_gen.gene_src_species ?
+_entity_src_gen.gene_src_strain COVID-19
+_entity_src_gen.gene_src_tissue ?
+_entity_src_gen.gene_src_tissue_fraction ?
+_entity_src_gen.gene_src_details ?
+_entity_src_gen.pdbx_gene_src_fragment ?
+_entity_src_gen.pdbx_gene_src_scientific_name 'Severe acute respiratory syndrome coronavirus 2'
+_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 2697049
+_entity_src_gen.pdbx_gene_src_variant ?
+_entity_src_gen.pdbx_gene_src_cell_line ?
+_entity_src_gen.pdbx_gene_src_atcc ?
+_entity_src_gen.pdbx_gene_src_organ ?
+_entity_src_gen.pdbx_gene_src_organelle ?
+_entity_src_gen.pdbx_gene_src_cell ?
+_entity_src_gen.pdbx_gene_src_cellular_location ?
+_entity_src_gen.host_org_common_name ?
+_entity_src_gen.pdbx_host_org_scientific_name 'Escherichia coli'
+_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 562
+_entity_src_gen.host_org_genus ?
+_entity_src_gen.pdbx_host_org_gene ?
+_entity_src_gen.pdbx_host_org_organ ?
+_entity_src_gen.host_org_species ?
+_entity_src_gen.pdbx_host_org_tissue ?
+_entity_src_gen.pdbx_host_org_tissue_fraction ?
+_entity_src_gen.pdbx_host_org_strain ?
+_entity_src_gen.pdbx_host_org_variant ?
+_entity_src_gen.pdbx_host_org_cell_line ?
+_entity_src_gen.pdbx_host_org_atcc ?
+_entity_src_gen.pdbx_host_org_culture_collection ?
+_entity_src_gen.pdbx_host_org_cell ?
+_entity_src_gen.pdbx_host_org_organelle ?
+_entity_src_gen.pdbx_host_org_cellular_location ?
+_entity_src_gen.pdbx_host_org_vector_type ?
+_entity_src_gen.pdbx_host_org_vector ?
+_entity_src_gen.host_org_details ?
+_entity_src_gen.expression_system_id ?
+_entity_src_gen.plasmid_name ?
+_entity_src_gen.plasmid_details ?
+_entity_src_gen.pdbx_description ?
+#
+_struct_ref.id 1
+_struct_ref.db_name PDB
+_struct_ref.db_code 6Y84
+_struct_ref.pdbx_db_accession 6Y84
+_struct_ref.pdbx_db_isoform ?
+_struct_ref.entity_id 1
+_struct_ref.pdbx_seq_one_letter_code ?
+_struct_ref.pdbx_align_begin 1
+#
+_struct_ref_seq.align_id 1
+_struct_ref_seq.ref_id 1
+_struct_ref_seq.pdbx_PDB_id_code 6Y84
+_struct_ref_seq.pdbx_strand_id A
+_struct_ref_seq.seq_align_beg 1
+_struct_ref_seq.pdbx_seq_align_beg_ins_code ?
+_struct_ref_seq.seq_align_end 306
+_struct_ref_seq.pdbx_seq_align_end_ins_code ?
+_struct_ref_seq.pdbx_db_accession 6Y84
+_struct_ref_seq.db_align_beg 1
+_struct_ref_seq.pdbx_db_align_beg_ins_code ?
+_struct_ref_seq.db_align_end 306
+_struct_ref_seq.pdbx_db_align_end_ins_code ?
+_struct_ref_seq.pdbx_auth_seq_align_beg 1
+_struct_ref_seq.pdbx_auth_seq_align_end 306
+#
+loop_
+_chem_comp.id
+_chem_comp.type
+_chem_comp.mon_nstd_flag
+_chem_comp.name
+_chem_comp.pdbx_synonyms
+_chem_comp.formula
+_chem_comp.formula_weight
+ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093
+ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209
+ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118
+ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103
+CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158
+DMS non-polymer . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S' 78.133
+GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144
+GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129
+GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067
+HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162
+HOH non-polymer . WATER ? 'H2 O' 18.015
+ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173
+LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173
+LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195
+MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211
+PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189
+PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130
+SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093
+THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119
+TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225
+TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189
+VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146
+#
+_exptl.absorpt_coefficient_mu ?
+_exptl.absorpt_correction_T_max ?
+_exptl.absorpt_correction_T_min ?
+_exptl.absorpt_correction_type ?
+_exptl.absorpt_process_details ?
+_exptl.entry_id 6Y84
+_exptl.crystals_number 1
+_exptl.details ?
+_exptl.method 'X-RAY DIFFRACTION'
+_exptl.method_details ?
+#
+_exptl_crystal.colour ?
+_exptl_crystal.density_diffrn ?
+_exptl_crystal.density_Matthews 1.92
+_exptl_crystal.density_method ?
+_exptl_crystal.density_percent_sol 35.89
+_exptl_crystal.description ?
+_exptl_crystal.F_000 ?
+_exptl_crystal.id 1
+_exptl_crystal.preparation ?
+_exptl_crystal.size_max ?
+_exptl_crystal.size_mid ?
+_exptl_crystal.size_min ?
+_exptl_crystal.size_rad ?
+_exptl_crystal.colour_lustre ?
+_exptl_crystal.colour_modifier ?
+_exptl_crystal.colour_primary ?
+_exptl_crystal.density_meas ?
+_exptl_crystal.density_meas_esd ?
+_exptl_crystal.density_meas_gt ?
+_exptl_crystal.density_meas_lt ?
+_exptl_crystal.density_meas_temp ?
+_exptl_crystal.density_meas_temp_esd ?
+_exptl_crystal.density_meas_temp_gt ?
+_exptl_crystal.density_meas_temp_lt ?
+_exptl_crystal.pdbx_crystal_image_url ?
+_exptl_crystal.pdbx_crystal_image_format ?
+_exptl_crystal.pdbx_mosaicity ?
+_exptl_crystal.pdbx_mosaicity_esd ?
+#
+_exptl_crystal_grow.apparatus ?
+_exptl_crystal_grow.atmosphere ?
+_exptl_crystal_grow.crystal_id 1
+_exptl_crystal_grow.details ?
+_exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP'
+_exptl_crystal_grow.method_ref ?
+_exptl_crystal_grow.pH 6.5
+_exptl_crystal_grow.pressure ?
+_exptl_crystal_grow.pressure_esd ?
+_exptl_crystal_grow.seeding ?
+_exptl_crystal_grow.seeding_ref ?
+_exptl_crystal_grow.temp 293
+_exptl_crystal_grow.temp_details ?
+_exptl_crystal_grow.temp_esd ?
+_exptl_crystal_grow.time ?
+_exptl_crystal_grow.pdbx_details
+;15% PEG 4000, 5% DMSO, 0.1M MES pH 6.5.
+0.15 microlitre protein + 0.3 microlitre reservoir + 0.05 microlitre seed stock
+;
+_exptl_crystal_grow.pdbx_pH_range ?
+#
+_diffrn.ambient_environment ?
+_diffrn.ambient_temp 100
+_diffrn.ambient_temp_details ?
+_diffrn.ambient_temp_esd ?
+_diffrn.crystal_id 1
+_diffrn.crystal_support ?
+_diffrn.crystal_treatment ?
+_diffrn.details ?
+_diffrn.id 1
+_diffrn.ambient_pressure ?
+_diffrn.ambient_pressure_esd ?
+_diffrn.ambient_pressure_gt ?
+_diffrn.ambient_pressure_lt ?
+_diffrn.ambient_temp_gt ?
+_diffrn.ambient_temp_lt ?
+_diffrn.pdbx_serial_crystal_experiment N
+#
+_diffrn_detector.details ?
+_diffrn_detector.detector PIXEL
+_diffrn_detector.diffrn_id 1
+_diffrn_detector.type 'DECTRIS PILATUS3 6M'
+_diffrn_detector.area_resol_mean ?
+_diffrn_detector.dtime ?
+_diffrn_detector.pdbx_frames_total ?
+_diffrn_detector.pdbx_collection_time_total ?
+_diffrn_detector.pdbx_collection_date 2020-02-24
+_diffrn_detector.pdbx_frequency ?
+#
+_diffrn_radiation.collimation ?
+_diffrn_radiation.diffrn_id 1
+_diffrn_radiation.filter_edge ?
+_diffrn_radiation.inhomogeneity ?
+_diffrn_radiation.monochromator ?
+_diffrn_radiation.polarisn_norm ?
+_diffrn_radiation.polarisn_ratio ?
+_diffrn_radiation.probe ?
+_diffrn_radiation.type ?
+_diffrn_radiation.xray_symbol ?
+_diffrn_radiation.wavelength_id 1
+_diffrn_radiation.pdbx_monochromatic_or_laue_m_l M
+_diffrn_radiation.pdbx_wavelength_list ?
+_diffrn_radiation.pdbx_wavelength ?
+_diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH'
+_diffrn_radiation.pdbx_analyzer ?
+_diffrn_radiation.pdbx_scattering_type x-ray
+#
+_diffrn_radiation_wavelength.id 1
+_diffrn_radiation_wavelength.wavelength 0.9126
+_diffrn_radiation_wavelength.wt 1.0
+#
+_diffrn_source.current ?
+_diffrn_source.details ?
+_diffrn_source.diffrn_id 1
+_diffrn_source.power ?
+_diffrn_source.size ?
+_diffrn_source.source SYNCHROTRON
+_diffrn_source.target ?
+_diffrn_source.type 'DIAMOND BEAMLINE I04-1'
+_diffrn_source.voltage ?
+_diffrn_source.take-off_angle ?
+_diffrn_source.pdbx_wavelength_list 0.9126
+_diffrn_source.pdbx_wavelength ?
+_diffrn_source.pdbx_synchrotron_beamline I04-1
+_diffrn_source.pdbx_synchrotron_site Diamond
+#
+_reflns.B_iso_Wilson_estimate 17.330
+_reflns.entry_id 6Y84
+_reflns.data_reduction_details ?
+_reflns.data_reduction_method ?
+_reflns.d_resolution_high 1.390
+_reflns.d_resolution_low 54.930
+_reflns.details ?
+_reflns.limit_h_max ?
+_reflns.limit_h_min ?
+_reflns.limit_k_max ?
+_reflns.limit_k_min ?
+_reflns.limit_l_max ?
+_reflns.limit_l_min ?
+_reflns.number_all ?
+_reflns.number_obs 50348
+_reflns.observed_criterion ?
+_reflns.observed_criterion_F_max ?
+_reflns.observed_criterion_F_min ?
+_reflns.observed_criterion_I_max ?
+_reflns.observed_criterion_I_min ?
+_reflns.observed_criterion_sigma_F ?
+_reflns.observed_criterion_sigma_I ?
+_reflns.percent_possible_obs 97.500
+_reflns.R_free_details ?
+_reflns.Rmerge_F_all ?
+_reflns.Rmerge_F_obs ?
+_reflns.Friedel_coverage ?
+_reflns.number_gt ?
+_reflns.threshold_expression ?
+_reflns.pdbx_redundancy 3.600
+_reflns.pdbx_Rmerge_I_obs 0.059
+_reflns.pdbx_Rmerge_I_all ?
+_reflns.pdbx_Rsym_value ?
+_reflns.pdbx_netI_over_av_sigmaI ?
+_reflns.pdbx_netI_over_sigmaI 9.700
+_reflns.pdbx_res_netI_over_av_sigmaI_2 ?
+_reflns.pdbx_res_netI_over_sigmaI_2 ?
+_reflns.pdbx_chi_squared ?
+_reflns.pdbx_scaling_rejects 602
+_reflns.pdbx_d_res_high_opt ?
+_reflns.pdbx_d_res_low_opt ?
+_reflns.pdbx_d_res_opt_method ?
+_reflns.phase_calculation_details ?
+_reflns.pdbx_Rrim_I_all 0.069
+_reflns.pdbx_Rpim_I_all 0.034
+_reflns.pdbx_d_opt ?
+_reflns.pdbx_number_measured_all 179937
+_reflns.pdbx_diffrn_id 1
+_reflns.pdbx_ordinal 1
+_reflns.pdbx_CC_half 0.997
+_reflns.pdbx_CC_star ?
+_reflns.pdbx_R_split ?
+#
+loop_
+_reflns_shell.d_res_high
+_reflns_shell.d_res_low
+_reflns_shell.meanI_over_sigI_all
+_reflns_shell.meanI_over_sigI_obs
+_reflns_shell.number_measured_all
+_reflns_shell.number_measured_obs
+_reflns_shell.number_possible
+_reflns_shell.number_unique_all
+_reflns_shell.number_unique_obs
+_reflns_shell.percent_possible_all
+_reflns_shell.percent_possible_obs
+_reflns_shell.Rmerge_F_all
+_reflns_shell.Rmerge_F_obs
+_reflns_shell.Rmerge_I_all
+_reflns_shell.Rmerge_I_obs
+_reflns_shell.meanI_over_sigI_gt
+_reflns_shell.meanI_over_uI_all
+_reflns_shell.meanI_over_uI_gt
+_reflns_shell.number_measured_gt
+_reflns_shell.number_unique_gt
+_reflns_shell.percent_possible_gt
+_reflns_shell.Rmerge_F_gt
+_reflns_shell.Rmerge_I_gt
+_reflns_shell.pdbx_redundancy
+_reflns_shell.pdbx_Rsym_value
+_reflns_shell.pdbx_chi_squared
+_reflns_shell.pdbx_netI_over_sigmaI_all
+_reflns_shell.pdbx_netI_over_sigmaI_obs
+_reflns_shell.pdbx_Rrim_I_all
+_reflns_shell.pdbx_Rpim_I_all
+_reflns_shell.pdbx_rejects
+_reflns_shell.pdbx_ordinal
+_reflns_shell.pdbx_diffrn_id
+_reflns_shell.pdbx_CC_half
+_reflns_shell.pdbx_CC_star
+_reflns_shell.pdbx_R_split
+1.390 1.410 ? ? 4394 ? ? ? 2074 80.700 ? ? ? ? 0.929 ? ? ? ? ? ? ? ? 2.100 ? ? ? 0.800 1.141 0.650 ? 1 1 0.481 ? ?
+7.610 54.930 ? ? 1425 ? ? ? 339 99.800 ? ? ? ? 0.022 ? ? ? ? ? ? ? ? 4.200 ? ? ? 32.500 0.025 0.012 ? 2 1 0.999 ? ?
+#
+_refine.aniso_B[1][1] -3.7809
+_refine.aniso_B[1][2] 0.0000
+_refine.aniso_B[1][3] 0.0422
+_refine.aniso_B[2][2] 0.6978
+_refine.aniso_B[2][3] 0.0000
+_refine.aniso_B[3][3] 3.0831
+_refine.B_iso_max 97.940
+_refine.B_iso_mean 21.0000
+_refine.B_iso_min 10.280
+_refine.correlation_coeff_Fo_to_Fc 0.9630
+_refine.correlation_coeff_Fo_to_Fc_free 0.9560
+_refine.details ?
+_refine.diff_density_max ?
+_refine.diff_density_max_esd ?
+_refine.diff_density_min ?
+_refine.diff_density_min_esd ?
+_refine.diff_density_rms ?
+_refine.diff_density_rms_esd ?
+_refine.entry_id 6Y84
+_refine.pdbx_refine_id 'X-RAY DIFFRACTION'
+_refine.ls_abs_structure_details ?
+_refine.ls_abs_structure_Flack ?
+_refine.ls_abs_structure_Flack_esd ?
+_refine.ls_abs_structure_Rogers ?
+_refine.ls_abs_structure_Rogers_esd ?
+_refine.ls_d_res_high 1.3900
+_refine.ls_d_res_low 54.9300
+_refine.ls_extinction_coef ?
+_refine.ls_extinction_coef_esd ?
+_refine.ls_extinction_expression ?
+_refine.ls_extinction_method ?
+_refine.ls_goodness_of_fit_all ?
+_refine.ls_goodness_of_fit_all_esd ?
+_refine.ls_goodness_of_fit_obs ?
+_refine.ls_goodness_of_fit_obs_esd ?
+_refine.ls_hydrogen_treatment ?
+_refine.ls_matrix_type ?
+_refine.ls_number_constraints ?
+_refine.ls_number_parameters ?
+_refine.ls_number_reflns_all ?
+_refine.ls_number_reflns_obs 50331
+_refine.ls_number_reflns_R_free 2498
+_refine.ls_number_reflns_R_work ?
+_refine.ls_number_restraints ?
+_refine.ls_percent_reflns_obs 97.5000
+_refine.ls_percent_reflns_R_free 4.9600
+_refine.ls_R_factor_all ?
+_refine.ls_R_factor_obs 0.1790
+_refine.ls_R_factor_R_free 0.2000
+_refine.ls_R_factor_R_free_error ?
+_refine.ls_R_factor_R_free_error_details ?
+_refine.ls_R_factor_R_work 0.1779
+_refine.ls_R_Fsqd_factor_obs ?
+_refine.ls_R_I_factor_obs ?
+_refine.ls_redundancy_reflns_all ?
+_refine.ls_redundancy_reflns_obs ?
+_refine.ls_restrained_S_all ?
+_refine.ls_restrained_S_obs ?
+_refine.ls_shift_over_esd_max ?
+_refine.ls_shift_over_esd_mean ?
+_refine.ls_structure_factor_coef ?
+_refine.ls_weighting_details ?
+_refine.ls_weighting_scheme ?
+_refine.ls_wR_factor_all ?
+_refine.ls_wR_factor_obs ?
+_refine.ls_wR_factor_R_free ?
+_refine.ls_wR_factor_R_work ?
+_refine.occupancy_max ?
+_refine.occupancy_min ?
+_refine.solvent_model_details ?
+_refine.solvent_model_param_bsol ?
+_refine.solvent_model_param_ksol ?
+_refine.pdbx_R_complete ?
+_refine.ls_R_factor_gt ?
+_refine.ls_goodness_of_fit_gt ?
+_refine.ls_goodness_of_fit_ref ?
+_refine.ls_shift_over_su_max ?
+_refine.ls_shift_over_su_max_lt ?
+_refine.ls_shift_over_su_mean ?
+_refine.ls_shift_over_su_mean_lt ?
+_refine.pdbx_ls_sigma_I ?
+_refine.pdbx_ls_sigma_F 0.000
+_refine.pdbx_ls_sigma_Fsqd ?
+_refine.pdbx_data_cutoff_high_absF ?
+_refine.pdbx_data_cutoff_high_rms_absF ?
+_refine.pdbx_data_cutoff_low_absF ?
+_refine.pdbx_isotropic_thermal_model ?
+_refine.pdbx_ls_cross_valid_method THROUGHOUT
+_refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT'
+_refine.pdbx_starting_model 6LU7
+_refine.pdbx_stereochemistry_target_values ?
+_refine.pdbx_R_Free_selection_details RANDOM
+_refine.pdbx_stereochem_target_val_spec_case ?
+_refine.pdbx_overall_ESU_R ?
+_refine.pdbx_overall_ESU_R_Free ?
+_refine.pdbx_solvent_vdw_probe_radii ?
+_refine.pdbx_solvent_ion_probe_radii ?
+_refine.pdbx_solvent_shrinkage_radii ?
+_refine.pdbx_real_space_R ?
+_refine.pdbx_density_correlation ?
+_refine.pdbx_pd_number_of_powder_patterns ?
+_refine.pdbx_pd_number_of_points ?
+_refine.pdbx_pd_meas_number_of_points ?
+_refine.pdbx_pd_proc_ls_prof_R_factor ?
+_refine.pdbx_pd_proc_ls_prof_wR_factor ?
+_refine.pdbx_pd_Marquardt_correlation_coeff ?
+_refine.pdbx_pd_Fsqrd_R_factor ?
+_refine.pdbx_pd_ls_matrix_band_width ?
+_refine.pdbx_overall_phase_error ?
+_refine.pdbx_overall_SU_R_free_Cruickshank_DPI 0.0680
+_refine.pdbx_overall_SU_R_free_Blow_DPI 0.0710
+_refine.pdbx_overall_SU_R_Blow_DPI 0.0740
+_refine.pdbx_TLS_residual_ADP_flag ?
+_refine.pdbx_diffrn_id 1
+_refine.overall_SU_B ?
+_refine.overall_SU_ML ?
+_refine.overall_SU_R_Cruickshank_DPI 0.0690
+_refine.overall_SU_R_free ?
+_refine.overall_FOM_free_R_set ?
+_refine.overall_FOM_work_R_set ?
+_refine.pdbx_average_fsc_overall ?
+_refine.pdbx_average_fsc_work ?
+_refine.pdbx_average_fsc_free ?
+#
+_refine_analyze.entry_id 6Y84
+_refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION'
+_refine_analyze.Luzzati_coordinate_error_free ?
+_refine_analyze.Luzzati_coordinate_error_obs 0.190
+_refine_analyze.Luzzati_d_res_low_free ?
+_refine_analyze.Luzzati_d_res_low_obs ?
+_refine_analyze.Luzzati_sigma_a_free ?
+_refine_analyze.Luzzati_sigma_a_free_details ?
+_refine_analyze.Luzzati_sigma_a_obs ?
+_refine_analyze.Luzzati_sigma_a_obs_details ?
+_refine_analyze.number_disordered_residues ?
+_refine_analyze.occupancy_sum_hydrogen ?
+_refine_analyze.occupancy_sum_non_hydrogen ?
+_refine_analyze.RG_d_res_high ?
+_refine_analyze.RG_d_res_low ?
+_refine_analyze.RG_free ?
+_refine_analyze.RG_work ?
+_refine_analyze.RG_free_work_ratio ?
+_refine_analyze.pdbx_Luzzati_d_res_high_obs ?
+#
+_refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION'
+_refine_hist.cycle_id final
+_refine_hist.details ?
+_refine_hist.d_res_high 1.3900
+_refine_hist.d_res_low 54.9300
+_refine_hist.number_atoms_solvent 391
+_refine_hist.number_atoms_total 2754
+_refine_hist.number_reflns_all ?
+_refine_hist.number_reflns_obs ?
+_refine_hist.number_reflns_R_free ?
+_refine_hist.number_reflns_R_work ?
+_refine_hist.R_factor_all ?
+_refine_hist.R_factor_obs ?
+_refine_hist.R_factor_R_free ?
+_refine_hist.R_factor_R_work ?
+_refine_hist.pdbx_number_residues_total 304
+_refine_hist.pdbx_B_iso_mean_ligand 33.83
+_refine_hist.pdbx_B_iso_mean_solvent 32.89
+_refine_hist.pdbx_number_atoms_protein 2347
+_refine_hist.pdbx_number_atoms_nucleic_acid 0
+_refine_hist.pdbx_number_atoms_ligand 16
+_refine_hist.pdbx_number_atoms_lipid ?
+_refine_hist.pdbx_number_atoms_carb ?
+_refine_hist.pdbx_pseudo_atom_details ?
+#
+loop_
+_refine_ls_restr.pdbx_refine_id
+_refine_ls_restr.criterion
+_refine_ls_restr.dev_ideal
+_refine_ls_restr.dev_ideal_target
+_refine_ls_restr.number
+_refine_ls_restr.rejects
+_refine_ls_restr.type
+_refine_ls_restr.weight
+_refine_ls_restr.pdbx_restraint_function
+'X-RAY DIFFRACTION' ? ? ? 909 ? t_dihedral_angle_d 2.000 SINUSOIDAL
+'X-RAY DIFFRACTION' ? ? ? ? ? t_trig_c_planes ? ?
+'X-RAY DIFFRACTION' ? ? ? 466 ? t_gen_planes 5.000 HARMONIC
+'X-RAY DIFFRACTION' ? ? ? 2628 ? t_it 10.000 HARMONIC
+'X-RAY DIFFRACTION' ? ? ? ? ? t_nbd ? ?
+'X-RAY DIFFRACTION' ? ? ? ? ? t_improper_torsion ? ?
+'X-RAY DIFFRACTION' ? ? ? ? ? t_pseud_angle ? ?
+'X-RAY DIFFRACTION' ? ? ? 340 ? t_chiral_improper_torsion 5.000 SEMIHARMONIC
+'X-RAY DIFFRACTION' ? ? ? ? ? t_sum_occupancies ? ?
+'X-RAY DIFFRACTION' ? ? ? ? ? t_utility_distance ? ?
+'X-RAY DIFFRACTION' ? ? ? ? ? t_utility_angle ? ?
+'X-RAY DIFFRACTION' ? ? ? ? ? t_utility_torsion ? ?
+'X-RAY DIFFRACTION' ? ? ? 3017 ? t_ideal_dist_contact 4.000 SEMIHARMONIC
+'X-RAY DIFFRACTION' ? 0.007 ? 2628 ? t_bond_d 2.000 HARMONIC
+'X-RAY DIFFRACTION' ? 0.980 ? 3595 ? t_angle_deg 2.000 HARMONIC
+'X-RAY DIFFRACTION' ? 3.920 ? ? ? t_omega_torsion ? ?
+'X-RAY DIFFRACTION' ? 14.640 ? ? ? t_other_torsion ? ?
+#
+_refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION'
+_refine_ls_shell.d_res_high 1.3900
+_refine_ls_shell.d_res_low 1.4000
+_refine_ls_shell.number_reflns_all 1007
+_refine_ls_shell.number_reflns_obs ?
+_refine_ls_shell.number_reflns_R_free 66
+_refine_ls_shell.number_reflns_R_work 941
+_refine_ls_shell.percent_reflns_obs 77.9900
+_refine_ls_shell.percent_reflns_R_free 6.5500
+_refine_ls_shell.R_factor_all 0.2107
+_refine_ls_shell.R_factor_obs ?
+_refine_ls_shell.R_factor_R_free 0.2075
+_refine_ls_shell.R_factor_R_free_error 0.0000
+_refine_ls_shell.R_factor_R_work 0.2109
+_refine_ls_shell.redundancy_reflns_all ?
+_refine_ls_shell.redundancy_reflns_obs ?
+_refine_ls_shell.wR_factor_all ?
+_refine_ls_shell.wR_factor_obs ?
+_refine_ls_shell.wR_factor_R_free ?
+_refine_ls_shell.wR_factor_R_work ?
+_refine_ls_shell.pdbx_R_complete ?
+_refine_ls_shell.pdbx_total_number_of_bins_used 51
+_refine_ls_shell.pdbx_phase_error ?
+_refine_ls_shell.pdbx_fsc_work ?
+_refine_ls_shell.pdbx_fsc_free ?
+#
+_struct.entry_id 6Y84
+_struct.title
+'COVID-19 main protease with unliganded active site (2019-nCoV, coronavirus disease 2019, SARS-CoV-2)'
+_struct.pdbx_descriptor 'Non-structural polyprotein 1ab'
+_struct.pdbx_model_details ?
+_struct.pdbx_formula_weight ?
+_struct.pdbx_formula_weight_method ?
+_struct.pdbx_model_type_details ?
+_struct.pdbx_CASP_flag N
+#
+_struct_keywords.entry_id 6Y84
+_struct_keywords.text 'protease, cysteine protease, VIRAL PROTEIN'
+_struct_keywords.pdbx_keywords 'VIRAL PROTEIN'
+#
+loop_
+_struct_asym.id
+_struct_asym.pdbx_blank_PDB_chainid_flag
+_struct_asym.pdbx_modified
+_struct_asym.entity_id
+_struct_asym.details
+A N N 1 ?
+B N N 2 ?
+C N N 2 ?
+D N N 2 ?
+E N N 2 ?
+F N N 3 ?
+#
+loop_
+_struct_conf.conf_type_id
+_struct_conf.id
+_struct_conf.pdbx_PDB_helix_id
+_struct_conf.beg_label_comp_id
+_struct_conf.beg_label_asym_id
+_struct_conf.beg_label_seq_id
+_struct_conf.pdbx_beg_PDB_ins_code
+_struct_conf.end_label_comp_id
+_struct_conf.end_label_asym_id
+_struct_conf.end_label_seq_id
+_struct_conf.pdbx_end_PDB_ins_code
+_struct_conf.beg_auth_comp_id
+_struct_conf.beg_auth_asym_id
+_struct_conf.beg_auth_seq_id
+_struct_conf.end_auth_comp_id
+_struct_conf.end_auth_asym_id
+_struct_conf.end_auth_seq_id
+_struct_conf.pdbx_PDB_helix_class
+_struct_conf.details
+_struct_conf.pdbx_PDB_helix_length
+HELX_P HELX_P1 AA1 SER A 10 ? GLY A 15 ? SER A 10 GLY A 15 1 ? 6
+HELX_P HELX_P2 AA2 HIS A 41 ? CYS A 44 ? HIS A 41 CYS A 44 5 ? 4
+HELX_P HELX_P3 AA3 GLU A 47 ? ASN A 51 ? GLU A 47 ASN A 51 5 ? 5
+HELX_P HELX_P4 AA4 ASN A 53 ? ARG A 60 ? ASN A 53 ARG A 60 1 ? 8
+HELX_P HELX_P5 AA5 LYS A 61 ? HIS A 64 ? LYS A 61 HIS A 64 5 ? 4
+HELX_P HELX_P6 AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15
+HELX_P HELX_P7 AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12
+HELX_P HELX_P8 AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8
+HELX_P HELX_P9 AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9
+HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16
+HELX_P HELX_P11 AB2 THR A 292 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11
+#
+_struct_conf_type.id HELX_P
+_struct_conf_type.criteria ?
+_struct_conf_type.reference ?
+#
+loop_
+_struct_sheet.id
+_struct_sheet.type
+_struct_sheet.number_strands
+_struct_sheet.details
+AA1 ? 7 ?
+AA2 ? 5 ?
+AA3 ? 3 ?
+#
+loop_
+_struct_sheet_order.sheet_id
+_struct_sheet_order.range_id_1
+_struct_sheet_order.range_id_2
+_struct_sheet_order.offset
+_struct_sheet_order.sense
+AA1 1 2 ? anti-parallel
+AA1 2 3 ? anti-parallel
+AA1 3 4 ? anti-parallel
+AA1 4 5 ? anti-parallel
+AA1 5 6 ? anti-parallel
+AA1 6 7 ? anti-parallel
+AA2 1 2 ? parallel
+AA2 2 3 ? anti-parallel
+AA2 3 4 ? anti-parallel
+AA2 4 5 ? anti-parallel
+AA3 1 2 ? parallel
+AA3 2 3 ? anti-parallel
+#
+loop_
+_struct_sheet_range.sheet_id
+_struct_sheet_range.id
+_struct_sheet_range.beg_label_comp_id
+_struct_sheet_range.beg_label_asym_id
+_struct_sheet_range.beg_label_seq_id
+_struct_sheet_range.pdbx_beg_PDB_ins_code
+_struct_sheet_range.end_label_comp_id
+_struct_sheet_range.end_label_asym_id
+_struct_sheet_range.end_label_seq_id
+_struct_sheet_range.pdbx_end_PDB_ins_code
+_struct_sheet_range.beg_auth_comp_id
+_struct_sheet_range.beg_auth_asym_id
+_struct_sheet_range.beg_auth_seq_id
+_struct_sheet_range.end_auth_comp_id
+_struct_sheet_range.end_auth_asym_id
+_struct_sheet_range.end_auth_seq_id
+AA1 1 VAL A 73 ? LEU A 75 ? VAL A 73 LEU A 75
+AA1 2 PHE A 66 ? ALA A 70 ? PHE A 66 ALA A 70
+AA1 3 MET A 17 ? CYS A 22 ? MET A 17 CYS A 22
+AA1 4 THR A 25 ? LEU A 32 ? THR A 25 LEU A 32
+AA1 5 VAL A 35 ? PRO A 39 ? VAL A 35 PRO A 39
+AA1 6 VAL A 86 ? VAL A 91 ? VAL A 86 VAL A 91
+AA1 7 VAL A 77 ? GLN A 83 ? VAL A 77 GLN A 83
+AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103
+AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166
+AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153
+AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118
+AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129
+AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103
+AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166
+AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175
+#
+loop_
+_pdbx_struct_sheet_hbond.sheet_id
+_pdbx_struct_sheet_hbond.range_id_1
+_pdbx_struct_sheet_hbond.range_id_2
+_pdbx_struct_sheet_hbond.range_1_label_atom_id
+_pdbx_struct_sheet_hbond.range_1_label_comp_id
+_pdbx_struct_sheet_hbond.range_1_label_asym_id
+_pdbx_struct_sheet_hbond.range_1_label_seq_id
+_pdbx_struct_sheet_hbond.range_1_PDB_ins_code
+_pdbx_struct_sheet_hbond.range_1_auth_atom_id
+_pdbx_struct_sheet_hbond.range_1_auth_comp_id
+_pdbx_struct_sheet_hbond.range_1_auth_asym_id
+_pdbx_struct_sheet_hbond.range_1_auth_seq_id
+_pdbx_struct_sheet_hbond.range_2_label_atom_id
+_pdbx_struct_sheet_hbond.range_2_label_comp_id
+_pdbx_struct_sheet_hbond.range_2_label_asym_id
+_pdbx_struct_sheet_hbond.range_2_label_seq_id
+_pdbx_struct_sheet_hbond.range_2_PDB_ins_code
+_pdbx_struct_sheet_hbond.range_2_auth_atom_id
+_pdbx_struct_sheet_hbond.range_2_auth_comp_id
+_pdbx_struct_sheet_hbond.range_2_auth_asym_id
+_pdbx_struct_sheet_hbond.range_2_auth_seq_id
+AA1 1 2 O LEU A 75 ? O LEU A 75 N VAL A 68 ? N VAL A 68
+AA1 2 3 O GLN A 69 ? O GLN A 69 N GLN A 19 ? N GLN A 19
+AA1 3 4 N VAL A 20 ? N VAL A 20 O LEU A 27 ? O LEU A 27
+AA1 4 5 N LEU A 30 ? N LEU A 30 O TYR A 37 ? O TYR A 37
+AA1 5 6 N CYS A 38 ? N CYS A 38 O LEU A 87 ? O LEU A 87
+AA1 6 7 O LYS A 88 ? O LYS A 88 N SER A 81 ? N SER A 81
+AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157
+AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151
+AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113
+AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123
+AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157
+AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173
+#
+loop_
+_struct_site.id
+_struct_site.pdbx_evidence_code
+_struct_site.pdbx_auth_asym_id
+_struct_site.pdbx_auth_comp_id
+_struct_site.pdbx_auth_seq_id
+_struct_site.pdbx_auth_ins_code
+_struct_site.pdbx_num_residues
+_struct_site.details
+AC1 Software A DMS 401 ? 8 'binding site for residue DMS A 401'
+AC2 Software A DMS 402 ? 2 'binding site for residue DMS A 402'
+AC3 Software A DMS 403 ? 6 'binding site for residue DMS A 403'
+AC4 Software A DMS 404 ? 5 'binding site for residue DMS A 404'
+#
+loop_
+_struct_site_gen.id
+_struct_site_gen.site_id
+_struct_site_gen.pdbx_num_res
+_struct_site_gen.label_comp_id
+_struct_site_gen.label_asym_id
+_struct_site_gen.label_seq_id
+_struct_site_gen.pdbx_auth_ins_code
+_struct_site_gen.auth_comp_id
+_struct_site_gen.auth_asym_id
+_struct_site_gen.auth_seq_id
+_struct_site_gen.label_atom_id
+_struct_site_gen.label_alt_id
+_struct_site_gen.symmetry
+_struct_site_gen.details
+1 AC1 8 GLN A 74 ? GLN A 74 . ? 1_555 ?
+2 AC1 8 LEU A 75 ? LEU A 75 . ? 1_555 ?
+3 AC1 8 ARG A 76 ? ARG A 76 . ? 1_555 ?
+4 AC1 8 PHE A 223 ? PHE A 223 . ? 1_546 ?
+5 AC1 8 THR A 224 ? THR A 224 . ? 1_546 ?
+6 AC1 8 ASP A 263 ? ASP A 263 . ? 1_546 ?
+7 AC1 8 HOH F . ? HOH A 570 . ? 1_546 ?
+8 AC1 8 HOH F . ? HOH A 579 . ? 1_555 ?
+9 AC2 2 HIS A 64 ? HIS A 64 . ? 1_555 ?
+10 AC2 2 ASN A 65 ? ASN A 65 . ? 1_555 ?
+11 AC3 6 MET A 6 ? MET A 6 . ? 1_555 ?
+12 AC3 6 PHE A 8 ? PHE A 8 . ? 1_555 ?
+13 AC3 6 SER A 123 ? SER A 123 . ? 2_555 ?
+14 AC3 6 GLN A 127 ? GLN A 127 . ? 1_555 ?
+15 AC3 6 ASP A 295 ? ASP A 295 . ? 1_555 ?
+16 AC3 6 ARG A 298 ? ARG A 298 . ? 1_555 ?
+17 AC4 5 GLY A 15 ? GLY A 15 . ? 1_555 ?
+18 AC4 5 MET A 17 ? MET A 17 . ? 1_555 ?
+19 AC4 5 LYS A 97 ? LYS A 97 . ? 1_555 ?
+20 AC4 5 HOH F . ? HOH A 620 . ? 1_555 ?
+21 AC4 5 HOH F . ? HOH A 654 . ? 1_555 ?
+#
+_atom_sites.entry_id 6Y84
+_atom_sites.Cartn_transf_matrix[1][1] ?
+_atom_sites.Cartn_transf_matrix[1][2] ?
+_atom_sites.Cartn_transf_matrix[1][3] ?
+_atom_sites.Cartn_transf_matrix[2][1] ?
+_atom_sites.Cartn_transf_matrix[2][2] ?
+_atom_sites.Cartn_transf_matrix[2][3] ?
+_atom_sites.Cartn_transf_matrix[3][1] ?
+_atom_sites.Cartn_transf_matrix[3][2] ?
+_atom_sites.Cartn_transf_matrix[3][3] ?
+_atom_sites.Cartn_transf_vector[1] ?
+_atom_sites.Cartn_transf_vector[2] ?
+_atom_sites.Cartn_transf_vector[3] ?
+_atom_sites.fract_transf_matrix[1][1] 0.008864
+_atom_sites.fract_transf_matrix[1][2] 0.000000
+_atom_sites.fract_transf_matrix[1][3] 0.002073
+_atom_sites.fract_transf_matrix[2][1] 0.000000
+_atom_sites.fract_transf_matrix[2][2] 0.018886
+_atom_sites.fract_transf_matrix[2][3] 0.000000
+_atom_sites.fract_transf_matrix[3][1] 0.000000
+_atom_sites.fract_transf_matrix[3][2] 0.000000
+_atom_sites.fract_transf_matrix[3][3] 0.023010
+_atom_sites.fract_transf_vector[1] 0.00000
+_atom_sites.fract_transf_vector[2] 0.00000
+_atom_sites.fract_transf_vector[3] 0.00000
+_atom_sites.solution_primary ?
+_atom_sites.solution_secondary ?
+_atom_sites.solution_hydrogens ?
+_atom_sites.special_details ?
+#
+loop_
+_atom_type.symbol
+C
+N
+O
+S
+#
+loop_
+_atom_site.group_PDB
+_atom_site.id
+_atom_site.type_symbol
+_atom_site.label_atom_id
+_atom_site.label_alt_id
+_atom_site.label_comp_id
+_atom_site.label_asym_id
+_atom_site.label_entity_id
+_atom_site.label_seq_id
+_atom_site.pdbx_PDB_ins_code
+_atom_site.Cartn_x
+_atom_site.Cartn_y
+_atom_site.Cartn_z
+_atom_site.occupancy
+_atom_site.B_iso_or_equiv
+_atom_site.pdbx_formal_charge
+_atom_site.auth_seq_id
+_atom_site.auth_comp_id
+_atom_site.auth_asym_id
+_atom_site.auth_atom_id
+_atom_site.pdbx_PDB_model_num
+ATOM 1 N N A SER A 1 1 ? -2.185 4.397 -17.079 0.50 26.55 ? 1 SER A N 1
+ATOM 2 N N B SER A 1 1 ? -2.224 4.310 -17.137 0.50 25.36 ? 1 SER A N 1
+ATOM 3 C CA A SER A 1 1 ? -2.021 5.695 -16.438 0.50 26.71 ? 1 SER A CA 1
+ATOM 4 C CA B SER A 1 1 ? -1.882 5.526 -16.417 0.50 25.40 ? 1 SER A CA 1
+ATOM 5 C C A SER A 1 1 ? -2.350 5.650 -14.945 0.50 25.98 ? 1 SER A C 1
+ATOM 6 C C B SER A 1 1 ? -2.298 5.476 -14.933 0.50 24.98 ? 1 SER A C 1
+ATOM 7 O O A SER A 1 1 ? -2.957 4.696 -14.446 0.50 25.86 ? 1 SER A O 1
+ATOM 8 O O B SER A 1 1 ? -2.988 4.551 -14.492 0.50 24.74 ? 1 SER A O 1
+ATOM 9 C CB A SER A 1 1 ? -2.819 6.777 -17.164 0.50 28.89 ? 1 SER A CB 1
+ATOM 10 C CB B SER A 1 1 ? -2.440 6.757 -17.134 0.50 27.08 ? 1 SER A CB 1
+ATOM 11 O OG A SER A 1 1 ? -2.052 7.417 -18.170 0.50 31.95 ? 1 SER A OG 1
+ATOM 12 O OG B SER A 1 1 ? -3.797 7.000 -16.801 0.50 29.72 ? 1 SER A OG 1
+ATOM 13 N N A GLY A 1 2 ? -1.917 6.679 -14.240 0.50 25.04 ? 2 GLY A N 1
+ATOM 14 N N B GLY A 1 2 ? -1.852 6.467 -14.178 0.50 24.37 ? 2 GLY A N 1
+ATOM 15 C CA A GLY A 1 2 ? -2.078 6.745 -12.803 0.50 24.62 ? 2 GLY A CA 1
+ATOM 16 C CA B GLY A 1 2 ? -2.122 6.541 -12.756 0.50 24.27 ? 2 GLY A CA 1
+ATOM 17 C C A GLY A 1 2 ? -0.786 6.340 -12.129 0.50 23.89 ? 2 GLY A C 1
+ATOM 18 C C B GLY A 1 2 ? -0.877 6.134 -12.010 0.50 23.87 ? 2 GLY A C 1
+ATOM 19 O O A GLY A 1 2 ? -0.004 5.553 -12.671 0.50 24.05 ? 2 GLY A O 1
+ATOM 20 O O B GLY A 1 2 ? -0.206 5.169 -12.398 0.50 24.00 ? 2 GLY A O 1
+ATOM 21 N N . PHE A 1 3 ? -0.560 6.863 -10.941 1.00 22.93 ? 3 PHE A N 1
+ATOM 22 C CA . PHE A 1 3 ? 0.639 6.585 -10.184 1.00 22.04 ? 3 PHE A CA 1
+ATOM 23 C C . PHE A 1 3 ? 0.290 6.604 -8.729 1.00 21.78 ? 3 PHE A C 1
+ATOM 24 O O . PHE A 1 3 ? -0.157 7.619 -8.198 1.00 23.62 ? 3 PHE A O 1
+ATOM 25 C CB . PHE A 1 3 ? 1.732 7.609 -10.538 1.00 21.01 ? 3 PHE A CB 1
+ATOM 26 C CG . PHE A 1 3 ? 3.117 7.084 -10.258 1.00 21.05 ? 3 PHE A CG 1
+ATOM 27 C CD1 . PHE A 1 3 ? 3.724 6.190 -11.120 1.00 21.40 ? 3 PHE A CD1 1
+ATOM 28 C CD2 . PHE A 1 3 ? 3.799 7.464 -9.122 1.00 21.44 ? 3 PHE A CD2 1
+ATOM 29 C CE1 . PHE A 1 3 ? 4.993 5.696 -10.852 1.00 22.14 ? 3 PHE A CE1 1
+ATOM 30 C CE2 . PHE A 1 3 ? 5.075 6.985 -8.870 1.00 21.61 ? 3 PHE A CE2 1
+ATOM 31 C CZ . PHE A 1 3 ? 5.652 6.081 -9.717 1.00 21.71 ? 3 PHE A CZ 1
+ATOM 32 N N . ARG A 1 4 ? 0.443 5.457 -8.087 1.00 19.43 ? 4 ARG A N 1
+ATOM 33 C CA . ARG A 1 4 ? 0.091 5.280 -6.693 1.00 18.12 ? 4 ARG A CA 1
+ATOM 34 C C . ARG A 1 4 ? 1.257 4.818 -5.846 1.00 17.46 ? 4 ARG A C 1
+ATOM 35 O O . ARG A 1 4 ? 2.173 4.183 -6.358 1.00 18.03 ? 4 ARG A O 1
+ATOM 36 C CB . ARG A 1 4 ? -0.984 4.179 -6.615 1.00 19.34 ? 4 ARG A CB 1
+ATOM 37 C CG . ARG A 1 4 ? -2.389 4.693 -6.846 1.00 22.46 ? 4 ARG A CG 1
+ATOM 38 C CD . ARG A 1 4 ? -2.962 5.187 -5.525 1.00 25.30 ? 4 ARG A CD 1
+ATOM 39 N NE . ARG A 1 4 ? -4.352 5.630 -5.666 1.00 28.96 ? 4 ARG A NE 1
+ATOM 40 C CZ . ARG A 1 4 ? -5.041 6.254 -4.713 1.00 31.07 ? 4 ARG A CZ 1
+ATOM 41 N NH1 . ARG A 1 4 ? -4.479 6.508 -3.538 1.00 31.07 ? 4 ARG A NH1 1
+ATOM 42 N NH2 . ARG A 1 4 ? -6.295 6.632 -4.932 1.00 28.97 ? 4 ARG A NH2 1
+ATOM 43 N N A LYS A 1 5 ? 1.185 5.069 -4.531 0.50 16.58 ? 5 LYS A N 1
+ATOM 44 N N B LYS A 1 5 ? 1.202 5.059 -4.523 0.50 16.76 ? 5 LYS A N 1
+ATOM 45 C CA A LYS A 1 5 ? 2.185 4.556 -3.613 0.50 16.63 ? 5 LYS A CA 1
+ATOM 46 C CA B LYS A 1 5 ? 2.235 4.584 -3.597 0.50 16.99 ? 5 LYS A CA 1
+ATOM 47 C C A LYS A 1 5 ? 1.841 3.080 -3.508 0.50 17.04 ? 5 LYS A C 1
+ATOM 48 C C B LYS A 1 5 ? 1.980 3.098 -3.369 0.50 17.63 ? 5 LYS A C 1
+ATOM 49 O O A LYS A 1 5 ? 0.747 2.726 -3.077 0.50 17.39 ? 5 LYS A O 1
+ATOM 50 O O B LYS A 1 5 ? 1.203 2.711 -2.496 0.50 18.57 ? 5 LYS A O 1
+ATOM 51 C CB A LYS A 1 5 ? 2.120 5.253 -2.246 0.50 17.92 ? 5 LYS A CB 1
+ATOM 52 C CB B LYS A 1 5 ? 2.196 5.363 -2.273 0.50 18.19 ? 5 LYS A CB 1
+ATOM 53 C CG A LYS A 1 5 ? 3.300 4.911 -1.342 0.50 21.29 ? 5 LYS A CG 1
+ATOM 54 C CG B LYS A 1 5 ? 3.332 5.005 -1.326 0.50 21.43 ? 5 LYS A CG 1
+ATOM 55 C CD A LYS A 1 5 ? 4.637 5.388 -1.894 0.50 24.62 ? 5 LYS A CD 1
+ATOM 56 C CD B LYS A 1 5 ? 4.694 5.391 -1.868 0.50 24.70 ? 5 LYS A CD 1
+ATOM 57 C CE A LYS A 1 5 ? 4.810 6.884 -1.795 0.50 27.77 ? 5 LYS A CE 1
+ATOM 58 C CE B LYS A 1 5 ? 4.925 6.879 -1.800 0.50 27.68 ? 5 LYS A CE 1
+ATOM 59 N NZ A LYS A 1 5 ? 4.611 7.386 -0.415 0.50 29.14 ? 5 LYS A NZ 1
+ATOM 60 N NZ B LYS A 1 5 ? 4.633 7.433 -0.457 0.50 28.93 ? 5 LYS A NZ 1
+ATOM 61 N N . MET A 1 6 ? 2.663 2.273 -4.148 1.00 17.01 ? 6 MET A N 1
+ATOM 62 C CA . MET A 1 6 ? 2.427 0.855 -4.239 1.00 17.12 ? 6 MET A CA 1
+ATOM 63 C C . MET A 1 6 ? 3.367 0.015 -3.454 1.00 15.93 ? 6 MET A C 1
+ATOM 64 O O . MET A 1 6 ? 4.570 0.202 -3.547 1.00 16.36 ? 6 MET A O 1
+ATOM 65 C CB . MET A 1 6 ? 2.580 0.517 -5.725 1.00 19.42 ? 6 MET A CB 1
+ATOM 66 C CG . MET A 1 6 ? 2.137 -0.836 -6.077 1.00 24.58 ? 6 MET A CG 1
+ATOM 67 S SD . MET A 1 6 ? 2.195 -0.979 -7.868 1.00 31.98 ? 6 MET A SD 1
+ATOM 68 C CE . MET A 1 6 ? 0.949 0.182 -8.339 1.00 27.76 ? 6 MET A CE 1
+ATOM 69 N N . ALA A 1 7 ? 2.820 -0.956 -2.733 1.00 14.89 ? 7 ALA A N 1
+ATOM 70 C CA . ALA A 1 7 ? 3.639 -1.900 -1.989 1.00 15.29 ? 7 ALA A CA 1
+ATOM 71 C C . ALA A 1 7 ? 3.744 -3.190 -2.803 1.00 15.57 ? 7 ALA A C 1
+ATOM 72 O O . ALA A 1 7 ? 2.963 -3.405 -3.734 1.00 16.04 ? 7 ALA A O 1
+ATOM 73 C CB . ALA A 1 7 ? 3.006 -2.185 -0.630 1.00 15.59 ? 7 ALA A CB 1
+ATOM 74 N N . PHE A 1 8 ? 4.742 -4.010 -2.521 1.00 15.58 ? 8 PHE A N 1
+ATOM 75 C CA . PHE A 1 8 ? 4.868 -5.305 -3.172 1.00 16.87 ? 8 PHE A CA 1
+ATOM 76 C C . PHE A 1 8 ? 3.750 -6.202 -2.661 1.00 16.69 ? 8 PHE A C 1
+ATOM 77 O O . PHE A 1 8 ? 3.298 -6.088 -1.511 1.00 16.04 ? 8 PHE A O 1
+ATOM 78 C CB . PHE A 1 8 ? 6.222 -5.940 -2.834 1.00 17.33 ? 8 PHE A CB 1
+ATOM 79 C CG . PHE A 1 8 ? 7.358 -5.313 -3.588 1.00 19.06 ? 8 PHE A CG 1
+ATOM 80 C CD1 . PHE A 1 8 ? 7.607 -5.651 -4.907 1.00 20.90 ? 8 PHE A CD1 1
+ATOM 81 C CD2 . PHE A 1 8 ? 8.164 -4.366 -2.990 1.00 20.60 ? 8 PHE A CD2 1
+ATOM 82 C CE1 . PHE A 1 8 ? 8.640 -5.049 -5.607 1.00 22.00 ? 8 PHE A CE1 1
+ATOM 83 C CE2 . PHE A 1 8 ? 9.209 -3.787 -3.685 1.00 21.94 ? 8 PHE A CE2 1
+ATOM 84 C CZ . PHE A 1 8 ? 9.433 -4.123 -4.991 1.00 22.08 ? 8 PHE A CZ 1
+ATOM 85 N N . PRO A 1 9 ? 3.322 -7.176 -3.489 1.00 17.15 ? 9 PRO A N 1
+ATOM 86 C CA . PRO A 1 9 ? 2.348 -8.173 -3.002 1.00 17.33 ? 9 PRO A CA 1
+ATOM 87 C C . PRO A 1 9 ? 2.939 -8.881 -1.771 1.00 17.30 ? 9 PRO A C 1
+ATOM 88 O O . PRO A 1 9 ? 4.125 -9.203 -1.771 1.00 19.22 ? 9 PRO A O 1
+ATOM 89 C CB . PRO A 1 9 ? 2.198 -9.124 -4.195 1.00 19.02 ? 9 PRO A CB 1
+ATOM 90 C CG . PRO A 1 9 ? 2.667 -8.338 -5.372 1.00 19.72 ? 9 PRO A CG 1
+ATOM 91 C CD . PRO A 1 9 ? 3.768 -7.478 -4.860 1.00 17.41 ? 9 PRO A CD 1
+ATOM 92 N N . SER A 1 10 ? 2.170 -8.982 -0.714 1.00 15.92 ? 10 SER A N 1
+ATOM 93 C CA . SER A 1 10 ? 2.701 -9.448 0.569 1.00 15.16 ? 10 SER A CA 1
+ATOM 94 C C . SER A 1 10 ? 2.612 -10.944 0.842 1.00 15.12 ? 10 SER A C 1
+ATOM 95 O O . SER A 1 10 ? 3.100 -11.378 1.869 1.00 14.73 ? 10 SER A O 1
+ATOM 96 C CB . SER A 1 10 ? 2.029 -8.690 1.705 1.00 15.91 ? 10 SER A CB 1
+ATOM 97 O OG . SER A 1 10 ? 0.623 -8.864 1.658 1.00 17.96 ? 10 SER A OG 1
+ATOM 98 N N . GLY A 1 11 ? 2.001 -11.708 -0.041 1.00 15.29 ? 11 GLY A N 1
+ATOM 99 C CA . GLY A 1 11 ? 1.797 -13.135 0.179 1.00 15.09 ? 11 GLY A CA 1
+ATOM 100 C C . GLY A 1 11 ? 3.008 -13.943 0.596 1.00 14.62 ? 11 GLY A C 1
+ATOM 101 O O . GLY A 1 11 ? 2.943 -14.731 1.548 1.00 15.34 ? 11 GLY A O 1
+ATOM 102 N N . LYS A 1 12 ? 4.126 -13.735 -0.106 1.00 13.99 ? 12 LYS A N 1
+ATOM 103 C CA . LYS A 1 12 ? 5.345 -14.487 0.193 1.00 14.02 ? 12 LYS A CA 1
+ATOM 104 C C . LYS A 1 12 ? 5.831 -14.217 1.613 1.00 14.16 ? 12 LYS A C 1
+ATOM 105 O O . LYS A 1 12 ? 6.375 -15.110 2.261 1.00 14.81 ? 12 LYS A O 1
+ATOM 106 C CB . LYS A 1 12 ? 6.449 -14.195 -0.821 1.00 15.54 ? 12 LYS A CB 1
+ATOM 107 C CG . LYS A 1 12 ? 6.209 -14.833 -2.180 1.00 19.84 ? 12 LYS A CG 1
+ATOM 108 C CD . LYS A 1 12 ? 7.166 -14.268 -3.223 1.00 25.38 ? 12 LYS A CD 1
+ATOM 109 C CE . LYS A 1 12 ? 6.905 -14.864 -4.589 1.00 30.94 ? 12 LYS A CE 1
+ATOM 110 N NZ . LYS A 1 12 ? 7.019 -16.342 -4.559 1.00 34.47 ? 12 LYS A NZ 1
+ATOM 111 N N . VAL A 1 13 ? 5.605 -12.996 2.114 1.00 13.22 ? 13 VAL A N 1
+ATOM 112 C CA . VAL A 1 13 ? 6.032 -12.646 3.468 1.00 12.21 ? 13 VAL A CA 1
+ATOM 113 C C . VAL A 1 13 ? 5.000 -13.074 4.500 1.00 11.66 ? 13 VAL A C 1
+ATOM 114 O O . VAL A 1 13 ? 5.364 -13.520 5.588 1.00 11.73 ? 13 VAL A O 1
+ATOM 115 C CB . VAL A 1 13 ? 6.355 -11.145 3.551 1.00 13.09 ? 13 VAL A CB 1
+ATOM 116 C CG1 . VAL A 1 13 ? 6.822 -10.761 4.950 1.00 14.14 ? 13 VAL A CG1 1
+ATOM 117 C CG2 . VAL A 1 13 ? 7.411 -10.784 2.519 1.00 14.34 ? 13 VAL A CG2 1
+ATOM 118 N N . GLU A 1 14 ? 3.701 -13.021 4.159 1.00 11.62 ? 14 GLU A N 1
+ATOM 119 C CA . GLU A 1 14 ? 2.641 -13.473 5.068 1.00 11.63 ? 14 GLU A CA 1
+ATOM 120 C C . GLU A 1 14 ? 2.876 -14.916 5.521 1.00 12.71 ? 14 GLU A C 1
+ATOM 121 O O . GLU A 1 14 ? 2.716 -15.224 6.703 1.00 13.03 ? 14 GLU A O 1
+ATOM 122 C CB . GLU A 1 14 ? 1.275 -13.399 4.373 1.00 12.59 ? 14 GLU A CB 1
+ATOM 123 C CG . GLU A 1 14 ? 0.756 -11.988 4.211 1.00 15.46 ? 14 GLU A CG 1
+ATOM 124 C CD . GLU A 1 14 ? -0.445 -11.950 3.292 1.00 18.75 ? 14 GLU A CD 1
+ATOM 125 O OE1 . GLU A 1 14 ? -1.417 -12.694 3.553 1.00 21.44 ? 14 GLU A OE1 1
+ATOM 126 O OE2 . GLU A 1 14 ? -0.390 -11.204 2.289 1.00 19.65 ? 14 GLU A OE2 1
+ATOM 127 N N . GLY A 1 15 ? 3.357 -15.745 4.598 1.00 12.90 ? 15 GLY A N 1
+ATOM 128 C CA . GLY A 1 15 ? 3.649 -17.145 4.878 1.00 12.73 ? 15 GLY A CA 1
+ATOM 129 C C . GLY A 1 15 ? 4.818 -17.392 5.810 1.00 12.45 ? 15 GLY A C 1
+ATOM 130 O O . GLY A 1 15 ? 5.068 -18.532 6.200 1.00 13.52 ? 15 GLY A O 1
+ATOM 131 N N . CYS A 1 16 ? 5.547 -16.341 6.161 1.00 11.59 ? 16 CYS A N 1
+ATOM 132 C CA . CYS A 1 16 ? 6.690 -16.411 7.064 1.00 11.47 ? 16 CYS A CA 1
+ATOM 133 C C . CYS A 1 16 ? 6.412 -15.838 8.439 1.00 11.91 ? 16 CYS A C 1
+ATOM 134 O O . CYS A 1 16 ? 7.299 -15.910 9.283 1.00 12.77 ? 16 CYS A O 1
+ATOM 135 C CB . CYS A 1 16 ? 7.899 -15.722 6.446 1.00 12.44 ? 16 CYS A CB 1
+ATOM 136 S SG . CYS A 1 16 ? 8.356 -16.342 4.810 1.00 15.98 ? 16 CYS A SG 1
+ATOM 137 N N . MET A 1 17 ? 5.240 -15.226 8.673 1.00 11.61 ? 17 MET A N 1
+ATOM 138 C CA . MET A 1 17 ? 5.017 -14.567 9.953 1.00 12.03 ? 17 MET A CA 1
+ATOM 139 C C . MET A 1 17 ? 4.535 -15.499 11.022 1.00 12.33 ? 17 MET A C 1
+ATOM 140 O O . MET A 1 17 ? 3.618 -16.266 10.806 1.00 12.97 ? 17 MET A O 1
+ATOM 141 C CB . MET A 1 17 ? 4.077 -13.372 9.816 1.00 12.21 ? 17 MET A CB 1
+ATOM 142 C CG . MET A 1 17 ? 4.535 -12.353 8.787 1.00 13.24 ? 17 MET A CG 1
+ATOM 143 S SD . MET A 1 17 ? 6.217 -11.703 9.005 1.00 14.39 ? 17 MET A SD 1
+ATOM 144 C CE . MET A 1 17 ? 6.158 -11.181 10.754 1.00 15.96 ? 17 MET A CE 1
+ATOM 145 N N . VAL A 1 18 ? 5.186 -15.438 12.176 1.00 11.86 ? 18 VAL A N 1
+ATOM 146 C CA . VAL A 1 18 ? 4.849 -16.234 13.343 1.00 12.74 ? 18 VAL A CA 1
+ATOM 147 C C . VAL A 1 18 ? 4.775 -15.312 14.559 1.00 12.62 ? 18 VAL A C 1
+ATOM 148 O O . VAL A 1 18 ? 5.220 -14.160 14.518 1.00 12.38 ? 18 VAL A O 1
+ATOM 149 C CB . VAL A 1 18 ? 5.882 -17.373 13.576 1.00 13.97 ? 18 VAL A CB 1
+ATOM 150 C CG1 . VAL A 1 18 ? 5.917 -18.341 12.404 1.00 14.87 ? 18 VAL A CG1 1
+ATOM 151 C CG2 . VAL A 1 18 ? 7.262 -16.802 13.868 1.00 13.93 ? 18 VAL A CG2 1
+ATOM 152 N N . GLN A 1 19 ? 4.185 -15.818 15.633 1.00 12.65 ? 19 GLN A N 1
+ATOM 153 C CA . GLN A 1 19 ? 4.107 -15.113 16.896 1.00 13.10 ? 19 GLN A CA 1
+ATOM 154 C C . GLN A 1 19 ? 5.221 -15.641 17.802 1.00 12.93 ? 19 GLN A C 1
+ATOM 155 O O . GLN A 1 19 ? 5.433 -16.850 17.868 1.00 12.86 ? 19 GLN A O 1
+ATOM 156 C CB . GLN A 1 19 ? 2.735 -15.376 17.520 1.00 14.90 ? 19 GLN A CB 1
+ATOM 157 C CG . GLN A 1 19 ? 2.552 -14.741 18.881 1.00 18.61 ? 19 GLN A CG 1
+ATOM 158 C CD . GLN A 1 19 ? 1.293 -15.237 19.530 1.00 24.25 ? 19 GLN A CD 1
+ATOM 159 O OE1 . GLN A 1 19 ? 1.285 -16.257 20.224 1.00 26.10 ? 19 GLN A OE1 1
+ATOM 160 N NE2 . GLN A 1 19 ? 0.206 -14.527 19.326 1.00 25.55 ? 19 GLN A NE2 1
+ATOM 161 N N . VAL A 1 20 ? 5.940 -14.742 18.500 1.00 12.43 ? 20 VAL A N 1
+ATOM 162 C CA . VAL A 1 20 ? 6.962 -15.171 19.450 1.00 13.22 ? 20 VAL A CA 1
+ATOM 163 C C . VAL A 1 20 ? 6.631 -14.580 20.807 1.00 13.82 ? 20 VAL A C 1
+ATOM 164 O O . VAL A 1 20 ? 6.435 -13.367 20.921 1.00 14.21 ? 20 VAL A O 1
+ATOM 165 C CB . VAL A 1 20 ? 8.405 -14.806 19.036 1.00 13.47 ? 20 VAL A CB 1
+ATOM 166 C CG1 . VAL A 1 20 ? 9.408 -15.330 20.066 1.00 14.22 ? 20 VAL A CG1 1
+ATOM 167 C CG2 . VAL A 1 20 ? 8.731 -15.348 17.650 1.00 13.91 ? 20 VAL A CG2 1
+ATOM 168 N N . THR A 1 21 ? 6.537 -15.429 21.823 1.00 14.34 ? 21 THR A N 1
+ATOM 169 C CA . THR A 1 21 ? 6.264 -14.970 23.174 1.00 15.62 ? 21 THR A CA 1
+ATOM 170 C C . THR A 1 21 ? 7.382 -15.417 24.085 1.00 16.58 ? 21 THR A C 1
+ATOM 171 O O . THR A 1 21 ? 7.797 -16.567 24.035 1.00 16.63 ? 21 THR A O 1
+ATOM 172 C CB . THR A 1 21 ? 4.920 -15.534 23.681 1.00 18.06 ? 21 THR A CB 1
+ATOM 173 O OG1 . THR A 1 21 ? 3.855 -15.130 22.823 1.00 19.40 ? 21 THR A OG1 1
+ATOM 174 C CG2 . THR A 1 21 ? 4.614 -15.109 25.110 1.00 19.50 ? 21 THR A CG2 1
+ATOM 175 N N . CYS A 1 22 ? 7.882 -14.511 24.909 1.00 17.62 ? 22 CYS A N 1
+ATOM 176 C CA . CYS A 1 22 ? 8.866 -14.862 25.915 1.00 19.68 ? 22 CYS A CA 1
+ATOM 177 C C . CYS A 1 22 ? 8.353 -14.192 27.181 1.00 22.21 ? 22 CYS A C 1
+ATOM 178 O O . CYS A 1 22 ? 8.185 -12.976 27.221 1.00 22.29 ? 22 CYS A O 1
+ATOM 179 C CB . CYS A 1 22 ? 10.273 -14.403 25.535 1.00 19.81 ? 22 CYS A CB 1
+ATOM 180 S SG . CYS A 1 22 ? 11.574 -15.049 26.614 1.00 26.04 ? 22 CYS A SG 1
+ATOM 181 N N . GLY A 1 23 ? 7.977 -15.014 28.151 1.00 24.20 ? 23 GLY A N 1
+ATOM 182 C CA . GLY A 1 23 ? 7.401 -14.541 29.403 1.00 25.86 ? 23 GLY A CA 1
+ATOM 183 C C . GLY A 1 23 ? 6.078 -13.859 29.141 1.00 27.25 ? 23 GLY A C 1
+ATOM 184 O O . GLY A 1 23 ? 5.164 -14.465 28.577 1.00 28.42 ? 23 GLY A O 1
+ATOM 185 N N . THR A 1 24 ? 6.013 -12.564 29.424 1.00 27.33 ? 24 THR A N 1
+ATOM 186 C CA . THR A 1 24 ? 4.800 -11.787 29.185 1.00 27.90 ? 24 THR A CA 1
+ATOM 187 C C . THR A 1 24 ? 4.849 -10.946 27.898 1.00 26.48 ? 24 THR A C 1
+ATOM 188 O O . THR A 1 24 ? 3.899 -10.223 27.618 1.00 27.56 ? 24 THR A O 1
+ATOM 189 C CB . THR A 1 24 ? 4.514 -10.899 30.395 1.00 31.42 ? 24 THR A CB 1
+ATOM 190 O OG1 . THR A 1 24 ? 5.534 -9.903 30.499 1.00 33.89 ? 24 THR A OG1 1
+ATOM 191 C CG2 . THR A 1 24 ? 4.440 -11.691 31.681 1.00 32.45 ? 24 THR A CG2 1
+ATOM 192 N N . THR A 1 25 ? 5.938 -11.023 27.128 1.00 24.11 ? 25 THR A N 1
+ATOM 193 C CA . THR A 1 25 ? 6.082 -10.214 25.922 1.00 22.53 ? 25 THR A CA 1
+ATOM 194 C C . THR A 1 25 ? 5.755 -11.009 24.671 1.00 21.00 ? 25 THR A C 1
+ATOM 195 O O . THR A 1 25 ? 6.304 -12.083 24.490 1.00 21.49 ? 25 THR A O 1
+ATOM 196 C CB . THR A 1 25 ? 7.503 -9.662 25.850 1.00 23.52 ? 25 THR A CB 1
+ATOM 197 O OG1 . THR A 1 25 ? 7.752 -8.858 27.011 1.00 24.80 ? 25 THR A OG1 1
+ATOM 198 C CG2 . THR A 1 25 ? 7.756 -8.862 24.584 1.00 23.98 ? 25 THR A CG2 1
+ATOM 199 N N . THR A 1 26 ? 4.880 -10.486 23.817 1.00 19.91 ? 26 THR A N 1
+ATOM 200 C CA . THR A 1 26 ? 4.539 -11.124 22.554 1.00 19.02 ? 26 THR A CA 1
+ATOM 201 C C . THR A 1 26 ? 4.814 -10.164 21.401 1.00 17.49 ? 26 THR A C 1
+ATOM 202 O O . THR A 1 26 ? 4.376 -9.013 21.413 1.00 18.04 ? 26 THR A O 1
+ATOM 203 C CB . THR A 1 26 ? 3.074 -11.584 22.541 1.00 20.95 ? 26 THR A CB 1
+ATOM 204 O OG1 . THR A 1 26 ? 2.900 -12.636 23.488 1.00 22.53 ? 26 THR A OG1 1
+ATOM 205 C CG2 . THR A 1 26 ? 2.634 -12.069 21.182 1.00 21.72 ? 26 THR A CG2 1
+ATOM 206 N N . LEU A 1 27 ? 5.539 -10.637 20.411 1.00 15.55 ? 27 LEU A N 1
+ATOM 207 C CA . LEU A 1 27 ? 5.787 -9.858 19.200 1.00 14.34 ? 27 LEU A CA 1
+ATOM 208 C C . LEU A 1 27 ? 5.841 -10.794 17.990 1.00 13.54 ? 27 LEU A C 1
+ATOM 209 O O . LEU A 1 27 ? 5.400 -11.943 18.087 1.00 13.86 ? 27 LEU A O 1
+ATOM 210 C CB . LEU A 1 27 ? 7.007 -8.909 19.344 1.00 13.99 ? 27 LEU A CB 1
+ATOM 211 C CG . LEU A 1 27 ? 8.263 -9.503 19.968 1.00 14.11 ? 27 LEU A CG 1
+ATOM 212 C CD1 . LEU A 1 27 ? 8.801 -10.671 19.161 1.00 14.29 ? 27 LEU A CD1 1
+ATOM 213 C CD2 . LEU A 1 27 ? 9.349 -8.450 20.127 1.00 14.70 ? 27 LEU A CD2 1
+ATOM 214 N N . ASN A 1 28 ? 6.313 -10.302 16.845 1.00 12.24 ? 28 ASN A N 1
+ATOM 215 C CA . ASN A 1 28 ? 6.346 -11.091 15.631 1.00 11.92 ? 28 ASN A CA 1
+ATOM 216 C C . ASN A 1 28 ? 7.714 -11.653 15.355 1.00 11.52 ? 28 ASN A C 1
+ATOM 217 O O . ASN A 1 28 ? 8.725 -11.066 15.710 1.00 11.85 ? 28 ASN A O 1
+ATOM 218 C CB . ASN A 1 28 ? 5.884 -10.259 14.427 1.00 13.05 ? 28 ASN A CB 1
+ATOM 219 C CG . ASN A 1 28 ? 4.569 -9.595 14.702 1.00 15.18 ? 28 ASN A CG 1
+ATOM 220 O OD1 . ASN A 1 28 ? 3.512 -10.223 14.621 1.00 15.52 ? 28 ASN A OD1 1
+ATOM 221 N ND2 . ASN A 1 28 ? 4.620 -8.331 15.068 1.00 15.66 ? 28 ASN A ND2 1
+ATOM 222 N N . GLY A 1 29 ? 7.713 -12.775 14.686 1.00 11.02 ? 29 GLY A N 1
+ATOM 223 C CA . GLY A 1 29 ? 8.925 -13.411 14.219 1.00 11.06 ? 29 GLY A CA 1
+ATOM 224 C C . GLY A 1 29 ? 8.812 -13.718 12.738 1.00 11.20 ? 29 GLY A C 1
+ATOM 225 O O . GLY A 1 29 ? 7.714 -13.803 12.179 1.00 11.95 ? 29 GLY A O 1
+ATOM 226 N N . LEU A 1 30 ? 9.956 -13.877 12.090 1.00 10.90 ? 30 LEU A N 1
+ATOM 227 C CA . LEU A 1 30 ? 10.046 -14.190 10.667 1.00 10.82 ? 30 LEU A CA 1
+ATOM 228 C C . LEU A 1 30 ? 10.616 -15.606 10.560 1.00 10.79 ? 30 LEU A C 1
+ATOM 229 O O . LEU A 1 30 ? 11.740 -15.840 11.002 1.00 11.77 ? 30 LEU A O 1
+ATOM 230 C CB . LEU A 1 30 ? 10.994 -13.195 9.995 1.00 10.42 ? 30 LEU A CB 1
+ATOM 231 C CG . LEU A 1 30 ? 11.086 -13.328 8.477 1.00 11.21 ? 30 LEU A CG 1
+ATOM 232 C CD1 . LEU A 1 30 ? 9.784 -12.894 7.816 1.00 12.16 ? 30 LEU A CD1 1
+ATOM 233 C CD2 . LEU A 1 30 ? 12.245 -12.507 7.952 1.00 12.12 ? 30 LEU A CD2 1
+ATOM 234 N N . TRP A 1 31 ? 9.866 -16.535 9.979 1.00 10.46 ? 31 TRP A N 1
+ATOM 235 C CA . TRP A 1 31 ? 10.255 -17.943 9.908 1.00 10.74 ? 31 TRP A CA 1
+ATOM 236 C C . TRP A 1 31 ? 10.711 -18.287 8.502 1.00 11.18 ? 31 TRP A C 1
+ATOM 237 O O . TRP A 1 31 ? 9.923 -18.273 7.553 1.00 11.15 ? 31 TRP A O 1
+ATOM 238 C CB . TRP A 1 31 ? 9.054 -18.777 10.353 1.00 11.08 ? 31 TRP A CB 1
+ATOM 239 C CG . TRP A 1 31 ? 9.218 -20.262 10.334 1.00 11.19 ? 31 TRP A CG 1
+ATOM 240 C CD1 . TRP A 1 31 ? 10.371 -20.974 10.511 1.00 11.87 ? 31 TRP A CD1 1
+ATOM 241 C CD2 . TRP A 1 31 ? 8.153 -21.221 10.295 1.00 11.18 ? 31 TRP A CD2 1
+ATOM 242 N NE1 . TRP A 1 31 ? 10.090 -22.323 10.513 1.00 11.94 ? 31 TRP A NE1 1
+ATOM 243 C CE2 . TRP A 1 31 ? 8.734 -22.499 10.412 1.00 11.98 ? 31 TRP A CE2 1
+ATOM 244 C CE3 . TRP A 1 31 ? 6.763 -21.123 10.121 1.00 11.96 ? 31 TRP A CE3 1
+ATOM 245 C CZ2 . TRP A 1 31 ? 7.976 -23.673 10.353 1.00 12.16 ? 31 TRP A CZ2 1
+ATOM 246 C CZ3 . TRP A 1 31 ? 6.013 -22.284 10.075 1.00 12.27 ? 31 TRP A CZ3 1
+ATOM 247 C CH2 . TRP A 1 31 ? 6.621 -23.544 10.169 1.00 12.25 ? 31 TRP A CH2 1
+ATOM 248 N N . LEU A 1 32 ? 12.025 -18.505 8.356 1.00 11.11 ? 32 LEU A N 1
+ATOM 249 C CA . LEU A 1 32 ? 12.646 -18.808 7.060 1.00 12.05 ? 32 LEU A CA 1
+ATOM 250 C C . LEU A 1 32 ? 13.464 -20.041 7.259 1.00 12.52 ? 32 LEU A C 1
+ATOM 251 O O . LEU A 1 32 ? 14.277 -20.097 8.192 1.00 12.39 ? 32 LEU A O 1
+ATOM 252 C CB . LEU A 1 32 ? 13.563 -17.678 6.627 1.00 12.45 ? 32 LEU A CB 1
+ATOM 253 C CG . LEU A 1 32 ? 12.892 -16.342 6.393 1.00 13.71 ? 32 LEU A CG 1
+ATOM 254 C CD1 . LEU A 1 32 ? 13.907 -15.285 6.173 1.00 13.62 ? 32 LEU A CD1 1
+ATOM 255 C CD2 . LEU A 1 32 ? 11.959 -16.400 5.210 1.00 14.51 ? 32 LEU A CD2 1
+ATOM 256 N N . ASP A 1 33 ? 13.193 -21.093 6.468 1.00 12.93 ? 33 ASP A N 1
+ATOM 257 C CA . ASP A 1 33 ? 13.854 -22.381 6.675 1.00 13.70 ? 33 ASP A CA 1
+ATOM 258 C C . ASP A 1 33 ? 13.561 -22.852 8.132 1.00 13.91 ? 33 ASP A C 1
+ATOM 259 O O . ASP A 1 33 ? 12.412 -22.706 8.557 1.00 14.60 ? 33 ASP A O 1
+ATOM 260 C CB . ASP A 1 33 ? 15.356 -22.306 6.311 1.00 16.27 ? 33 ASP A CB 1
+ATOM 261 C CG . ASP A 1 33 ? 15.597 -21.887 4.883 1.00 21.63 ? 33 ASP A CG 1
+ATOM 262 O OD1 . ASP A 1 33 ? 14.817 -22.304 4.008 1.00 23.84 ? 33 ASP A OD1 1
+ATOM 263 O OD2 . ASP A 1 33 ? 16.574 -21.142 4.642 1.00 23.06 ? 33 ASP A OD2 1
+ATOM 264 N N . ASP A 1 34 ? 14.549 -23.299 8.901 1.00 12.95 ? 34 ASP A N 1
+ATOM 265 C CA . ASP A 1 34 ? 14.306 -23.727 10.265 1.00 12.62 ? 34 ASP A CA 1
+ATOM 266 C C . ASP A 1 34 ? 14.745 -22.702 11.278 1.00 12.42 ? 34 ASP A C 1
+ATOM 267 O O . ASP A 1 34 ? 15.104 -23.073 12.395 1.00 13.06 ? 34 ASP A O 1
+ATOM 268 C CB . ASP A 1 34 ? 14.988 -25.077 10.522 1.00 13.51 ? 34 ASP A CB 1
+ATOM 269 C CG . ASP A 1 34 ? 16.497 -25.078 10.331 1.00 17.85 ? 34 ASP A CG 1
+ATOM 270 O OD1 . ASP A 1 34 ? 17.037 -24.076 9.798 1.00 17.68 ? 34 ASP A OD1 1
+ATOM 271 O OD2 . ASP A 1 34 ? 17.138 -26.087 10.709 1.00 20.21 ? 34 ASP A OD2 1
+ATOM 272 N N . VAL A 1 35 ? 14.689 -21.404 10.928 1.00 11.43 ? 35 VAL A N 1
+ATOM 273 C CA . VAL A 1 35 ? 15.074 -20.358 11.868 1.00 12.04 ? 35 VAL A CA 1
+ATOM 274 C C . VAL A 1 35 ? 13.987 -19.307 11.950 1.00 11.65 ? 35 VAL A C 1
+ATOM 275 O O . VAL A 1 35 ? 13.400 -18.939 10.930 1.00 12.01 ? 35 VAL A O 1
+ATOM 276 C CB . VAL A 1 35 ? 16.424 -19.702 11.481 1.00 13.42 ? 35 VAL A CB 1
+ATOM 277 C CG1 . VAL A 1 35 ? 16.824 -18.604 12.473 1.00 13.93 ? 35 VAL A CG1 1
+ATOM 278 C CG2 . VAL A 1 35 ? 17.519 -20.750 11.384 1.00 14.17 ? 35 VAL A CG2 1
+ATOM 279 N N . VAL A 1 36 ? 13.699 -18.861 13.164 1.00 11.24 ? 36 VAL A N 1
+ATOM 280 C CA . VAL A 1 36 ? 12.775 -17.774 13.408 1.00 11.41 ? 36 VAL A CA 1
+ATOM 281 C C . VAL A 1 36 ? 13.589 -16.584 13.895 1.00 11.05 ? 36 VAL A C 1
+ATOM 282 O O . VAL A 1 36 ? 14.339 -16.704 14.855 1.00 10.78 ? 36 VAL A O 1
+ATOM 283 C CB . VAL A 1 36 ? 11.676 -18.169 14.404 1.00 12.20 ? 36 VAL A CB 1
+ATOM 284 C CG1 . VAL A 1 36 ? 10.833 -16.957 14.781 1.00 12.52 ? 36 VAL A CG1 1
+ATOM 285 C CG2 . VAL A 1 36 ? 10.810 -19.281 13.826 1.00 12.70 ? 36 VAL A CG2 1
+ATOM 286 N N . TYR A 1 37 ? 13.465 -15.444 13.220 1.00 11.02 ? 37 TYR A N 1
+ATOM 287 C CA . TYR A 1 37 ? 14.205 -14.229 13.566 1.00 10.75 ? 37 TYR A CA 1
+ATOM 288 C C . TYR A 1 37 ? 13.256 -13.286 14.257 1.00 11.13 ? 37 TYR A C 1
+ATOM 289 O O . TYR A 1 37 ? 12.130 -13.095 13.787 1.00 11.97 ? 37 TYR A O 1
+ATOM 290 C CB . TYR A 1 37 ? 14.693 -13.529 12.285 1.00 10.59 ? 37 TYR A CB 1
+ATOM 291 C CG . TYR A 1 37 ? 15.597 -14.400 11.453 1.00 11.51 ? 37 TYR A CG 1
+ATOM 292 C CD1 . TYR A 1 37 ? 15.076 -15.318 10.558 1.00 12.49 ? 37 TYR A CD1 1
+ATOM 293 C CD2 . TYR A 1 37 ? 16.974 -14.306 11.565 1.00 12.68 ? 37 TYR A CD2 1
+ATOM 294 C CE1 . TYR A 1 37 ? 15.904 -16.163 9.830 1.00 13.67 ? 37 TYR A CE1 1
+ATOM 295 C CE2 . TYR A 1 37 ? 17.814 -15.115 10.809 1.00 13.61 ? 37 TYR A CE2 1
+ATOM 296 C CZ . TYR A 1 37 ? 17.275 -16.032 9.932 1.00 14.78 ? 37 TYR A CZ 1
+ATOM 297 O OH . TYR A 1 37 ? 18.101 -16.885 9.229 1.00 17.25 ? 37 TYR A OH 1
+ATOM 298 N N . CYS A 1 38 ? 13.677 -12.713 15.375 1.00 10.69 ? 38 CYS A N 1
+ATOM 299 C CA . CYS A 1 38 ? 12.825 -11.757 16.071 1.00 10.98 ? 38 CYS A CA 1
+ATOM 300 C C . CYS A 1 38 ? 13.672 -10.755 16.841 1.00 11.25 ? 38 CYS A C 1
+ATOM 301 O O . CYS A 1 38 ? 14.846 -11.012 17.094 1.00 11.69 ? 38 CYS A O 1
+ATOM 302 C CB . CYS A 1 38 ? 11.815 -12.484 16.958 1.00 11.60 ? 38 CYS A CB 1
+ATOM 303 S SG . CYS A 1 38 ? 12.515 -13.143 18.487 1.00 13.48 ? 38 CYS A SG 1
+ATOM 304 N N . PRO A 1 39 ? 13.111 -9.604 17.244 1.00 10.96 ? 39 PRO A N 1
+ATOM 305 C CA . PRO A 1 39 ? 13.899 -8.651 18.033 1.00 10.74 ? 39 PRO A CA 1
+ATOM 306 C C . PRO A 1 39 ? 14.331 -9.281 19.350 1.00 11.52 ? 39 PRO A C 1
+ATOM 307 O O . PRO A 1 39 ? 13.544 -9.987 19.992 1.00 12.03 ? 39 PRO A O 1
+ATOM 308 C CB . PRO A 1 39 ? 12.903 -7.512 18.282 1.00 11.14 ? 39 PRO A CB 1
+ATOM 309 C CG . PRO A 1 39 ? 11.956 -7.602 17.126 1.00 11.48 ? 39 PRO A CG 1
+ATOM 310 C CD . PRO A 1 39 ? 11.753 -9.084 16.998 1.00 10.66 ? 39 PRO A CD 1
+ATOM 311 N N . ARG A 1 40 ? 15.581 -9.024 19.762 1.00 11.03 ? 40 ARG A N 1
+ATOM 312 C CA . ARG A 1 40 ? 16.049 -9.593 21.020 1.00 11.30 ? 40 ARG A CA 1
+ATOM 313 C C . ARG A 1 40 ? 15.284 -9.013 22.218 1.00 12.95 ? 40 ARG A C 1
+ATOM 314 O O . ARG A 1 40 ? 15.228 -9.680 23.250 1.00 13.60 ? 40 ARG A O 1
+ATOM 315 C CB . ARG A 1 40 ? 17.549 -9.444 21.184 1.00 11.64 ? 40 ARG A CB 1
+ATOM 316 C CG . ARG A 1 40 ? 17.977 -8.012 21.332 1.00 12.88 ? 40 ARG A CG 1
+ATOM 317 C CD . ARG A 1 40 ? 19.457 -7.968 21.572 1.00 13.12 ? 40 ARG A CD 1
+ATOM 318 N NE . ARG A 1 40 ? 19.935 -6.599 21.666 1.00 14.21 ? 40 ARG A NE 1
+ATOM 319 C CZ . ARG A 1 40 ? 21.174 -6.261 21.996 1.00 15.68 ? 40 ARG A CZ 1
+ATOM 320 N NH1 . ARG A 1 40 ? 22.082 -7.197 22.248 1.00 15.22 ? 40 ARG A NH1 1
+ATOM 321 N NH2 . ARG A 1 40 ? 21.519 -4.983 22.070 1.00 15.20 ? 40 ARG A NH2 1
+ATOM 322 N N . HIS A 1 41 ? 14.628 -7.836 22.073 1.00 13.07 ? 41 HIS A N 1
+ATOM 323 C CA . HIS A 1 41 ? 13.892 -7.269 23.196 1.00 13.76 ? 41 HIS A CA 1
+ATOM 324 C C . HIS A 1 41 ? 12.612 -8.048 23.529 1.00 14.57 ? 41 HIS A C 1
+ATOM 325 O O . HIS A 1 41 ? 11.970 -7.700 24.519 1.00 14.99 ? 41 HIS A O 1
+ATOM 326 C CB . HIS A 1 41 ? 13.651 -5.754 23.097 1.00 14.02 ? 41 HIS A CB 1
+ATOM 327 C CG . HIS A 1 41 ? 12.654 -5.295 22.083 1.00 16.36 ? 41 HIS A CG 1
+ATOM 328 N ND1 . HIS A 1 41 ? 11.296 -5.507 22.253 1.00 19.44 ? 41 HIS A ND1 1
+ATOM 329 C CD2 . HIS A 1 41 ? 12.838 -4.516 20.993 1.00 17.15 ? 41 HIS A CD2 1
+ATOM 330 C CE1 . HIS A 1 41 ? 10.708 -4.914 21.223 1.00 19.39 ? 41 HIS A CE1 1
+ATOM 331 N NE2 . HIS A 1 41 ? 11.596 -4.303 20.441 1.00 18.52 ? 41 HIS A NE2 1
+ATOM 332 N N . VAL A 1 42 ? 12.320 -9.175 22.827 1.00 14.08 ? 42 VAL A N 1
+ATOM 333 C CA . VAL A 1 42 ? 11.239 -10.064 23.272 1.00 14.58 ? 42 VAL A CA 1
+ATOM 334 C C . VAL A 1 42 ? 11.547 -10.606 24.697 1.00 15.27 ? 42 VAL A C 1
+ATOM 335 O O . VAL A 1 42 ? 10.628 -10.903 25.447 1.00 16.44 ? 42 VAL A O 1
+ATOM 336 C CB . VAL A 1 42 ? 10.982 -11.221 22.276 1.00 14.96 ? 42 VAL A CB 1
+ATOM 337 C CG1 . VAL A 1 42 ? 12.125 -12.225 22.274 1.00 14.97 ? 42 VAL A CG1 1
+ATOM 338 C CG2 . VAL A 1 42 ? 9.651 -11.914 22.559 1.00 15.69 ? 42 VAL A CG2 1
+ATOM 339 N N . ILE A 1 43 ? 12.839 -10.667 25.091 1.00 14.68 ? 43 ILE A N 1
+ATOM 340 C CA . ILE A 1 43 ? 13.211 -11.149 26.424 1.00 15.70 ? 43 ILE A CA 1
+ATOM 341 C C . ILE A 1 43 ? 13.082 -10.078 27.518 1.00 18.13 ? 43 ILE A C 1
+ATOM 342 O O . ILE A 1 43 ? 13.347 -10.366 28.682 1.00 18.87 ? 43 ILE A O 1
+ATOM 343 C CB . ILE A 1 43 ? 14.635 -11.767 26.406 1.00 15.42 ? 43 ILE A CB 1
+ATOM 344 C CG1 . ILE A 1 43 ? 15.718 -10.687 26.276 1.00 15.89 ? 43 ILE A CG1 1
+ATOM 345 C CG2 . ILE A 1 43 ? 14.757 -12.817 25.294 1.00 15.89 ? 43 ILE A CG2 1
+ATOM 346 C CD1 . ILE A 1 43 ? 17.155 -11.214 26.301 1.00 17.16 ? 43 ILE A CD1 1
+ATOM 347 N N . CYS A 1 44 ? 12.700 -8.851 27.161 1.00 19.70 ? 44 CYS A N 1
+ATOM 348 C CA . CYS A 1 44 ? 12.587 -7.761 28.109 1.00 22.56 ? 44 CYS A CA 1
+ATOM 349 C C . CYS A 1 44 ? 11.166 -7.545 28.562 1.00 26.82 ? 44 CYS A C 1
+ATOM 350 O O . CYS A 1 44 ? 10.221 -7.737 27.806 1.00 27.66 ? 44 CYS A O 1
+ATOM 351 C CB . CYS A 1 44 ? 13.121 -6.476 27.485 1.00 22.30 ? 44 CYS A CB 1
+ATOM 352 S SG . CYS A 1 44 ? 14.871 -6.530 27.050 1.00 22.16 ? 44 CYS A SG 1
+ATOM 353 N N . THR A 1 45 ? 11.039 -7.011 29.755 1.00 29.51 ? 45 THR A N 1
+ATOM 354 C CA . THR A 1 45 ? 9.787 -6.494 30.270 1.00 32.18 ? 45 THR A CA 1
+ATOM 355 C C . THR A 1 45 ? 9.827 -4.970 29.895 1.00 34.36 ? 45 THR A C 1
+ATOM 356 O O . THR A 1 45 ? 10.846 -4.488 29.368 1.00 34.59 ? 45 THR A O 1
+ATOM 357 C CB . THR A 1 45 ? 9.740 -6.707 31.794 1.00 34.04 ? 45 THR A CB 1
+ATOM 358 O OG1 . THR A 1 45 ? 10.699 -5.849 32.419 1.00 35.60 ? 45 THR A OG1 1
+ATOM 359 C CG2 . THR A 1 45 ? 10.010 -8.155 32.194 1.00 34.58 ? 45 THR A CG2 1
+ATOM 360 N N . SER A 1 46 ? 8.754 -4.205 30.188 1.00 35.48 ? 46 SER A N 1
+ATOM 361 C CA . SER A 1 46 ? 8.778 -2.760 29.936 1.00 36.69 ? 46 SER A CA 1
+ATOM 362 C C . SER A 1 46 ? 9.855 -2.090 30.824 1.00 37.23 ? 46 SER A C 1
+ATOM 363 O O . SER A 1 46 ? 10.511 -1.144 30.383 1.00 37.54 ? 46 SER A O 1
+ATOM 364 C CB . SER A 1 46 ? 7.409 -2.137 30.185 1.00 38.60 ? 46 SER A CB 1
+ATOM 365 O OG . SER A 1 46 ? 7.293 -0.915 29.474 1.00 42.31 ? 46 SER A OG 1
+ATOM 366 N N . GLU A 1 47 ? 10.064 -2.620 32.051 1.00 37.15 ? 47 GLU A N 1
+ATOM 367 C CA . GLU A 1 47 ? 11.067 -2.151 33.007 1.00 37.30 ? 47 GLU A CA 1
+ATOM 368 C C . GLU A 1 47 ? 12.485 -2.408 32.486 1.00 36.61 ? 47 GLU A C 1
+ATOM 369 O O . GLU A 1 47 ? 13.323 -1.506 32.541 1.00 37.19 ? 47 GLU A O 1
+ATOM 370 C CB . GLU A 1 47 ? 10.871 -2.832 34.379 1.00 40.16 ? 47 GLU A CB 1
+ATOM 371 C CG . GLU A 1 47 ? 11.899 -2.401 35.412 1.00 46.08 ? 47 GLU A CG 1
+ATOM 372 C CD . GLU A 1 47 ? 11.871 -3.137 36.739 1.00 53.53 ? 47 GLU A CD 1
+ATOM 373 O OE1 . GLU A 1 47 ? 11.167 -4.168 36.840 1.00 55.04 ? 47 GLU A OE1 1
+ATOM 374 O OE2 . GLU A 1 47 ? 12.559 -2.680 37.681 1.00 56.09 ? 47 GLU A OE2 1
+ATOM 375 N N . ASP A 1 48 ? 12.752 -3.629 31.971 1.00 35.12 ? 48 ASP A N 1
+ATOM 376 C CA . ASP A 1 48 ? 14.071 -3.994 31.442 1.00 34.07 ? 48 ASP A CA 1
+ATOM 377 C C . ASP A 1 48 ? 14.517 -3.050 30.338 1.00 32.73 ? 48 ASP A C 1
+ATOM 378 O O . ASP A 1 48 ? 15.695 -2.736 30.268 1.00 32.68 ? 48 ASP A O 1
+ATOM 379 C CB . ASP A 1 48 ? 14.089 -5.430 30.884 1.00 35.22 ? 48 ASP A CB 1
+ATOM 380 C CG . ASP A 1 48 ? 14.024 -6.544 31.907 1.00 39.53 ? 48 ASP A CG 1
+ATOM 381 O OD1 . ASP A 1 48 ? 14.540 -6.353 33.029 1.00 39.78 ? 48 ASP A OD1 1
+ATOM 382 O OD2 . ASP A 1 48 ? 13.467 -7.614 31.581 1.00 41.68 ? 48 ASP A OD2 1
+ATOM 383 N N . MET A 1 49 ? 13.587 -2.587 29.486 1.00 31.75 ? 49 MET A N 1
+ATOM 384 C CA . MET A 1 49 ? 13.915 -1.698 28.369 1.00 31.02 ? 49 MET A CA 1
+ATOM 385 C C . MET A 1 49 ? 14.627 -0.405 28.761 1.00 30.28 ? 49 MET A C 1
+ATOM 386 O O . MET A 1 49 ? 15.313 0.164 27.924 1.00 29.65 ? 49 MET A O 1
+ATOM 387 C CB . MET A 1 49 ? 12.679 -1.384 27.513 1.00 31.35 ? 49 MET A CB 1
+ATOM 388 C CG . MET A 1 49 ? 12.174 -2.572 26.724 1.00 32.65 ? 49 MET A CG 1
+ATOM 389 S SD . MET A 1 49 ? 13.436 -3.315 25.650 1.00 33.34 ? 49 MET A SD 1
+ATOM 390 C CE . MET A 1 49 ? 13.560 -2.060 24.368 1.00 27.71 ? 49 MET A CE 1
+ATOM 391 N N . LEU A 1 50 ? 14.493 0.050 30.009 1.00 30.11 ? 50 LEU A N 1
+ATOM 392 C CA . LEU A 1 50 ? 15.162 1.274 30.453 1.00 30.70 ? 50 LEU A CA 1
+ATOM 393 C C . LEU A 1 50 ? 16.689 1.159 30.403 1.00 30.56 ? 50 LEU A C 1
+ATOM 394 O O . LEU A 1 50 ? 17.345 2.089 29.955 1.00 31.26 ? 50 LEU A O 1
+ATOM 395 C CB . LEU A 1 50 ? 14.682 1.683 31.851 1.00 31.34 ? 50 LEU A CB 1
+ATOM 396 C CG . LEU A 1 50 ? 13.191 1.988 31.949 1.00 33.68 ? 50 LEU A CG 1
+ATOM 397 C CD1 . LEU A 1 50 ? 12.778 2.229 33.387 1.00 34.43 ? 50 LEU A CD1 1
+ATOM 398 C CD2 . LEU A 1 50 ? 12.806 3.173 31.059 1.00 34.52 ? 50 LEU A CD2 1
+ATOM 399 N N . ASN A 1 51 ? 17.251 0.022 30.820 1.00 29.29 ? 51 ASN A N 1
+ATOM 400 C CA . ASN A 1 51 ? 18.701 -0.204 30.771 1.00 28.56 ? 51 ASN A CA 1
+ATOM 401 C C . ASN A 1 51 ? 18.964 -1.718 30.692 1.00 26.51 ? 51 ASN A C 1
+ATOM 402 O O . ASN A 1 51 ? 19.400 -2.327 31.674 1.00 26.96 ? 51 ASN A O 1
+ATOM 403 C CB . ASN A 1 51 ? 19.381 0.398 32.009 1.00 30.92 ? 51 ASN A CB 1
+ATOM 404 C CG . ASN A 1 51 ? 20.892 0.388 31.942 1.00 35.07 ? 51 ASN A CG 1
+ATOM 405 O OD1 . ASN A 1 51 ? 21.493 0.225 30.873 1.00 36.86 ? 51 ASN A OD1 1
+ATOM 406 N ND2 . ASN A 1 51 ? 21.539 0.567 33.085 1.00 36.16 ? 51 ASN A ND2 1
+ATOM 407 N N . PRO A 1 52 ? 18.640 -2.362 29.557 1.00 23.74 ? 52 PRO A N 1
+ATOM 408 C CA . PRO A 1 52 ? 18.791 -3.824 29.494 1.00 22.58 ? 52 PRO A CA 1
+ATOM 409 C C . PRO A 1 52 ? 20.203 -4.339 29.261 1.00 21.84 ? 52 PRO A C 1
+ATOM 410 O O . PRO A 1 52 ? 20.938 -3.775 28.461 1.00 23.02 ? 52 PRO A O 1
+ATOM 411 C CB . PRO A 1 52 ? 17.858 -4.228 28.347 1.00 23.00 ? 52 PRO A CB 1
+ATOM 412 C CG . PRO A 1 52 ? 17.799 -3.012 27.462 1.00 23.84 ? 52 PRO A CG 1
+ATOM 413 C CD . PRO A 1 52 ? 18.087 -1.804 28.306 1.00 23.00 ? 52 PRO A CD 1
+ATOM 414 N N . ASN A 1 53 ? 20.579 -5.426 29.948 1.00 20.08 ? 53 ASN A N 1
+ATOM 415 C CA . ASN A 1 53 ? 21.843 -6.098 29.676 1.00 19.44 ? 53 ASN A CA 1
+ATOM 416 C C . ASN A 1 53 ? 21.378 -7.382 29.004 1.00 19.09 ? 53 ASN A C 1
+ATOM 417 O O . ASN A 1 53 ? 20.976 -8.328 29.682 1.00 19.86 ? 53 ASN A O 1
+ATOM 418 C CB . ASN A 1 53 ? 22.650 -6.418 30.934 1.00 20.41 ? 53 ASN A CB 1
+ATOM 419 C CG . ASN A 1 53 ? 24.001 -6.990 30.569 1.00 23.36 ? 53 ASN A CG 1
+ATOM 420 O OD1 . ASN A 1 53 ? 24.112 -7.970 29.818 1.00 24.42 ? 53 ASN A OD1 1
+ATOM 421 N ND2 . ASN A 1 53 ? 25.063 -6.397 31.086 1.00 23.75 ? 53 ASN A ND2 1
+ATOM 422 N N . TYR A 1 54 ? 21.348 -7.382 27.684 1.00 18.47 ? 54 TYR A N 1
+ATOM 423 C CA . TYR A 1 54 ? 20.814 -8.489 26.923 1.00 17.26 ? 54 TYR A CA 1
+ATOM 424 C C . TYR A 1 54 ? 21.500 -9.801 27.153 1.00 17.52 ? 54 TYR A C 1
+ATOM 425 O O . TYR A 1 54 ? 20.800 -10.791 27.331 1.00 17.53 ? 54 TYR A O 1
+ATOM 426 C CB . TYR A 1 54 ? 20.781 -8.147 25.448 1.00 15.88 ? 54 TYR A CB 1
+ATOM 427 C CG . TYR A 1 54 ? 19.666 -7.180 25.141 1.00 15.71 ? 54 TYR A CG 1
+ATOM 428 C CD1 . TYR A 1 54 ? 18.353 -7.614 25.039 1.00 16.04 ? 54 TYR A CD1 1
+ATOM 429 C CD2 . TYR A 1 54 ? 19.916 -5.823 25.004 1.00 15.93 ? 54 TYR A CD2 1
+ATOM 430 C CE1 . TYR A 1 54 ? 17.320 -6.725 24.759 1.00 16.34 ? 54 TYR A CE1 1
+ATOM 431 C CE2 . TYR A 1 54 ? 18.897 -4.929 24.714 1.00 16.57 ? 54 TYR A CE2 1
+ATOM 432 C CZ . TYR A 1 54 ? 17.596 -5.382 24.598 1.00 17.28 ? 54 TYR A CZ 1
+ATOM 433 O OH . TYR A 1 54 ? 16.582 -4.489 24.330 1.00 18.46 ? 54 TYR A OH 1
+ATOM 434 N N . GLU A 1 55 ? 22.849 -9.837 27.217 1.00 18.17 ? 55 GLU A N 1
+ATOM 435 C CA . GLU A 1 55 ? 23.536 -11.110 27.478 1.00 18.88 ? 55 GLU A CA 1
+ATOM 436 C C . GLU A 1 55 ? 23.132 -11.677 28.833 1.00 19.05 ? 55 GLU A C 1
+ATOM 437 O O . GLU A 1 55 ? 22.911 -12.883 28.953 1.00 19.30 ? 55 GLU A O 1
+ATOM 438 C CB . GLU A 1 55 ? 25.069 -10.991 27.409 1.00 22.09 ? 55 GLU A CB 1
+ATOM 439 C CG . GLU A 1 55 ? 25.638 -10.894 26.003 1.00 27.99 ? 55 GLU A CG 1
+ATOM 440 C CD . GLU A 1 55 ? 25.669 -12.141 25.133 1.00 34.81 ? 55 GLU A CD 1
+ATOM 441 O OE1 . GLU A 1 55 ? 25.127 -13.194 25.538 1.00 33.74 ? 55 GLU A OE1 1
+ATOM 442 O OE2 . GLU A 1 55 ? 26.209 -12.043 24.007 1.00 39.00 ? 55 GLU A OE2 1
+ATOM 443 N N . ASP A 1 56 ? 22.991 -10.802 29.841 1.00 18.58 ? 56 ASP A N 1
+ATOM 444 C CA . ASP A 1 56 ? 22.594 -11.263 31.171 1.00 18.89 ? 56 ASP A CA 1
+ATOM 445 C C . ASP A 1 56 ? 21.151 -11.742 31.203 1.00 19.04 ? 56 ASP A C 1
+ATOM 446 O O . ASP A 1 56 ? 20.872 -12.782 31.794 1.00 20.06 ? 56 ASP A O 1
+ATOM 447 C CB . ASP A 1 56 ? 22.838 -10.181 32.232 1.00 20.13 ? 56 ASP A CB 1
+ATOM 448 C CG . ASP A 1 56 ? 24.304 -9.937 32.525 1.00 23.92 ? 56 ASP A CG 1
+ATOM 449 O OD1 . ASP A 1 56 ? 25.133 -10.830 32.216 1.00 23.66 ? 56 ASP A OD1 1
+ATOM 450 O OD2 . ASP A 1 56 ? 24.630 -8.853 33.067 1.00 25.46 ? 56 ASP A OD2 1
+ATOM 451 N N . LEU A 1 57 ? 20.235 -11.002 30.566 1.00 18.53 ? 57 LEU A N 1
+ATOM 452 C CA . LEU A 1 57 ? 18.835 -11.405 30.531 1.00 18.71 ? 57 LEU A CA 1
+ATOM 453 C C . LEU A 1 57 ? 18.663 -12.733 29.781 1.00 18.63 ? 57 LEU A C 1
+ATOM 454 O O . LEU A 1 57 ? 17.847 -13.565 30.166 1.00 18.76 ? 57 LEU A O 1
+ATOM 455 C CB . LEU A 1 57 ? 17.989 -10.323 29.851 1.00 19.11 ? 57 LEU A CB 1
+ATOM 456 C CG . LEU A 1 57 ? 17.861 -9.013 30.615 1.00 21.19 ? 57 LEU A CG 1
+ATOM 457 C CD1 . LEU A 1 57 ? 17.170 -7.968 29.770 1.00 22.03 ? 57 LEU A CD1 1
+ATOM 458 C CD2 . LEU A 1 57 ? 17.084 -9.216 31.913 1.00 22.04 ? 57 LEU A CD2 1
+ATOM 459 N N . LEU A 1 58 ? 19.446 -12.932 28.724 1.00 17.87 ? 58 LEU A N 1
+ATOM 460 C CA . LEU A 1 58 ? 19.353 -14.126 27.908 1.00 18.31 ? 58 LEU A CA 1
+ATOM 461 C C . LEU A 1 58 ? 19.824 -15.379 28.634 1.00 18.99 ? 58 LEU A C 1
+ATOM 462 O O . LEU A 1 58 ? 19.291 -16.458 28.361 1.00 19.97 ? 58 LEU A O 1
+ATOM 463 C CB . LEU A 1 58 ? 20.098 -13.912 26.579 1.00 18.33 ? 58 LEU A CB 1
+ATOM 464 C CG . LEU A 1 58 ? 19.768 -14.878 25.447 1.00 19.20 ? 58 LEU A CG 1
+ATOM 465 C CD1 . LEU A 1 58 ? 18.284 -14.903 25.133 1.00 18.38 ? 58 LEU A CD1 1
+ATOM 466 C CD2 . LEU A 1 58 ? 20.620 -14.581 24.225 1.00 20.01 ? 58 LEU A CD2 1
+ATOM 467 N N . ILE A 1 59 ? 20.748 -15.251 29.613 1.00 18.93 ? 59 ILE A N 1
+ATOM 468 C CA . ILE A 1 59 ? 21.213 -16.402 30.410 1.00 20.28 ? 59 ILE A CA 1
+ATOM 469 C C . ILE A 1 59 ? 20.039 -17.065 31.138 1.00 20.86 ? 59 ILE A C 1
+ATOM 470 O O . ILE A 1 59 ? 20.042 -18.276 31.340 1.00 21.11 ? 59 ILE A O 1
+ATOM 471 C CB . ILE A 1 59 ? 22.308 -15.997 31.439 1.00 22.03 ? 59 ILE A CB 1
+ATOM 472 C CG1 . ILE A 1 59 ? 23.587 -15.552 30.751 1.00 24.25 ? 59 ILE A CG1 1
+ATOM 473 C CG2 . ILE A 1 59 ? 22.606 -17.132 32.438 1.00 23.10 ? 59 ILE A CG2 1
+ATOM 474 C CD1 . ILE A 1 59 ? 24.600 -14.933 31.734 1.00 26.45 ? 59 ILE A CD1 1
+ATOM 475 N N . ARG A 1 60 ? 19.043 -16.267 31.544 1.00 21.21 ? 60 ARG A N 1
+ATOM 476 C CA . ARG A 1 60 ? 17.885 -16.790 32.250 1.00 22.07 ? 60 ARG A CA 1
+ATOM 477 C C . ARG A 1 60 ? 16.844 -17.440 31.336 1.00 21.30 ? 60 ARG A C 1
+ATOM 478 O O . ARG A 1 60 ? 15.812 -17.882 31.826 1.00 22.28 ? 60 ARG A O 1
+ATOM 479 C CB . ARG A 1 60 ? 17.247 -15.694 33.120 1.00 24.65 ? 60 ARG A CB 1
+ATOM 480 C CG . ARG A 1 60 ? 18.246 -14.947 33.999 1.00 29.44 ? 60 ARG A CG 1
+ATOM 481 C CD . ARG A 1 60 ? 18.917 -15.852 35.008 1.00 33.62 ? 60 ARG A CD 1
+ATOM 482 N NE . ARG A 1 60 ? 20.227 -15.335 35.399 1.00 37.98 ? 60 ARG A NE 1
+ATOM 483 C CZ . ARG A 1 60 ? 21.142 -16.030 36.067 1.00 40.16 ? 60 ARG A CZ 1
+ATOM 484 N NH1 . ARG A 1 60 ? 22.307 -15.479 36.372 1.00 39.79 ? 60 ARG A NH1 1
+ATOM 485 N NH2 . ARG A 1 60 ? 20.898 -17.284 36.432 1.00 40.17 ? 60 ARG A NH2 1
+ATOM 486 N N . LYS A 1 61 ? 17.089 -17.491 30.014 1.00 19.36 ? 61 LYS A N 1
+ATOM 487 C CA . LYS A 1 61 ? 16.134 -18.067 29.078 1.00 18.81 ? 61 LYS A CA 1
+ATOM 488 C C . LYS A 1 61 ? 16.645 -19.373 28.501 1.00 19.17 ? 61 LYS A C 1
+ATOM 489 O O . LYS A 1 61 ? 17.832 -19.513 28.216 1.00 20.35 ? 61 LYS A O 1
+ATOM 490 C CB . LYS A 1 61 ? 15.853 -17.072 27.936 1.00 19.82 ? 61 LYS A CB 1
+ATOM 491 C CG . LYS A 1 61 ? 15.324 -15.717 28.401 1.00 22.51 ? 61 LYS A CG 1
+ATOM 492 C CD . LYS A 1 61 ? 14.023 -15.821 29.196 1.00 26.00 ? 61 LYS A CD 1
+ATOM 493 C CE . LYS A 1 61 ? 13.493 -14.456 29.568 1.00 29.36 ? 61 LYS A CE 1
+ATOM 494 N NZ . LYS A 1 61 ? 12.260 -14.538 30.405 1.00 32.04 ? 61 LYS A NZ 1
+ATOM 495 N N . SER A 1 62 ? 15.745 -20.338 28.359 1.00 17.84 ? 62 SER A N 1
+ATOM 496 C CA . SER A 1 62 ? 16.030 -21.625 27.751 1.00 17.70 ? 62 SER A CA 1
+ATOM 497 C C . SER A 1 62 ? 15.168 -21.747 26.476 1.00 16.11 ? 62 SER A C 1
+ATOM 498 O O . SER A 1 62 ? 14.219 -20.985 26.286 1.00 15.44 ? 62 SER A O 1
+ATOM 499 C CB . SER A 1 62 ? 15.673 -22.756 28.709 1.00 20.52 ? 62 SER A CB 1
+ATOM 500 O OG . SER A 1 62 ? 16.454 -22.685 29.891 1.00 23.82 ? 62 SER A OG 1
+ATOM 501 N N . ASN A 1 63 ? 15.466 -22.730 25.611 1.00 15.74 ? 63 ASN A N 1
+ATOM 502 C CA . ASN A 1 63 ? 14.663 -22.963 24.399 1.00 15.24 ? 63 ASN A CA 1
+ATOM 503 C C . ASN A 1 63 ? 13.166 -23.023 24.663 1.00 15.14 ? 63 ASN A C 1
+ATOM 504 O O . ASN A 1 63 ? 12.399 -22.427 23.914 1.00 15.00 ? 63 ASN A O 1
+ATOM 505 C CB . ASN A 1 63 ? 15.077 -24.261 23.732 1.00 15.61 ? 63 ASN A CB 1
+ATOM 506 C CG . ASN A 1 63 ? 16.449 -24.203 23.162 1.00 17.36 ? 63 ASN A CG 1
+ATOM 507 O OD1 . ASN A 1 63 ? 16.926 -23.144 22.757 1.00 17.17 ? 63 ASN A OD1 1
+ATOM 508 N ND2 . ASN A 1 63 ? 17.110 -25.341 23.087 1.00 17.34 ? 63 ASN A ND2 1
+ATOM 509 N N . HIS A 1 64 ? 12.750 -23.729 25.736 1.00 15.18 ? 64 HIS A N 1
+ATOM 510 C CA . HIS A 1 64 ? 11.332 -23.876 26.064 1.00 15.34 ? 64 HIS A CA 1
+ATOM 511 C C . HIS A 1 64 ? 10.643 -22.586 26.518 1.00 15.59 ? 64 HIS A C 1
+ATOM 512 O O . HIS A 1 64 ? 9.414 -22.564 26.635 1.00 16.33 ? 64 HIS A O 1
+ATOM 513 C CB . HIS A 1 64 ? 11.090 -25.001 27.087 1.00 16.13 ? 64 HIS A CB 1
+ATOM 514 C CG . HIS A 1 64 ? 11.550 -24.698 28.481 1.00 17.26 ? 64 HIS A CG 1
+ATOM 515 N ND1 . HIS A 1 64 ? 12.805 -25.063 28.912 1.00 18.51 ? 64 HIS A ND1 1
+ATOM 516 C CD2 . HIS A 1 64 ? 10.890 -24.109 29.506 1.00 18.35 ? 64 HIS A CD2 1
+ATOM 517 C CE1 . HIS A 1 64 ? 12.887 -24.663 30.171 1.00 18.91 ? 64 HIS A CE1 1
+ATOM 518 N NE2 . HIS A 1 64 ? 11.768 -24.069 30.566 1.00 19.00 ? 64 HIS A NE2 1
+ATOM 519 N N . ASN A 1 65 ? 11.413 -21.525 26.808 1.00 14.89 ? 65 ASN A N 1
+ATOM 520 C CA . ASN A 1 65 ? 10.825 -20.244 27.197 1.00 15.45 ? 65 ASN A CA 1
+ATOM 521 C C . ASN A 1 65 ? 10.364 -19.437 25.979 1.00 15.62 ? 65 ASN A C 1
+ATOM 522 O O . ASN A 1 65 ? 9.615 -18.487 26.144 1.00 16.44 ? 65 ASN A O 1
+ATOM 523 C CB . ASN A 1 65 ? 11.814 -19.399 27.993 1.00 16.32 ? 65 ASN A CB 1
+ATOM 524 C CG . ASN A 1 65 ? 12.130 -19.936 29.354 1.00 20.06 ? 65 ASN A CG 1
+ATOM 525 O OD1 . ASN A 1 65 ? 13.288 -19.972 29.757 1.00 21.53 ? 65 ASN A OD1 1
+ATOM 526 N ND2 . ASN A 1 65 ? 11.113 -20.354 30.094 1.00 20.32 ? 65 ASN A ND2 1
+ATOM 527 N N . PHE A 1 66 ? 10.834 -19.782 24.766 1.00 14.81 ? 66 PHE A N 1
+ATOM 528 C CA . PHE A 1 66 ? 10.445 -19.072 23.556 1.00 14.55 ? 66 PHE A CA 1
+ATOM 529 C C . PHE A 1 66 ? 9.285 -19.790 22.901 1.00 15.70 ? 66 PHE A C 1
+ATOM 530 O O . PHE A 1 66 ? 9.473 -20.833 22.284 1.00 17.06 ? 66 PHE A O 1
+ATOM 531 C CB . PHE A 1 66 ? 11.624 -18.973 22.581 1.00 13.81 ? 66 PHE A CB 1
+ATOM 532 C CG . PHE A 1 66 ? 12.755 -18.158 23.140 1.00 14.30 ? 66 PHE A CG 1
+ATOM 533 C CD1 . PHE A 1 66 ? 12.739 -16.779 23.058 1.00 15.07 ? 66 PHE A CD1 1
+ATOM 534 C CD2 . PHE A 1 66 ? 13.840 -18.771 23.734 1.00 14.97 ? 66 PHE A CD2 1
+ATOM 535 C CE1 . PHE A 1 66 ? 13.791 -16.027 23.574 1.00 15.66 ? 66 PHE A CE1 1
+ATOM 536 C CE2 . PHE A 1 66 ? 14.884 -18.017 24.257 1.00 15.64 ? 66 PHE A CE2 1
+ATOM 537 C CZ . PHE A 1 66 ? 14.840 -16.648 24.190 1.00 15.18 ? 66 PHE A CZ 1
+ATOM 538 N N . LEU A 1 67 ? 8.095 -19.249 23.059 1.00 14.73 ? 67 LEU A N 1
+ATOM 539 C CA . LEU A 1 67 ? 6.890 -19.851 22.496 1.00 15.02 ? 67 LEU A CA 1
+ATOM 540 C C . LEU A 1 67 ? 6.660 -19.315 21.087 1.00 14.82 ? 67 LEU A C 1
+ATOM 541 O O . LEU A 1 67 ? 6.407 -18.125 20.903 1.00 14.57 ? 67 LEU A O 1
+ATOM 542 C CB . LEU A 1 67 ? 5.687 -19.563 23.389 1.00 16.22 ? 67 LEU A CB 1
+ATOM 543 C CG . LEU A 1 67 ? 5.825 -20.012 24.845 1.00 19.15 ? 67 LEU A CG 1
+ATOM 544 C CD1 . LEU A 1 67 ? 4.603 -19.600 25.664 1.00 20.19 ? 67 LEU A CD1 1
+ATOM 545 C CD2 . LEU A 1 67 ? 6.082 -21.512 24.947 1.00 20.70 ? 67 LEU A CD2 1
+ATOM 546 N N . VAL A 1 68 ? 6.797 -20.185 20.094 1.00 13.69 ? 68 VAL A N 1
+ATOM 547 C CA . VAL A 1 68 ? 6.672 -19.779 18.702 1.00 13.84 ? 68 VAL A CA 1
+ATOM 548 C C . VAL A 1 68 ? 5.478 -20.455 18.106 1.00 14.57 ? 68 VAL A C 1
+ATOM 549 O O . VAL A 1 68 ? 5.380 -21.671 18.188 1.00 14.93 ? 68 VAL A O 1
+ATOM 550 C CB . VAL A 1 68 ? 7.958 -20.136 17.936 1.00 14.82 ? 68 VAL A CB 1
+ATOM 551 C CG1 . VAL A 1 68 ? 7.847 -19.711 16.467 1.00 14.89 ? 68 VAL A CG1 1
+ATOM 552 C CG2 . VAL A 1 68 ? 9.173 -19.485 18.597 1.00 15.58 ? 68 VAL A CG2 1
+ATOM 553 N N . GLN A 1 69 ? 4.540 -19.672 17.571 1.00 14.79 ? 69 GLN A N 1
+ATOM 554 C CA . GLN A 1 69 ? 3.320 -20.238 17.038 1.00 16.19 ? 69 GLN A CA 1
+ATOM 555 C C . GLN A 1 69 ? 3.083 -19.685 15.636 1.00 17.21 ? 69 GLN A C 1
+ATOM 556 O O . GLN A 1 69 ? 3.122 -18.475 15.425 1.00 16.72 ? 69 GLN A O 1
+ATOM 557 C CB . GLN A 1 69 ? 2.170 -19.888 17.999 1.00 18.04 ? 69 GLN A CB 1
+ATOM 558 C CG . GLN A 1 69 ? 0.888 -20.656 17.771 1.00 21.51 ? 69 GLN A CG 1
+ATOM 559 C CD . GLN A 1 69 ? -0.161 -20.174 18.731 1.00 25.03 ? 69 GLN A CD 1
+ATOM 560 O OE1 . GLN A 1 69 ? 0.106 -19.927 19.909 1.00 25.84 ? 69 GLN A OE1 1
+ATOM 561 N NE2 . GLN A 1 69 ? -1.385 -20.021 18.241 1.00 26.21 ? 69 GLN A NE2 1
+ATOM 562 N N . ALA A 1 70 ? 2.875 -20.594 14.677 1.00 19.00 ? 70 ALA A N 1
+ATOM 563 C CA . ALA A 1 70 ? 2.620 -20.293 13.267 1.00 20.96 ? 70 ALA A CA 1
+ATOM 564 C C . ALA A 1 70 ? 1.139 -20.600 13.043 1.00 23.17 ? 70 ALA A C 1
+ATOM 565 O O . ALA A 1 70 ? 0.751 -21.762 13.002 1.00 23.52 ? 70 ALA A O 1
+ATOM 566 C CB . ALA A 1 70 ? 3.471 -21.204 12.398 1.00 20.97 ? 70 ALA A CB 1
+ATOM 567 N N . GLY A 1 71 ? 0.297 -19.573 13.046 1.00 24.68 ? 71 GLY A N 1
+ATOM 568 C CA . GLY A 1 71 ? -1.148 -19.764 12.969 1.00 25.82 ? 71 GLY A CA 1
+ATOM 569 C C . GLY A 1 71 ? -1.586 -20.403 14.272 1.00 26.30 ? 71 GLY A C 1
+ATOM 570 O O . GLY A 1 71 ? -1.283 -19.875 15.340 1.00 27.29 ? 71 GLY A O 1
+ATOM 571 N N A ASN A 1 72 ? -2.203 -21.577 14.195 0.50 25.88 ? 72 ASN A N 1
+ATOM 572 N N B ASN A 1 72 ? -2.232 -21.574 14.208 0.50 26.13 ? 72 ASN A N 1
+ATOM 573 C CA A ASN A 1 72 ? -2.607 -22.309 15.390 0.50 25.81 ? 72 ASN A CA 1
+ATOM 574 C CA B ASN A 1 72 ? -2.637 -22.282 15.426 0.50 26.29 ? 72 ASN A CA 1
+ATOM 575 C C A ASN A 1 72 ? -1.585 -23.402 15.775 0.50 25.30 ? 72 ASN A C 1
+ATOM 576 C C B ASN A 1 72 ? -1.713 -23.458 15.794 0.50 25.45 ? 72 ASN A C 1
+ATOM 577 O O A ASN A 1 72 ? -1.765 -24.044 16.810 0.50 25.73 ? 72 ASN A O 1
+ATOM 578 O O B ASN A 1 72 ? -2.036 -24.222 16.705 0.50 25.81 ? 72 ASN A O 1
+ATOM 579 C CB A ASN A 1 72 ? -3.990 -22.935 15.174 0.50 27.13 ? 72 ASN A CB 1
+ATOM 580 C CB B ASN A 1 72 ? -4.102 -22.729 15.351 0.50 28.37 ? 72 ASN A CB 1
+ATOM 581 C CG A ASN A 1 72 ? -4.706 -23.325 16.447 0.50 29.97 ? 72 ASN A CG 1
+ATOM 582 C CG B ASN A 1 72 ? -4.444 -23.658 14.208 0.50 32.49 ? 72 ASN A CG 1
+ATOM 583 O OD1 A ASN A 1 72 ? -4.849 -22.526 17.378 0.50 30.90 ? 72 ASN A OD1 1
+ATOM 584 O OD1 B ASN A 1 72 ? -3.749 -24.647 13.927 0.50 34.05 ? 72 ASN A OD1 1
+ATOM 585 N ND2 A ASN A 1 72 ? -5.171 -24.566 16.514 0.50 30.55 ? 72 ASN A ND2 1
+ATOM 586 N ND2 B ASN A 1 72 ? -5.547 -23.372 13.532 0.50 33.10 ? 72 ASN A ND2 1
+ATOM 587 N N A VAL A 1 73 ? -0.530 -23.633 14.956 0.75 24.08 ? 73 VAL A N 1
+ATOM 588 N N B VAL A 1 73 ? -0.584 -23.618 15.080 0.25 23.95 ? 73 VAL A N 1
+ATOM 589 C CA A VAL A 1 73 ? 0.414 -24.705 15.245 0.75 23.44 ? 73 VAL A CA 1
+ATOM 590 C CA B VAL A 1 73 ? 0.344 -24.718 15.304 0.25 22.97 ? 73 VAL A CA 1
+ATOM 591 C C A VAL A 1 73 ? 1.668 -24.214 15.976 0.75 21.47 ? 73 VAL A C 1
+ATOM 592 C C B VAL A 1 73 ? 1.640 -24.244 15.966 0.25 21.72 ? 73 VAL A C 1
+ATOM 593 O O A VAL A 1 73 ? 2.283 -23.222 15.597 0.75 20.54 ? 73 VAL A O 1
+ATOM 594 O O B VAL A 1 73 ? 2.279 -23.304 15.502 0.25 21.51 ? 73 VAL A O 1
+ATOM 595 C CB A VAL A 1 73 ? 0.763 -25.565 14.001 0.75 24.81 ? 73 VAL A CB 1
+ATOM 596 C CB B VAL A 1 73 ? 0.577 -25.518 13.997 0.25 23.51 ? 73 VAL A CB 1
+ATOM 597 C CG1 A VAL A 1 73 ? 1.636 -24.807 13.009 0.75 25.84 ? 73 VAL A CG1 1
+ATOM 598 C CG1 B VAL A 1 73 ? 1.798 -26.431 14.097 0.25 24.00 ? 73 VAL A CG1 1
+ATOM 599 C CG2 A VAL A 1 73 ? 1.436 -26.868 14.414 0.75 25.38 ? 73 VAL A CG2 1
+ATOM 600 C CG2 B VAL A 1 73 ? -0.667 -26.320 13.638 0.25 23.85 ? 73 VAL A CG2 1
+ATOM 601 N N . GLN A 1 74 ? 2.014 -24.909 17.059 1.00 20.75 ? 74 GLN A N 1
+ATOM 602 C CA . GLN A 1 74 ? 3.186 -24.589 17.836 1.00 19.17 ? 74 GLN A CA 1
+ATOM 603 C C . GLN A 1 74 ? 4.454 -25.134 17.203 1.00 18.22 ? 74 GLN A C 1
+ATOM 604 O O . GLN A 1 74 ? 4.478 -26.264 16.693 1.00 18.47 ? 74 GLN A O 1
+ATOM 605 C CB . GLN A 1 74 ? 3.034 -25.162 19.243 1.00 19.18 ? 74 GLN A CB 1
+ATOM 606 C CG . GLN A 1 74 ? 3.779 -24.366 20.307 1.00 19.39 ? 74 GLN A CG 1
+ATOM 607 C CD . GLN A 1 74 ? 3.183 -23.013 20.563 1.00 21.32 ? 74 GLN A CD 1
+ATOM 608 O OE1 . GLN A 1 74 ? 2.013 -22.747 20.265 1.00 21.97 ? 74 GLN A OE1 1
+ATOM 609 N NE2 . GLN A 1 74 ? 3.972 -22.133 21.159 1.00 21.51 ? 74 GLN A NE2 1
+ATOM 610 N N . LEU A 1 75 ? 5.519 -24.334 17.242 1.00 17.05 ? 75 LEU A N 1
+ATOM 611 C CA . LEU A 1 75 ? 6.809 -24.770 16.729 1.00 17.04 ? 75 LEU A CA 1
+ATOM 612 C C . LEU A 1 75 ? 7.735 -25.145 17.865 1.00 16.56 ? 75 LEU A C 1
+ATOM 613 O O . LEU A 1 75 ? 7.725 -24.505 18.912 1.00 17.40 ? 75 LEU A O 1
+ATOM 614 C CB . LEU A 1 75 ? 7.454 -23.702 15.837 1.00 17.69 ? 75 LEU A CB 1
+ATOM 615 C CG . LEU A 1 75 ? 6.621 -23.233 14.636 1.00 19.89 ? 75 LEU A CG 1
+ATOM 616 C CD1 . LEU A 1 75 ? 7.402 -22.256 13.792 1.00 20.45 ? 75 LEU A CD1 1
+ATOM 617 C CD2 . LEU A 1 75 ? 6.150 -24.405 13.778 1.00 21.66 ? 75 LEU A CD2 1
+ATOM 618 N N . ARG A 1 76 ? 8.516 -26.197 17.669 1.00 14.98 ? 76 ARG A N 1
+ATOM 619 C CA . ARG A 1 76 ? 9.440 -26.670 18.686 1.00 14.65 ? 76 ARG A CA 1
+ATOM 620 C C . ARG A 1 76 ? 10.784 -25.974 18.535 1.00 15.18 ? 76 ARG A C 1
+ATOM 621 O O . ARG A 1 76 ? 11.405 -26.099 17.487 1.00 16.02 ? 76 ARG A O 1
+ATOM 622 C CB . ARG A 1 76 ? 9.611 -28.184 18.570 1.00 15.16 ? 76 ARG A CB 1
+ATOM 623 C CG . ARG A 1 76 ? 10.429 -28.788 19.702 1.00 15.73 ? 76 ARG A CG 1
+ATOM 624 C CD . ARG A 1 76 ? 10.493 -30.311 19.588 1.00 16.39 ? 76 ARG A CD 1
+ATOM 625 N NE . ARG A 1 76 ? 9.152 -30.898 19.628 1.00 17.45 ? 76 ARG A NE 1
+ATOM 626 C CZ . ARG A 1 76 ? 8.486 -31.179 20.744 1.00 18.47 ? 76 ARG A CZ 1
+ATOM 627 N NH1 . ARG A 1 76 ? 9.049 -30.980 21.932 1.00 17.24 ? 76 ARG A NH1 1
+ATOM 628 N NH2 . ARG A 1 76 ? 7.256 -31.675 20.681 1.00 18.11 ? 76 ARG A NH2 1
+ATOM 629 N N . VAL A 1 77 ? 11.234 -25.254 19.574 1.00 14.60 ? 77 VAL A N 1
+ATOM 630 C CA . VAL A 1 77 ? 12.504 -24.530 19.581 1.00 14.79 ? 77 VAL A CA 1
+ATOM 631 C C . VAL A 1 77 ? 13.634 -25.433 20.060 1.00 15.27 ? 77 VAL A C 1
+ATOM 632 O O . VAL A 1 77 ? 13.610 -25.910 21.200 1.00 15.58 ? 77 VAL A O 1
+ATOM 633 C CB . VAL A 1 77 ? 12.396 -23.241 20.417 1.00 14.63 ? 77 VAL A CB 1
+ATOM 634 C CG1 . VAL A 1 77 ? 13.738 -22.496 20.457 1.00 15.23 ? 77 VAL A CG1 1
+ATOM 635 C CG2 . VAL A 1 77 ? 11.286 -22.353 19.859 1.00 15.19 ? 77 VAL A CG2 1
+ATOM 636 N N . ILE A 1 78 ? 14.606 -25.704 19.183 1.00 14.95 ? 78 ILE A N 1
+ATOM 637 C CA . ILE A 1 78 ? 15.726 -26.579 19.519 1.00 15.44 ? 78 ILE A CA 1
+ATOM 638 C C . ILE A 1 78 ? 17.072 -25.865 19.681 1.00 15.44 ? 78 ILE A C 1
+ATOM 639 O O . ILE A 1 78 ? 18.089 -26.513 19.933 1.00 16.12 ? 78 ILE A O 1
+ATOM 640 C CB . ILE A 1 78 ? 15.821 -27.724 18.493 1.00 16.42 ? 78 ILE A CB 1
+ATOM 641 C CG1 . ILE A 1 78 ? 16.122 -27.179 17.085 1.00 17.67 ? 78 ILE A CG1 1
+ATOM 642 C CG2 . ILE A 1 78 ? 14.532 -28.525 18.490 1.00 16.90 ? 78 ILE A CG2 1
+ATOM 643 C CD1 . ILE A 1 78 ? 16.430 -28.295 16.044 1.00 18.94 ? 78 ILE A CD1 1
+ATOM 644 N N . GLY A 1 79 ? 17.071 -24.547 19.607 1.00 15.03 ? 79 GLY A N 1
+ATOM 645 C CA . GLY A 1 79 ? 18.273 -23.758 19.811 1.00 15.04 ? 79 GLY A CA 1
+ATOM 646 C C . GLY A 1 79 ? 17.946 -22.286 19.759 1.00 15.10 ? 79 GLY A C 1
+ATOM 647 O O . GLY A 1 79 ? 16.938 -21.896 19.168 1.00 14.94 ? 79 GLY A O 1
+ATOM 648 N N . HIS A 1 80 ? 18.773 -21.465 20.388 1.00 14.85 ? 80 HIS A N 1
+ATOM 649 C CA . HIS A 1 80 ? 18.582 -20.020 20.321 1.00 14.66 ? 80 HIS A CA 1
+ATOM 650 C C . HIS A 1 80 ? 19.904 -19.333 20.423 1.00 15.30 ? 80 HIS A C 1
+ATOM 651 O O . HIS A 1 80 ? 20.814 -19.802 21.123 1.00 15.86 ? 80 HIS A O 1
+ATOM 652 C CB . HIS A 1 80 ? 17.588 -19.490 21.366 1.00 14.91 ? 80 HIS A CB 1
+ATOM 653 C CG . HIS A 1 80 ? 18.070 -19.617 22.771 1.00 16.66 ? 80 HIS A CG 1
+ATOM 654 N ND1 . HIS A 1 80 ? 17.910 -20.787 23.482 1.00 17.48 ? 80 HIS A ND1 1
+ATOM 655 C CD2 . HIS A 1 80 ? 18.705 -18.716 23.556 1.00 17.84 ? 80 HIS A CD2 1
+ATOM 656 C CE1 . HIS A 1 80 ? 18.440 -20.563 24.674 1.00 18.30 ? 80 HIS A CE1 1
+ATOM 657 N NE2 . HIS A 1 80 ? 18.929 -19.326 24.760 1.00 18.47 ? 80 HIS A NE2 1
+ATOM 658 N N . SER A 1 81 ? 20.031 -18.237 19.705 1.00 14.84 ? 81 SER A N 1
+ATOM 659 C CA . SER A 1 81 ? 21.265 -17.465 19.755 1.00 14.86 ? 81 SER A CA 1
+ATOM 660 C C . SER A 1 81 ? 20.972 -16.018 19.462 1.00 14.66 ? 81 SER A C 1
+ATOM 661 O O . SER A 1 81 ? 19.970 -15.697 18.822 1.00 15.19 ? 81 SER A O 1
+ATOM 662 C CB . SER A 1 81 ? 22.291 -18.011 18.768 1.00 16.73 ? 81 SER A CB 1
+ATOM 663 O OG . SER A 1 81 ? 21.809 -17.919 17.441 1.00 20.31 ? 81 SER A OG 1
+ATOM 664 N N A MET A 1 82 ? 21.828 -15.125 19.951 0.50 14.30 ? 82 MET A N 1
+ATOM 665 N N B MET A 1 82 ? 21.839 -15.141 19.938 0.50 14.04 ? 82 MET A N 1
+ATOM 666 C CA A MET A 1 82 ? 21.664 -13.700 19.723 0.50 14.74 ? 82 MET A CA 1
+ATOM 667 C CA B MET A 1 82 ? 21.699 -13.721 19.712 0.50 14.21 ? 82 MET A CA 1
+ATOM 668 C C A MET A 1 82 ? 22.712 -13.224 18.723 0.50 15.23 ? 82 MET A C 1
+ATOM 669 C C B MET A 1 82 ? 22.718 -13.294 18.664 0.50 14.88 ? 82 MET A C 1
+ATOM 670 O O A MET A 1 82 ? 23.905 -13.470 18.919 0.50 16.17 ? 82 MET A O 1
+ATOM 671 O O B MET A 1 82 ? 23.890 -13.665 18.753 0.50 15.61 ? 82 MET A O 1
+ATOM 672 C CB A MET A 1 82 ? 21.801 -12.929 21.041 0.50 15.23 ? 82 MET A CB 1
+ATOM 673 C CB B MET A 1 82 ? 21.937 -12.966 21.026 0.50 14.18 ? 82 MET A CB 1
+ATOM 674 C CG A MET A 1 82 ? 21.614 -11.442 20.874 0.50 17.47 ? 82 MET A CG 1
+ATOM 675 C CG B MET A 1 82 ? 21.759 -11.474 20.898 0.50 15.64 ? 82 MET A CG 1
+ATOM 676 S SD A MET A 1 82 ? 21.828 -10.548 22.424 0.50 20.86 ? 82 MET A SD 1
+ATOM 677 S SD B MET A 1 82 ? 21.374 -10.707 22.484 0.50 15.97 ? 82 MET A SD 1
+ATOM 678 C CE A MET A 1 82 ? 20.402 -11.108 23.302 0.50 20.46 ? 82 MET A CE 1
+ATOM 679 C CE B MET A 1 82 ? 22.877 -11.090 23.413 0.50 12.42 ? 82 MET A CE 1
+ATOM 680 N N . GLN A 1 83 ? 22.270 -12.561 17.647 1.00 15.01 ? 83 GLN A N 1
+ATOM 681 C CA . GLN A 1 83 ? 23.164 -12.017 16.627 1.00 15.04 ? 83 GLN A CA 1
+ATOM 682 C C . GLN A 1 83 ? 22.849 -10.536 16.608 1.00 13.84 ? 83 GLN A C 1
+ATOM 683 O O . GLN A 1 83 ? 21.761 -10.157 16.187 1.00 14.15 ? 83 GLN A O 1
+ATOM 684 C CB . GLN A 1 83 ? 22.915 -12.619 15.247 1.00 17.78 ? 83 GLN A CB 1
+ATOM 685 C CG . GLN A 1 83 ? 23.871 -12.027 14.206 1.00 22.38 ? 83 GLN A CG 1
+ATOM 686 C CD . GLN A 1 83 ? 23.630 -12.527 12.802 1.00 27.19 ? 83 GLN A CD 1
+ATOM 687 O OE1 . GLN A 1 83 ? 22.667 -13.246 12.515 1.00 27.58 ? 83 GLN A OE1 1
+ATOM 688 N NE2 . GLN A 1 83 ? 24.504 -12.142 11.883 1.00 28.65 ? 83 GLN A NE2 1
+ATOM 689 N N . ASN A 1 84 ? 23.741 -9.705 17.152 1.00 13.13 ? 84 ASN A N 1
+ATOM 690 C CA . ASN A 1 84 ? 23.516 -8.266 17.264 1.00 12.86 ? 84 ASN A CA 1
+ATOM 691 C C . ASN A 1 84 ? 22.187 -8.003 18.043 1.00 12.30 ? 84 ASN A C 1
+ATOM 692 O O . ASN A 1 84 ? 22.073 -8.505 19.170 1.00 13.18 ? 84 ASN A O 1
+ATOM 693 C CB . ASN A 1 84 ? 23.643 -7.595 15.893 1.00 13.60 ? 84 ASN A CB 1
+ATOM 694 C CG . ASN A 1 84 ? 24.979 -7.902 15.287 1.00 16.97 ? 84 ASN A CG 1
+ATOM 695 O OD1 . ASN A 1 84 ? 26.030 -7.659 15.897 1.00 18.65 ? 84 ASN A OD1 1
+ATOM 696 N ND2 . ASN A 1 84 ? 24.965 -8.478 14.103 1.00 17.35 ? 84 ASN A ND2 1
+ATOM 697 N N . CYS A 1 85 ? 21.183 -7.327 17.448 1.00 11.65 ? 85 CYS A N 1
+ATOM 698 C CA . CYS A 1 85 ? 19.935 -7.077 18.150 1.00 11.74 ? 85 CYS A CA 1
+ATOM 699 C C . CYS A 1 85 ? 18.805 -8.021 17.785 1.00 11.93 ? 85 CYS A C 1
+ATOM 700 O O . CYS A 1 85 ? 17.658 -7.743 18.135 1.00 12.25 ? 85 CYS A O 1
+ATOM 701 C CB . CYS A 1 85 ? 19.518 -5.626 17.998 1.00 12.25 ? 85 CYS A CB 1
+ATOM 702 S SG . CYS A 1 85 ? 20.771 -4.475 18.599 1.00 14.49 ? 85 CYS A SG 1
+ATOM 703 N N . VAL A 1 86 ? 19.106 -9.142 17.124 1.00 11.92 ? 86 VAL A N 1
+ATOM 704 C CA A VAL A 1 86 ? 18.063 -10.123 16.816 0.80 12.69 ? 86 VAL A CA 1
+ATOM 705 C CA B VAL A 1 86 ? 18.084 -10.108 16.770 0.20 12.62 ? 86 VAL A CA 1
+ATOM 706 C C . VAL A 1 86 ? 18.368 -11.466 17.447 1.00 13.31 ? 86 VAL A C 1
+ATOM 707 O O . VAL A 1 86 ? 19.522 -11.792 17.744 1.00 13.89 ? 86 VAL A O 1
+ATOM 708 C CB A VAL A 1 86 ? 17.715 -10.290 15.315 0.80 13.96 ? 86 VAL A CB 1
+ATOM 709 C CB B VAL A 1 86 ? 17.964 -10.163 15.216 0.20 13.40 ? 86 VAL A CB 1
+ATOM 710 C CG1 A VAL A 1 86 ? 17.232 -8.980 14.704 0.80 14.98 ? 86 VAL A CG1 1
+ATOM 711 C CG1 B VAL A 1 86 ? 17.427 -11.492 14.704 0.20 13.91 ? 86 VAL A CG1 1
+ATOM 712 C CG2 A VAL A 1 86 ? 18.874 -10.884 14.538 0.80 14.71 ? 86 VAL A CG2 1
+ATOM 713 C CG2 B VAL A 1 86 ? 17.115 -9.007 14.699 0.20 14.01 ? 86 VAL A CG2 1
+ATOM 714 N N . LEU A 1 87 ? 17.311 -12.214 17.743 1.00 12.95 ? 87 LEU A N 1
+ATOM 715 C CA . LEU A 1 87 ? 17.437 -13.555 18.248 1.00 13.45 ? 87 LEU A CA 1
+ATOM 716 C C . LEU A 1 87 ? 17.087 -14.460 17.060 1.00 12.81 ? 87 LEU A C 1
+ATOM 717 O O . LEU A 1 87 ? 16.214 -14.148 16.232 1.00 12.84 ? 87 LEU A O 1
+ATOM 718 C CB . LEU A 1 87 ? 16.456 -13.848 19.385 1.00 14.73 ? 87 LEU A CB 1
+ATOM 719 C CG . LEU A 1 87 ? 16.676 -13.104 20.677 1.00 17.21 ? 87 LEU A CG 1
+ATOM 720 C CD1 . LEU A 1 87 ? 15.555 -13.409 21.659 1.00 17.72 ? 87 LEU A CD1 1
+ATOM 721 C CD2 . LEU A 1 87 ? 18.026 -13.431 21.279 1.00 19.12 ? 87 LEU A CD2 1
+ATOM 722 N N . LYS A 1 88 ? 17.808 -15.569 16.962 1.00 12.70 ? 88 LYS A N 1
+ATOM 723 C CA . LYS A 1 88 ? 17.600 -16.588 15.957 1.00 12.67 ? 88 LYS A CA 1
+ATOM 724 C C . LYS A 1 88 ? 17.188 -17.806 16.736 1.00 12.90 ? 88 LYS A C 1
+ATOM 725 O O . LYS A 1 88 ? 17.975 -18.321 17.525 1.00 13.84 ? 88 LYS A O 1
+ATOM 726 C CB . LYS A 1 88 ? 18.899 -16.875 15.190 1.00 13.93 ? 88 LYS A CB 1
+ATOM 727 C CG . LYS A 1 88 ? 19.258 -15.755 14.219 1.00 17.96 ? 88 LYS A CG 1
+ATOM 728 C CD . LYS A 1 88 ? 20.490 -16.070 13.376 1.00 22.34 ? 88 LYS A CD 1
+ATOM 729 C CE . LYS A 1 88 ? 21.738 -16.137 14.208 1.00 26.94 ? 88 LYS A CE 1
+ATOM 730 N NZ . LYS A 1 88 ? 22.952 -15.999 13.363 1.00 28.94 ? 88 LYS A NZ 1
+ATOM 731 N N . LEU A 1 89 ? 15.950 -18.220 16.574 1.00 12.44 ? 89 LEU A N 1
+ATOM 732 C CA . LEU A 1 89 ? 15.403 -19.373 17.256 1.00 12.59 ? 89 LEU A CA 1
+ATOM 733 C C . LEU A 1 89 ? 15.367 -20.511 16.264 1.00 12.94 ? 89 LEU A C 1
+ATOM 734 O O . LEU A 1 89 ? 14.620 -20.459 15.287 1.00 13.54 ? 89 LEU A O 1
+ATOM 735 C CB . LEU A 1 89 ? 13.982 -19.063 17.753 1.00 12.75 ? 89 LEU A CB 1
+ATOM 736 C CG . LEU A 1 89 ? 13.831 -17.772 18.569 1.00 13.26 ? 89 LEU A CG 1
+ATOM 737 C CD1 . LEU A 1 89 ? 12.360 -17.539 18.932 1.00 14.00 ? 89 LEU A CD1 1
+ATOM 738 C CD2 . LEU A 1 89 ? 14.701 -17.814 19.810 1.00 14.04 ? 89 LEU A CD2 1
+ATOM 739 N N . LYS A 1 90 ? 16.203 -21.522 16.472 1.00 12.58 ? 90 LYS A N 1
+ATOM 740 C CA . LYS A 1 90 ? 16.232 -22.674 15.595 1.00 13.10 ? 90 LYS A CA 1
+ATOM 741 C C . LYS A 1 90 ? 15.051 -23.539 15.962 1.00 13.08 ? 90 LYS A C 1
+ATOM 742 O O . LYS A 1 90 ? 14.830 -23.805 17.137 1.00 13.52 ? 90 LYS A O 1
+ATOM 743 C CB . LYS A 1 90 ? 17.536 -23.458 15.769 1.00 15.25 ? 90 LYS A CB 1
+ATOM 744 C CG . LYS A 1 90 ? 17.687 -24.519 14.697 1.00 19.98 ? 90 LYS A CG 1
+ATOM 745 C CD . LYS A 1 90 ? 18.937 -25.357 14.862 1.00 26.70 ? 90 LYS A CD 1
+ATOM 746 C CE . LYS A 1 90 ? 18.950 -26.460 13.827 1.00 31.95 ? 90 LYS A CE 1
+ATOM 747 N NZ . LYS A 1 90 ? 20.250 -27.184 13.784 1.00 34.61 ? 90 LYS A NZ 1
+ATOM 748 N N . VAL A 1 91 ? 14.239 -23.892 14.982 1.00 13.01 ? 91 VAL A N 1
+ATOM 749 C CA . VAL A 1 91 ? 13.080 -24.738 15.204 1.00 13.59 ? 91 VAL A CA 1
+ATOM 750 C C . VAL A 1 91 ? 13.290 -26.080 14.510 1.00 13.94 ? 91 VAL A C 1
+ATOM 751 O O . VAL A 1 91 ? 14.153 -26.193 13.635 1.00 14.24 ? 91 VAL A O 1
+ATOM 752 C CB . VAL A 1 91 ? 11.760 -24.046 14.810 1.00 13.54 ? 91 VAL A CB 1
+ATOM 753 C CG1 . VAL A 1 91 ? 11.470 -22.870 15.748 1.00 13.86 ? 91 VAL A CG1 1
+ATOM 754 C CG2 . VAL A 1 91 ? 11.792 -23.576 13.358 1.00 13.61 ? 91 VAL A CG2 1
+ATOM 755 N N . ASP A 1 92 ? 12.510 -27.098 14.887 1.00 14.52 ? 92 ASP A N 1
+ATOM 756 C CA . ASP A 1 92 ? 12.713 -28.432 14.308 1.00 15.39 ? 92 ASP A CA 1
+ATOM 757 C C . ASP A 1 92 ? 12.040 -28.640 12.940 1.00 16.15 ? 92 ASP A C 1
+ATOM 758 O O . ASP A 1 92 ? 12.151 -29.724 12.366 1.00 17.58 ? 92 ASP A O 1
+ATOM 759 C CB . ASP A 1 92 ? 12.298 -29.535 15.300 1.00 16.92 ? 92 ASP A CB 1
+ATOM 760 C CG . ASP A 1 92 ? 10.803 -29.782 15.434 1.00 21.75 ? 92 ASP A CG 1
+ATOM 761 O OD1 . ASP A 1 92 ? 10.011 -28.950 14.931 1.00 21.92 ? 92 ASP A OD1 1
+ATOM 762 O OD2 . ASP A 1 92 ? 10.423 -30.804 16.052 1.00 24.89 ? 92 ASP A OD2 1
+ATOM 763 N N . THR A 1 93 ? 11.319 -27.629 12.442 1.00 15.46 ? 93 THR A N 1
+ATOM 764 C CA . THR A 1 93 ? 10.601 -27.740 11.184 1.00 15.98 ? 93 THR A CA 1
+ATOM 765 C C . THR A 1 93 ? 10.936 -26.576 10.273 1.00 15.60 ? 93 THR A C 1
+ATOM 766 O O . THR A 1 93 ? 10.857 -25.414 10.682 1.00 15.87 ? 93 THR A O 1
+ATOM 767 C CB . THR A 1 93 ? 9.091 -27.772 11.474 1.00 18.02 ? 93 THR A CB 1
+ATOM 768 O OG1 . THR A 1 93 ? 8.807 -28.909 12.282 1.00 19.65 ? 93 THR A OG1 1
+ATOM 769 C CG2 . THR A 1 93 ? 8.231 -27.818 10.214 1.00 18.56 ? 93 THR A CG2 1
+ATOM 770 N N . ALA A 1 94 ? 11.321 -26.885 9.036 1.00 15.11 ? 94 ALA A N 1
+ATOM 771 C CA . ALA A 1 94 ? 11.580 -25.846 8.051 1.00 15.27 ? 94 ALA A CA 1
+ATOM 772 C C . ALA A 1 94 ? 10.227 -25.287 7.629 1.00 14.37 ? 94 ALA A C 1
+ATOM 773 O O . ALA A 1 94 ? 9.266 -26.049 7.472 1.00 14.40 ? 94 ALA A O 1
+ATOM 774 C CB . ALA A 1 94 ? 12.280 -26.436 6.838 1.00 15.99 ? 94 ALA A CB 1
+ATOM 775 N N . ASN A 1 95 ? 10.133 -23.953 7.445 1.00 13.14 ? 95 ASN A N 1
+ATOM 776 C CA . ASN A 1 95 ? 8.883 -23.366 6.989 1.00 12.83 ? 95 ASN A CA 1
+ATOM 777 C C . ASN A 1 95 ? 8.594 -23.845 5.583 1.00 14.44 ? 95 ASN A C 1
+ATOM 778 O O . ASN A 1 95 ? 9.373 -23.554 4.678 1.00 15.01 ? 95 ASN A O 1
+ATOM 779 C CB . ASN A 1 95 ? 8.974 -21.836 7.015 1.00 11.70 ? 95 ASN A CB 1
+ATOM 780 C CG . ASN A 1 95 ? 7.671 -21.166 6.662 1.00 12.68 ? 95 ASN A CG 1
+ATOM 781 O OD1 . ASN A 1 95 ? 6.665 -21.818 6.312 1.00 12.65 ? 95 ASN A OD1 1
+ATOM 782 N ND2 . ASN A 1 95 ? 7.654 -19.854 6.755 1.00 13.33 ? 95 ASN A ND2 1
+ATOM 783 N N . PRO A 1 96 ? 7.498 -24.592 5.381 1.00 15.09 ? 96 PRO A N 1
+ATOM 784 C CA . PRO A 1 96 ? 7.194 -25.071 4.022 1.00 15.91 ? 96 PRO A CA 1
+ATOM 785 C C . PRO A 1 96 ? 6.869 -23.969 3.029 1.00 16.81 ? 96 PRO A C 1
+ATOM 786 O O . PRO A 1 96 ? 6.955 -24.177 1.819 1.00 18.67 ? 96 PRO A O 1
+ATOM 787 C CB . PRO A 1 96 ? 6.007 -26.020 4.234 1.00 16.85 ? 96 PRO A CB 1
+ATOM 788 C CG . PRO A 1 96 ? 5.365 -25.537 5.452 1.00 17.21 ? 96 PRO A CG 1
+ATOM 789 C CD . PRO A 1 96 ? 6.454 -24.999 6.343 1.00 15.27 ? 96 PRO A CD 1
+ATOM 790 N N A LYS A 1 97 ? 6.497 -22.792 3.536 0.50 16.18 ? 97 LYS A N 1
+ATOM 791 N N B LYS A 1 97 ? 6.498 -22.794 3.526 0.50 15.87 ? 97 LYS A N 1
+ATOM 792 C CA A LYS A 1 97 ? 6.197 -21.633 2.715 0.50 16.25 ? 97 LYS A CA 1
+ATOM 793 C CA B LYS A 1 97 ? 6.186 -21.657 2.678 0.50 15.62 ? 97 LYS A CA 1
+ATOM 794 C C A LYS A 1 97 ? 7.398 -20.685 2.599 0.50 16.20 ? 97 LYS A C 1
+ATOM 795 C C B LYS A 1 97 ? 7.397 -20.733 2.479 0.50 15.87 ? 97 LYS A C 1
+ATOM 796 O O A LYS A 1 97 ? 7.196 -19.507 2.312 0.50 16.30 ? 97 LYS A O 1
+ATOM 797 O O B LYS A 1 97 ? 7.210 -19.616 1.997 0.50 15.98 ? 97 LYS A O 1
+ATOM 798 C CB A LYS A 1 97 ? 4.997 -20.876 3.290 0.50 17.71 ? 97 LYS A CB 1
+ATOM 799 C CB B LYS A 1 97 ? 5.028 -20.859 3.292 0.50 16.13 ? 97 LYS A CB 1
+ATOM 800 C CG A LYS A 1 97 ? 3.707 -21.681 3.258 0.50 21.36 ? 97 LYS A CG 1
+ATOM 801 C CG B LYS A 1 97 ? 3.787 -21.702 3.563 0.50 18.13 ? 97 LYS A CG 1
+ATOM 802 C CD A LYS A 1 97 ? 2.514 -20.817 3.626 0.50 25.21 ? 97 LYS A CD 1
+ATOM 803 C CD B LYS A 1 97 ? 2.659 -20.874 4.168 0.50 20.47 ? 97 LYS A CD 1
+ATOM 804 C CE A LYS A 1 97 ? 1.247 -21.628 3.735 0.50 28.84 ? 97 LYS A CE 1
+ATOM 805 C CE B LYS A 1 97 ? 1.497 -21.748 4.586 0.50 23.28 ? 97 LYS A CE 1
+ATOM 806 N NZ A LYS A 1 97 ? 1.311 -22.583 4.872 0.50 31.00 ? 97 LYS A NZ 1
+ATOM 807 N NZ B LYS A 1 97 ? 0.450 -20.970 5.306 0.50 24.86 ? 97 LYS A NZ 1
+ATOM 808 N N . THR A 1 98 ? 8.635 -21.173 2.838 1.00 15.64 ? 98 THR A N 1
+ATOM 809 C CA . THR A 1 98 ? 9.819 -20.315 2.707 1.00 15.75 ? 98 THR A CA 1
+ATOM 810 C C . THR A 1 98 ? 10.036 -19.955 1.256 1.00 17.30 ? 98 THR A C 1
+ATOM 811 O O . THR A 1 98 ? 10.207 -20.836 0.419 1.00 18.89 ? 98 THR A O 1
+ATOM 812 C CB . THR A 1 98 ? 11.098 -20.973 3.223 1.00 15.79 ? 98 THR A CB 1
+ATOM 813 O OG1 . THR A 1 98 ? 10.913 -21.371 4.576 1.00 14.95 ? 98 THR A OG1 1
+ATOM 814 C CG2 . THR A 1 98 ? 12.291 -20.020 3.161 1.00 16.33 ? 98 THR A CG2 1
+ATOM 815 N N . PRO A 1 99 ? 9.971 -18.662 0.943 1.00 17.35 ? 99 PRO A N 1
+ATOM 816 C CA . PRO A 1 99 ? 10.220 -18.251 -0.440 1.00 17.36 ? 99 PRO A CA 1
+ATOM 817 C C . PRO A 1 99 ? 11.719 -18.183 -0.682 1.00 17.89 ? 99 PRO A C 1
+ATOM 818 O O . PRO A 1 99 ? 12.539 -18.301 0.246 1.00 18.10 ? 99 PRO A O 1
+ATOM 819 C CB . PRO A 1 99 ? 9.616 -16.844 -0.472 1.00 17.74 ? 99 PRO A CB 1
+ATOM 820 C CG . PRO A 1 99 ? 9.944 -16.303 0.908 1.00 18.63 ? 99 PRO A CG 1
+ATOM 821 C CD . PRO A 1 99 ? 9.806 -17.493 1.835 1.00 16.90 ? 99 PRO A CD 1
+ATOM 822 N N . LYS A 1 100 ? 12.124 -17.929 -1.950 1.00 18.01 ? 100 LYS A N 1
+ATOM 823 C CA . LYS A 1 100 ? 13.535 -17.625 -2.236 1.00 17.86 ? 100 LYS A CA 1
+ATOM 824 C C . LYS A 1 100 ? 13.794 -16.281 -1.557 1.00 16.86 ? 100 LYS A C 1
+ATOM 825 O O . LYS A 1 100 ? 12.915 -15.410 -1.609 1.00 17.12 ? 100 LYS A O 1
+ATOM 826 C CB . LYS A 1 100 ? 13.781 -17.459 -3.727 1.00 20.30 ? 100 LYS A CB 1
+ATOM 827 C CG . LYS A 1 100 ? 13.806 -18.781 -4.460 1.00 25.36 ? 100 LYS A CG 1
+ATOM 828 C CD . LYS A 1 100 ? 13.957 -18.552 -5.942 1.00 30.62 ? 100 LYS A CD 1
+ATOM 829 C CE . LYS A 1 100 ? 13.870 -19.846 -6.690 1.00 34.80 ? 100 LYS A CE 1
+ATOM 830 N NZ . LYS A 1 100 ? 13.923 -19.616 -8.154 1.00 37.87 ? 100 LYS A NZ 1
+ATOM 831 N N . TYR A 1 101 ? 14.880 -16.181 -0.805 1.00 16.48 ? 101 TYR A N 1
+ATOM 832 C CA . TYR A 1 101 ? 15.128 -14.952 -0.066 1.00 16.55 ? 101 TYR A CA 1
+ATOM 833 C C . TYR A 1 101 ? 16.581 -14.602 0.070 1.00 17.45 ? 101 TYR A C 1
+ATOM 834 O O . TYR A 1 101 ? 17.465 -15.432 -0.117 1.00 18.21 ? 101 TYR A O 1
+ATOM 835 C CB . TYR A 1 101 ? 14.446 -14.990 1.329 1.00 15.77 ? 101 TYR A CB 1
+ATOM 836 C CG . TYR A 1 101 ? 15.146 -15.902 2.316 1.00 15.73 ? 101 TYR A CG 1
+ATOM 837 C CD1 . TYR A 1 101 ? 14.886 -17.261 2.336 1.00 15.94 ? 101 TYR A CD1 1
+ATOM 838 C CD2 . TYR A 1 101 ? 16.069 -15.402 3.228 1.00 16.30 ? 101 TYR A CD2 1
+ATOM 839 C CE1 . TYR A 1 101 ? 15.528 -18.107 3.223 1.00 17.03 ? 101 TYR A CE1 1
+ATOM 840 C CE2 . TYR A 1 101 ? 16.721 -16.242 4.126 1.00 16.87 ? 101 TYR A CE2 1
+ATOM 841 C CZ . TYR A 1 101 ? 16.426 -17.592 4.137 1.00 18.00 ? 101 TYR A CZ 1
+ATOM 842 O OH . TYR A 1 101 ? 17.050 -18.451 5.005 1.00 19.69 ? 101 TYR A OH 1
+ATOM 843 N N . LYS A 1 102 ? 16.813 -13.342 0.419 1.00 17.07 ? 102 LYS A N 1
+ATOM 844 C CA . LYS A 1 102 ? 18.117 -12.782 0.702 1.00 17.29 ? 102 LYS A CA 1
+ATOM 845 C C . LYS A 1 102 ? 17.931 -11.785 1.830 1.00 17.01 ? 102 LYS A C 1
+ATOM 846 O O . LYS A 1 102 ? 16.841 -11.228 2.005 1.00 17.36 ? 102 LYS A O 1
+ATOM 847 C CB . LYS A 1 102 ? 18.666 -12.018 -0.521 1.00 19.57 ? 102 LYS A CB 1
+ATOM 848 C CG . LYS A 1 102 ? 19.172 -12.891 -1.652 1.00 25.57 ? 102 LYS A CG 1
+ATOM 849 C CD . LYS A 1 102 ? 19.560 -12.019 -2.838 1.00 30.51 ? 102 LYS A CD 1
+ATOM 850 C CE . LYS A 1 102 ? 19.942 -12.850 -4.039 1.00 34.71 ? 102 LYS A CE 1
+ATOM 851 N NZ . LYS A 1 102 ? 20.222 -11.998 -5.223 1.00 37.67 ? 102 LYS A NZ 1
+ATOM 852 N N . PHE A 1 103 ? 18.997 -11.533 2.573 1.00 16.41 ? 103 PHE A N 1
+ATOM 853 C CA . PHE A 1 103 ? 18.994 -10.484 3.584 1.00 16.22 ? 103 PHE A CA 1
+ATOM 854 C C . PHE A 1 103 ? 19.847 -9.382 3.004 1.00 16.98 ? 103 PHE A C 1
+ATOM 855 O O . PHE A 1 103 ? 20.994 -9.634 2.601 1.00 18.29 ? 103 PHE A O 1
+ATOM 856 C CB . PHE A 1 103 ? 19.613 -10.957 4.902 1.00 15.69 ? 103 PHE A CB 1
+ATOM 857 C CG . PHE A 1 103 ? 18.795 -11.943 5.708 1.00 15.24 ? 103 PHE A CG 1
+ATOM 858 C CD1 . PHE A 1 103 ? 17.445 -12.132 5.446 1.00 15.08 ? 103 PHE A CD1 1
+ATOM 859 C CD2 . PHE A 1 103 ? 19.352 -12.609 6.784 1.00 15.50 ? 103 PHE A CD2 1
+ATOM 860 C CE1 . PHE A 1 103 ? 16.690 -13.014 6.217 1.00 15.35 ? 103 PHE A CE1 1
+ATOM 861 C CE2 . PHE A 1 103 ? 18.597 -13.493 7.545 1.00 15.76 ? 103 PHE A CE2 1
+ATOM 862 C CZ . PHE A 1 103 ? 17.267 -13.671 7.274 1.00 15.43 ? 103 PHE A CZ 1
+ATOM 863 N N . VAL A 1 104 ? 19.279 -8.182 2.889 1.00 16.37 ? 104 VAL A N 1
+ATOM 864 C CA . VAL A 1 104 ? 20.033 -7.044 2.376 1.00 17.50 ? 104 VAL A CA 1
+ATOM 865 C C . VAL A 1 104 ? 19.980 -5.887 3.348 1.00 17.45 ? 104 VAL A C 1
+ATOM 866 O O . VAL A 1 104 ? 18.977 -5.694 4.025 1.00 18.38 ? 104 VAL A O 1
+ATOM 867 C CB . VAL A 1 104 ? 19.568 -6.605 0.972 1.00 19.51 ? 104 VAL A CB 1
+ATOM 868 C CG1 . VAL A 1 104 ? 19.602 -7.772 -0.011 1.00 20.51 ? 104 VAL A CG1 1
+ATOM 869 C CG2 . VAL A 1 104 ? 18.188 -5.980 1.030 1.00 21.03 ? 104 VAL A CG2 1
+ATOM 870 N N . ARG A 1 105 ? 21.056 -5.114 3.423 1.00 15.80 ? 105 ARG A N 1
+ATOM 871 C CA . ARG A 1 105 ? 21.085 -3.918 4.245 1.00 15.43 ? 105 ARG A CA 1
+ATOM 872 C C . ARG A 1 105 ? 20.948 -2.766 3.265 1.00 16.07 ? 105 ARG A C 1
+ATOM 873 O O . ARG A 1 105 ? 21.814 -2.585 2.403 1.00 16.45 ? 105 ARG A O 1
+ATOM 874 C CB . ARG A 1 105 ? 22.391 -3.812 5.050 1.00 15.61 ? 105 ARG A CB 1
+ATOM 875 C CG . ARG A 1 105 ? 22.422 -2.551 5.896 1.00 16.10 ? 105 ARG A CG 1
+ATOM 876 C CD . ARG A 1 105 ? 23.630 -2.518 6.815 1.00 16.65 ? 105 ARG A CD 1
+ATOM 877 N NE . ARG A 1 105 ? 23.615 -1.344 7.690 1.00 16.81 ? 105 ARG A NE 1
+ATOM 878 C CZ . ARG A 1 105 ? 22.963 -1.276 8.847 1.00 17.76 ? 105 ARG A CZ 1
+ATOM 879 N NH1 . ARG A 1 105 ? 22.257 -2.313 9.283 1.00 15.50 ? 105 ARG A NH1 1
+ATOM 880 N NH2 . ARG A 1 105 ? 23.019 -0.174 9.580 1.00 16.68 ? 105 ARG A NH2 1
+ATOM 881 N N . ILE A 1 106 ? 19.843 -2.020 3.359 1.00 16.34 ? 106 ILE A N 1
+ATOM 882 C CA . ILE A 1 106 ? 19.591 -0.952 2.403 1.00 17.54 ? 106 ILE A CA 1
+ATOM 883 C C . ILE A 1 106 ? 20.273 0.351 2.775 1.00 18.38 ? 106 ILE A C 1
+ATOM 884 O O . ILE A 1 106 ? 20.686 0.548 3.914 1.00 18.30 ? 106 ILE A O 1
+ATOM 885 C CB . ILE A 1 106 ? 18.079 -0.754 2.154 1.00 18.39 ? 106 ILE A CB 1
+ATOM 886 C CG1 . ILE A 1 106 ? 17.349 -0.412 3.456 1.00 18.46 ? 106 ILE A CG1 1
+ATOM 887 C CG2 . ILE A 1 106 ? 17.482 -1.941 1.420 1.00 19.36 ? 106 ILE A CG2 1
+ATOM 888 C CD1 . ILE A 1 106 ? 15.965 0.091 3.254 1.00 19.73 ? 106 ILE A CD1 1
+ATOM 889 N N . GLN A 1 107 ? 20.428 1.226 1.782 1.00 19.23 ? 107 GLN A N 1
+ATOM 890 C CA . GLN A 1 107 ? 20.997 2.545 1.964 1.00 19.73 ? 107 GLN A CA 1
+ATOM 891 C C . GLN A 1 107 ? 19.865 3.537 2.207 1.00 18.47 ? 107 GLN A C 1
+ATOM 892 O O . GLN A 1 107 ? 18.742 3.340 1.721 1.00 17.38 ? 107 GLN A O 1
+ATOM 893 C CB . GLN A 1 107 ? 21.745 2.950 0.676 1.00 23.23 ? 107 GLN A CB 1
+ATOM 894 C CG . GLN A 1 107 ? 22.876 1.997 0.305 1.00 29.27 ? 107 GLN A CG 1
+ATOM 895 C CD . GLN A 1 107 ? 24.026 2.049 1.285 1.00 36.32 ? 107 GLN A CD 1
+ATOM 896 O OE1 . GLN A 1 107 ? 24.225 3.026 2.019 1.00 38.70 ? 107 GLN A OE1 1
+ATOM 897 N NE2 . GLN A 1 107 ? 24.829 0.996 1.300 1.00 37.97 ? 107 GLN A NE2 1
+ATOM 898 N N . PRO A 1 108 ? 20.146 4.681 2.862 1.00 18.14 ? 108 PRO A N 1
+ATOM 899 C CA . PRO A 1 108 ? 19.108 5.716 2.987 1.00 17.93 ? 108 PRO A CA 1
+ATOM 900 C C . PRO A 1 108 ? 18.660 6.165 1.590 1.00 17.22 ? 108 PRO A C 1
+ATOM 901 O O . PRO A 1 108 ? 19.462 6.189 0.647 1.00 17.68 ? 108 PRO A O 1
+ATOM 902 C CB . PRO A 1 108 ? 19.811 6.845 3.755 1.00 19.73 ? 108 PRO A CB 1
+ATOM 903 C CG . PRO A 1 108 ? 21.269 6.568 3.594 1.00 21.30 ? 108 PRO A CG 1
+ATOM 904 C CD . PRO A 1 108 ? 21.423 5.100 3.467 1.00 19.01 ? 108 PRO A CD 1
+ATOM 905 N N . GLY A 1 109 ? 17.382 6.434 1.449 1.00 15.99 ? 109 GLY A N 1
+ATOM 906 C CA . GLY A 1 109 ? 16.807 6.791 0.158 1.00 16.21 ? 109 GLY A CA 1
+ATOM 907 C C . GLY A 1 109 ? 16.074 5.638 -0.506 1.00 16.96 ? 109 GLY A C 1
+ATOM 908 O O . GLY A 1 109 ? 15.191 5.862 -1.338 1.00 18.41 ? 109 GLY A O 1
+ATOM 909 N N A GLN A 1 110 ? 16.422 4.397 -0.138 0.75 16.76 ? 110 GLN A N 1
+ATOM 910 N N B GLN A 1 110 ? 16.445 4.390 -0.161 0.25 16.16 ? 110 GLN A N 1
+ATOM 911 C CA A GLN A 1 110 ? 15.768 3.237 -0.714 0.75 16.95 ? 110 GLN A CA 1
+ATOM 912 C CA B GLN A 1 110 ? 15.829 3.187 -0.717 0.25 15.84 ? 110 GLN A CA 1
+ATOM 913 C C A GLN A 1 110 ? 14.440 2.952 -0.068 0.75 16.11 ? 110 GLN A C 1
+ATOM 914 C C B GLN A 1 110 ? 14.470 2.926 -0.075 0.25 15.71 ? 110 GLN A C 1
+ATOM 915 O O A GLN A 1 110 ? 14.240 3.191 1.125 0.75 16.11 ? 110 GLN A O 1
+ATOM 916 O O B GLN A 1 110 ? 14.293 3.143 1.123 0.25 15.80 ? 110 GLN A O 1
+ATOM 917 C CB A GLN A 1 110 ? 16.693 2.020 -0.709 0.75 19.14 ? 110 GLN A CB 1
+ATOM 918 C CB B GLN A 1 110 ? 16.764 1.974 -0.537 0.25 16.49 ? 110 GLN A CB 1
+ATOM 919 C CG A GLN A 1 110 ? 17.940 2.248 -1.555 0.75 23.45 ? 110 GLN A CG 1
+ATOM 920 C CG B GLN A 1 110 ? 16.218 0.644 -1.057 0.25 17.81 ? 110 GLN A CG 1
+ATOM 921 C CD A GLN A 1 110 ? 17.625 2.582 -2.992 0.75 30.28 ? 110 GLN A CD 1
+ATOM 922 C CD B GLN A 1 110 ? 15.922 0.672 -2.535 0.25 19.23 ? 110 GLN A CD 1
+ATOM 923 O OE1 A GLN A 1 110 ? 17.015 1.792 -3.727 0.75 33.04 ? 110 GLN A OE1 1
+ATOM 924 O OE1 B GLN A 1 110 ? 16.709 1.161 -3.348 0.25 20.49 ? 110 GLN A OE1 1
+ATOM 925 N NE2 A GLN A 1 110 ? 18.015 3.774 -3.418 0.75 30.91 ? 110 GLN A NE2 1
+ATOM 926 N NE2 B GLN A 1 110 ? 14.760 0.153 -2.910 0.25 17.17 ? 110 GLN A NE2 1
+ATOM 927 N N . THR A 1 111 ? 13.508 2.467 -0.876 1.00 15.42 ? 111 THR A N 1
+ATOM 928 C CA . THR A 1 111 ? 12.177 2.177 -0.420 1.00 15.01 ? 111 THR A CA 1
+ATOM 929 C C . THR A 1 111 ? 12.007 0.676 -0.190 1.00 14.44 ? 111 THR A C 1
+ATOM 930 O O . THR A 1 111 ? 12.800 -0.137 -0.654 1.00 15.56 ? 111 THR A O 1
+ATOM 931 C CB . THR A 1 111 ? 11.189 2.708 -1.461 1.00 15.57 ? 111 THR A CB 1
+ATOM 932 O OG1 . THR A 1 111 ? 11.488 2.051 -2.697 1.00 16.40 ? 111 THR A OG1 1
+ATOM 933 C CG2 . THR A 1 111 ? 11.297 4.211 -1.623 1.00 15.53 ? 111 THR A CG2 1
+ATOM 934 N N . PHE A 1 112 ? 10.950 0.319 0.518 1.00 13.51 ? 112 PHE A N 1
+ATOM 935 C CA . PHE A 1 112 ? 10.598 -1.063 0.784 1.00 13.06 ? 112 PHE A CA 1
+ATOM 936 C C . PHE A 1 112 ? 9.173 -1.129 1.275 1.00 12.87 ? 112 PHE A C 1
+ATOM 937 O O . PHE A 1 112 ? 8.617 -0.121 1.728 1.00 12.86 ? 112 PHE A O 1
+ATOM 938 C CB . PHE A 1 112 ? 11.550 -1.690 1.813 1.00 13.30 ? 112 PHE A CB 1
+ATOM 939 C CG . PHE A 1 112 ? 11.648 -0.996 3.149 1.00 13.25 ? 112 PHE A CG 1
+ATOM 940 C CD1 . PHE A 1 112 ? 12.527 0.058 3.340 1.00 14.26 ? 112 PHE A CD1 1
+ATOM 941 C CD2 . PHE A 1 112 ? 10.881 -1.409 4.218 1.00 13.58 ? 112 PHE A CD2 1
+ATOM 942 C CE1 . PHE A 1 112 ? 12.649 0.667 4.581 1.00 14.94 ? 112 PHE A CE1 1
+ATOM 943 C CE2 . PHE A 1 112 ? 11.024 -0.820 5.466 1.00 14.05 ? 112 PHE A CE2 1
+ATOM 944 C CZ . PHE A 1 112 ? 11.895 0.226 5.637 1.00 14.59 ? 112 PHE A CZ 1
+ATOM 945 N N . SER A 1 113 ? 8.584 -2.325 1.254 1.00 12.27 ? 113 SER A N 1
+ATOM 946 C CA . SER A 1 113 ? 7.231 -2.520 1.754 1.00 12.47 ? 113 SER A CA 1
+ATOM 947 C C . SER A 1 113 ? 7.324 -3.072 3.152 1.00 12.94 ? 113 SER A C 1
+ATOM 948 O O . SER A 1 113 ? 8.199 -3.891 3.424 1.00 13.55 ? 113 SER A O 1
+ATOM 949 C CB . SER A 1 113 ? 6.494 -3.535 0.894 1.00 13.09 ? 113 SER A CB 1
+ATOM 950 O OG . SER A 1 113 ? 6.426 -3.026 -0.426 1.00 14.30 ? 113 SER A OG 1
+ATOM 951 N N . VAL A 1 114 ? 6.388 -2.710 4.000 1.00 12.29 ? 114 VAL A N 1
+ATOM 952 C CA . VAL A 1 114 ? 6.309 -3.243 5.354 1.00 12.81 ? 114 VAL A CA 1
+ATOM 953 C C . VAL A 1 114 ? 5.016 -4.014 5.481 1.00 13.03 ? 114 VAL A C 1
+ATOM 954 O O . VAL A 1 114 ? 3.956 -3.520 5.093 1.00 13.21 ? 114 VAL A O 1
+ATOM 955 C CB . VAL A 1 114 ? 6.321 -2.096 6.393 1.00 12.98 ? 114 VAL A CB 1
+ATOM 956 C CG1 . VAL A 1 114 ? 5.995 -2.605 7.800 1.00 13.23 ? 114 VAL A CG1 1
+ATOM 957 C CG2 . VAL A 1 114 ? 7.642 -1.359 6.377 1.00 13.58 ? 114 VAL A CG2 1
+ATOM 958 N N . LEU A 1 115 ? 5.084 -5.218 6.060 1.00 12.47 ? 115 LEU A N 1
+ATOM 959 C CA . LEU A 1 115 ? 3.894 -5.974 6.346 1.00 12.54 ? 115 LEU A CA 1
+ATOM 960 C C . LEU A 1 115 ? 3.703 -5.818 7.851 1.00 12.81 ? 115 LEU A C 1
+ATOM 961 O O . LEU A 1 115 ? 4.403 -6.474 8.629 1.00 13.18 ? 115 LEU A O 1
+ATOM 962 C CB . LEU A 1 115 ? 4.037 -7.458 5.964 1.00 12.90 ? 115 LEU A CB 1
+ATOM 963 C CG . LEU A 1 115 ? 2.822 -8.307 6.284 1.00 14.50 ? 115 LEU A CG 1
+ATOM 964 C CD1 . LEU A 1 115 ? 1.620 -7.870 5.469 1.00 15.37 ? 115 LEU A CD1 1
+ATOM 965 C CD2 . LEU A 1 115 ? 3.100 -9.764 6.033 1.00 14.68 ? 115 LEU A CD2 1
+ATOM 966 N N A ALA A 1 116 ? 2.831 -4.892 8.282 0.50 12.53 ? 116 ALA A N 1
+ATOM 967 N N B ALA A 1 116 ? 2.781 -4.931 8.250 0.50 12.98 ? 116 ALA A N 1
+ATOM 968 C CA A ALA A 1 116 ? 2.624 -4.675 9.718 0.50 13.17 ? 116 ALA A CA 1
+ATOM 969 C CA B ALA A 1 116 ? 2.439 -4.683 9.648 0.50 14.18 ? 116 ALA A CA 1
+ATOM 970 C C A ALA A 1 116 ? 1.810 -5.835 10.275 0.50 13.37 ? 116 ALA A C 1
+ATOM 971 C C B ALA A 1 116 ? 1.816 -5.963 10.194 0.50 14.72 ? 116 ALA A C 1
+ATOM 972 O O A ALA A 1 116 ? 0.739 -6.137 9.755 0.50 13.60 ? 116 ALA A O 1
+ATOM 973 O O B ALA A 1 116 ? 0.984 -6.577 9.520 0.50 15.10 ? 116 ALA A O 1
+ATOM 974 C CB A ALA A 1 116 ? 1.907 -3.354 9.963 0.50 13.83 ? 116 ALA A CB 1
+ATOM 975 C CB B ALA A 1 116 ? 1.442 -3.535 9.736 0.50 14.78 ? 116 ALA A CB 1
+ATOM 976 N N A CYS A 1 117 ? 2.327 -6.495 11.304 0.75 13.30 ? 117 CYS A N 1
+ATOM 977 N N B CYS A 1 117 ? 2.247 -6.387 11.372 0.25 14.79 ? 117 CYS A N 1
+ATOM 978 C CA A CYS A 1 117 ? 1.697 -7.643 11.954 0.75 13.87 ? 117 CYS A CA 1
+ATOM 979 C CA B CYS A 1 117 ? 1.815 -7.651 11.942 0.25 15.40 ? 117 CYS A CA 1
+ATOM 980 C C A CYS A 1 117 ? 1.506 -7.426 13.414 0.75 14.56 ? 117 CYS A C 1
+ATOM 981 C C B CYS A 1 117 ? 1.597 -7.519 13.450 0.25 15.40 ? 117 CYS A C 1
+ATOM 982 O O A CYS A 1 117 ? 2.265 -6.683 14.028 0.75 14.38 ? 117 CYS A O 1
+ATOM 983 O O B CYS A 1 117 ? 2.357 -6.821 14.110 0.25 15.48 ? 117 CYS A O 1
+ATOM 984 C CB A CYS A 1 117 ? 2.543 -8.892 11.752 0.75 14.43 ? 117 CYS A CB 1
+ATOM 985 C CB B CYS A 1 117 ? 2.882 -8.701 11.636 0.25 16.62 ? 117 CYS A CB 1
+ATOM 986 S SG A CYS A 1 117 ? 2.803 -9.323 10.034 0.75 14.59 ? 117 CYS A SG 1
+ATOM 987 S SG B CYS A 1 117 ? 2.292 -10.412 11.656 0.25 20.52 ? 117 CYS A SG 1
+ATOM 988 N N . TYR A 1 118 ? 0.570 -8.188 13.997 1.00 15.18 ? 118 TYR A N 1
+ATOM 989 C CA . TYR A 1 118 ? 0.296 -8.220 15.447 1.00 16.61 ? 118 TYR A CA 1
+ATOM 990 C C . TYR A 1 118 ? -0.002 -9.668 15.797 1.00 18.17 ? 118 TYR A C 1
+ATOM 991 O O . TYR A 1 118 ? -0.763 -10.310 15.085 1.00 18.33 ? 118 TYR A O 1
+ATOM 992 C CB . TYR A 1 118 ? -0.905 -7.330 15.835 1.00 17.19 ? 118 TYR A CB 1
+ATOM 993 C CG . TYR A 1 118 ? -0.613 -5.889 15.531 1.00 17.88 ? 118 TYR A CG 1
+ATOM 994 C CD1 . TYR A 1 118 ? 0.120 -5.113 16.416 1.00 18.60 ? 118 TYR A CD1 1
+ATOM 995 C CD2 . TYR A 1 118 ? -0.904 -5.351 14.286 1.00 18.85 ? 118 TYR A CD2 1
+ATOM 996 C CE1 . TYR A 1 118 ? 0.471 -3.810 16.108 1.00 19.34 ? 118 TYR A CE1 1
+ATOM 997 C CE2 . TYR A 1 118 ? -0.509 -4.069 13.946 1.00 19.60 ? 118 TYR A CE2 1
+ATOM 998 C CZ . TYR A 1 118 ? 0.167 -3.297 14.865 1.00 20.22 ? 118 TYR A CZ 1
+ATOM 999 O OH . TYR A 1 118 ? 0.539 -2.027 14.526 1.00 21.79 ? 118 TYR A OH 1
+ATOM 1000 N N . ASN A 1 119 ? 0.643 -10.210 16.842 1.00 18.87 ? 119 ASN A N 1
+ATOM 1001 C CA . ASN A 1 119 ? 0.439 -11.600 17.254 1.00 20.10 ? 119 ASN A CA 1
+ATOM 1002 C C . ASN A 1 119 ? 0.702 -12.594 16.117 1.00 19.55 ? 119 ASN A C 1
+ATOM 1003 O O . ASN A 1 119 ? -0.008 -13.593 15.977 1.00 20.20 ? 119 ASN A O 1
+ATOM 1004 C CB . ASN A 1 119 ? -0.981 -11.790 17.805 1.00 22.64 ? 119 ASN A CB 1
+ATOM 1005 C CG . ASN A 1 119 ? -1.294 -10.896 18.970 1.00 27.97 ? 119 ASN A CG 1
+ATOM 1006 O OD1 . ASN A 1 119 ? -2.158 -10.021 18.891 1.00 30.85 ? 119 ASN A OD1 1
+ATOM 1007 N ND2 . ASN A 1 119 ? -0.591 -11.091 20.070 1.00 29.18 ? 119 ASN A ND2 1
+ATOM 1008 N N . GLY A 1 120 ? 1.679 -12.285 15.272 1.00 18.20 ? 120 GLY A N 1
+ATOM 1009 C CA . GLY A 1 120 ? 2.021 -13.141 14.143 1.00 17.98 ? 120 GLY A CA 1
+ATOM 1010 C C . GLY A 1 120 ? 1.039 -13.089 12.987 1.00 18.05 ? 120 GLY A C 1
+ATOM 1011 O O . GLY A 1 120 ? 1.168 -13.860 12.037 1.00 18.15 ? 120 GLY A O 1
+ATOM 1012 N N . SER A 1 121 ? 0.031 -12.200 13.059 1.00 17.88 ? 121 SER A N 1
+ATOM 1013 C CA . SER A 1 121 ? -0.988 -12.098 12.025 1.00 19.05 ? 121 SER A CA 1
+ATOM 1014 C C . SER A 1 121 ? -0.884 -10.784 11.263 1.00 19.31 ? 121 SER A C 1
+ATOM 1015 O O . SER A 1 121 ? -0.858 -9.709 11.855 1.00 18.83 ? 121 SER A O 1
+ATOM 1016 C CB . SER A 1 121 ? -2.379 -12.227 12.637 1.00 21.46 ? 121 SER A CB 1
+ATOM 1017 O OG . SER A 1 121 ? -2.553 -13.527 13.175 1.00 25.54 ? 121 SER A OG 1
+ATOM 1018 N N . PRO A 1 122 ? -0.842 -10.855 9.929 1.00 20.18 ? 122 PRO A N 1
+ATOM 1019 C CA . PRO A 1 122 ? -0.716 -9.623 9.136 1.00 20.36 ? 122 PRO A CA 1
+ATOM 1020 C C . PRO A 1 122 ? -1.952 -8.725 9.210 1.00 20.01 ? 122 PRO A C 1
+ATOM 1021 O O . PRO A 1 122 ? -3.095 -9.193 9.177 1.00 20.24 ? 122 PRO A O 1
+ATOM 1022 C CB . PRO A 1 122 ? -0.453 -10.148 7.715 1.00 22.14 ? 122 PRO A CB 1
+ATOM 1023 C CG . PRO A 1 122 ? 0.095 -11.574 7.925 1.00 22.93 ? 122 PRO A CG 1
+ATOM 1024 C CD . PRO A 1 122 ? -0.761 -12.055 9.076 1.00 20.91 ? 122 PRO A CD 1
+ATOM 1025 N N . SER A 1 123 ? -1.723 -7.421 9.339 1.00 19.28 ? 123 SER A N 1
+ATOM 1026 C CA . SER A 1 123 ? -2.812 -6.455 9.398 1.00 19.98 ? 123 SER A CA 1
+ATOM 1027 C C . SER A 1 123 ? -2.866 -5.587 8.166 1.00 19.22 ? 123 SER A C 1
+ATOM 1028 O O . SER A 1 123 ? -3.958 -5.209 7.743 1.00 19.82 ? 123 SER A O 1
+ATOM 1029 C CB . SER A 1 123 ? -2.716 -5.583 10.640 1.00 23.07 ? 123 SER A CB 1
+ATOM 1030 O OG . SER A 1 123 ? -1.507 -4.852 10.632 1.00 27.68 ? 123 SER A OG 1
+ATOM 1031 N N . GLY A 1 124 ? -1.705 -5.226 7.622 1.00 17.37 ? 124 GLY A N 1
+ATOM 1032 C CA . GLY A 1 124 ? -1.677 -4.368 6.453 1.00 16.81 ? 124 GLY A CA 1
+ATOM 1033 C C . GLY A 1 124 ? -0.319 -4.237 5.824 1.00 15.64 ? 124 GLY A C 1
+ATOM 1034 O O . GLY A 1 124 ? 0.683 -4.635 6.408 1.00 14.83 ? 124 GLY A O 1
+ATOM 1035 N N . VAL A 1 125 ? -0.281 -3.697 4.620 1.00 15.52 ? 125 VAL A N 1
+ATOM 1036 C CA . VAL A 1 125 ? 0.955 -3.526 3.900 1.00 16.15 ? 125 VAL A CA 1
+ATOM 1037 C C . VAL A 1 125 ? 1.037 -2.116 3.362 1.00 16.23 ? 125 VAL A C 1
+ATOM 1038 O O . VAL A 1 125 ? 0.028 -1.552 2.933 1.00 16.69 ? 125 VAL A O 1
+ATOM 1039 C CB . VAL A 1 125 ? 1.136 -4.627 2.825 1.00 18.52 ? 125 VAL A CB 1
+ATOM 1040 C CG1 . VAL A 1 125 ? 0.022 -4.589 1.791 1.00 20.02 ? 125 VAL A CG1 1
+ATOM 1041 C CG2 . VAL A 1 125 ? 2.511 -4.563 2.175 1.00 19.01 ? 125 VAL A CG2 1
+ATOM 1042 N N . TYR A 1 126 ? 2.205 -1.514 3.481 1.00 16.20 ? 126 TYR A N 1
+ATOM 1043 C CA . TYR A 1 126 ? 2.408 -0.148 3.015 1.00 16.17 ? 126 TYR A CA 1
+ATOM 1044 C C . TYR A 1 126 ? 3.842 0.066 2.588 1.00 15.60 ? 126 TYR A C 1
+ATOM 1045 O O . TYR A 1 126 ? 4.736 -0.688 2.960 1.00 15.94 ? 126 TYR A O 1
+ATOM 1046 C CB . TYR A 1 126 ? 1.958 0.884 4.064 1.00 16.49 ? 126 TYR A CB 1
+ATOM 1047 C CG . TYR A 1 126 ? 2.669 0.757 5.389 1.00 17.12 ? 126 TYR A CG 1
+ATOM 1048 C CD1 . TYR A 1 126 ? 3.901 1.356 5.601 1.00 17.77 ? 126 TYR A CD1 1
+ATOM 1049 C CD2 . TYR A 1 126 ? 2.115 0.027 6.430 1.00 18.46 ? 126 TYR A CD2 1
+ATOM 1050 C CE1 . TYR A 1 126 ? 4.560 1.241 6.817 1.00 18.59 ? 126 TYR A CE1 1
+ATOM 1051 C CE2 . TYR A 1 126 ? 2.758 -0.085 7.654 1.00 19.26 ? 126 TYR A CE2 1
+ATOM 1052 C CZ . TYR A 1 126 ? 3.979 0.529 7.845 1.00 19.71 ? 126 TYR A CZ 1
+ATOM 1053 O OH . TYR A 1 126 ? 4.608 0.427 9.064 1.00 22.38 ? 126 TYR A OH 1
+ATOM 1054 N N A GLN A 1 127 ? 4.050 1.061 1.748 0.50 15.62 ? 127 GLN A N 1
+ATOM 1055 N N B GLN A 1 127 ? 4.090 1.164 1.886 0.50 15.49 ? 127 GLN A N 1
+ATOM 1056 C CA A GLN A 1 127 ? 5.336 1.360 1.175 0.50 15.80 ? 127 GLN A CA 1
+ATOM 1057 C CA B GLN A 1 127 ? 5.413 1.506 1.423 0.50 15.72 ? 127 GLN A CA 1
+ATOM 1058 C C A GLN A 1 127 ? 5.965 2.540 1.890 0.50 16.49 ? 127 GLN A C 1
+ATOM 1059 C C B GLN A 1 127 ? 6.095 2.480 2.372 0.50 16.20 ? 127 GLN A C 1
+ATOM 1060 O O A GLN A 1 127 ? 5.306 3.560 2.092 0.50 16.63 ? 127 GLN A O 1
+ATOM 1061 O O B GLN A 1 127 ? 5.462 3.402 2.878 0.50 16.36 ? 127 GLN A O 1
+ATOM 1062 C CB A GLN A 1 127 ? 5.117 1.674 -0.313 0.50 16.38 ? 127 GLN A CB 1
+ATOM 1063 C CB B GLN A 1 127 ? 5.315 2.096 0.015 0.50 17.00 ? 127 GLN A CB 1
+ATOM 1064 C CG A GLN A 1 127 ? 6.368 1.792 -1.131 0.50 18.09 ? 127 GLN A CG 1
+ATOM 1065 C CG B GLN A 1 127 ? 6.631 2.112 -0.715 0.50 19.17 ? 127 GLN A CG 1
+ATOM 1066 C CD A GLN A 1 127 ? 7.089 0.490 -1.349 0.50 18.85 ? 127 GLN A CD 1
+ATOM 1067 C CD B GLN A 1 127 ? 7.033 0.761 -1.249 0.50 19.69 ? 127 GLN A CD 1
+ATOM 1068 O OE1 A GLN A 1 127 ? 6.666 -0.598 -0.912 0.50 18.45 ? 127 GLN A OE1 1
+ATOM 1069 O OE1 B GLN A 1 127 ? 6.501 -0.300 -0.868 0.50 20.09 ? 127 GLN A OE1 1
+ATOM 1070 N NE2 A GLN A 1 127 ? 8.210 0.583 -2.023 0.50 19.51 ? 127 GLN A NE2 1
+ATOM 1071 N NE2 B GLN A 1 127 ? 8.008 0.774 -2.125 0.50 19.03 ? 127 GLN A NE2 1
+ATOM 1072 N N A CYS A 1 128 ? 7.225 2.400 2.294 0.50 16.47 ? 128 CYS A N 1
+ATOM 1073 N N B CYS A 1 128 ? 7.382 2.261 2.606 0.50 16.43 ? 128 CYS A N 1
+ATOM 1074 C CA A CYS A 1 128 ? 7.942 3.478 2.975 0.50 16.78 ? 128 CYS A CA 1
+ATOM 1075 C CA B CYS A 1 128 ? 8.255 3.071 3.448 0.50 17.09 ? 128 CYS A CA 1
+ATOM 1076 C C A CYS A 1 128 ? 9.416 3.592 2.486 0.50 16.85 ? 128 CYS A C 1
+ATOM 1077 C C B CYS A 1 128 ? 9.557 3.356 2.718 0.50 17.04 ? 128 CYS A C 1
+ATOM 1078 O O A CYS A 1 128 ? 9.746 3.008 1.463 0.50 16.70 ? 128 CYS A O 1
+ATOM 1079 O O B CYS A 1 128 ? 9.936 2.632 1.810 0.50 16.87 ? 128 CYS A O 1
+ATOM 1080 C CB A CYS A 1 128 ? 7.831 3.331 4.489 0.50 17.30 ? 128 CYS A CB 1
+ATOM 1081 C CB B CYS A 1 128 ? 8.549 2.332 4.751 0.50 18.43 ? 128 CYS A CB 1
+ATOM 1082 S SG A CYS A 1 128 ? 8.691 1.883 5.141 0.50 19.72 ? 128 CYS A SG 1
+ATOM 1083 S SG B CYS A 1 128 ? 7.272 2.509 6.011 0.50 23.03 ? 128 CYS A SG 1
+ATOM 1084 N N . ALA A 1 129 ? 10.286 4.364 3.171 1.00 17.09 ? 129 ALA A N 1
+ATOM 1085 C CA . ALA A 1 129 ? 11.650 4.578 2.712 1.00 17.20 ? 129 ALA A CA 1
+ATOM 1086 C C . ALA A 1 129 ? 12.538 4.679 3.922 1.00 16.36 ? 129 ALA A C 1
+ATOM 1087 O O . ALA A 1 129 ? 12.115 5.142 4.987 1.00 17.23 ? 129 ALA A O 1
+ATOM 1088 C CB . ALA A 1 129 ? 11.767 5.848 1.894 1.00 17.51 ? 129 ALA A CB 1
+ATOM 1089 N N . MET A 1 130 ? 13.787 4.272 3.753 1.00 14.85 ? 130 MET A N 1
+ATOM 1090 C CA . MET A 1 130 ? 14.793 4.474 4.787 1.00 14.43 ? 130 MET A CA 1
+ATOM 1091 C C . MET A 1 130 ? 15.149 5.964 4.667 1.00 14.95 ? 130 MET A C 1
+ATOM 1092 O O . MET A 1 130 ? 15.626 6.382 3.618 1.00 15.32 ? 130 MET A O 1
+ATOM 1093 C CB . MET A 1 130 ? 16.023 3.600 4.511 1.00 14.88 ? 130 MET A CB 1
+ATOM 1094 C CG . MET A 1 130 ? 17.144 3.773 5.526 1.00 16.66 ? 130 MET A CG 1
+ATOM 1095 S SD . MET A 1 130 ? 16.663 3.502 7.255 1.00 17.10 ? 130 MET A SD 1
+ATOM 1096 C CE . MET A 1 130 ? 15.931 1.868 7.146 1.00 15.89 ? 130 MET A CE 1
+ATOM 1097 N N . ARG A 1 131 ? 14.805 6.763 5.672 1.00 14.67 ? 131 ARG A N 1
+ATOM 1098 C CA . ARG A 1 131 ? 15.075 8.199 5.615 1.00 14.63 ? 131 ARG A CA 1
+ATOM 1099 C C . ARG A 1 131 ? 16.579 8.470 5.700 1.00 15.11 ? 131 ARG A C 1
+ATOM 1100 O O . ARG A 1 131 ? 17.321 7.663 6.261 1.00 15.31 ? 131 ARG A O 1
+ATOM 1101 C CB . ARG A 1 131 ? 14.359 8.906 6.784 1.00 14.75 ? 131 ARG A CB 1
+ATOM 1102 C CG . ARG A 1 131 ? 12.853 8.693 6.868 1.00 15.21 ? 131 ARG A CG 1
+ATOM 1103 C CD . ARG A 1 131 ? 12.112 9.087 5.600 1.00 15.22 ? 131 ARG A CD 1
+ATOM 1104 N NE . ARG A 1 131 ? 12.512 10.422 5.144 1.00 14.93 ? 131 ARG A NE 1
+ATOM 1105 C CZ . ARG A 1 131 ? 12.205 10.925 3.951 1.00 14.97 ? 131 ARG A CZ 1
+ATOM 1106 N NH1 . ARG A 1 131 ? 11.460 10.230 3.101 1.00 14.04 ? 131 ARG A NH1 1
+ATOM 1107 N NH2 . ARG A 1 131 ? 12.629 12.136 3.606 1.00 14.38 ? 131 ARG A NH2 1
+ATOM 1108 N N . PRO A 1 132 ? 17.057 9.636 5.226 1.00 15.38 ? 132 PRO A N 1
+ATOM 1109 C CA . PRO A 1 132 ? 18.491 9.948 5.366 1.00 15.82 ? 132 PRO A CA 1
+ATOM 1110 C C . PRO A 1 132 ? 18.982 9.985 6.832 1.00 16.21 ? 132 PRO A C 1
+ATOM 1111 O O . PRO A 1 132 ? 20.180 9.803 7.070 1.00 17.50 ? 132 PRO A O 1
+ATOM 1112 C CB . PRO A 1 132 ? 18.614 11.299 4.676 1.00 16.65 ? 132 PRO A CB 1
+ATOM 1113 C CG . PRO A 1 132 ? 17.506 11.284 3.656 1.00 16.44 ? 132 PRO A CG 1
+ATOM 1114 C CD . PRO A 1 132 ? 16.361 10.665 4.424 1.00 15.17 ? 132 PRO A CD 1
+ATOM 1115 N N . ASN A 1 133 ? 18.087 10.206 7.816 1.00 14.91 ? 133 ASN A N 1
+ATOM 1116 C CA . ASN A 1 133 ? 18.488 10.161 9.234 1.00 14.67 ? 133 ASN A CA 1
+ATOM 1117 C C . ASN A 1 133 ? 18.338 8.731 9.835 1.00 14.76 ? 133 ASN A C 1
+ATOM 1118 O O . ASN A 1 133 ? 18.393 8.562 11.050 1.00 14.97 ? 133 ASN A O 1
+ATOM 1119 C CB . ASN A 1 133 ? 17.697 11.176 10.071 1.00 15.33 ? 133 ASN A CB 1
+ATOM 1120 C CG . ASN A 1 133 ? 16.214 10.909 10.098 1.00 15.79 ? 133 ASN A CG 1
+ATOM 1121 O OD1 . ASN A 1 133 ? 15.728 9.883 9.605 1.00 15.06 ? 133 ASN A OD1 1
+ATOM 1122 N ND2 . ASN A 1 133 ? 15.454 11.831 10.669 1.00 16.61 ? 133 ASN A ND2 1
+ATOM 1123 N N . PHE A 1 134 ? 18.104 7.718 8.982 1.00 14.43 ? 134 PHE A N 1
+ATOM 1124 C CA . PHE A 1 134 ? 18.012 6.312 9.351 1.00 15.16 ? 134 PHE A CA 1
+ATOM 1125 C C . PHE A 1 134 ? 16.803 5.931 10.198 1.00 15.02 ? 134 PHE A C 1
+ATOM 1126 O O . PHE A 1 134 ? 16.792 4.877 10.839 1.00 15.26 ? 134 PHE A O 1
+ATOM 1127 C CB . PHE A 1 134 ? 19.291 5.830 10.006 1.00 15.66 ? 134 PHE A CB 1
+ATOM 1128 C CG . PHE A 1 134 ? 20.480 5.964 9.086 1.00 17.62 ? 134 PHE A CG 1
+ATOM 1129 C CD1 . PHE A 1 134 ? 20.732 5.016 8.114 1.00 19.31 ? 134 PHE A CD1 1
+ATOM 1130 C CD2 . PHE A 1 134 ? 21.369 7.012 9.226 1.00 19.06 ? 134 PHE A CD2 1
+ATOM 1131 C CE1 . PHE A 1 134 ? 21.843 5.131 7.281 1.00 20.53 ? 134 PHE A CE1 1
+ATOM 1132 C CE2 . PHE A 1 134 ? 22.476 7.120 8.396 1.00 20.32 ? 134 PHE A CE2 1
+ATOM 1133 C CZ . PHE A 1 134 ? 22.710 6.176 7.437 1.00 20.35 ? 134 PHE A CZ 1
+ATOM 1134 N N . THR A 1 135 ? 15.760 6.743 10.140 1.00 14.48 ? 135 THR A N 1
+ATOM 1135 C CA . THR A 1 135 ? 14.475 6.389 10.724 1.00 14.62 ? 135 THR A CA 1
+ATOM 1136 C C . THR A 1 135 ? 13.558 5.992 9.541 1.00 14.74 ? 135 THR A C 1
+ATOM 1137 O O . THR A 1 135 ? 13.902 6.189 8.367 1.00 14.52 ? 135 THR A O 1
+ATOM 1138 C CB . THR A 1 135 ? 13.860 7.611 11.436 1.00 15.36 ? 135 THR A CB 1
+ATOM 1139 O OG1 . THR A 1 135 ? 13.529 8.620 10.477 1.00 16.63 ? 135 THR A OG1 1
+ATOM 1140 C CG2 . THR A 1 135 ? 14.745 8.161 12.529 1.00 15.23 ? 135 THR A CG2 1
+ATOM 1141 N N . ILE A 1 136 ? 12.395 5.430 9.852 1.00 14.48 ? 136 ILE A N 1
+ATOM 1142 C CA . ILE A 1 136 ? 11.362 5.231 8.863 1.00 15.24 ? 136 ILE A CA 1
+ATOM 1143 C C . ILE A 1 136 ? 10.103 5.840 9.436 1.00 15.66 ? 136 ILE A C 1
+ATOM 1144 O O . ILE A 1 136 ? 9.949 5.927 10.654 1.00 15.42 ? 136 ILE A O 1
+ATOM 1145 C CB . ILE A 1 136 ? 11.154 3.773 8.380 1.00 16.56 ? 136 ILE A CB 1
+ATOM 1146 C CG1 . ILE A 1 136 ? 10.532 2.890 9.459 1.00 17.44 ? 136 ILE A CG1 1
+ATOM 1147 C CG2 . ILE A 1 136 ? 12.448 3.165 7.826 1.00 17.63 ? 136 ILE A CG2 1
+ATOM 1148 C CD1 . ILE A 1 136 ? 9.987 1.590 8.900 1.00 18.35 ? 136 ILE A CD1 1
+ATOM 1149 N N A LYS A 1 137 ? 9.196 6.293 8.569 0.50 16.39 ? 137 LYS A N 1
+ATOM 1150 N N B LYS A 1 137 ? 9.209 6.274 8.558 0.50 16.47 ? 137 LYS A N 1
+ATOM 1151 C CA A LYS A 1 137 ? 7.929 6.844 9.037 0.50 17.56 ? 137 LYS A CA 1
+ATOM 1152 C CA B LYS A 1 137 ? 7.936 6.833 8.974 0.50 17.72 ? 137 LYS A CA 1
+ATOM 1153 C C A LYS A 1 137 ? 6.887 5.782 8.750 0.50 17.91 ? 137 LYS A C 1
+ATOM 1154 C C B LYS A 1 137 ? 6.920 5.736 8.717 0.50 17.94 ? 137 LYS A C 1
+ATOM 1155 O O A LYS A 1 137 ? 6.343 5.738 7.658 0.50 18.13 ? 137 LYS A O 1
+ATOM 1156 O O B LYS A 1 137 ? 6.413 5.631 7.608 0.50 18.10 ? 137 LYS A O 1
+ATOM 1157 C CB A LYS A 1 137 ? 7.610 8.173 8.334 0.50 20.10 ? 137 LYS A CB 1
+ATOM 1158 C CB B LYS A 1 137 ? 7.601 8.067 8.115 0.50 20.49 ? 137 LYS A CB 1
+ATOM 1159 C CG A LYS A 1 137 ? 8.672 9.240 8.580 0.50 24.65 ? 137 LYS A CG 1
+ATOM 1160 C CG B LYS A 1 137 ? 8.547 9.239 8.322 0.50 25.54 ? 137 LYS A CG 1
+ATOM 1161 C CD A LYS A 1 137 ? 8.340 10.542 7.865 0.50 28.93 ? 137 LYS A CD 1
+ATOM 1162 C CD B LYS A 1 137 ? 8.454 10.239 7.173 0.50 29.94 ? 137 LYS A CD 1
+ATOM 1163 C CE A LYS A 1 137 ? 7.600 11.508 8.754 0.50 32.40 ? 137 LYS A CE 1
+ATOM 1164 C CE B LYS A 1 137 ? 8.724 11.649 7.635 0.50 33.45 ? 137 LYS A CE 1
+ATOM 1165 N NZ A LYS A 1 137 ? 8.483 12.051 9.819 0.50 34.48 ? 137 LYS A NZ 1
+ATOM 1166 N NZ B LYS A 1 137 ? 9.352 12.475 6.565 0.50 34.98 ? 137 LYS A NZ 1
+ATOM 1167 N N . GLY A 1 138 ? 6.673 4.891 9.709 1.00 17.84 ? 138 GLY A N 1
+ATOM 1168 C CA . GLY A 1 138 ? 5.745 3.780 9.550 1.00 18.27 ? 138 GLY A CA 1
+ATOM 1169 C C . GLY A 1 138 ? 4.449 3.921 10.307 1.00 17.75 ? 138 GLY A C 1
+ATOM 1170 O O . GLY A 1 138 ? 4.066 5.022 10.697 1.00 18.35 ? 138 GLY A O 1
+ATOM 1171 N N . SER A 1 139 ? 3.747 2.813 10.483 1.00 16.95 ? 139 SER A N 1
+ATOM 1172 C CA . SER A 1 139 ? 2.511 2.779 11.237 1.00 17.34 ? 139 SER A CA 1
+ATOM 1173 C C . SER A 1 139 ? 2.627 1.538 12.081 1.00 18.01 ? 139 SER A C 1
+ATOM 1174 O O . SER A 1 139 ? 2.438 0.427 11.594 1.00 18.46 ? 139 SER A O 1
+ATOM 1175 C CB . SER A 1 139 ? 1.310 2.717 10.300 1.00 18.70 ? 139 SER A CB 1
+ATOM 1176 O OG . SER A 1 139 ? 0.131 2.477 11.049 1.00 23.01 ? 139 SER A OG 1
+ATOM 1177 N N . PHE A 1 140 ? 3.090 1.719 13.311 1.00 17.22 ? 140 PHE A N 1
+ATOM 1178 C CA . PHE A 1 140 ? 3.374 0.600 14.192 1.00 17.88 ? 140 PHE A CA 1
+ATOM 1179 C C . PHE A 1 140 ? 2.824 0.838 15.576 1.00 20.15 ? 140 PHE A C 1
+ATOM 1180 O O . PHE A 1 140 ? 3.184 1.818 16.205 1.00 21.50 ? 140 PHE A O 1
+ATOM 1181 C CB . PHE A 1 140 ? 4.896 0.431 14.317 1.00 16.98 ? 140 PHE A CB 1
+ATOM 1182 C CG . PHE A 1 140 ? 5.648 0.038 13.067 1.00 16.74 ? 140 PHE A CG 1
+ATOM 1183 C CD1 . PHE A 1 140 ? 5.592 -1.254 12.584 1.00 17.75 ? 140 PHE A CD1 1
+ATOM 1184 C CD2 . PHE A 1 140 ? 6.484 0.939 12.430 1.00 16.89 ? 140 PHE A CD2 1
+ATOM 1185 C CE1 . PHE A 1 140 ? 6.315 -1.619 11.454 1.00 17.58 ? 140 PHE A CE1 1
+ATOM 1186 C CE2 . PHE A 1 140 ? 7.224 0.564 11.320 1.00 17.58 ? 140 PHE A CE2 1
+ATOM 1187 C CZ . PHE A 1 140 ? 7.144 -0.713 10.843 1.00 17.08 ? 140 PHE A CZ 1
+ATOM 1188 N N . LEU A 1 141 ? 2.006 -0.071 16.069 1.00 20.53 ? 141 LEU A N 1
+ATOM 1189 C CA . LEU A 1 141 ? 1.467 0.022 17.427 1.00 22.25 ? 141 LEU A CA 1
+ATOM 1190 C C . LEU A 1 141 ? 2.194 -0.996 18.303 1.00 22.71 ? 141 LEU A C 1
+ATOM 1191 O O . LEU A 1 141 ? 3.009 -1.765 17.799 1.00 22.61 ? 141 LEU A O 1
+ATOM 1192 C CB . LEU A 1 141 ? -0.022 -0.321 17.412 1.00 23.61 ? 141 LEU A CB 1
+ATOM 1193 C CG . LEU A 1 141 ? -0.880 0.558 16.561 1.00 26.86 ? 141 LEU A CG 1
+ATOM 1194 C CD1 . LEU A 1 141 ? -2.217 -0.070 16.370 1.00 28.11 ? 141 LEU A CD1 1
+ATOM 1195 C CD2 . LEU A 1 141 ? -1.000 1.953 17.161 1.00 27.94 ? 141 LEU A CD2 1
+ATOM 1196 N N . ASN A 1 142 ? 1.876 -1.054 19.615 1.00 23.13 ? 142 ASN A N 1
+ATOM 1197 C CA . ASN A 1 142 ? 2.473 -2.056 20.495 1.00 23.46 ? 142 ASN A CA 1
+ATOM 1198 C C . ASN A 1 142 ? 2.080 -3.453 20.002 1.00 21.95 ? 142 ASN A C 1
+ATOM 1199 O O . ASN A 1 142 ? 0.950 -3.667 19.566 1.00 22.17 ? 142 ASN A O 1
+ATOM 1200 C CB . ASN A 1 142 ? 2.077 -1.814 21.953 1.00 26.50 ? 142 ASN A CB 1
+ATOM 1201 C CG . ASN A 1 142 ? 2.744 -0.586 22.522 1.00 33.37 ? 142 ASN A CG 1
+ATOM 1202 O OD1 . ASN A 1 142 ? 3.924 -0.317 22.266 1.00 35.67 ? 142 ASN A OD1 1
+ATOM 1203 N ND2 . ASN A 1 142 ? 2.005 0.198 23.302 1.00 35.11 ? 142 ASN A ND2 1
+ATOM 1204 N N . GLY A 1 143 ? 3.065 -4.323 19.913 1.00 20.23 ? 143 GLY A N 1
+ATOM 1205 C CA . GLY A 1 143 ? 2.872 -5.658 19.374 1.00 18.71 ? 143 GLY A CA 1
+ATOM 1206 C C . GLY A 1 143 ? 3.365 -5.788 17.939 1.00 16.65 ? 143 GLY A C 1
+ATOM 1207 O O . GLY A 1 143 ? 3.442 -6.903 17.428 1.00 16.13 ? 143 GLY A O 1
+ATOM 1208 N N . SER A 1 144 ? 3.691 -4.663 17.268 1.00 15.41 ? 144 SER A N 1
+ATOM 1209 C CA . SER A 1 144 ? 4.151 -4.716 15.875 1.00 14.02 ? 144 SER A CA 1
+ATOM 1210 C C . SER A 1 144 ? 5.623 -5.030 15.716 1.00 13.25 ? 144 SER A C 1
+ATOM 1211 O O . SER A 1 144 ? 6.059 -5.283 14.594 1.00 12.34 ? 144 SER A O 1
+ATOM 1212 C CB . SER A 1 144 ? 3.856 -3.411 15.150 1.00 14.75 ? 144 SER A CB 1
+ATOM 1213 O OG . SER A 1 144 ? 4.555 -2.361 15.795 1.00 16.91 ? 144 SER A OG 1
+ATOM 1214 N N . CYS A 1 145 ? 6.413 -5.035 16.803 1.00 13.27 ? 145 CYS A N 1
+ATOM 1215 C CA . CYS A 1 145 ? 7.837 -5.364 16.678 1.00 13.16 ? 145 CYS A CA 1
+ATOM 1216 C C . CYS A 1 145 ? 8.043 -6.722 16.046 1.00 12.44 ? 145 CYS A C 1
+ATOM 1217 O O . CYS A 1 145 ? 7.218 -7.618 16.221 1.00 12.76 ? 145 CYS A O 1
+ATOM 1218 C CB . CYS A 1 145 ? 8.549 -5.254 18.016 1.00 14.52 ? 145 CYS A CB 1
+ATOM 1219 S SG . CYS A 1 145 ? 8.542 -3.580 18.699 1.00 19.18 ? 145 CYS A SG 1
+ATOM 1220 N N . GLY A 1 146 ? 9.054 -6.812 15.211 1.00 11.62 ? 146 GLY A N 1
+ATOM 1221 C CA . GLY A 1 146 ? 9.297 -8.040 14.474 1.00 11.65 ? 146 GLY A CA 1
+ATOM 1222 C C . GLY A 1 146 ? 8.639 -8.028 13.111 1.00 11.50 ? 146 GLY A C 1
+ATOM 1223 O O . GLY A 1 146 ? 8.938 -8.880 12.282 1.00 12.48 ? 146 GLY A O 1
+ATOM 1224 N N . SER A 1 147 ? 7.753 -7.040 12.831 1.00 11.19 ? 147 SER A N 1
+ATOM 1225 C CA . SER A 1 147 ? 7.204 -6.880 11.475 1.00 11.25 ? 147 SER A CA 1
+ATOM 1226 C C . SER A 1 147 ? 8.385 -6.510 10.565 1.00 11.68 ? 147 SER A C 1
+ATOM 1227 O O . SER A 1 147 ? 9.322 -5.827 11.010 1.00 11.33 ? 147 SER A O 1
+ATOM 1228 C CB . SER A 1 147 ? 6.210 -5.723 11.428 1.00 12.25 ? 147 SER A CB 1
+ATOM 1229 O OG . SER A 1 147 ? 5.054 -6.012 12.198 1.00 13.30 ? 147 SER A OG 1
+ATOM 1230 N N . VAL A 1 148 ? 8.354 -6.970 9.308 1.00 11.17 ? 148 VAL A N 1
+ATOM 1231 C CA . VAL A 1 148 ? 9.493 -6.779 8.444 1.00 11.78 ? 148 VAL A CA 1
+ATOM 1232 C C . VAL A 1 148 ? 9.223 -5.923 7.220 1.00 12.04 ? 148 VAL A C 1
+ATOM 1233 O O . VAL A 1 148 ? 8.088 -5.781 6.767 1.00 11.94 ? 148 VAL A O 1
+ATOM 1234 C CB . VAL A 1 148 ? 10.129 -8.138 8.036 1.00 12.63 ? 148 VAL A CB 1
+ATOM 1235 C CG1 . VAL A 1 148 ? 10.607 -8.914 9.260 1.00 12.66 ? 148 VAL A CG1 1
+ATOM 1236 C CG2 . VAL A 1 148 ? 9.180 -8.973 7.195 1.00 13.55 ? 148 VAL A CG2 1
+ATOM 1237 N N . GLY A 1 149 ? 10.312 -5.371 6.699 1.00 12.16 ? 149 GLY A N 1
+ATOM 1238 C CA . GLY A 1 149 ? 10.362 -4.619 5.460 1.00 12.30 ? 149 GLY A CA 1
+ATOM 1239 C C . GLY A 1 149 ? 11.095 -5.441 4.419 1.00 12.43 ? 149 GLY A C 1
+ATOM 1240 O O . GLY A 1 149 ? 12.033 -6.187 4.731 1.00 12.20 ? 149 GLY A O 1
+ATOM 1241 N N . PHE A 1 150 ? 10.650 -5.327 3.175 1.00 12.00 ? 150 PHE A N 1
+ATOM 1242 C CA . PHE A 1 150 ? 11.198 -6.146 2.114 1.00 13.19 ? 150 PHE A CA 1
+ATOM 1243 C C . PHE A 1 150 ? 10.981 -5.537 0.748 1.00 14.59 ? 150 PHE A C 1
+ATOM 1244 O O . PHE A 1 150 ? 10.124 -4.675 0.576 1.00 14.07 ? 150 PHE A O 1
+ATOM 1245 C CB . PHE A 1 150 ? 10.498 -7.529 2.164 1.00 13.42 ? 150 PHE A CB 1
+ATOM 1246 C CG . PHE A 1 150 ? 8.997 -7.465 1.967 1.00 14.35 ? 150 PHE A CG 1
+ATOM 1247 C CD1 . PHE A 1 150 ? 8.154 -7.170 3.021 1.00 15.42 ? 150 PHE A CD1 1
+ATOM 1248 C CD2 . PHE A 1 150 ? 8.432 -7.691 0.721 1.00 15.45 ? 150 PHE A CD2 1
+ATOM 1249 C CE1 . PHE A 1 150 ? 6.783 -7.040 2.825 1.00 16.35 ? 150 PHE A CE1 1
+ATOM 1250 C CE2 . PHE A 1 150 ? 7.052 -7.611 0.541 1.00 16.30 ? 150 PHE A CE2 1
+ATOM 1251 C CZ . PHE A 1 150 ? 6.239 -7.292 1.593 1.00 15.96 ? 150 PHE A CZ 1
+ATOM 1252 N N . ASN A 1 151 ? 11.734 -6.041 -0.222 1.00 15.13 ? 151 ASN A N 1
+ATOM 1253 C CA . ASN A 1 151 ? 11.561 -5.768 -1.644 1.00 16.70 ? 151 ASN A CA 1
+ATOM 1254 C C . ASN A 1 151 ? 11.469 -7.132 -2.334 1.00 18.24 ? 151 ASN A C 1
+ATOM 1255 O O . ASN A 1 151 ? 11.926 -8.137 -1.785 1.00 17.68 ? 151 ASN A O 1
+ATOM 1256 C CB . ASN A 1 151 ? 12.736 -4.982 -2.203 1.00 17.55 ? 151 ASN A CB 1
+ATOM 1257 C CG . ASN A 1 151 ? 12.678 -3.526 -1.848 1.00 21.16 ? 151 ASN A CG 1
+ATOM 1258 O OD1 . ASN A 1 151 ? 12.018 -2.729 -2.525 1.00 23.71 ? 151 ASN A OD1 1
+ATOM 1259 N ND2 . ASN A 1 151 ? 13.342 -3.149 -0.770 1.00 19.82 ? 151 ASN A ND2 1
+ATOM 1260 N N . ILE A 1 152 ? 10.860 -7.188 -3.527 1.00 19.82 ? 152 ILE A N 1
+ATOM 1261 C CA . ILE A 1 152 ? 10.779 -8.458 -4.255 1.00 22.59 ? 152 ILE A CA 1
+ATOM 1262 C C . ILE A 1 152 ? 11.333 -8.271 -5.655 1.00 25.21 ? 152 ILE A C 1
+ATOM 1263 O O . ILE A 1 152 ? 11.049 -7.265 -6.296 1.00 25.64 ? 152 ILE A O 1
+ATOM 1264 C CB . ILE A 1 152 ? 9.350 -9.069 -4.286 1.00 23.47 ? 152 ILE A CB 1
+ATOM 1265 C CG1 . ILE A 1 152 ? 8.720 -9.144 -2.884 1.00 24.58 ? 152 ILE A CG1 1
+ATOM 1266 C CG2 . ILE A 1 152 ? 9.360 -10.453 -4.972 1.00 24.13 ? 152 ILE A CG2 1
+ATOM 1267 C CD1 . ILE A 1 152 ? 7.304 -9.608 -2.866 1.00 25.76 ? 152 ILE A CD1 1
+ATOM 1268 N N . ASP A 1 153 ? 12.157 -9.211 -6.114 1.00 26.83 ? 153 ASP A N 1
+ATOM 1269 C CA . ASP A 1 153 ? 12.655 -9.198 -7.484 1.00 28.74 ? 153 ASP A CA 1
+ATOM 1270 C C . ASP A 1 153 ? 12.170 -10.512 -8.056 1.00 29.83 ? 153 ASP A C 1
+ATOM 1271 O O . ASP A 1 153 ? 12.773 -11.548 -7.779 1.00 30.55 ? 153 ASP A O 1
+ATOM 1272 C CB . ASP A 1 153 ? 14.184 -9.123 -7.546 1.00 31.89 ? 153 ASP A CB 1
+ATOM 1273 C CG . ASP A 1 153 ? 14.688 -8.981 -8.971 1.00 40.02 ? 153 ASP A CG 1
+ATOM 1274 O OD1 . ASP A 1 153 ? 13.977 -8.356 -9.795 1.00 41.47 ? 153 ASP A OD1 1
+ATOM 1275 O OD2 . ASP A 1 153 ? 15.789 -9.501 -9.268 1.00 43.80 ? 153 ASP A OD2 1
+ATOM 1276 N N . TYR A 1 154 ? 11.037 -10.469 -8.789 1.00 29.57 ? 154 TYR A N 1
+ATOM 1277 C CA . TYR A 1 154 ? 10.327 -11.603 -9.381 1.00 30.13 ? 154 TYR A CA 1
+ATOM 1278 C C . TYR A 1 154 ? 9.896 -12.627 -8.298 1.00 29.86 ? 154 TYR A C 1
+ATOM 1279 O O . TYR A 1 154 ? 8.809 -12.476 -7.736 1.00 30.57 ? 154 TYR A O 1
+ATOM 1280 C CB . TYR A 1 154 ? 11.081 -12.243 -10.574 0.50 30.31 ? 154 TYR A CB 1
+ATOM 1281 C CG . TYR A 1 154 ? 10.357 -13.446 -11.143 0.50 31.41 ? 154 TYR A CG 1
+ATOM 1282 C CD1 . TYR A 1 154 ? 9.054 -13.341 -11.609 0.50 32.51 ? 154 TYR A CD1 1
+ATOM 1283 C CD2 . TYR A 1 154 ? 10.964 -14.693 -11.188 0.50 32.38 ? 154 TYR A CD2 1
+ATOM 1284 C CE1 . TYR A 1 154 ? 8.372 -14.447 -12.100 0.50 33.48 ? 154 TYR A CE1 1
+ATOM 1285 C CE2 . TYR A 1 154 ? 10.290 -15.808 -11.669 0.50 33.42 ? 154 TYR A CE2 1
+ATOM 1286 C CZ . TYR A 1 154 ? 8.994 -15.680 -12.131 0.50 34.48 ? 154 TYR A CZ 1
+ATOM 1287 O OH . TYR A 1 154 ? 8.328 -16.774 -12.627 0.50 36.31 ? 154 TYR A OH 1
+ATOM 1288 N N . ASP A 1 155 ? 10.732 -13.629 -7.970 1.00 28.99 ? 155 ASP A N 1
+ATOM 1289 C CA . ASP A 1 155 ? 10.368 -14.624 -6.961 1.00 28.27 ? 155 ASP A CA 1
+ATOM 1290 C C . ASP A 1 155 ? 11.249 -14.600 -5.720 1.00 26.66 ? 155 ASP A C 1
+ATOM 1291 O O . ASP A 1 155 ? 11.085 -15.455 -4.854 1.00 27.06 ? 155 ASP A O 1
+ATOM 1292 C CB . ASP A 1 155 ? 10.346 -16.038 -7.566 1.00 30.93 ? 155 ASP A CB 1
+ATOM 1293 C CG . ASP A 1 155 ? 11.673 -16.511 -8.140 1.00 36.67 ? 155 ASP A CG 1
+ATOM 1294 O OD1 . ASP A 1 155 ? 12.607 -15.683 -8.250 1.00 37.43 ? 155 ASP A OD1 1
+ATOM 1295 O OD2 . ASP A 1 155 ? 11.772 -17.708 -8.495 1.00 39.58 ? 155 ASP A OD2 1
+ATOM 1296 N N . CYS A 1 156 ? 12.175 -13.637 -5.622 1.00 24.66 ? 156 CYS A N 1
+ATOM 1297 C CA . CYS A 1 156 ? 13.076 -13.566 -4.484 1.00 23.25 ? 156 CYS A CA 1
+ATOM 1298 C C . CYS A 1 156 ? 12.758 -12.398 -3.587 1.00 20.76 ? 156 CYS A C 1
+ATOM 1299 O O . CYS A 1 156 ? 12.827 -11.248 -4.023 1.00 20.48 ? 156 CYS A O 1
+ATOM 1300 C CB . CYS A 1 156 ? 14.525 -13.518 -4.955 1.00 24.48 ? 156 CYS A CB 1
+ATOM 1301 S SG . CYS A 1 156 ? 15.738 -13.478 -3.610 1.00 27.04 ? 156 CYS A SG 1
+ATOM 1302 N N . VAL A 1 157 ? 12.484 -12.680 -2.310 1.00 18.60 ? 157 VAL A N 1
+ATOM 1303 C CA . VAL A 1 157 ? 12.218 -11.620 -1.344 1.00 17.05 ? 157 VAL A CA 1
+ATOM 1304 C C . VAL A 1 157 ? 13.514 -11.180 -0.700 1.00 15.71 ? 157 VAL A C 1
+ATOM 1305 O O . VAL A 1 157 ? 14.196 -11.995 -0.084 1.00 15.50 ? 157 VAL A O 1
+ATOM 1306 C CB . VAL A 1 157 ? 11.247 -12.102 -0.243 1.00 17.28 ? 157 VAL A CB 1
+ATOM 1307 C CG1 . VAL A 1 157 ? 10.950 -10.990 0.757 1.00 17.60 ? 157 VAL A CG1 1
+ATOM 1308 C CG2 . VAL A 1 157 ? 9.958 -12.653 -0.847 1.00 18.06 ? 157 VAL A CG2 1
+ATOM 1309 N N . SER A 1 158 ? 13.840 -9.894 -0.794 1.00 15.06 ? 158 SER A N 1
+ATOM 1310 C CA . SER A 1 158 ? 15.008 -9.358 -0.111 1.00 14.90 ? 158 SER A CA 1
+ATOM 1311 C C . SER A 1 158 ? 14.517 -8.654 1.138 1.00 14.32 ? 158 SER A C 1
+ATOM 1312 O O . SER A 1 158 ? 13.944 -7.567 1.050 1.00 14.24 ? 158 SER A O 1
+ATOM 1313 C CB . SER A 1 158 ? 15.755 -8.366 -0.997 1.00 17.17 ? 158 SER A CB 1
+ATOM 1314 O OG . SER A 1 158 ? 16.436 -9.063 -2.024 1.00 20.62 ? 158 SER A OG 1
+ATOM 1315 N N . PHE A 1 159 ? 14.725 -9.276 2.299 1.00 13.50 ? 159 PHE A N 1
+ATOM 1316 C CA . PHE A 1 159 ? 14.327 -8.676 3.565 1.00 13.12 ? 159 PHE A CA 1
+ATOM 1317 C C . PHE A 1 159 ? 15.366 -7.649 3.959 1.00 12.99 ? 159 PHE A C 1
+ATOM 1318 O O . PHE A 1 159 ? 16.559 -7.954 3.983 1.00 13.40 ? 159 PHE A O 1
+ATOM 1319 C CB . PHE A 1 159 ? 14.245 -9.749 4.654 1.00 12.61 ? 159 PHE A CB 1
+ATOM 1320 C CG . PHE A 1 159 ? 13.131 -10.726 4.411 1.00 11.64 ? 159 PHE A CG 1
+ATOM 1321 C CD1 . PHE A 1 159 ? 11.819 -10.392 4.702 1.00 12.23 ? 159 PHE A CD1 1
+ATOM 1322 C CD2 . PHE A 1 159 ? 13.391 -11.978 3.887 1.00 11.94 ? 159 PHE A CD2 1
+ATOM 1323 C CE1 . PHE A 1 159 ? 10.793 -11.300 4.508 1.00 12.59 ? 159 PHE A CE1 1
+ATOM 1324 C CE2 . PHE A 1 159 ? 12.357 -12.881 3.669 1.00 12.59 ? 159 PHE A CE2 1
+ATOM 1325 C CZ . PHE A 1 159 ? 11.064 -12.538 3.991 1.00 12.27 ? 159 PHE A CZ 1
+ATOM 1326 N N . CYS A 1 160 ? 14.918 -6.444 4.317 1.00 12.93 ? 160 CYS A N 1
+ATOM 1327 C CA . CYS A 1 160 ? 15.839 -5.365 4.668 1.00 13.50 ? 160 CYS A CA 1
+ATOM 1328 C C . CYS A 1 160 ? 15.596 -4.739 6.011 1.00 13.22 ? 160 CYS A C 1
+ATOM 1329 O O . CYS A 1 160 ? 16.451 -3.984 6.456 1.00 13.85 ? 160 CYS A O 1
+ATOM 1330 C CB . CYS A 1 160 ? 15.838 -4.296 3.580 1.00 14.93 ? 160 CYS A CB 1
+ATOM 1331 S SG . CYS A 1 160 ? 14.213 -3.572 3.272 1.00 15.19 ? 160 CYS A SG 1
+ATOM 1332 N N . TYR A 1 161 ? 14.433 -4.952 6.614 1.00 12.04 ? 161 TYR A N 1
+ATOM 1333 C CA . TYR A 1 161 ? 14.112 -4.270 7.849 1.00 11.92 ? 161 TYR A CA 1
+ATOM 1334 C C . TYR A 1 161 ? 13.335 -5.134 8.797 1.00 11.21 ? 161 TYR A C 1
+ATOM 1335 O O . TYR A 1 161 ? 12.520 -5.929 8.377 1.00 11.05 ? 161 TYR A O 1
+ATOM 1336 C CB . TYR A 1 161 ? 13.272 -3.020 7.497 1.00 11.04 ? 161 TYR A CB 1
+ATOM 1337 C CG . TYR A 1 161 ? 12.873 -2.174 8.686 1.00 11.13 ? 161 TYR A CG 1
+ATOM 1338 C CD1 . TYR A 1 161 ? 13.734 -1.221 9.206 1.00 12.22 ? 161 TYR A CD1 1
+ATOM 1339 C CD2 . TYR A 1 161 ? 11.614 -2.292 9.256 1.00 11.72 ? 161 TYR A CD2 1
+ATOM 1340 C CE1 . TYR A 1 161 ? 13.370 -0.445 10.303 1.00 12.77 ? 161 TYR A CE1 1
+ATOM 1341 C CE2 . TYR A 1 161 ? 11.245 -1.535 10.356 1.00 12.42 ? 161 TYR A CE2 1
+ATOM 1342 C CZ . TYR A 1 161 ? 12.120 -0.604 10.873 1.00 12.57 ? 161 TYR A CZ 1
+ATOM 1343 O OH . TYR A 1 161 ? 11.751 0.138 11.977 1.00 12.95 ? 161 TYR A OH 1
+ATOM 1344 N N . MET A 1 162 ? 13.585 -4.974 10.085 1.00 10.28 ? 162 MET A N 1
+ATOM 1345 C CA . MET A 1 162 ? 12.783 -5.594 11.126 1.00 10.68 ? 162 MET A CA 1
+ATOM 1346 C C . MET A 1 162 ? 12.509 -4.476 12.131 1.00 10.72 ? 162 MET A C 1
+ATOM 1347 O O . MET A 1 162 ? 13.429 -3.757 12.531 1.00 10.71 ? 162 MET A O 1
+ATOM 1348 C CB . MET A 1 162 ? 13.469 -6.782 11.785 1.00 11.91 ? 162 MET A CB 1
+ATOM 1349 C CG . MET A 1 162 ? 12.631 -7.332 12.936 1.00 12.92 ? 162 MET A CG 1
+ATOM 1350 S SD . MET A 1 162 ? 13.162 -8.961 13.503 1.00 15.17 ? 162 MET A SD 1
+ATOM 1351 C CE . MET A 1 162 ? 12.432 -9.997 12.218 1.00 16.30 ? 162 MET A CE 1
+ATOM 1352 N N . HIS A 1 163 ? 11.245 -4.306 12.496 1.00 10.85 ? 163 HIS A N 1
+ATOM 1353 C CA . HIS A 1 163 ? 10.862 -3.230 13.394 1.00 10.78 ? 163 HIS A CA 1
+ATOM 1354 C C . HIS A 1 163 ? 11.218 -3.501 14.829 1.00 10.88 ? 163 HIS A C 1
+ATOM 1355 O O . HIS A 1 163 ? 10.858 -4.554 15.333 1.00 11.36 ? 163 HIS A O 1
+ATOM 1356 C CB . HIS A 1 163 ? 9.363 -2.967 13.299 1.00 11.80 ? 163 HIS A CB 1
+ATOM 1357 C CG . HIS A 1 163 ? 8.995 -1.754 14.072 1.00 12.60 ? 163 HIS A CG 1
+ATOM 1358 N ND1 . HIS A 1 163 ? 9.637 -0.545 13.857 1.00 13.89 ? 163 HIS A ND1 1
+ATOM 1359 C CD2 . HIS A 1 163 ? 8.139 -1.619 15.105 1.00 13.61 ? 163 HIS A CD2 1
+ATOM 1360 C CE1 . HIS A 1 163 ? 9.124 0.289 14.740 1.00 14.58 ? 163 HIS A CE1 1
+ATOM 1361 N NE2 . HIS A 1 163 ? 8.222 -0.307 15.514 1.00 14.16 ? 163 HIS A NE2 1
+ATOM 1362 N N . HIS A 1 164 ? 11.850 -2.524 15.504 1.00 10.72 ? 164 HIS A N 1
+ATOM 1363 C CA . HIS A 1 164 ? 12.191 -2.691 16.911 1.00 12.02 ? 164 HIS A CA 1
+ATOM 1364 C C . HIS A 1 164 ? 11.654 -1.626 17.827 1.00 13.54 ? 164 HIS A C 1
+ATOM 1365 O O . HIS A 1 164 ? 11.296 -1.961 18.960 1.00 14.57 ? 164 HIS A O 1
+ATOM 1366 C CB . HIS A 1 164 ? 13.720 -2.699 17.140 1.00 12.32 ? 164 HIS A CB 1
+ATOM 1367 C CG . HIS A 1 164 ? 14.408 -3.927 16.654 1.00 11.31 ? 164 HIS A CG 1
+ATOM 1368 N ND1 . HIS A 1 164 ? 15.090 -4.762 17.524 1.00 11.61 ? 164 HIS A ND1 1
+ATOM 1369 C CD2 . HIS A 1 164 ? 14.549 -4.392 15.393 1.00 11.50 ? 164 HIS A CD2 1
+ATOM 1370 C CE1 . HIS A 1 164 ? 15.623 -5.706 16.765 1.00 11.94 ? 164 HIS A CE1 1
+ATOM 1371 N NE2 . HIS A 1 164 ? 15.308 -5.537 15.478 1.00 12.33 ? 164 HIS A NE2 1
+ATOM 1372 N N A MET A 1 165 ? 11.586 -0.360 17.376 0.50 14.49 ? 165 MET A N 1
+ATOM 1373 N N B MET A 1 165 ? 11.783 -0.326 17.439 0.50 13.59 ? 165 MET A N 1
+ATOM 1374 C CA A MET A 1 165 ? 11.139 0.666 18.305 0.50 16.09 ? 165 MET A CA 1
+ATOM 1375 C CA B MET A 1 165 ? 11.504 0.797 18.336 0.50 14.00 ? 165 MET A CA 1
+ATOM 1376 C C A MET A 1 165 ? 10.595 1.912 17.722 0.50 15.90 ? 165 MET A C 1
+ATOM 1377 C C B MET A 1 165 ? 10.702 1.944 17.739 0.50 14.88 ? 165 MET A C 1
+ATOM 1378 O O A MET A 1 165 ? 10.776 2.215 16.550 0.50 15.72 ? 165 MET A O 1
+ATOM 1379 O O B MET A 1 165 ? 10.842 2.241 16.560 0.50 14.65 ? 165 MET A O 1
+ATOM 1380 C CB A MET A 1 165 ? 12.260 1.033 19.260 0.50 18.07 ? 165 MET A CB 1
+ATOM 1381 C CB B MET A 1 165 ? 12.844 1.448 18.767 0.50 13.85 ? 165 MET A CB 1
+ATOM 1382 C CG A MET A 1 165 ? 13.510 1.441 18.567 0.50 21.85 ? 165 MET A CG 1
+ATOM 1383 C CG B MET A 1 165 ? 13.883 0.481 19.312 0.50 14.29 ? 165 MET A CG 1
+ATOM 1384 S SD A MET A 1 165 ? 14.871 1.411 19.737 0.50 29.90 ? 165 MET A SD 1
+ATOM 1385 S SD B MET A 1 165 ? 13.470 -0.155 20.945 0.50 15.29 ? 165 MET A SD 1
+ATOM 1386 C CE A MET A 1 165 ? 14.286 0.130 20.907 0.50 30.34 ? 165 MET A CE 1
+ATOM 1387 C CE B MET A 1 165 ? 13.829 1.249 21.920 0.50 19.00 ? 165 MET A CE 1
+ATOM 1388 N N . GLU A 1 166 ? 9.962 2.669 18.591 1.00 16.13 ? 166 GLU A N 1
+ATOM 1389 C CA . GLU A 1 166 ? 9.355 3.908 18.240 1.00 17.53 ? 166 GLU A CA 1
+ATOM 1390 C C . GLU A 1 166 ? 10.049 4.945 19.115 1.00 19.53 ? 166 GLU A C 1
+ATOM 1391 O O . GLU A 1 166 ? 10.099 4.793 20.337 1.00 20.14 ? 166 GLU A O 1
+ATOM 1392 C CB . GLU A 1 166 ? 7.885 3.883 18.595 1.00 19.56 ? 166 GLU A CB 1
+ATOM 1393 C CG . GLU A 1 166 ? 7.200 5.177 18.243 1.00 23.51 ? 166 GLU A CG 1
+ATOM 1394 C CD . GLU A 1 166 ? 5.719 4.914 18.267 1.00 27.84 ? 166 GLU A CD 1
+ATOM 1395 O OE1 . GLU A 1 166 ? 5.148 4.841 19.378 1.00 29.33 ? 166 GLU A OE1 1
+ATOM 1396 O OE2 . GLU A 1 166 ? 5.144 4.697 17.176 1.00 27.18 ? 166 GLU A OE2 1
+ATOM 1397 N N . LEU A 1 167 ? 10.596 5.973 18.494 1.00 20.80 ? 167 LEU A N 1
+ATOM 1398 C CA . LEU A 1 167 ? 11.246 7.053 19.220 1.00 23.30 ? 167 LEU A CA 1
+ATOM 1399 C C . LEU A 1 167 ? 10.170 7.948 19.834 1.00 25.62 ? 167 LEU A C 1
+ATOM 1400 O O . LEU A 1 167 ? 9.054 8.016 19.312 1.00 25.54 ? 167 LEU A O 1
+ATOM 1401 C CB . LEU A 1 167 ? 12.109 7.853 18.227 1.00 24.19 ? 167 LEU A CB 1
+ATOM 1402 C CG . LEU A 1 167 ? 13.150 7.045 17.422 1.00 26.98 ? 167 LEU A CG 1
+ATOM 1403 C CD1 . LEU A 1 167 ? 14.029 7.967 16.621 1.00 28.28 ? 167 LEU A CD1 1
+ATOM 1404 C CD2 . LEU A 1 167 ? 14.022 6.155 18.327 1.00 27.79 ? 167 LEU A CD2 1
+ATOM 1405 N N . PRO A 1 168 ? 10.502 8.716 20.885 1.00 27.44 ? 168 PRO A N 1
+ATOM 1406 C CA . PRO A 1 168 ? 9.495 9.604 21.486 1.00 28.84 ? 168 PRO A CA 1
+ATOM 1407 C C . PRO A 1 168 ? 8.854 10.601 20.525 1.00 30.15 ? 168 PRO A C 1
+ATOM 1408 O O . PRO A 1 168 ? 7.806 11.147 20.853 1.00 31.65 ? 168 PRO A O 1
+ATOM 1409 C CB . PRO A 1 168 ? 10.264 10.307 22.605 1.00 29.60 ? 168 PRO A CB 1
+ATOM 1410 C CG . PRO A 1 168 ? 11.376 9.380 22.945 1.00 29.87 ? 168 PRO A CG 1
+ATOM 1411 C CD . PRO A 1 168 ? 11.767 8.736 21.646 1.00 27.74 ? 168 PRO A CD 1
+ATOM 1412 N N . THR A 1 169 ? 9.448 10.838 19.342 1.00 29.64 ? 169 THR A N 1
+ATOM 1413 C CA . THR A 1 169 ? 8.869 11.743 18.351 1.00 29.70 ? 169 THR A CA 1
+ATOM 1414 C C . THR A 1 169 ? 7.931 11.078 17.330 1.00 29.13 ? 169 THR A C 1
+ATOM 1415 O O . THR A 1 169 ? 7.497 11.738 16.388 1.00 29.33 ? 169 THR A O 1
+ATOM 1416 C CB . THR A 1 169 ? 9.946 12.533 17.623 1.00 31.65 ? 169 THR A CB 1
+ATOM 1417 O OG1 . THR A 1 169 ? 10.933 11.626 17.118 1.00 32.87 ? 169 THR A OG1 1
+ATOM 1418 C CG2 . THR A 1 169 ? 10.574 13.602 18.502 1.00 32.20 ? 169 THR A CG2 1
+ATOM 1419 N N . GLY A 1 170 ? 7.618 9.799 17.517 1.00 28.09 ? 170 GLY A N 1
+ATOM 1420 C CA . GLY A 1 170 ? 6.690 9.104 16.634 1.00 27.29 ? 170 GLY A CA 1
+ATOM 1421 C C . GLY A 1 170 ? 7.276 8.478 15.392 1.00 25.98 ? 170 GLY A C 1
+ATOM 1422 O O . GLY A 1 170 ? 6.531 7.969 14.548 1.00 26.76 ? 170 GLY A O 1
+ATOM 1423 N N . VAL A 1 171 ? 8.602 8.553 15.235 1.00 23.64 ? 171 VAL A N 1
+ATOM 1424 C CA . VAL A 1 171 ? 9.262 7.930 14.096 1.00 21.19 ? 171 VAL A CA 1
+ATOM 1425 C C . VAL A 1 171 ? 9.803 6.561 14.543 1.00 17.38 ? 171 VAL A C 1
+ATOM 1426 O O . VAL A 1 171 ? 9.847 6.266 15.735 1.00 17.18 ? 171 VAL A O 1
+ATOM 1427 C CB . VAL A 1 171 ? 10.323 8.817 13.418 1.00 22.74 ? 171 VAL A CB 1
+ATOM 1428 C CG1 . VAL A 1 171 ? 9.690 10.084 12.853 1.00 23.85 ? 171 VAL A CG1 1
+ATOM 1429 C CG2 . VAL A 1 171 ? 11.443 9.141 14.386 1.00 23.08 ? 171 VAL A CG2 1
+ATOM 1430 N N . HIS A 1 172 ? 10.166 5.722 13.586 1.00 15.44 ? 172 HIS A N 1
+ATOM 1431 C CA . HIS A 1 172 ? 10.508 4.343 13.854 1.00 13.98 ? 172 HIS A CA 1
+ATOM 1432 C C . HIS A 1 172 ? 11.940 3.965 13.543 1.00 13.47 ? 172 HIS A C 1
+ATOM 1433 O O . HIS A 1 172 ? 12.551 4.481 12.612 1.00 13.64 ? 172 HIS A O 1
+ATOM 1434 C CB . HIS A 1 172 ? 9.512 3.472 13.081 1.00 13.55 ? 172 HIS A CB 1
+ATOM 1435 C CG . HIS A 1 172 ? 8.096 3.784 13.471 1.00 13.40 ? 172 HIS A CG 1
+ATOM 1436 N ND1 . HIS A 1 172 ? 7.228 4.426 12.601 1.00 14.72 ? 172 HIS A ND1 1
+ATOM 1437 C CD2 . HIS A 1 172 ? 7.501 3.693 14.686 1.00 14.40 ? 172 HIS A CD2 1
+ATOM 1438 C CE1 . HIS A 1 172 ? 6.107 4.609 13.283 1.00 15.27 ? 172 HIS A CE1 1
+ATOM 1439 N NE2 . HIS A 1 172 ? 6.228 4.194 14.544 1.00 15.66 ? 172 HIS A NE2 1
+ATOM 1440 N N . ALA A 1 173 ? 12.452 3.012 14.322 1.00 12.95 ? 173 ALA A N 1
+ATOM 1441 C CA . ALA A 1 173 ? 13.821 2.530 14.168 1.00 12.79 ? 173 ALA A CA 1
+ATOM 1442 C C . ALA A 1 173 ? 13.843 1.028 14.231 1.00 12.27 ? 173 ALA A C 1
+ATOM 1443 O O . ALA A 1 173 ? 13.033 0.406 14.916 1.00 12.33 ? 173 ALA A O 1
+ATOM 1444 C CB . ALA A 1 173 ? 14.713 3.092 15.263 1.00 13.06 ? 173 ALA A CB 1
+ATOM 1445 N N . GLY A 1 174 ? 14.761 0.447 13.481 1.00 11.78 ? 174 GLY A N 1
+ATOM 1446 C CA . GLY A 1 174 ? 14.888 -0.994 13.445 1.00 11.54 ? 174 GLY A CA 1
+ATOM 1447 C C . GLY A 1 174 ? 16.188 -1.435 12.847 1.00 11.18 ? 174 GLY A C 1
+ATOM 1448 O O . GLY A 1 174 ? 17.097 -0.636 12.618 1.00 11.32 ? 174 GLY A O 1
+ATOM 1449 N N . THR A 1 175 ? 16.261 -2.716 12.564 1.00 10.81 ? 175 THR A N 1
+ATOM 1450 C CA . THR A 1 175 ? 17.491 -3.329 12.129 1.00 10.66 ? 175 THR A CA 1
+ATOM 1451 C C . THR A 1 175 ? 17.367 -3.974 10.774 1.00 10.85 ? 175 THR A C 1
+ATOM 1452 O O . THR A 1 175 ? 16.261 -4.147 10.274 1.00 11.09 ? 175 THR A O 1
+ATOM 1453 C CB . THR A 1 175 ? 17.861 -4.455 13.166 1.00 11.46 ? 175 THR A CB 1
+ATOM 1454 O OG1 . THR A 1 175 ? 16.924 -5.534 13.087 1.00 11.86 ? 175 THR A OG1 1
+ATOM 1455 C CG2 . THR A 1 175 ? 17.958 -3.963 14.586 1.00 10.45 ? 175 THR A CG2 1
+ATOM 1456 N N . ASP A 1 176 ? 18.499 -4.410 10.211 1.00 10.92 ? 176 ASP A N 1
+ATOM 1457 C CA . ASP A 1 176 ? 18.444 -5.296 9.071 1.00 11.27 ? 176 ASP A CA 1
+ATOM 1458 C C . ASP A 1 176 ? 18.223 -6.736 9.677 1.00 12.10 ? 176 ASP A C 1
+ATOM 1459 O O . ASP A 1 176 ? 18.096 -6.893 10.907 1.00 12.09 ? 176 ASP A O 1
+ATOM 1460 C CB . ASP A 1 176 ? 19.709 -5.176 8.218 1.00 12.43 ? 176 ASP A CB 1
+ATOM 1461 C CG . ASP A 1 176 ? 20.997 -5.503 8.928 1.00 14.28 ? 176 ASP A CG 1
+ATOM 1462 O OD1 . ASP A 1 176 ? 20.945 -6.153 10.000 1.00 12.59 ? 176 ASP A OD1 1
+ATOM 1463 O OD2 . ASP A 1 176 ? 22.059 -5.109 8.421 1.00 16.57 ? 176 ASP A OD2 1
+ATOM 1464 N N . LEU A 1 177 ? 18.214 -7.776 8.839 1.00 12.56 ? 177 LEU A N 1
+ATOM 1465 C CA . LEU A 1 177 ? 17.977 -9.134 9.340 1.00 13.37 ? 177 LEU A CA 1
+ATOM 1466 C C . LEU A 1 177 ? 19.229 -9.788 9.950 1.00 14.68 ? 177 LEU A C 1
+ATOM 1467 O O . LEU A 1 177 ? 19.141 -10.901 10.466 1.00 15.23 ? 177 LEU A O 1
+ATOM 1468 C CB . LEU A 1 177 ? 17.292 -10.027 8.318 1.00 13.37 ? 177 LEU A CB 1
+ATOM 1469 C CG . LEU A 1 177 ? 15.764 -9.973 8.325 1.00 14.51 ? 177 LEU A CG 1
+ATOM 1470 C CD1 . LEU A 1 177 ? 15.215 -10.582 9.597 1.00 15.35 ? 177 LEU A CD1 1
+ATOM 1471 C CD2 . LEU A 1 177 ? 15.227 -8.547 8.101 1.00 15.65 ? 177 LEU A CD2 1
+ATOM 1472 N N . GLU A 1 178 ? 20.370 -9.083 9.938 1.00 14.29 ? 178 GLU A N 1
+ATOM 1473 C CA . GLU A 1 178 ? 21.541 -9.484 10.702 1.00 13.76 ? 178 GLU A CA 1
+ATOM 1474 C C . GLU A 1 178 ? 21.486 -8.861 12.125 1.00 13.43 ? 178 GLU A C 1
+ATOM 1475 O O . GLU A 1 178 ? 22.376 -9.100 12.928 1.00 13.86 ? 178 GLU A O 1
+ATOM 1476 C CB . GLU A 1 178 ? 22.832 -9.097 9.978 1.00 15.67 ? 178 GLU A CB 1
+ATOM 1477 C CG . GLU A 1 178 ? 22.961 -9.834 8.661 1.00 20.95 ? 178 GLU A CG 1
+ATOM 1478 C CD . GLU A 1 178 ? 24.223 -9.546 7.877 1.00 29.38 ? 178 GLU A CD 1
+ATOM 1479 O OE1 . GLU A 1 178 ? 24.984 -8.632 8.273 1.00 29.50 ? 178 GLU A OE1 1
+ATOM 1480 O OE2 . GLU A 1 178 ? 24.452 -10.242 6.861 1.00 33.24 ? 178 GLU A OE2 1
+ATOM 1481 N N . GLY A 1 179 ? 20.467 -8.044 12.419 1.00 13.13 ? 179 GLY A N 1
+ATOM 1482 C CA . GLY A 1 179 ? 20.307 -7.465 13.737 1.00 12.66 ? 179 GLY A CA 1
+ATOM 1483 C C . GLY A 1 179 ? 21.024 -6.160 13.973 1.00 12.23 ? 179 GLY A C 1
+ATOM 1484 O O . GLY A 1 179 ? 21.067 -5.710 15.109 1.00 12.53 ? 179 GLY A O 1
+ATOM 1485 N N . ASN A 1 180 ? 21.583 -5.550 12.928 1.00 11.78 ? 180 ASN A N 1
+ATOM 1486 C CA . ASN A 1 180 ? 22.268 -4.273 13.077 1.00 12.01 ? 180 ASN A CA 1
+ATOM 1487 C C . ASN A 1 180 ? 21.296 -3.149 12.821 1.00 11.40 ? 180 ASN A C 1
+ATOM 1488 O O . ASN A 1 180 ? 20.701 -3.072 11.748 1.00 10.73 ? 180 ASN A O 1
+ATOM 1489 C CB . ASN A 1 180 ? 23.447 -4.180 12.113 1.00 13.42 ? 180 ASN A CB 1
+ATOM 1490 C CG . ASN A 1 180 ? 24.560 -5.117 12.483 1.00 16.66 ? 180 ASN A CG 1
+ATOM 1491 O OD1 . ASN A 1 180 ? 25.033 -5.908 11.663 1.00 18.84 ? 180 ASN A OD1 1
+ATOM 1492 N ND2 . ASN A 1 180 ? 24.992 -5.054 13.726 1.00 16.09 ? 180 ASN A ND2 1
+ATOM 1493 N N . PHE A 1 181 ? 21.136 -2.246 13.795 1.00 11.37 ? 181 PHE A N 1
+ATOM 1494 C CA . PHE A 1 181 ? 20.248 -1.104 13.610 1.00 11.91 ? 181 PHE A CA 1
+ATOM 1495 C C . PHE A 1 181 ? 20.686 -0.235 12.452 1.00 12.38 ? 181 PHE A C 1
+ATOM 1496 O O . PHE A 1 181 ? 21.881 -0.094 12.176 1.00 12.34 ? 181 PHE A O 1
+ATOM 1497 C CB . PHE A 1 181 ? 20.201 -0.235 14.871 1.00 12.24 ? 181 PHE A CB 1
+ATOM 1498 C CG . PHE A 1 181 ? 19.085 -0.590 15.813 1.00 12.39 ? 181 PHE A CG 1
+ATOM 1499 C CD1 . PHE A 1 181 ? 19.280 -1.514 16.825 1.00 12.74 ? 181 PHE A CD1 1
+ATOM 1500 C CD2 . PHE A 1 181 ? 17.854 0.039 15.721 1.00 12.69 ? 181 PHE A CD2 1
+ATOM 1501 C CE1 . PHE A 1 181 ? 18.258 -1.822 17.714 1.00 12.99 ? 181 PHE A CE1 1
+ATOM 1502 C CE2 . PHE A 1 181 ? 16.828 -0.277 16.600 1.00 13.19 ? 181 PHE A CE2 1
+ATOM 1503 C CZ . PHE A 1 181 ? 17.031 -1.207 17.593 1.00 13.05 ? 181 PHE A CZ 1
+ATOM 1504 N N . TYR A 1 182 ? 19.702 0.341 11.784 1.00 11.78 ? 182 TYR A N 1
+ATOM 1505 C CA . TYR A 1 182 ? 19.973 1.380 10.817 1.00 12.63 ? 182 TYR A CA 1
+ATOM 1506 C C . TYR A 1 182 ? 20.218 2.634 11.653 1.00 13.60 ? 182 TYR A C 1
+ATOM 1507 O O . TYR A 1 182 ? 19.486 2.909 12.615 1.00 14.08 ? 182 TYR A O 1
+ATOM 1508 C CB . TYR A 1 182 ? 18.765 1.574 9.929 1.00 12.36 ? 182 TYR A CB 1
+ATOM 1509 C CG . TYR A 1 182 ? 18.689 0.495 8.878 1.00 12.38 ? 182 TYR A CG 1
+ATOM 1510 C CD1 . TYR A 1 182 ? 19.511 0.528 7.766 1.00 12.83 ? 182 TYR A CD1 1
+ATOM 1511 C CD2 . TYR A 1 182 ? 17.862 -0.604 9.045 1.00 12.57 ? 182 TYR A CD2 1
+ATOM 1512 C CE1 . TYR A 1 182 ? 19.456 -0.465 6.802 1.00 12.90 ? 182 TYR A CE1 1
+ATOM 1513 C CE2 . TYR A 1 182 ? 17.792 -1.601 8.089 1.00 12.93 ? 182 TYR A CE2 1
+ATOM 1514 C CZ . TYR A 1 182 ? 18.601 -1.534 6.970 1.00 13.28 ? 182 TYR A CZ 1
+ATOM 1515 O OH . TYR A 1 182 ? 18.538 -2.508 5.998 1.00 13.15 ? 182 TYR A OH 1
+ATOM 1516 N N . GLY A 1 183 ? 21.282 3.338 11.320 1.00 13.88 ? 183 GLY A N 1
+ATOM 1517 C CA . GLY A 1 183 ? 21.632 4.549 12.030 1.00 15.00 ? 183 GLY A CA 1
+ATOM 1518 C C . GLY A 1 183 ? 22.167 4.279 13.408 1.00 15.58 ? 183 GLY A C 1
+ATOM 1519 O O . GLY A 1 183 ? 22.626 3.178 13.716 1.00 15.49 ? 183 GLY A O 1
+ATOM 1520 N N . PRO A 1 184 ? 22.081 5.295 14.261 1.00 15.71 ? 184 PRO A N 1
+ATOM 1521 C CA . PRO A 1 184 ? 22.700 5.199 15.592 1.00 15.80 ? 184 PRO A CA 1
+ATOM 1522 C C . PRO A 1 184 ? 21.818 4.666 16.712 1.00 15.71 ? 184 PRO A C 1
+ATOM 1523 O O . PRO A 1 184 ? 22.202 4.708 17.880 1.00 16.85 ? 184 PRO A O 1
+ATOM 1524 C CB . PRO A 1 184 ? 23.004 6.662 15.886 1.00 16.92 ? 184 PRO A CB 1
+ATOM 1525 C CG . PRO A 1 184 ? 21.820 7.366 15.282 1.00 17.42 ? 184 PRO A CG 1
+ATOM 1526 C CD . PRO A 1 184 ? 21.576 6.658 13.991 1.00 15.87 ? 184 PRO A CD 1
+ATOM 1527 N N . PHE A 1 185 ? 20.626 4.205 16.356 1.00 15.02 ? 185 PHE A N 1
+ATOM 1528 C CA . PHE A 1 185 ? 19.631 3.816 17.322 1.00 15.08 ? 185 PHE A CA 1
+ATOM 1529 C C . PHE A 1 185 ? 19.972 2.543 18.048 1.00 15.67 ? 185 PHE A C 1
+ATOM 1530 O O . PHE A 1 185 ? 20.717 1.701 17.548 1.00 15.41 ? 185 PHE A O 1
+ATOM 1531 C CB . PHE A 1 185 ? 18.245 3.763 16.665 1.00 14.67 ? 185 PHE A CB 1
+ATOM 1532 C CG . PHE A 1 185 ? 17.918 5.097 16.038 1.00 14.96 ? 185 PHE A CG 1
+ATOM 1533 C CD1 . PHE A 1 185 ? 17.777 6.231 16.819 1.00 15.71 ? 185 PHE A CD1 1
+ATOM 1534 C CD2 . PHE A 1 185 ? 17.856 5.235 14.665 1.00 15.58 ? 185 PHE A CD2 1
+ATOM 1535 C CE1 . PHE A 1 185 ? 17.550 7.473 16.232 1.00 15.86 ? 185 PHE A CE1 1
+ATOM 1536 C CE2 . PHE A 1 185 ? 17.627 6.471 14.088 1.00 15.63 ? 185 PHE A CE2 1
+ATOM 1537 C CZ . PHE A 1 185 ? 17.450 7.580 14.874 1.00 15.37 ? 185 PHE A CZ 1
+ATOM 1538 N N . VAL A 1 186 ? 19.484 2.448 19.269 1.00 16.07 ? 186 VAL A N 1
+ATOM 1539 C CA . VAL A 1 186 ? 19.714 1.295 20.124 1.00 16.52 ? 186 VAL A CA 1
+ATOM 1540 C C . VAL A 1 186 ? 18.408 0.767 20.679 1.00 16.78 ? 186 VAL A C 1
+ATOM 1541 O O . VAL A 1 186 ? 17.436 1.513 20.778 1.00 17.71 ? 186 VAL A O 1
+ATOM 1542 C CB . VAL A 1 186 ? 20.699 1.623 21.273 1.00 17.66 ? 186 VAL A CB 1
+ATOM 1543 C CG1 . VAL A 1 186 ? 22.088 1.924 20.725 1.00 18.92 ? 186 VAL A CG1 1
+ATOM 1544 C CG2 . VAL A 1 186 ? 20.188 2.782 22.130 1.00 18.38 ? 186 VAL A CG2 1
+ATOM 1545 N N . ASP A 1 187 ? 18.386 -0.515 21.077 1.00 15.60 ? 187 ASP A N 1
+ATOM 1546 C CA . ASP A 1 187 ? 17.180 -1.106 21.642 1.00 15.58 ? 187 ASP A CA 1
+ATOM 1547 C C . ASP A 1 187 ? 17.101 -0.911 23.133 1.00 16.90 ? 187 ASP A C 1
+ATOM 1548 O O . ASP A 1 187 ? 17.132 -1.857 23.916 1.00 16.91 ? 187 ASP A O 1
+ATOM 1549 C CB . ASP A 1 187 ? 16.973 -2.565 21.246 1.00 15.08 ? 187 ASP A CB 1
+ATOM 1550 C CG . ASP A 1 187 ? 18.169 -3.478 21.361 1.00 15.13 ? 187 ASP A CG 1
+ATOM 1551 O OD1 . ASP A 1 187 ? 19.244 -3.005 21.797 1.00 15.07 ? 187 ASP A OD1 1
+ATOM 1552 O OD2 . ASP A 1 187 ? 18.030 -4.666 21.026 1.00 14.64 ? 187 ASP A OD2 1
+ATOM 1553 N N . ARG A 1 188 ? 16.993 0.352 23.513 1.00 18.27 ? 188 ARG A N 1
+ATOM 1554 C CA . ARG A 1 188 ? 16.915 0.803 24.882 1.00 20.54 ? 188 ARG A CA 1
+ATOM 1555 C C . ARG A 1 188 ? 15.979 2.000 24.892 1.00 22.19 ? 188 ARG A C 1
+ATOM 1556 O O . ARG A 1 188 ? 16.006 2.826 23.979 1.00 21.85 ? 188 ARG A O 1
+ATOM 1557 C CB . ARG A 1 188 ? 18.315 1.222 25.371 1.00 23.06 ? 188 ARG A CB 1
+ATOM 1558 C CG . ARG A 1 188 ? 18.378 1.486 26.858 1.00 28.82 ? 188 ARG A CG 1
+ATOM 1559 C CD . ARG A 1 188 ? 19.755 1.913 27.332 1.00 34.58 ? 188 ARG A CD 1
+ATOM 1560 N NE . ARG A 1 188 ? 19.637 2.726 28.541 1.00 39.48 ? 188 ARG A NE 1
+ATOM 1561 C CZ . ARG A 1 188 ? 20.650 3.073 29.325 1.00 42.92 ? 188 ARG A CZ 1
+ATOM 1562 N NH1 . ARG A 1 188 ? 21.884 2.678 29.040 1.00 43.29 ? 188 ARG A NH1 1
+ATOM 1563 N NH2 . ARG A 1 188 ? 20.434 3.803 30.412 1.00 43.34 ? 188 ARG A NH2 1
+ATOM 1564 N N . GLN A 1 189 ? 15.143 2.089 25.912 1.00 24.10 ? 189 GLN A N 1
+ATOM 1565 C CA . GLN A 1 189 ? 14.193 3.177 26.044 1.00 26.30 ? 189 GLN A CA 1
+ATOM 1566 C C . GLN A 1 189 ? 14.930 4.350 26.661 1.00 28.13 ? 189 GLN A C 1
+ATOM 1567 O O . GLN A 1 189 ? 14.955 4.501 27.883 1.00 28.84 ? 189 GLN A O 1
+ATOM 1568 C CB . GLN A 1 189 ? 13.013 2.731 26.905 1.00 28.62 ? 189 GLN A CB 1
+ATOM 1569 C CG . GLN A 1 189 ? 11.848 3.700 26.891 1.00 33.55 ? 189 GLN A CG 1
+ATOM 1570 C CD . GLN A 1 189 ? 10.793 3.236 27.855 1.00 39.90 ? 189 GLN A CD 1
+ATOM 1571 O OE1 . GLN A 1 189 ? 10.375 2.071 27.855 1.00 41.94 ? 189 GLN A OE1 1
+ATOM 1572 N NE2 . GLN A 1 189 ? 10.354 4.137 28.711 1.00 40.98 ? 189 GLN A NE2 1
+ATOM 1573 N N . THR A 1 190 ? 15.597 5.137 25.811 1.00 29.21 ? 190 THR A N 1
+ATOM 1574 C CA . THR A 1 190 ? 16.412 6.287 26.208 1.00 30.97 ? 190 THR A CA 1
+ATOM 1575 C C . THR A 1 190 ? 16.145 7.506 25.303 1.00 31.77 ? 190 THR A C 1
+ATOM 1576 O O . THR A 1 190 ? 15.420 7.392 24.308 1.00 32.40 ? 190 THR A O 1
+ATOM 1577 C CB . THR A 1 190 ? 17.915 5.902 26.162 1.00 33.71 ? 190 THR A CB 1
+ATOM 1578 O OG1 . THR A 1 190 ? 18.225 5.263 24.922 1.00 35.59 ? 190 THR A OG1 1
+ATOM 1579 C CG2 . THR A 1 190 ? 18.348 5.087 27.338 1.00 34.74 ? 190 THR A CG2 1
+ATOM 1580 N N . ALA A 1 191 ? 16.753 8.667 25.625 1.00 31.73 ? 191 ALA A N 1
+ATOM 1581 C CA . ALA A 1 191 ? 16.636 9.844 24.794 1.00 32.04 ? 191 ALA A CA 1
+ATOM 1582 C C . ALA A 1 191 ? 17.438 9.584 23.530 1.00 32.03 ? 191 ALA A C 1
+ATOM 1583 O O . ALA A 1 191 ? 18.667 9.639 23.539 1.00 33.57 ? 191 ALA A O 1
+ATOM 1584 C CB . ALA A 1 191 ? 17.189 11.058 25.515 1.00 32.37 ? 191 ALA A CB 1
+ATOM 1585 N N . GLN A 1 192 ? 16.744 9.214 22.473 1.00 30.11 ? 192 GLN A N 1
+ATOM 1586 C CA . GLN A 1 192 ? 17.362 8.979 21.185 1.00 28.86 ? 192 GLN A CA 1
+ATOM 1587 C C . GLN A 1 192 ? 16.641 9.910 20.261 1.00 28.78 ? 192 GLN A C 1
+ATOM 1588 O O . GLN A 1 192 ? 15.459 9.689 19.992 1.00 30.27 ? 192 GLN A O 1
+ATOM 1589 C CB . GLN A 1 192 ? 17.121 7.544 20.715 1.00 28.03 ? 192 GLN A CB 1
+ATOM 1590 C CG . GLN A 1 192 ? 17.466 6.488 21.725 1.00 27.39 ? 192 GLN A CG 1
+ATOM 1591 C CD . GLN A 1 192 ? 17.504 5.185 21.001 1.00 24.21 ? 192 GLN A CD 1
+ATOM 1592 O OE1 . GLN A 1 192 ? 18.318 5.000 20.097 1.00 22.45 ? 192 GLN A OE1 1
+ATOM 1593 N NE2 . GLN A 1 192 ? 16.608 4.276 21.359 1.00 23.00 ? 192 GLN A NE2 1
+ATOM 1594 N N . ALA A 1 193 ? 17.306 10.977 19.816 1.00 27.11 ? 193 ALA A N 1
+ATOM 1595 C CA . ALA A 1 193 ? 16.657 11.916 18.912 1.00 26.29 ? 193 ALA A CA 1
+ATOM 1596 C C . ALA A 1 193 ? 17.154 11.718 17.499 1.00 25.22 ? 193 ALA A C 1
+ATOM 1597 O O . ALA A 1 193 ? 18.320 11.376 17.282 1.00 25.57 ? 193 ALA A O 1
+ATOM 1598 C CB . ALA A 1 193 ? 16.894 13.340 19.361 1.00 26.29 ? 193 ALA A CB 1
+ATOM 1599 N N . ALA A 1 194 ? 16.261 11.895 16.535 1.00 23.81 ? 194 ALA A N 1
+ATOM 1600 C CA . ALA A 1 194 ? 16.617 11.758 15.133 1.00 22.55 ? 194 ALA A CA 1
+ATOM 1601 C C . ALA A 1 194 ? 17.257 13.041 14.614 1.00 20.69 ? 194 ALA A C 1
+ATOM 1602 O O . ALA A 1 194 ? 16.939 14.141 15.065 1.00 20.78 ? 194 ALA A O 1
+ATOM 1603 C CB . ALA A 1 194 ? 15.384 11.422 14.309 1.00 22.80 ? 194 ALA A CB 1
+ATOM 1604 N N . GLY A 1 195 ? 18.140 12.891 13.641 1.00 18.81 ? 195 GLY A N 1
+ATOM 1605 C CA . GLY A 1 195 ? 18.752 14.027 12.981 1.00 18.20 ? 195 GLY A CA 1
+ATOM 1606 C C . GLY A 1 195 ? 17.782 14.641 11.989 1.00 17.45 ? 195 GLY A C 1
+ATOM 1607 O O . GLY A 1 195 ? 16.600 14.274 11.937 1.00 17.25 ? 195 GLY A O 1
+ATOM 1608 N N . THR A 1 196 ? 18.293 15.530 11.144 1.00 16.59 ? 196 THR A N 1
+ATOM 1609 C CA . THR A 1 196 ? 17.483 16.239 10.165 1.00 16.96 ? 196 THR A CA 1
+ATOM 1610 C C . THR A 1 196 ? 16.846 15.288 9.210 1.00 17.50 ? 196 THR A C 1
+ATOM 1611 O O . THR A 1 196 ? 17.541 14.425 8.663 1.00 17.04 ? 196 THR A O 1
+ATOM 1612 C CB . THR A 1 196 ? 18.339 17.238 9.386 1.00 18.41 ? 196 THR A CB 1
+ATOM 1613 O OG1 . THR A 1 196 ? 19.041 18.066 10.303 1.00 19.49 ? 196 THR A OG1 1
+ATOM 1614 C CG2 . THR A 1 196 ? 17.516 18.113 8.465 1.00 19.24 ? 196 THR A CG2 1
+ATOM 1615 N N . ASP A 1 197 ? 15.517 15.412 9.024 1.00 17.89 ? 197 ASP A N 1
+ATOM 1616 C CA . ASP A 1 197 ? 14.850 14.565 8.047 1.00 18.28 ? 197 ASP A CA 1
+ATOM 1617 C C . ASP A 1 197 ? 14.922 15.240 6.692 1.00 17.83 ? 197 ASP A C 1
+ATOM 1618 O O . ASP A 1 197 ? 13.995 15.929 6.257 1.00 20.27 ? 197 ASP A O 1
+ATOM 1619 C CB . ASP A 1 197 ? 13.431 14.139 8.441 1.00 20.37 ? 197 ASP A CB 1
+ATOM 1620 C CG . ASP A 1 197 ? 12.899 12.932 7.682 1.00 23.82 ? 197 ASP A CG 1
+ATOM 1621 O OD1 . ASP A 1 197 ? 13.654 12.353 6.864 1.00 20.44 ? 197 ASP A OD1 1
+ATOM 1622 O OD2 . ASP A 1 197 ? 11.747 12.542 7.934 1.00 28.73 ? 197 ASP A OD2 1
+ATOM 1623 N N A THR A 1 198 ? 16.073 15.084 6.036 0.50 16.35 ? 198 THR A N 1
+ATOM 1624 N N B THR A 1 198 ? 16.027 14.973 6.021 0.50 16.18 ? 198 THR A N 1
+ATOM 1625 C CA A THR A 1 198 ? 16.273 15.688 4.726 0.50 15.97 ? 198 THR A CA 1
+ATOM 1626 C CA B THR A 1 198 ? 16.431 15.485 4.722 0.50 15.73 ? 198 THR A CA 1
+ATOM 1627 C C A THR A 1 198 ? 15.435 14.991 3.669 0.50 15.27 ? 198 THR A C 1
+ATOM 1628 C C B THR A 1 198 ? 15.577 14.886 3.597 0.50 15.16 ? 198 THR A C 1
+ATOM 1629 O O A THR A 1 198 ? 14.972 13.861 3.855 0.50 15.28 ? 198 THR A O 1
+ATOM 1630 O O B THR A 1 198 ? 15.248 13.702 3.663 0.50 15.19 ? 198 THR A O 1
+ATOM 1631 C CB A THR A 1 198 ? 17.753 15.778 4.371 0.50 17.51 ? 198 THR A CB 1
+ATOM 1632 C CB B THR A 1 198 ? 17.918 15.133 4.570 0.50 16.74 ? 198 THR A CB 1
+ATOM 1633 O OG1 A THR A 1 198 ? 18.310 14.471 4.399 0.50 18.42 ? 198 THR A OG1 1
+ATOM 1634 O OG1 B THR A 1 198 ? 18.659 15.683 5.672 0.50 17.41 ? 198 THR A OG1 1
+ATOM 1635 C CG2 A THR A 1 198 ? 18.524 16.703 5.296 0.50 17.78 ? 198 THR A CG2 1
+ATOM 1636 C CG2 B THR A 1 198 ? 18.499 15.622 3.285 0.50 17.17 ? 198 THR A CG2 1
+ATOM 1637 N N . THR A 1 199 ? 15.201 15.692 2.578 1.00 14.19 ? 199 THR A N 1
+ATOM 1638 C CA . THR A 1 199 ? 14.404 15.175 1.472 1.00 13.47 ? 199 THR A CA 1
+ATOM 1639 C C . THR A 1 199 ? 15.302 14.448 0.475 1.00 12.86 ? 199 THR A C 1
+ATOM 1640 O O . THR A 1 199 ? 16.404 14.913 0.194 1.00 13.34 ? 199 THR A O 1
+ATOM 1641 C CB . THR A 1 199 ? 13.546 16.279 0.859 1.00 14.60 ? 199 THR A CB 1
+ATOM 1642 O OG1 . THR A 1 199 ? 12.711 16.839 1.874 1.00 15.22 ? 199 THR A OG1 1
+ATOM 1643 C CG2 . THR A 1 199 ? 12.667 15.765 -0.281 1.00 15.03 ? 199 THR A CG2 1
+ATOM 1644 N N . ILE A 1 200 ? 14.861 13.264 -0.011 1.00 12.06 ? 200 ILE A N 1
+ATOM 1645 C CA . ILE A 1 200 ? 15.633 12.442 -0.950 1.00 12.31 ? 200 ILE A CA 1
+ATOM 1646 C C . ILE A 1 200 ? 15.432 12.991 -2.363 1.00 11.85 ? 200 ILE A C 1
+ATOM 1647 O O . ILE A 1 200 ? 14.510 12.616 -3.089 1.00 11.58 ? 200 ILE A O 1
+ATOM 1648 C CB . ILE A 1 200 ? 15.218 10.951 -0.852 1.00 12.52 ? 200 ILE A CB 1
+ATOM 1649 C CG1 . ILE A 1 200 ? 15.204 10.474 0.626 1.00 12.89 ? 200 ILE A CG1 1
+ATOM 1650 C CG2 . ILE A 1 200 ? 16.162 10.099 -1.689 1.00 12.93 ? 200 ILE A CG2 1
+ATOM 1651 C CD1 . ILE A 1 200 ? 14.183 9.365 0.910 1.00 14.24 ? 200 ILE A CD1 1
+ATOM 1652 N N . THR A 1 201 ? 16.317 13.911 -2.732 1.00 11.75 ? 201 THR A N 1
+ATOM 1653 C CA . THR A 1 201 ? 16.264 14.631 -3.995 1.00 12.03 ? 201 THR A CA 1
+ATOM 1654 C C . THR A 1 201 ? 16.083 13.743 -5.217 1.00 12.46 ? 201 THR A C 1
+ATOM 1655 O O . THR A 1 201 ? 15.218 14.024 -6.052 1.00 13.25 ? 201 THR A O 1
+ATOM 1656 C CB . THR A 1 201 ? 17.526 15.476 -4.150 1.00 13.15 ? 201 THR A CB 1
+ATOM 1657 O OG1 . THR A 1 201 ? 17.749 16.207 -2.951 1.00 13.77 ? 201 THR A OG1 1
+ATOM 1658 C CG2 . THR A 1 201 ? 17.479 16.386 -5.360 1.00 14.00 ? 201 THR A CG2 1
+ATOM 1659 N N . VAL A 1 202 ? 16.888 12.675 -5.341 1.00 11.54 ? 202 VAL A N 1
+ATOM 1660 C CA . VAL A 1 202 ? 16.798 11.804 -6.519 1.00 12.15 ? 202 VAL A CA 1
+ATOM 1661 C C . VAL A 1 202 ? 15.402 11.170 -6.634 1.00 12.21 ? 202 VAL A C 1
+ATOM 1662 O O . VAL A 1 202 ? 14.899 10.999 -7.736 1.00 12.15 ? 202 VAL A O 1
+ATOM 1663 C CB . VAL A 1 202 ? 17.929 10.751 -6.579 1.00 13.19 ? 202 VAL A CB 1
+ATOM 1664 C CG1 . VAL A 1 202 ? 17.770 9.698 -5.480 1.00 14.16 ? 202 VAL A CG1 1
+ATOM 1665 C CG2 . VAL A 1 202 ? 18.012 10.102 -7.959 1.00 14.05 ? 202 VAL A CG2 1
+ATOM 1666 N N . ASN A 1 203 ? 14.756 10.889 -5.487 1.00 12.28 ? 203 ASN A N 1
+ATOM 1667 C CA . ASN A 1 203 ? 13.419 10.315 -5.495 1.00 12.14 ? 203 ASN A CA 1
+ATOM 1668 C C . ASN A 1 203 ? 12.385 11.343 -5.906 1.00 12.09 ? 203 ASN A C 1
+ATOM 1669 O O . ASN A 1 203 ? 11.470 11.014 -6.664 1.00 12.27 ? 203 ASN A O 1
+ATOM 1670 C CB . ASN A 1 203 ? 13.086 9.747 -4.116 1.00 12.23 ? 203 ASN A CB 1
+ATOM 1671 C CG . ASN A 1 203 ? 13.839 8.482 -3.781 1.00 12.94 ? 203 ASN A CG 1
+ATOM 1672 O OD1 . ASN A 1 203 ? 14.704 8.031 -4.528 1.00 12.49 ? 203 ASN A OD1 1
+ATOM 1673 N ND2 . ASN A 1 203 ? 13.543 7.903 -2.603 1.00 12.93 ? 203 ASN A ND2 1
+ATOM 1674 N N . VAL A 1 204 ? 12.549 12.612 -5.486 1.00 11.53 ? 204 VAL A N 1
+ATOM 1675 C CA . VAL A 1 204 ? 11.614 13.665 -5.908 1.00 11.74 ? 204 VAL A CA 1
+ATOM 1676 C C . VAL A 1 204 ? 11.696 13.853 -7.408 1.00 12.06 ? 204 VAL A C 1
+ATOM 1677 O O . VAL A 1 204 ? 10.667 13.959 -8.069 1.00 12.65 ? 204 VAL A O 1
+ATOM 1678 C CB . VAL A 1 204 ? 11.899 14.998 -5.193 1.00 12.37 ? 204 VAL A CB 1
+ATOM 1679 C CG1 . VAL A 1 204 ? 10.971 16.096 -5.711 1.00 12.86 ? 204 VAL A CG1 1
+ATOM 1680 C CG2 . VAL A 1 204 ? 11.731 14.836 -3.687 1.00 11.91 ? 204 VAL A CG2 1
+ATOM 1681 N N . LEU A 1 205 ? 12.920 13.831 -7.961 1.00 11.62 ? 205 LEU A N 1
+ATOM 1682 C CA . LEU A 1 205 ? 13.080 13.980 -9.409 1.00 11.61 ? 205 LEU A CA 1
+ATOM 1683 C C . LEU A 1 205 ? 12.439 12.817 -10.129 1.00 12.03 ? 205 LEU A C 1
+ATOM 1684 O O . LEU A 1 205 ? 11.742 13.024 -11.120 1.00 11.50 ? 205 LEU A O 1
+ATOM 1685 C CB . LEU A 1 205 ? 14.560 14.080 -9.785 1.00 11.82 ? 205 LEU A CB 1
+ATOM 1686 C CG . LEU A 1 205 ? 15.223 15.375 -9.349 1.00 12.51 ? 205 LEU A CG 1
+ATOM 1687 C CD1 . LEU A 1 205 ? 16.733 15.246 -9.360 1.00 13.36 ? 205 LEU A CD1 1
+ATOM 1688 C CD2 . LEU A 1 205 ? 14.733 16.542 -10.186 1.00 13.75 ? 205 LEU A CD2 1
+ATOM 1689 N N . ALA A 1 206 ? 12.630 11.587 -9.620 1.00 12.01 ? 206 ALA A N 1
+ATOM 1690 C CA . ALA A 1 206 ? 12.019 10.411 -10.254 1.00 12.58 ? 206 ALA A CA 1
+ATOM 1691 C C . ALA A 1 206 ? 10.483 10.546 -10.260 1.00 13.06 ? 206 ALA A C 1
+ATOM 1692 O O . ALA A 1 206 ? 9.841 10.284 -11.270 1.00 12.97 ? 206 ALA A O 1
+ATOM 1693 C CB . ALA A 1 206 ? 12.426 9.154 -9.509 1.00 13.02 ? 206 ALA A CB 1
+ATOM 1694 N N . TRP A 1 207 ? 9.924 11.046 -9.151 1.00 12.31 ? 207 TRP A N 1
+ATOM 1695 C CA . TRP A 1 207 ? 8.484 11.237 -9.044 1.00 12.72 ? 207 TRP A CA 1
+ATOM 1696 C C . TRP A 1 207 ? 7.993 12.353 -9.993 1.00 12.88 ? 207 TRP A C 1
+ATOM 1697 O O . TRP A 1 207 ? 6.919 12.226 -10.565 1.00 13.64 ? 207 TRP A O 1
+ATOM 1698 C CB . TRP A 1 207 ? 8.134 11.468 -7.574 1.00 13.10 ? 207 TRP A CB 1
+ATOM 1699 C CG . TRP A 1 207 ? 6.764 11.990 -7.302 1.00 13.61 ? 207 TRP A CG 1
+ATOM 1700 C CD1 . TRP A 1 207 ? 5.613 11.271 -7.141 1.00 14.89 ? 207 TRP A CD1 1
+ATOM 1701 C CD2 . TRP A 1 207 ? 6.432 13.349 -7.037 1.00 13.53 ? 207 TRP A CD2 1
+ATOM 1702 N NE1 . TRP A 1 207 ? 4.581 12.114 -6.796 1.00 15.38 ? 207 TRP A NE1 1
+ATOM 1703 C CE2 . TRP A 1 207 ? 5.061 13.396 -6.721 1.00 14.69 ? 207 TRP A CE2 1
+ATOM 1704 C CE3 . TRP A 1 207 ? 7.177 14.530 -6.990 1.00 14.59 ? 207 TRP A CE3 1
+ATOM 1705 C CZ2 . TRP A 1 207 ? 4.421 14.585 -6.382 1.00 15.53 ? 207 TRP A CZ2 1
+ATOM 1706 C CZ3 . TRP A 1 207 ? 6.536 15.709 -6.670 1.00 15.61 ? 207 TRP A CZ3 1
+ATOM 1707 C CH2 . TRP A 1 207 ? 5.175 15.729 -6.384 1.00 15.54 ? 207 TRP A CH2 1
+ATOM 1708 N N . LEU A 1 208 ? 8.814 13.381 -10.235 1.00 12.37 ? 208 LEU A N 1
+ATOM 1709 C CA . LEU A 1 208 ? 8.452 14.412 -11.218 1.00 12.13 ? 208 LEU A CA 1
+ATOM 1710 C C . LEU A 1 208 ? 8.433 13.799 -12.619 1.00 12.89 ? 208 LEU A C 1
+ATOM 1711 O O . LEU A 1 208 ? 7.538 14.110 -13.409 1.00 13.49 ? 208 LEU A O 1
+ATOM 1712 C CB . LEU A 1 208 ? 9.446 15.566 -11.142 1.00 11.68 ? 208 LEU A CB 1
+ATOM 1713 C CG . LEU A 1 208 ? 9.330 16.445 -9.891 1.00 13.13 ? 208 LEU A CG 1
+ATOM 1714 C CD1 . LEU A 1 208 ? 10.419 17.506 -9.884 1.00 13.35 ? 208 LEU A CD1 1
+ATOM 1715 C CD2 . LEU A 1 208 ? 7.956 17.130 -9.824 1.00 13.49 ? 208 LEU A CD2 1
+ATOM 1716 N N . TYR A 1 209 ? 9.367 12.870 -12.916 1.00 12.85 ? 209 TYR A N 1
+ATOM 1717 C CA . TYR A 1 209 ? 9.341 12.143 -14.193 1.00 13.30 ? 209 TYR A CA 1
+ATOM 1718 C C . TYR A 1 209 ? 8.069 11.310 -14.283 1.00 14.51 ? 209 TYR A C 1
+ATOM 1719 O O . TYR A 1 209 ? 7.423 11.315 -15.316 1.00 15.06 ? 209 TYR A O 1
+ATOM 1720 C CB . TYR A 1 209 ? 10.556 11.234 -14.364 1.00 12.99 ? 209 TYR A CB 1
+ATOM 1721 C CG . TYR A 1 209 ? 11.758 11.992 -14.871 1.00 13.05 ? 209 TYR A CG 1
+ATOM 1722 C CD1 . TYR A 1 209 ? 11.814 12.446 -16.178 1.00 13.88 ? 209 TYR A CD1 1
+ATOM 1723 C CD2 . TYR A 1 209 ? 12.843 12.240 -14.048 1.00 13.62 ? 209 TYR A CD2 1
+ATOM 1724 C CE1 . TYR A 1 209 ? 12.907 13.155 -16.649 1.00 14.59 ? 209 TYR A CE1 1
+ATOM 1725 C CE2 . TYR A 1 209 ? 13.943 12.953 -14.506 1.00 14.55 ? 209 TYR A CE2 1
+ATOM 1726 C CZ . TYR A 1 209 ? 13.975 13.397 -15.814 1.00 14.96 ? 209 TYR A CZ 1
+ATOM 1727 O OH . TYR A 1 209 ? 15.049 14.115 -16.279 1.00 16.11 ? 209 TYR A OH 1
+ATOM 1728 N N . ALA A 1 210 ? 7.680 10.629 -13.183 1.00 14.89 ? 210 ALA A N 1
+ATOM 1729 C CA . ALA A 1 210 ? 6.429 9.851 -13.171 1.00 15.35 ? 210 ALA A CA 1
+ATOM 1730 C C . ALA A 1 210 ? 5.231 10.755 -13.445 1.00 16.18 ? 210 ALA A C 1
+ATOM 1731 O O . ALA A 1 210 ? 4.309 10.368 -14.163 1.00 16.64 ? 210 ALA A O 1
+ATOM 1732 C CB . ALA A 1 210 ? 6.246 9.164 -11.820 1.00 15.41 ? 210 ALA A CB 1
+ATOM 1733 N N . ALA A 1 211 ? 5.247 11.971 -12.900 1.00 15.83 ? 211 ALA A N 1
+ATOM 1734 C CA . ALA A 1 211 ? 4.178 12.927 -13.105 1.00 15.93 ? 211 ALA A CA 1
+ATOM 1735 C C . ALA A 1 211 ? 4.077 13.306 -14.578 1.00 16.27 ? 211 ALA A C 1
+ATOM 1736 O O . ALA A 1 211 ? 2.978 13.279 -15.138 1.00 17.39 ? 211 ALA A O 1
+ATOM 1737 C CB . ALA A 1 211 ? 4.407 14.152 -12.240 1.00 16.23 ? 211 ALA A CB 1
+ATOM 1738 N N . VAL A 1 212 ? 5.210 13.588 -15.237 1.00 15.64 ? 212 VAL A N 1
+ATOM 1739 C CA . VAL A 1 212 ? 5.187 13.927 -16.663 1.00 16.48 ? 212 VAL A CA 1
+ATOM 1740 C C . VAL A 1 212 ? 4.654 12.777 -17.487 1.00 18.29 ? 212 VAL A C 1
+ATOM 1741 O O . VAL A 1 212 ? 3.796 12.996 -18.351 1.00 19.31 ? 212 VAL A O 1
+ATOM 1742 C CB . VAL A 1 212 ? 6.574 14.389 -17.150 1.00 16.59 ? 212 VAL A CB 1
+ATOM 1743 C CG1 . VAL A 1 212 ? 6.583 14.581 -18.668 1.00 16.85 ? 212 VAL A CG1 1
+ATOM 1744 C CG2 . VAL A 1 212 ? 6.969 15.674 -16.451 1.00 17.06 ? 212 VAL A CG2 1
+ATOM 1745 N N . ILE A 1 213 ? 5.112 11.552 -17.202 1.00 19.03 ? 213 ILE A N 1
+ATOM 1746 C CA . ILE A 1 213 ? 4.654 10.357 -17.930 1.00 20.91 ? 213 ILE A CA 1
+ATOM 1747 C C . ILE A 1 213 ? 3.142 10.195 -17.791 1.00 23.56 ? 213 ILE A C 1
+ATOM 1748 O O . ILE A 1 213 ? 2.457 9.941 -18.777 1.00 24.76 ? 213 ILE A O 1
+ATOM 1749 C CB . ILE A 1 213 ? 5.416 9.109 -17.418 1.00 21.25 ? 213 ILE A CB 1
+ATOM 1750 C CG1 . ILE A 1 213 ? 6.904 9.189 -17.803 1.00 21.73 ? 213 ILE A CG1 1
+ATOM 1751 C CG2 . ILE A 1 213 ? 4.783 7.803 -17.918 1.00 21.99 ? 213 ILE A CG2 1
+ATOM 1752 C CD1 . ILE A 1 213 ? 7.788 8.246 -17.083 1.00 22.87 ? 213 ILE A CD1 1
+ATOM 1753 N N . ASN A 1 214 ? 2.620 10.439 -16.588 1.00 24.22 ? 214 ASN A N 1
+ATOM 1754 C CA . ASN A 1 214 ? 1.204 10.282 -16.300 1.00 26.05 ? 214 ASN A CA 1
+ATOM 1755 C C . ASN A 1 214 ? 0.343 11.544 -16.522 1.00 27.69 ? 214 ASN A C 1
+ATOM 1756 O O . ASN A 1 214 ? -0.799 11.581 -16.055 1.00 29.91 ? 214 ASN A O 1
+ATOM 1757 C CB . ASN A 1 214 ? 1.016 9.716 -14.899 1.00 27.31 ? 214 ASN A CB 1
+ATOM 1758 C CG . ASN A 1 214 ? 1.479 8.279 -14.822 1.00 30.24 ? 214 ASN A CG 1
+ATOM 1759 O OD1 . ASN A 1 214 ? 0.744 7.346 -15.163 1.00 32.47 ? 214 ASN A OD1 1
+ATOM 1760 N ND2 . ASN A 1 214 ? 2.714 8.047 -14.430 1.00 29.78 ? 214 ASN A ND2 1
+ATOM 1761 N N . GLY A 1 215 ? 0.848 12.529 -17.260 1.00 26.51 ? 215 GLY A N 1
+ATOM 1762 C CA . GLY A 1 215 ? 0.065 13.709 -17.623 1.00 26.05 ? 215 GLY A CA 1
+ATOM 1763 C C . GLY A 1 215 ? 0.186 15.021 -16.870 1.00 24.55 ? 215 GLY A C 1
+ATOM 1764 O O . GLY A 1 215 ? -0.239 16.059 -17.380 1.00 25.20 ? 215 GLY A O 1
+ATOM 1765 N N A ASP A 1 216 ? 0.744 14.999 -15.654 0.50 23.04 ? 216 ASP A N 1
+ATOM 1766 N N B ASP A 1 216 ? 0.748 14.992 -15.660 0.50 23.39 ? 216 ASP A N 1
+ATOM 1767 C CA A ASP A 1 216 ? 0.891 16.222 -14.868 0.50 22.25 ? 216 ASP A CA 1
+ATOM 1768 C CA B ASP A 1 216 ? 0.909 16.203 -14.862 0.50 22.94 ? 216 ASP A CA 1
+ATOM 1769 C C A ASP A 1 216 ? 2.182 16.909 -15.280 0.50 22.70 ? 216 ASP A C 1
+ATOM 1770 C C B ASP A 1 216 ? 2.192 16.893 -15.307 0.50 23.02 ? 216 ASP A C 1
+ATOM 1771 O O A ASP A 1 216 ? 3.265 16.409 -14.988 0.50 23.46 ? 216 ASP A O 1
+ATOM 1772 O O B ASP A 1 216 ? 3.280 16.379 -15.060 0.50 23.77 ? 216 ASP A O 1
+ATOM 1773 C CB A ASP A 1 216 ? 0.863 15.910 -13.369 0.50 22.37 ? 216 ASP A CB 1
+ATOM 1774 C CB B ASP A 1 216 ? 0.959 15.849 -13.368 0.50 24.09 ? 216 ASP A CB 1
+ATOM 1775 C CG A ASP A 1 216 ? -0.442 15.298 -12.907 0.50 24.19 ? 216 ASP A CG 1
+ATOM 1776 C CG B ASP A 1 216 ? -0.170 16.456 -12.563 0.50 27.89 ? 216 ASP A CG 1
+ATOM 1777 O OD1 A ASP A 1 216 ? -1.477 15.540 -13.561 0.50 24.19 ? 216 ASP A OD1 1
+ATOM 1778 O OD1 B ASP A 1 216 ? -0.595 17.580 -12.895 0.50 28.66 ? 216 ASP A OD1 1
+ATOM 1779 O OD2 A ASP A 1 216 ? -0.430 14.579 -11.889 0.50 25.07 ? 216 ASP A OD2 1
+ATOM 1780 O OD2 B ASP A 1 216 ? -0.618 15.812 -11.589 0.50 29.52 ? 216 ASP A OD2 1
+ATOM 1781 N N . ARG A 1 217 ? 2.073 18.016 -16.019 1.00 21.99 ? 217 ARG A N 1
+ATOM 1782 C CA . ARG A 1 217 ? 3.233 18.713 -16.564 1.00 20.81 ? 217 ARG A CA 1
+ATOM 1783 C C . ARG A 1 217 ? 3.263 20.218 -16.299 1.00 19.92 ? 217 ARG A C 1
+ATOM 1784 O O . ARG A 1 217 ? 4.105 20.898 -16.881 1.00 19.51 ? 217 ARG A O 1
+ATOM 1785 C CB . ARG A 1 217 ? 3.252 18.535 -18.107 0.50 21.37 ? 217 ARG A CB 1
+ATOM 1786 C CG . ARG A 1 217 ? 2.978 17.127 -18.645 0.50 23.57 ? 217 ARG A CG 1
+ATOM 1787 C CD . ARG A 1 217 ? 2.523 17.152 -20.100 0.50 25.14 ? 217 ARG A CD 1
+ATOM 1788 N NE . ARG A 1 217 ? 3.525 17.746 -20.981 0.50 25.70 ? 217 ARG A NE 1
+ATOM 1789 C CZ . ARG A 1 217 ? 4.427 17.041 -21.650 0.50 25.29 ? 217 ARG A CZ 1
+ATOM 1790 N NH1 . ARG A 1 217 ? 5.318 17.652 -22.418 0.50 24.48 ? 217 ARG A NH1 1
+ATOM 1791 N NH2 . ARG A 1 217 ? 4.448 15.719 -21.555 0.50 23.66 ? 217 ARG A NH2 1
+ATOM 1792 N N . TRP A 1 218 ? 2.347 20.759 -15.483 1.00 19.50 ? 218 TRP A N 1
+ATOM 1793 C CA . TRP A 1 218 ? 2.290 22.214 -15.276 1.00 19.27 ? 218 TRP A CA 1
+ATOM 1794 C C . TRP A 1 218 ? 3.589 22.829 -14.740 1.00 19.18 ? 218 TRP A C 1
+ATOM 1795 O O . TRP A 1 218 ? 3.833 24.006 -14.958 1.00 19.69 ? 218 TRP A O 1
+ATOM 1796 C CB . TRP A 1 218 ? 1.102 22.617 -14.384 1.00 19.08 ? 218 TRP A CB 1
+ATOM 1797 C CG . TRP A 1 218 ? 1.172 22.070 -12.987 1.00 18.92 ? 218 TRP A CG 1
+ATOM 1798 C CD1 . TRP A 1 218 ? 0.547 20.956 -12.513 1.00 19.63 ? 218 TRP A CD1 1
+ATOM 1799 C CD2 . TRP A 1 218 ? 1.858 22.655 -11.864 1.00 19.21 ? 218 TRP A CD2 1
+ATOM 1800 N NE1 . TRP A 1 218 ? 0.866 20.766 -11.187 1.00 19.83 ? 218 TRP A NE1 1
+ATOM 1801 C CE2 . TRP A 1 218 ? 1.651 21.805 -10.761 1.00 19.68 ? 218 TRP A CE2 1
+ATOM 1802 C CE3 . TRP A 1 218 ? 2.647 23.803 -11.692 1.00 19.71 ? 218 TRP A CE3 1
+ATOM 1803 C CZ2 . TRP A 1 218 ? 2.230 22.048 -9.514 1.00 19.83 ? 218 TRP A CZ2 1
+ATOM 1804 C CZ3 . TRP A 1 218 ? 3.229 24.034 -10.460 1.00 20.19 ? 218 TRP A CZ3 1
+ATOM 1805 C CH2 . TRP A 1 218 ? 3.000 23.174 -9.383 1.00 20.04 ? 218 TRP A CH2 1
+ATOM 1806 N N . PHE A 1 219 ? 4.383 22.040 -14.003 1.00 18.30 ? 219 PHE A N 1
+ATOM 1807 C CA . PHE A 1 219 ? 5.624 22.483 -13.356 1.00 17.79 ? 219 PHE A CA 1
+ATOM 1808 C C . PHE A 1 219 ? 6.842 22.530 -14.276 1.00 18.51 ? 219 PHE A C 1
+ATOM 1809 O O . PHE A 1 219 ? 7.911 22.994 -13.861 1.00 18.69 ? 219 PHE A O 1
+ATOM 1810 C CB . PHE A 1 219 ? 5.920 21.590 -12.136 1.00 16.65 ? 219 PHE A CB 1
+ATOM 1811 C CG . PHE A 1 219 ? 5.997 20.133 -12.506 1.00 15.65 ? 219 PHE A CG 1
+ATOM 1812 C CD1 . PHE A 1 219 ? 7.163 19.591 -13.018 1.00 15.83 ? 219 PHE A CD1 1
+ATOM 1813 C CD2 . PHE A 1 219 ? 4.885 19.316 -12.400 1.00 15.39 ? 219 PHE A CD2 1
+ATOM 1814 C CE1 . PHE A 1 219 ? 7.210 18.266 -13.417 1.00 15.82 ? 219 PHE A CE1 1
+ATOM 1815 C CE2 . PHE A 1 219 ? 4.956 17.985 -12.749 1.00 15.80 ? 219 PHE A CE2 1
+ATOM 1816 C CZ . PHE A 1 219 ? 6.103 17.475 -13.293 1.00 15.51 ? 219 PHE A CZ 1
+ATOM 1817 N N . LEU A 1 220 ? 6.703 22.044 -15.520 1.00 18.09 ? 220 LEU A N 1
+ATOM 1818 C CA . LEU A 1 220 ? 7.800 22.117 -16.472 1.00 19.03 ? 220 LEU A CA 1
+ATOM 1819 C C . LEU A 1 220 ? 7.971 23.571 -16.859 1.00 20.12 ? 220 LEU A C 1
+ATOM 1820 O O . LEU A 1 220 ? 6.988 24.309 -16.991 1.00 20.85 ? 220 LEU A O 1
+ATOM 1821 C CB . LEU A 1 220 ? 7.525 21.266 -17.709 1.00 19.05 ? 220 LEU A CB 1
+ATOM 1822 C CG . LEU A 1 220 ? 7.424 19.768 -17.467 1.00 19.56 ? 220 LEU A CG 1
+ATOM 1823 C CD1 . LEU A 1 220 ? 7.122 19.044 -18.764 1.00 19.47 ? 220 LEU A CD1 1
+ATOM 1824 C CD2 . LEU A 1 220 ? 8.694 19.212 -16.777 1.00 20.00 ? 220 LEU A CD2 1
+ATOM 1825 N N . ASN A 1 221 ? 9.214 23.996 -16.965 1.00 20.10 ? 221 ASN A N 1
+ATOM 1826 C CA . ASN A 1 221 ? 9.510 25.383 -17.252 1.00 20.10 ? 221 ASN A CA 1
+ATOM 1827 C C . ASN A 1 221 ? 10.545 25.542 -18.362 1.00 19.74 ? 221 ASN A C 1
+ATOM 1828 O O . ASN A 1 221 ? 11.001 24.563 -18.944 1.00 20.14 ? 221 ASN A O 1
+ATOM 1829 C CB . ASN A 1 221 ? 9.905 26.097 -15.960 1.00 20.92 ? 221 ASN A CB 1
+ATOM 1830 C CG . ASN A 1 221 ? 11.146 25.546 -15.329 1.00 23.14 ? 221 ASN A CG 1
+ATOM 1831 O OD1 . ASN A 1 221 ? 12.101 25.106 -15.998 1.00 22.57 ? 221 ASN A OD1 1
+ATOM 1832 N ND2 . ASN A 1 221 ? 11.167 25.582 -14.017 1.00 23.81 ? 221 ASN A ND2 1
+ATOM 1833 N N . ARG A 1 222 ? 10.877 26.784 -18.683 1.00 18.88 ? 222 ARG A N 1
+ATOM 1834 C CA . ARG A 1 222 ? 11.832 27.102 -19.726 1.00 18.93 ? 222 ARG A CA 1
+ATOM 1835 C C . ARG A 1 222 ? 13.271 27.127 -19.238 1.00 18.41 ? 222 ARG A C 1
+ATOM 1836 O O . ARG A 1 222 ? 14.134 27.579 -19.982 1.00 18.72 ? 222 ARG A O 1
+ATOM 1837 C CB . ARG A 1 222 ? 11.491 28.498 -20.253 1.00 20.02 ? 222 ARG A CB 1
+ATOM 1838 C CG . ARG A 1 222 ? 10.094 28.584 -20.823 1.00 23.44 ? 222 ARG A CG 1
+ATOM 1839 C CD . ARG A 1 222 ? 9.746 29.989 -21.277 1.00 26.45 ? 222 ARG A CD 1
+ATOM 1840 N NE . ARG A 1 222 ? 8.499 29.999 -22.037 1.00 28.59 ? 222 ARG A NE 1
+ATOM 1841 C CZ . ARG A 1 222 ? 8.402 29.730 -23.335 1.00 31.63 ? 222 ARG A CZ 1
+ATOM 1842 N NH1 . ARG A 1 222 ? 9.488 29.449 -24.047 1.00 31.12 ? 222 ARG A NH1 1
+ATOM 1843 N NH2 . ARG A 1 222 ? 7.218 29.741 -23.933 1.00 31.84 ? 222 ARG A NH2 1
+ATOM 1844 N N . PHE A 1 223 ? 13.552 26.663 -18.016 1.00 17.24 ? 223 PHE A N 1
+ATOM 1845 C CA . PHE A 1 223 ? 14.877 26.810 -17.437 1.00 17.43 ? 223 PHE A CA 1
+ATOM 1846 C C . PHE A 1 223 ? 15.704 25.551 -17.362 1.00 15.35 ? 223 PHE A C 1
+ATOM 1847 O O . PHE A 1 223 ? 15.192 24.438 -17.466 1.00 15.55 ? 223 PHE A O 1
+ATOM 1848 C CB . PHE A 1 223 ? 14.761 27.413 -16.009 1.00 18.71 ? 223 PHE A CB 1
+ATOM 1849 C CG . PHE A 1 223 ? 13.758 28.531 -15.821 1.00 20.74 ? 223 PHE A CG 1
+ATOM 1850 C CD1 . PHE A 1 223 ? 13.624 29.530 -16.768 1.00 22.13 ? 223 PHE A CD1 1
+ATOM 1851 C CD2 . PHE A 1 223 ? 12.977 28.595 -14.684 1.00 22.23 ? 223 PHE A CD2 1
+ATOM 1852 C CE1 . PHE A 1 223 ? 12.696 30.547 -16.598 1.00 23.38 ? 223 PHE A CE1 1
+ATOM 1853 C CE2 . PHE A 1 223 ? 12.071 29.627 -14.501 1.00 23.56 ? 223 PHE A CE2 1
+ATOM 1854 C CZ . PHE A 1 223 ? 11.935 30.596 -15.459 1.00 23.59 ? 223 PHE A CZ 1
+ATOM 1855 N N . THR A 1 224 ? 17.002 25.743 -17.157 1.00 14.22 ? 224 THR A N 1
+ATOM 1856 C CA . THR A 1 224 ? 17.923 24.681 -16.819 1.00 13.87 ? 224 THR A CA 1
+ATOM 1857 C C . THR A 1 224 ? 18.777 25.156 -15.619 1.00 14.09 ? 224 THR A C 1
+ATOM 1858 O O . THR A 1 224 ? 18.645 26.293 -15.133 1.00 14.76 ? 224 THR A O 1
+ATOM 1859 C CB . THR A 1 224 ? 18.695 24.154 -18.032 1.00 14.52 ? 224 THR A CB 1
+ATOM 1860 O OG1 . THR A 1 224 ? 19.214 22.865 -17.666 1.00 14.05 ? 224 THR A OG1 1
+ATOM 1861 C CG2 . THR A 1 224 ? 19.849 25.052 -18.412 1.00 14.98 ? 224 THR A CG2 1
+ATOM 1862 N N . THR A 1 225 ? 19.601 24.275 -15.099 1.00 13.19 ? 225 THR A N 1
+ATOM 1863 C CA . THR A 1 225 ? 20.500 24.563 -14.003 1.00 13.50 ? 225 THR A CA 1
+ATOM 1864 C C . THR A 1 225 ? 21.729 23.647 -14.160 1.00 13.55 ? 225 THR A C 1
+ATOM 1865 O O . THR A 1 225 ? 21.844 22.918 -15.145 1.00 13.01 ? 225 THR A O 1
+ATOM 1866 C CB . THR A 1 225 ? 19.759 24.407 -12.648 1.00 15.53 ? 225 THR A CB 1
+ATOM 1867 O OG1 . THR A 1 225 ? 20.659 24.812 -11.628 1.00 17.08 ? 225 THR A OG1 1
+ATOM 1868 C CG2 . THR A 1 225 ? 19.333 22.975 -12.374 1.00 16.36 ? 225 THR A CG2 1
+ATOM 1869 N N . THR A 1 226 ? 22.671 23.746 -13.226 1.00 13.79 ? 226 THR A N 1
+ATOM 1870 C CA . THR A 1 226 ? 23.834 22.885 -13.142 1.00 13.97 ? 226 THR A CA 1
+ATOM 1871 C C . THR A 1 226 ? 23.718 22.116 -11.827 1.00 14.17 ? 226 THR A C 1
+ATOM 1872 O O . THR A 1 226 ? 22.936 22.501 -10.957 1.00 13.64 ? 226 THR A O 1
+ATOM 1873 C CB . THR A 1 226 ? 25.130 23.738 -13.146 1.00 16.08 ? 226 THR A CB 1
+ATOM 1874 O OG1 . THR A 1 226 ? 25.192 24.499 -11.938 1.00 16.64 ? 226 THR A OG1 1
+ATOM 1875 C CG2 . THR A 1 226 ? 25.245 24.618 -14.361 1.00 17.33 ? 226 THR A CG2 1
+ATOM 1876 N N A LEU A 1 227 ? 24.519 21.061 -11.653 0.50 14.30 ? 227 LEU A N 1
+ATOM 1877 N N B LEU A 1 227 ? 24.524 21.056 -11.640 0.50 14.01 ? 227 LEU A N 1
+ATOM 1878 C CA A LEU A 1 227 ? 24.520 20.302 -10.408 0.50 15.27 ? 227 LEU A CA 1
+ATOM 1879 C CA B LEU A 1 227 ? 24.508 20.322 -10.373 0.50 14.69 ? 227 LEU A CA 1
+ATOM 1880 C C A LEU A 1 227 ? 24.897 21.190 -9.216 0.50 15.82 ? 227 LEU A C 1
+ATOM 1881 C C B LEU A 1 227 ? 24.873 21.224 -9.206 0.50 15.51 ? 227 LEU A C 1
+ATOM 1882 O O A LEU A 1 227 ? 24.223 21.149 -8.192 0.50 16.27 ? 227 LEU A O 1
+ATOM 1883 O O B LEU A 1 227 ? 24.172 21.226 -8.197 0.50 15.90 ? 227 LEU A O 1
+ATOM 1884 C CB A LEU A 1 227 ? 25.476 19.108 -10.535 0.50 15.64 ? 227 LEU A CB 1
+ATOM 1885 C CB B LEU A 1 227 ? 25.440 19.112 -10.410 0.50 14.62 ? 227 LEU A CB 1
+ATOM 1886 C CG A LEU A 1 227 ? 25.138 17.847 -9.735 0.50 17.11 ? 227 LEU A CG 1
+ATOM 1887 C CG B LEU A 1 227 ? 24.906 17.875 -11.109 0.50 15.35 ? 227 LEU A CG 1
+ATOM 1888 C CD1 A LEU A 1 227 ? 23.676 17.439 -9.907 0.50 17.60 ? 227 LEU A CD1 1
+ATOM 1889 C CD1 B LEU A 1 227 ? 25.881 16.725 -10.955 0.50 15.25 ? 227 LEU A CD1 1
+ATOM 1890 C CD2 A LEU A 1 227 ? 26.019 16.702 -10.161 0.50 17.33 ? 227 LEU A CD2 1
+ATOM 1891 C CD2 B LEU A 1 227 ? 23.531 17.463 -10.562 0.50 15.94 ? 227 LEU A CD2 1
+ATOM 1892 N N . ASN A 1 228 ? 25.916 22.051 -9.374 1.00 15.51 ? 228 ASN A N 1
+ATOM 1893 C CA . ASN A 1 228 ? 26.326 22.950 -8.300 1.00 15.00 ? 228 ASN A CA 1
+ATOM 1894 C C . ASN A 1 228 ? 25.286 24.033 -7.986 1.00 14.90 ? 228 ASN A C 1
+ATOM 1895 O O . ASN A 1 228 ? 25.056 24.317 -6.813 1.00 15.98 ? 228 ASN A O 1
+ATOM 1896 C CB . ASN A 1 228 ? 27.700 23.551 -8.581 1.00 15.85 ? 228 ASN A CB 1
+ATOM 1897 C CG . ASN A 1 228 ? 28.840 22.550 -8.522 1.00 19.59 ? 228 ASN A CG 1
+ATOM 1898 O OD1 . ASN A 1 228 ? 29.929 22.794 -9.060 1.00 21.73 ? 228 ASN A OD1 1
+ATOM 1899 N ND2 . ASN A 1 228 ? 28.635 21.411 -7.881 1.00 20.10 ? 228 ASN A ND2 1
+ATOM 1900 N N . ASP A 1 229 ? 24.638 24.604 -9.002 1.00 14.47 ? 229 ASP A N 1
+ATOM 1901 C CA . ASP A 1 229 ? 23.626 25.638 -8.756 1.00 14.83 ? 229 ASP A CA 1
+ATOM 1902 C C . ASP A 1 229 ? 22.417 25.008 -8.087 1.00 15.00 ? 229 ASP A C 1
+ATOM 1903 O O . ASP A 1 229 ? 21.915 25.535 -7.090 1.00 15.74 ? 229 ASP A O 1
+ATOM 1904 C CB . ASP A 1 229 ? 23.213 26.348 -10.049 1.00 17.00 ? 229 ASP A CB 1
+ATOM 1905 C CG . ASP A 1 229 ? 22.101 27.337 -9.811 1.00 23.28 ? 229 ASP A CG 1
+ATOM 1906 O OD1 . ASP A 1 229 ? 22.347 28.337 -9.109 1.00 25.03 ? 229 ASP A OD1 1
+ATOM 1907 O OD2 . ASP A 1 229 ? 20.957 27.068 -10.265 1.00 24.97 ? 229 ASP A OD2 1
+ATOM 1908 N N . PHE A 1 230 ? 21.979 23.838 -8.584 1.00 14.41 ? 230 PHE A N 1
+ATOM 1909 C CA . PHE A 1 230 ? 20.850 23.142 -7.980 1.00 14.40 ? 230 PHE A CA 1
+ATOM 1910 C C . PHE A 1 230 ? 21.151 22.818 -6.516 1.00 15.23 ? 230 PHE A C 1
+ATOM 1911 O O . PHE A 1 230 ? 20.308 23.067 -5.661 1.00 16.01 ? 230 PHE A O 1
+ATOM 1912 C CB . PHE A 1 230 ? 20.527 21.845 -8.745 1.00 13.67 ? 230 PHE A CB 1
+ATOM 1913 C CG . PHE A 1 230 ? 19.422 21.092 -8.049 1.00 14.69 ? 230 PHE A CG 1
+ATOM 1914 C CD1 . PHE A 1 230 ? 18.100 21.467 -8.213 1.00 15.26 ? 230 PHE A CD1 1
+ATOM 1915 C CD2 . PHE A 1 230 ? 19.715 20.119 -7.106 1.00 15.80 ? 230 PHE A CD2 1
+ATOM 1916 C CE1 . PHE A 1 230 ? 17.088 20.834 -7.504 1.00 16.46 ? 230 PHE A CE1 1
+ATOM 1917 C CE2 . PHE A 1 230 ? 18.704 19.520 -6.370 1.00 16.25 ? 230 PHE A CE2 1
+ATOM 1918 C CZ . PHE A 1 230 ? 17.399 19.868 -6.589 1.00 16.71 ? 230 PHE A CZ 1
+ATOM 1919 N N . ASN A 1 231 ? 22.374 22.361 -6.232 1.00 15.00 ? 231 ASN A N 1
+ATOM 1920 C CA . ASN A 1 231 ? 22.758 22.003 -4.873 1.00 15.46 ? 231 ASN A CA 1
+ATOM 1921 C C . ASN A 1 231 ? 22.802 23.158 -3.914 1.00 16.96 ? 231 ASN A C 1
+ATOM 1922 O O . ASN A 1 231 ? 22.591 22.932 -2.725 1.00 17.72 ? 231 ASN A O 1
+ATOM 1923 C CB . ASN A 1 231 ? 24.050 21.215 -4.849 1.00 16.36 ? 231 ASN A CB 1
+ATOM 1924 C CG . ASN A 1 231 ? 23.829 19.796 -5.314 1.00 18.15 ? 231 ASN A CG 1
+ATOM 1925 O OD1 . ASN A 1 231 ? 22.721 19.254 -5.242 1.00 18.68 ? 231 ASN A OD1 1
+ATOM 1926 N ND2 . ASN A 1 231 ? 24.868 19.145 -5.804 1.00 19.47 ? 231 ASN A ND2 1
+ATOM 1927 N N . LEU A 1 232 ? 22.976 24.394 -4.396 1.00 17.68 ? 232 LEU A N 1
+ATOM 1928 C CA . LEU A 1 232 ? 22.885 25.567 -3.519 1.00 19.22 ? 232 LEU A CA 1
+ATOM 1929 C C . LEU A 1 232 ? 21.437 25.670 -3.002 1.00 19.67 ? 232 LEU A C 1
+ATOM 1930 O O . LEU A 1 232 ? 21.223 25.880 -1.806 1.00 20.80 ? 232 LEU A O 1
+ATOM 1931 C CB . LEU A 1 232 ? 23.257 26.842 -4.289 1.00 20.79 ? 232 LEU A CB 1
+ATOM 1932 C CG . LEU A 1 232 ? 24.717 26.974 -4.677 1.00 23.66 ? 232 LEU A CG 1
+ATOM 1933 C CD1 . LEU A 1 232 ? 24.933 28.250 -5.452 1.00 24.78 ? 232 LEU A CD1 1
+ATOM 1934 C CD2 . LEU A 1 232 ? 25.615 26.984 -3.447 1.00 24.66 ? 232 LEU A CD2 1
+ATOM 1935 N N . VAL A 1 233 ? 20.459 25.417 -3.886 1.00 18.99 ? 233 VAL A N 1
+ATOM 1936 C CA . VAL A 1 233 ? 19.045 25.406 -3.533 1.00 18.83 ? 233 VAL A CA 1
+ATOM 1937 C C . VAL A 1 233 ? 18.700 24.193 -2.684 1.00 18.78 ? 233 VAL A C 1
+ATOM 1938 O O . VAL A 1 233 ? 18.008 24.331 -1.675 1.00 19.12 ? 233 VAL A O 1
+ATOM 1939 C CB . VAL A 1 233 ? 18.177 25.464 -4.804 1.00 20.10 ? 233 VAL A CB 1
+ATOM 1940 C CG1 . VAL A 1 233 ? 16.694 25.454 -4.446 1.00 20.95 ? 233 VAL A CG1 1
+ATOM 1941 C CG2 . VAL A 1 233 ? 18.525 26.699 -5.624 1.00 20.92 ? 233 VAL A CG2 1
+ATOM 1942 N N . ALA A 1 234 ? 19.239 23.018 -3.016 1.00 18.51 ? 234 ALA A N 1
+ATOM 1943 C CA . ALA A 1 234 ? 18.996 21.802 -2.227 1.00 19.45 ? 234 ALA A CA 1
+ATOM 1944 C C . ALA A 1 234 ? 19.449 22.000 -0.771 1.00 20.44 ? 234 ALA A C 1
+ATOM 1945 O O . ALA A 1 234 ? 18.700 21.699 0.153 1.00 20.35 ? 234 ALA A O 1
+ATOM 1946 C CB . ALA A 1 234 ? 19.732 20.621 -2.849 1.00 19.88 ? 234 ALA A CB 1
+ATOM 1947 N N . MET A 1 235 ? 20.620 22.616 -0.569 1.00 20.53 ? 235 MET A N 1
+ATOM 1948 C CA . MET A 1 235 ? 21.139 22.894 0.770 1.00 21.06 ? 235 MET A CA 1
+ATOM 1949 C C . MET A 1 235 ? 20.163 23.771 1.556 1.00 19.75 ? 235 MET A C 1
+ATOM 1950 O O . MET A 1 235 ? 19.813 23.447 2.691 1.00 19.72 ? 235 MET A O 1
+ATOM 1951 C CB . MET A 1 235 ? 22.522 23.574 0.668 1.00 23.60 ? 235 MET A CB 1
+ATOM 1952 C CG . MET A 1 235 ? 23.037 24.121 1.984 1.00 29.30 ? 235 MET A CG 1
+ATOM 1953 S SD . MET A 1 235 ? 24.257 23.025 2.705 1.00 42.88 ? 235 MET A SD 1
+ATOM 1954 C CE . MET A 1 235 ? 25.589 23.247 1.552 1.00 39.42 ? 235 MET A CE 1
+ATOM 1955 N N . LYS A 1 236 ? 19.700 24.853 0.927 1.00 18.47 ? 236 LYS A N 1
+ATOM 1956 C CA . LYS A 1 236 ? 18.792 25.785 1.563 1.00 17.97 ? 236 LYS A CA 1
+ATOM 1957 C C . LYS A 1 236 ? 17.493 25.121 2.014 1.00 17.43 ? 236 LYS A C 1
+ATOM 1958 O O . LYS A 1 236 ? 16.951 25.470 3.058 1.00 18.51 ? 236 LYS A O 1
+ATOM 1959 C CB . LYS A 1 236 ? 18.530 26.978 0.623 1.00 20.89 ? 236 LYS A CB 1
+ATOM 1960 C CG . LYS A 1 236 ? 17.528 27.986 1.164 1.00 26.53 ? 236 LYS A CG 1
+ATOM 1961 C CD . LYS A 1 236 ? 17.172 29.030 0.127 1.00 33.01 ? 236 LYS A CD 1
+ATOM 1962 C CE . LYS A 1 236 ? 15.990 29.854 0.572 1.00 37.50 ? 236 LYS A CE 1
+ATOM 1963 N NZ . LYS A 1 236 ? 16.358 30.835 1.631 1.00 40.05 ? 236 LYS A NZ 1
+ATOM 1964 N N . TYR A 1 237 ? 17.020 24.124 1.260 1.00 15.66 ? 237 TYR A N 1
+ATOM 1965 C CA . TYR A 1 237 ? 15.746 23.472 1.564 1.00 14.78 ? 237 TYR A CA 1
+ATOM 1966 C C . TYR A 1 237 ? 15.852 22.109 2.238 1.00 14.96 ? 237 TYR A C 1
+ATOM 1967 O O . TYR A 1 237 ? 14.861 21.366 2.262 1.00 15.72 ? 237 TYR A O 1
+ATOM 1968 C CB . TYR A 1 237 ? 14.899 23.373 0.286 1.00 14.56 ? 237 TYR A CB 1
+ATOM 1969 C CG . TYR A 1 237 ? 14.367 24.728 -0.118 1.00 15.63 ? 237 TYR A CG 1
+ATOM 1970 C CD1 . TYR A 1 237 ? 13.223 25.245 0.467 1.00 16.68 ? 237 TYR A CD1 1
+ATOM 1971 C CD2 . TYR A 1 237 ? 15.067 25.534 -1.005 1.00 16.39 ? 237 TYR A CD2 1
+ATOM 1972 C CE1 . TYR A 1 237 ? 12.778 26.527 0.169 1.00 17.54 ? 237 TYR A CE1 1
+ATOM 1973 C CE2 . TYR A 1 237 ? 14.617 26.808 -1.333 1.00 16.88 ? 237 TYR A CE2 1
+ATOM 1974 C CZ . TYR A 1 237 ? 13.486 27.312 -0.721 1.00 18.39 ? 237 TYR A CZ 1
+ATOM 1975 O OH . TYR A 1 237 ? 13.013 28.560 -1.046 1.00 19.90 ? 237 TYR A OH 1
+ATOM 1976 N N A ASN A 1 238 ? 17.029 21.783 2.777 0.50 14.71 ? 238 ASN A N 1
+ATOM 1977 N N B ASN A 1 238 ? 17.031 21.780 2.788 0.50 14.49 ? 238 ASN A N 1
+ATOM 1978 C CA A ASN A 1 238 ? 17.254 20.514 3.458 0.50 15.20 ? 238 ASN A CA 1
+ATOM 1979 C CA B ASN A 1 238 ? 17.284 20.504 3.467 0.50 14.74 ? 238 ASN A CA 1
+ATOM 1980 C C A ASN A 1 238 ? 16.986 19.323 2.549 0.50 14.96 ? 238 ASN A C 1
+ATOM 1981 C C B ASN A 1 238 ? 17.054 19.295 2.568 0.50 14.80 ? 238 ASN A C 1
+ATOM 1982 O O A ASN A 1 238 ? 16.317 18.373 2.941 0.50 15.04 ? 238 ASN A O 1
+ATOM 1983 O O B ASN A 1 238 ? 16.509 18.281 3.000 0.50 14.95 ? 238 ASN A O 1
+ATOM 1984 C CB A ASN A 1 238 ? 16.460 20.437 4.761 0.50 17.13 ? 238 ASN A CB 1
+ATOM 1985 C CB B ASN A 1 238 ? 16.506 20.379 4.782 0.50 15.99 ? 238 ASN A CB 1
+ATOM 1986 C CG A ASN A 1 238 ? 16.882 21.508 5.733 0.50 21.05 ? 238 ASN A CG 1
+ATOM 1987 C CG B ASN A 1 238 ? 17.068 21.220 5.903 0.50 18.49 ? 238 ASN A CG 1
+ATOM 1988 O OD1 A ASN A 1 238 ? 16.104 22.393 6.115 0.50 22.39 ? 238 ASN A OD1 1
+ATOM 1989 O OD1 B ASN A 1 238 ? 18.118 21.861 5.772 0.50 18.96 ? 238 ASN A OD1 1
+ATOM 1990 N ND2 A ASN A 1 238 ? 18.142 21.469 6.126 0.50 21.55 ? 238 ASN A ND2 1
+ATOM 1991 N ND2 B ASN A 1 238 ? 16.368 21.244 7.026 0.50 19.10 ? 238 ASN A ND2 1
+ATOM 1992 N N . TYR A 1 239 ? 17.462 19.417 1.309 1.00 14.63 ? 239 TYR A N 1
+ATOM 1993 C CA . TYR A 1 239 ? 17.378 18.342 0.336 1.00 14.81 ? 239 TYR A CA 1
+ATOM 1994 C C . TYR A 1 239 ? 18.779 17.746 0.260 1.00 15.52 ? 239 TYR A C 1
+ATOM 1995 O O . TYR A 1 239 ? 19.769 18.452 0.460 1.00 16.11 ? 239 TYR A O 1
+ATOM 1996 C CB . TYR A 1 239 ? 17.039 18.905 -1.050 1.00 14.64 ? 239 TYR A CB 1
+ATOM 1997 C CG . TYR A 1 239 ? 15.569 18.840 -1.373 1.00 14.52 ? 239 TYR A CG 1
+ATOM 1998 C CD1 . TYR A 1 239 ? 14.637 19.491 -0.584 1.00 14.91 ? 239 TYR A CD1 1
+ATOM 1999 C CD2 . TYR A 1 239 ? 15.115 18.175 -2.502 1.00 14.55 ? 239 TYR A CD2 1
+ATOM 2000 C CE1 . TYR A 1 239 ? 13.281 19.426 -0.871 1.00 15.52 ? 239 TYR A CE1 1
+ATOM 2001 C CE2 . TYR A 1 239 ? 13.766 18.114 -2.809 1.00 15.01 ? 239 TYR A CE2 1
+ATOM 2002 C CZ . TYR A 1 239 ? 12.850 18.743 -1.992 1.00 15.84 ? 239 TYR A CZ 1
+ATOM 2003 O OH . TYR A 1 239 ? 11.509 18.631 -2.269 1.00 16.32 ? 239 TYR A OH 1
+ATOM 2004 N N A GLU A 1 240 ? 18.870 16.448 -0.030 0.50 15.37 ? 240 GLU A N 1
+ATOM 2005 N N B GLU A 1 240 ? 18.868 16.461 -0.067 0.50 15.60 ? 240 GLU A N 1
+ATOM 2006 C CA A GLU A 1 240 ? 20.154 15.777 -0.186 0.50 16.23 ? 240 GLU A CA 1
+ATOM 2007 C CA B GLU A 1 240 ? 20.151 15.796 -0.223 0.50 16.61 ? 240 GLU A CA 1
+ATOM 2008 C C A GLU A 1 240 ? 20.879 16.322 -1.420 0.50 16.43 ? 240 GLU A C 1
+ATOM 2009 C C B GLU A 1 240 ? 20.878 16.350 -1.428 0.50 16.61 ? 240 GLU A C 1
+ATOM 2010 O O A GLU A 1 240 ? 20.244 16.585 -2.438 0.50 15.69 ? 240 GLU A O 1
+ATOM 2011 O O B GLU A 1 240 ? 20.249 16.611 -2.453 0.50 15.86 ? 240 GLU A O 1
+ATOM 2012 C CB A GLU A 1 240 ? 19.925 14.265 -0.355 0.50 18.78 ? 240 GLU A CB 1
+ATOM 2013 C CB B GLU A 1 240 ? 19.929 14.302 -0.446 0.50 19.82 ? 240 GLU A CB 1
+ATOM 2014 C CG A GLU A 1 240 ? 19.511 13.580 0.931 0.50 23.01 ? 240 GLU A CG 1
+ATOM 2015 C CG B GLU A 1 240 ? 19.757 13.549 0.847 0.50 25.74 ? 240 GLU A CG 1
+ATOM 2016 C CD A GLU A 1 240 ? 20.607 13.558 1.976 0.50 27.97 ? 240 GLU A CD 1
+ATOM 2017 C CD B GLU A 1 240 ? 19.839 12.057 0.654 0.50 32.83 ? 240 GLU A CD 1
+ATOM 2018 O OE1 A GLU A 1 240 ? 21.558 12.757 1.825 0.50 28.30 ? 240 GLU A OE1 1
+ATOM 2019 O OE1 B GLU A 1 240 ? 19.029 11.520 -0.134 0.50 34.72 ? 240 GLU A OE1 1
+ATOM 2020 O OE2 A GLU A 1 240 ? 20.521 14.346 2.943 0.50 29.56 ? 240 GLU A OE2 1
+ATOM 2021 O OE2 B GLU A 1 240 ? 20.715 11.421 1.281 0.50 35.82 ? 240 GLU A OE2 1
+ATOM 2022 N N . PRO A 1 241 ? 22.205 16.501 -1.358 1.00 17.14 ? 241 PRO A N 1
+ATOM 2023 C CA . PRO A 1 241 ? 22.942 16.989 -2.541 1.00 18.08 ? 241 PRO A CA 1
+ATOM 2024 C C . PRO A 1 241 ? 22.812 15.998 -3.698 1.00 17.98 ? 241 PRO A C 1
+ATOM 2025 O O . PRO A 1 241 ? 22.874 14.796 -3.468 1.00 18.99 ? 241 PRO A O 1
+ATOM 2026 C CB . PRO A 1 241 ? 24.400 17.037 -2.063 1.00 19.59 ? 241 PRO A CB 1
+ATOM 2027 C CG . PRO A 1 241 ? 24.323 17.034 -0.568 1.00 19.93 ? 241 PRO A CG 1
+ATOM 2028 C CD . PRO A 1 241 ? 23.111 16.247 -0.217 1.00 17.24 ? 241 PRO A CD 1
+ATOM 2029 N N . LEU A 1 242 ? 22.540 16.485 -4.895 1.00 17.16 ? 242 LEU A N 1
+ATOM 2030 C CA . LEU A 1 242 ? 22.418 15.624 -6.060 1.00 17.79 ? 242 LEU A CA 1
+ATOM 2031 C C . LEU A 1 242 ? 23.822 15.392 -6.612 1.00 17.81 ? 242 LEU A C 1
+ATOM 2032 O O . LEU A 1 242 ? 24.618 16.325 -6.735 1.00 17.96 ? 242 LEU A O 1
+ATOM 2033 C CB . LEU A 1 242 ? 21.514 16.262 -7.115 1.00 18.10 ? 242 LEU A CB 1
+ATOM 2034 C CG . LEU A 1 242 ? 20.945 15.279 -8.128 1.00 19.57 ? 242 LEU A CG 1
+ATOM 2035 C CD1 . LEU A 1 242 ? 19.885 14.396 -7.492 1.00 20.27 ? 242 LEU A CD1 1
+ATOM 2036 C CD2 . LEU A 1 242 ? 20.350 16.000 -9.280 1.00 19.83 ? 242 LEU A CD2 1
+ATOM 2037 N N . THR A 1 243 ? 24.131 14.138 -6.881 1.00 18.16 ? 243 THR A N 1
+ATOM 2038 C CA . THR A 1 243 ? 25.435 13.756 -7.399 1.00 18.67 ? 243 THR A CA 1
+ATOM 2039 C C . THR A 1 243 ? 25.333 13.318 -8.861 1.00 19.12 ? 243 THR A C 1
+ATOM 2040 O O . THR A 1 243 ? 24.223 13.074 -9.370 1.00 18.82 ? 243 THR A O 1
+ATOM 2041 C CB . THR A 1 243 ? 26.018 12.618 -6.543 1.00 19.51 ? 243 THR A CB 1
+ATOM 2042 O OG1 . THR A 1 243 ? 25.257 11.425 -6.756 1.00 19.15 ? 243 THR A OG1 1
+ATOM 2043 C CG2 . THR A 1 243 ? 26.099 12.973 -5.073 1.00 20.65 ? 243 THR A CG2 1
+ATOM 2044 N N . GLN A 1 244 ? 26.491 13.150 -9.526 1.00 19.36 ? 244 GLN A N 1
+ATOM 2045 C CA . GLN A 1 244 ? 26.496 12.626 -10.886 1.00 19.60 ? 244 GLN A CA 1
+ATOM 2046 C C . GLN A 1 244 ? 25.936 11.192 -10.896 1.00 19.31 ? 244 GLN A C 1
+ATOM 2047 O O . GLN A 1 244 ? 25.228 10.841 -11.832 1.00 19.52 ? 244 GLN A O 1
+ATOM 2048 C CB . GLN A 1 244 ? 27.908 12.662 -11.481 1.00 21.32 ? 244 GLN A CB 1
+ATOM 2049 C CG . GLN A 1 244 ? 27.948 12.291 -12.963 1.00 24.67 ? 244 GLN A CG 1
+ATOM 2050 C CD . GLN A 1 244 ? 27.099 13.215 -13.796 1.00 27.50 ? 244 GLN A CD 1
+ATOM 2051 O OE1 . GLN A 1 244 ? 27.194 14.445 -13.689 1.00 28.95 ? 244 GLN A OE1 1
+ATOM 2052 N NE2 . GLN A 1 244 ? 26.239 12.644 -14.629 1.00 26.25 ? 244 GLN A NE2 1
+ATOM 2053 N N . ASP A 1 245 ? 26.150 10.409 -9.818 1.00 18.53 ? 245 ASP A N 1
+ATOM 2054 C CA . ASP A 1 245 ? 25.574 9.066 -9.707 1.00 18.09 ? 245 ASP A CA 1
+ATOM 2055 C C . ASP A 1 245 ? 24.045 9.134 -9.768 1.00 16.92 ? 245 ASP A C 1
+ATOM 2056 O O . ASP A 1 245 ? 23.437 8.335 -10.466 1.00 17.01 ? 245 ASP A O 1
+ATOM 2057 C CB . ASP A 1 245 ? 26.001 8.387 -8.399 1.00 20.87 ? 245 ASP A CB 1
+ATOM 2058 C CG . ASP A 1 245 ? 27.274 7.574 -8.483 1.00 27.71 ? 245 ASP A CG 1
+ATOM 2059 O OD1 . ASP A 1 245 ? 28.003 7.709 -9.493 1.00 28.66 ? 245 ASP A OD1 1
+ATOM 2060 O OD2 . ASP A 1 245 ? 27.551 6.809 -7.530 1.00 30.69 ? 245 ASP A OD2 1
+ATOM 2061 N N . HIS A 1 246 ? 23.429 10.114 -9.083 1.00 15.98 ? 246 HIS A N 1
+ATOM 2062 C CA . HIS A 1 246 ? 21.969 10.269 -9.127 1.00 15.49 ? 246 HIS A CA 1
+ATOM 2063 C C . HIS A 1 246 ? 21.504 10.639 -10.533 1.00 15.40 ? 246 HIS A C 1
+ATOM 2064 O O . HIS A 1 246 ? 20.479 10.138 -10.994 1.00 15.05 ? 246 HIS A O 1
+ATOM 2065 C CB . HIS A 1 246 ? 21.508 11.368 -8.176 1.00 15.78 ? 246 HIS A CB 1
+ATOM 2066 C CG . HIS A 1 246 ? 21.770 11.078 -6.743 1.00 17.82 ? 246 HIS A CG 1
+ATOM 2067 N ND1 . HIS A 1 246 ? 22.203 12.070 -5.882 1.00 19.11 ? 246 HIS A ND1 1
+ATOM 2068 C CD2 . HIS A 1 246 ? 21.645 9.920 -6.061 1.00 19.14 ? 246 HIS A CD2 1
+ATOM 2069 C CE1 . HIS A 1 246 ? 22.337 11.483 -4.706 1.00 19.83 ? 246 HIS A CE1 1
+ATOM 2070 N NE2 . HIS A 1 246 ? 21.998 10.194 -4.760 1.00 20.16 ? 246 HIS A NE2 1
+ATOM 2071 N N . VAL A 1 247 ? 22.246 11.522 -11.204 1.00 15.42 ? 247 VAL A N 1
+ATOM 2072 C CA . VAL A 1 247 ? 21.930 11.926 -12.569 1.00 15.51 ? 247 VAL A CA 1
+ATOM 2073 C C . VAL A 1 247 ? 21.958 10.715 -13.495 1.00 16.08 ? 247 VAL A C 1
+ATOM 2074 O O . VAL A 1 247 ? 21.051 10.539 -14.308 1.00 16.35 ? 247 VAL A O 1
+ATOM 2075 C CB . VAL A 1 247 ? 22.896 13.023 -13.073 1.00 16.23 ? 247 VAL A CB 1
+ATOM 2076 C CG1 . VAL A 1 247 ? 22.681 13.298 -14.560 1.00 17.00 ? 247 VAL A CG1 1
+ATOM 2077 C CG2 . VAL A 1 247 ? 22.733 14.297 -12.255 1.00 17.00 ? 247 VAL A CG2 1
+ATOM 2078 N N . ASP A 1 248 ? 22.964 9.855 -13.327 1.00 16.47 ? 248 ASP A N 1
+ATOM 2079 C CA . ASP A 1 248 ? 23.084 8.653 -14.146 1.00 17.07 ? 248 ASP A CA 1
+ATOM 2080 C C . ASP A 1 248 ? 21.953 7.675 -13.877 1.00 17.14 ? 248 ASP A C 1
+ATOM 2081 O O . ASP A 1 248 ? 21.438 7.067 -14.812 1.00 17.79 ? 248 ASP A O 1
+ATOM 2082 C CB . ASP A 1 248 ? 24.433 7.972 -13.911 1.00 18.42 ? 248 ASP A CB 1
+ATOM 2083 C CG . ASP A 1 248 ? 25.621 8.798 -14.361 1.00 21.95 ? 248 ASP A CG 1
+ATOM 2084 O OD1 . ASP A 1 248 ? 25.426 9.733 -15.170 1.00 22.47 ? 248 ASP A OD1 1
+ATOM 2085 O OD2 . ASP A 1 248 ? 26.742 8.511 -13.904 1.00 24.76 ? 248 ASP A OD2 1
+ATOM 2086 N N . ILE A 1 249 ? 21.549 7.528 -12.614 1.00 16.87 ? 249 ILE A N 1
+ATOM 2087 C CA . ILE A 1 249 ? 20.432 6.648 -12.257 1.00 17.46 ? 249 ILE A CA 1
+ATOM 2088 C C . ILE A 1 249 ? 19.119 7.132 -12.904 1.00 16.76 ? 249 ILE A C 1
+ATOM 2089 O O . ILE A 1 249 ? 18.263 6.320 -13.253 1.00 17.06 ? 249 ILE A O 1
+ATOM 2090 C CB . ILE A 1 249 ? 20.323 6.530 -10.715 1.00 19.59 ? 249 ILE A CB 1
+ATOM 2091 C CG1 . ILE A 1 249 ? 21.526 5.765 -10.147 1.00 20.92 ? 249 ILE A CG1 1
+ATOM 2092 C CG2 . ILE A 1 249 ? 19.034 5.855 -10.297 1.00 21.07 ? 249 ILE A CG2 1
+ATOM 2093 C CD1 . ILE A 1 249 ? 21.709 5.942 -8.653 1.00 22.51 ? 249 ILE A CD1 1
+ATOM 2094 N N . LEU A 1 250 ? 18.972 8.455 -13.087 1.00 15.50 ? 250 LEU A N 1
+ATOM 2095 C CA . LEU A 1 250 ? 17.794 9.034 -13.730 1.00 15.60 ? 250 LEU A CA 1
+ATOM 2096 C C . LEU A 1 250 ? 17.834 8.995 -15.268 1.00 16.87 ? 250 LEU A C 1
+ATOM 2097 O O . LEU A 1 250 ? 16.844 9.354 -15.898 1.00 17.10 ? 250 LEU A O 1
+ATOM 2098 C CB . LEU A 1 250 ? 17.591 10.474 -13.267 1.00 14.27 ? 250 LEU A CB 1
+ATOM 2099 C CG . LEU A 1 250 ? 17.215 10.646 -11.808 1.00 14.27 ? 250 LEU A CG 1
+ATOM 2100 C CD1 . LEU A 1 250 ? 17.430 12.094 -11.372 1.00 14.67 ? 250 LEU A CD1 1
+ATOM 2101 C CD2 . LEU A 1 250 ? 15.762 10.236 -11.577 1.00 14.78 ? 250 LEU A CD2 1
+ATOM 2102 N N . GLY A 1 251 ? 18.940 8.525 -15.843 1.00 17.02 ? 251 GLY A N 1
+ATOM 2103 C CA . GLY A 1 251 ? 19.134 8.385 -17.284 1.00 18.15 ? 251 GLY A CA 1
+ATOM 2104 C C . GLY A 1 251 ? 17.975 7.739 -18.021 1.00 19.09 ? 251 GLY A C 1
+ATOM 2105 O O . GLY A 1 251 ? 17.410 8.357 -18.923 1.00 19.38 ? 251 GLY A O 1
+ATOM 2106 N N . PRO A 1 252 ? 17.540 6.528 -17.623 1.00 19.11 ? 252 PRO A N 1
+ATOM 2107 C CA . PRO A 1 252 ? 16.394 5.908 -18.309 1.00 19.24 ? 252 PRO A CA 1
+ATOM 2108 C C . PRO A 1 252 ? 15.110 6.745 -18.294 1.00 18.83 ? 252 PRO A C 1
+ATOM 2109 O O . PRO A 1 252 ? 14.431 6.798 -19.315 1.00 19.47 ? 252 PRO A O 1
+ATOM 2110 C CB . PRO A 1 252 ? 16.246 4.562 -17.589 1.00 20.19 ? 252 PRO A CB 1
+ATOM 2111 C CG . PRO A 1 252 ? 17.626 4.268 -17.093 1.00 20.99 ? 252 PRO A CG 1
+ATOM 2112 C CD . PRO A 1 252 ? 18.109 5.617 -16.617 1.00 19.33 ? 252 PRO A CD 1
+ATOM 2113 N N . LEU A 1 253 ? 14.785 7.429 -17.181 1.00 18.06 ? 253 LEU A N 1
+ATOM 2114 C CA . LEU A 1 253 ? 13.586 8.275 -17.140 1.00 17.83 ? 253 LEU A CA 1
+ATOM 2115 C C . LEU A 1 253 ? 13.741 9.519 -18.012 1.00 18.44 ? 253 LEU A C 1
+ATOM 2116 O O . LEU A 1 253 ? 12.785 9.977 -18.635 1.00 19.17 ? 253 LEU A O 1
+ATOM 2117 C CB . LEU A 1 253 ? 13.221 8.666 -15.706 1.00 17.36 ? 253 LEU A CB 1
+ATOM 2118 C CG . LEU A 1 253 ? 12.642 7.523 -14.882 1.00 18.39 ? 253 LEU A CG 1
+ATOM 2119 C CD1 . LEU A 1 253 ? 12.522 7.914 -13.415 1.00 18.47 ? 253 LEU A CD1 1
+ATOM 2120 C CD2 . LEU A 1 253 ? 11.285 7.102 -15.419 1.00 19.76 ? 253 LEU A CD2 1
+ATOM 2121 N N . SER A 1 254 ? 14.956 10.052 -18.077 1.00 18.35 ? 254 SER A N 1
+ATOM 2122 C CA . SER A 1 254 ? 15.269 11.190 -18.918 1.00 18.83 ? 254 SER A CA 1
+ATOM 2123 C C . SER A 1 254 ? 15.130 10.789 -20.399 1.00 19.74 ? 254 SER A C 1
+ATOM 2124 O O . SER A 1 254 ? 14.617 11.567 -21.210 1.00 20.29 ? 254 SER A O 1
+ATOM 2125 C CB . SER A 1 254 ? 16.703 11.640 -18.638 1.00 19.93 ? 254 SER A CB 1
+ATOM 2126 O OG . SER A 1 254 ? 17.063 12.706 -19.494 1.00 22.09 ? 254 SER A OG 1
+ATOM 2127 N N . ALA A 1 255 ? 15.585 9.585 -20.748 1.00 19.75 ? 255 ALA A N 1
+ATOM 2128 C CA . ALA A 1 255 ? 15.515 9.100 -22.123 1.00 20.73 ? 255 ALA A CA 1
+ATOM 2129 C C . ALA A 1 255 ? 14.080 8.868 -22.550 1.00 22.35 ? 255 ALA A C 1
+ATOM 2130 O O . ALA A 1 255 ? 13.724 9.175 -23.692 1.00 22.53 ? 255 ALA A O 1
+ATOM 2131 C CB . ALA A 1 255 ? 16.321 7.819 -22.267 1.00 20.66 ? 255 ALA A CB 1
+ATOM 2132 N N . GLN A 1 256 ? 13.260 8.330 -21.643 1.00 22.99 ? 256 GLN A N 1
+ATOM 2133 C CA . GLN A 1 256 ? 11.861 8.039 -21.931 1.00 24.03 ? 256 GLN A CA 1
+ATOM 2134 C C . GLN A 1 256 ? 11.033 9.298 -22.174 1.00 23.74 ? 256 GLN A C 1
+ATOM 2135 O O . GLN A 1 256 ? 10.254 9.350 -23.132 1.00 24.91 ? 256 GLN A O 1
+ATOM 2136 C CB . GLN A 1 256 ? 11.252 7.200 -20.805 1.00 26.63 ? 256 GLN A CB 1
+ATOM 2137 C CG . GLN A 1 256 ? 9.818 6.770 -21.073 1.00 31.24 ? 256 GLN A CG 1
+ATOM 2138 C CD . GLN A 1 256 ? 9.199 6.054 -19.898 1.00 36.62 ? 256 GLN A CD 1
+ATOM 2139 O OE1 . GLN A 1 256 ? 9.885 5.560 -18.983 1.00 38.38 ? 256 GLN A OE1 1
+ATOM 2140 N NE2 . GLN A 1 256 ? 7.876 5.983 -19.902 1.00 37.67 ? 256 GLN A NE2 1
+ATOM 2141 N N . THR A 1 257 ? 11.226 10.325 -21.350 1.00 21.63 ? 257 THR A N 1
+ATOM 2142 C CA . THR A 1 257 ? 10.447 11.552 -21.456 1.00 20.74 ? 257 THR A CA 1
+ATOM 2143 C C . THR A 1 257 ? 11.055 12.627 -22.354 1.00 20.66 ? 257 THR A C 1
+ATOM 2144 O O . THR A 1 257 ? 10.367 13.578 -22.708 1.00 21.25 ? 257 THR A O 1
+ATOM 2145 C CB . THR A 1 257 ? 10.244 12.132 -20.061 1.00 21.06 ? 257 THR A CB 1
+ATOM 2146 O OG1 . THR A 1 257 ? 11.535 12.470 -19.536 1.00 21.29 ? 257 THR A OG1 1
+ATOM 2147 C CG2 . THR A 1 257 ? 9.565 11.151 -19.127 1.00 21.27 ? 257 THR A CG2 1
+ATOM 2148 N N . GLY A 1 258 ? 12.336 12.508 -22.660 1.00 19.65 ? 258 GLY A N 1
+ATOM 2149 C CA . GLY A 1 258 ? 13.033 13.522 -23.440 1.00 19.47 ? 258 GLY A CA 1
+ATOM 2150 C C . GLY A 1 258 ? 13.360 14.765 -22.637 1.00 18.75 ? 258 GLY A C 1
+ATOM 2151 O O . GLY A 1 258 ? 13.782 15.770 -23.207 1.00 18.83 ? 258 GLY A O 1
+ATOM 2152 N N . ILE A 1 259 ? 13.206 14.712 -21.284 1.00 17.30 ? 259 ILE A N 1
+ATOM 2153 C CA . ILE A 1 259 ? 13.516 15.858 -20.450 1.00 17.01 ? 259 ILE A CA 1
+ATOM 2154 C C . ILE A 1 259 ? 14.840 15.605 -19.784 1.00 16.46 ? 259 ILE A C 1
+ATOM 2155 O O . ILE A 1 259 ? 14.980 14.653 -19.015 1.00 16.95 ? 259 ILE A O 1
+ATOM 2156 C CB . ILE A 1 259 ? 12.396 16.138 -19.416 1.00 18.00 ? 259 ILE A CB 1
+ATOM 2157 C CG1 . ILE A 1 259 ? 11.064 16.389 -20.148 1.00 19.63 ? 259 ILE A CG1 1
+ATOM 2158 C CG2 . ILE A 1 259 ? 12.766 17.336 -18.557 1.00 18.35 ? 259 ILE A CG2 1
+ATOM 2159 C CD1 . ILE A 1 259 ? 9.876 16.454 -19.229 1.00 21.54 ? 259 ILE A CD1 1
+ATOM 2160 N N . ALA A 1 260 ? 15.837 16.436 -20.095 1.00 15.60 ? 260 ALA A N 1
+ATOM 2161 C CA . ALA A 1 260 ? 17.170 16.324 -19.512 1.00 15.26 ? 260 ALA A CA 1
+ATOM 2162 C C . ALA A 1 260 ? 17.099 16.416 -17.996 1.00 14.60 ? 260 ALA A C 1
+ATOM 2163 O O . ALA A 1 260 ? 16.278 17.168 -17.463 1.00 14.60 ? 260 ALA A O 1
+ATOM 2164 C CB . ALA A 1 260 ? 18.067 17.431 -20.055 1.00 16.18 ? 260 ALA A CB 1
+ATOM 2165 N N . VAL A 1 261 ? 17.925 15.638 -17.296 1.00 13.65 ? 261 VAL A N 1
+ATOM 2166 C CA . VAL A 1 261 ? 17.923 15.636 -15.837 1.00 13.86 ? 261 VAL A CA 1
+ATOM 2167 C C . VAL A 1 261 ? 18.078 17.028 -15.244 1.00 13.55 ? 261 VAL A C 1
+ATOM 2168 O O . VAL A 1 261 ? 17.313 17.391 -14.351 1.00 14.19 ? 261 VAL A O 1
+ATOM 2169 C CB . VAL A 1 261 ? 18.954 14.647 -15.258 1.00 15.10 ? 261 VAL A CB 1
+ATOM 2170 C CG1 . VAL A 1 261 ? 19.013 14.754 -13.744 1.00 14.97 ? 261 VAL A CG1 1
+ATOM 2171 C CG2 . VAL A 1 261 ? 18.624 13.214 -15.680 1.00 16.65 ? 261 VAL A CG2 1
+ATOM 2172 N N . LEU A 1 262 ? 19.005 17.831 -15.794 1.00 13.28 ? 262 LEU A N 1
+ATOM 2173 C CA . LEU A 1 262 ? 19.208 19.180 -15.273 1.00 13.56 ? 262 LEU A CA 1
+ATOM 2174 C C . LEU A 1 262 ? 18.028 20.109 -15.552 1.00 13.51 ? 262 LEU A C 1
+ATOM 2175 O O . LEU A 1 262 ? 17.795 21.025 -14.755 1.00 13.73 ? 262 LEU A O 1
+ATOM 2176 C CB . LEU A 1 262 ? 20.526 19.768 -15.738 1.00 13.70 ? 262 LEU A CB 1
+ATOM 2177 C CG . LEU A 1 262 ? 21.765 19.061 -15.162 1.00 15.11 ? 262 LEU A CG 1
+ATOM 2178 C CD1 . LEU A 1 262 ? 23.038 19.609 -15.783 1.00 15.85 ? 262 LEU A CD1 1
+ATOM 2179 C CD2 . LEU A 1 262 ? 21.832 19.171 -13.652 1.00 15.29 ? 262 LEU A CD2 1
+ATOM 2180 N N . ASP A 1 263 ? 17.252 19.857 -16.630 1.00 13.50 ? 263 ASP A N 1
+ATOM 2181 C CA . ASP A 1 263 ? 16.044 20.647 -16.866 1.00 13.09 ? 263 ASP A CA 1
+ATOM 2182 C C . ASP A 1 263 ? 15.008 20.287 -15.786 1.00 14.28 ? 263 ASP A C 1
+ATOM 2183 O O . ASP A 1 263 ? 14.352 21.181 -15.249 1.00 15.00 ? 263 ASP A O 1
+ATOM 2184 C CB . ASP A 1 263 ? 15.460 20.397 -18.251 1.00 13.77 ? 263 ASP A CB 1
+ATOM 2185 C CG . ASP A 1 263 ? 16.333 20.842 -19.408 1.00 14.89 ? 263 ASP A CG 1
+ATOM 2186 O OD1 . ASP A 1 263 ? 17.440 21.396 -19.156 1.00 14.07 ? 263 ASP A OD1 1
+ATOM 2187 O OD2 . ASP A 1 263 ? 15.912 20.661 -20.549 1.00 16.19 ? 263 ASP A OD2 1
+ATOM 2188 N N . MET A 1 264 ? 14.883 18.991 -15.442 1.00 13.23 ? 264 MET A N 1
+ATOM 2189 C CA . MET A 1 264 ? 13.973 18.598 -14.358 1.00 12.75 ? 264 MET A CA 1
+ATOM 2190 C C . MET A 1 264 ? 14.443 19.193 -13.029 1.00 13.28 ? 264 MET A C 1
+ATOM 2191 O O . MET A 1 264 ? 13.626 19.638 -12.230 1.00 14.09 ? 264 MET A O 1
+ATOM 2192 C CB . MET A 1 264 ? 13.808 17.085 -14.252 1.00 13.83 ? 264 MET A CB 1
+ATOM 2193 C CG . MET A 1 264 ? 12.620 16.710 -13.385 1.00 14.70 ? 264 MET A CG 1
+ATOM 2194 S SD . MET A 1 264 ? 11.043 17.204 -14.145 1.00 16.49 ? 264 MET A SD 1
+ATOM 2195 C CE . MET A 1 264 ? 10.741 15.784 -15.174 1.00 18.99 ? 264 MET A CE 1
+ATOM 2196 N N . CYS A 1 265 ? 15.767 19.296 -12.823 1.00 12.88 ? 265 CYS A N 1
+ATOM 2197 C CA . CYS A 1 265 ? 16.310 19.936 -11.623 1.00 13.13 ? 265 CYS A CA 1
+ATOM 2198 C C . CYS A 1 265 ? 15.888 21.399 -11.572 1.00 13.37 ? 265 CYS A C 1
+ATOM 2199 O O . CYS A 1 265 ? 15.599 21.895 -10.489 1.00 13.84 ? 265 CYS A O 1
+ATOM 2200 C CB . CYS A 1 265 ? 17.828 19.815 -11.597 1.00 13.18 ? 265 CYS A CB 1
+ATOM 2201 S SG . CYS A 1 265 ? 18.430 18.150 -11.239 1.00 13.95 ? 265 CYS A SG 1
+ATOM 2202 N N . ALA A 1 266 ? 15.814 22.076 -12.734 1.00 13.18 ? 266 ALA A N 1
+ATOM 2203 C CA . ALA A 1 266 ? 15.388 23.477 -12.773 1.00 14.34 ? 266 ALA A CA 1
+ATOM 2204 C C . ALA A 1 266 ? 13.907 23.600 -12.453 1.00 15.13 ? 266 ALA A C 1
+ATOM 2205 O O . ALA A 1 266 ? 13.510 24.582 -11.826 1.00 16.07 ? 266 ALA A O 1
+ATOM 2206 C CB . ALA A 1 266 ? 15.692 24.101 -14.119 1.00 15.34 ? 266 ALA A CB 1
+ATOM 2207 N N . SER A 1 267 ? 13.093 22.600 -12.841 1.00 14.73 ? 267 SER A N 1
+ATOM 2208 C CA . SER A 1 267 ? 11.680 22.574 -12.475 1.00 15.16 ? 267 SER A CA 1
+ATOM 2209 C C . SER A 1 267 ? 11.573 22.402 -10.957 1.00 14.35 ? 267 SER A C 1
+ATOM 2210 O O . SER A 1 267 ? 10.788 23.086 -10.302 1.00 14.65 ? 267 SER A O 1
+ATOM 2211 C CB . SER A 1 267 ? 10.953 21.421 -13.163 1.00 17.63 ? 267 SER A CB 1
+ATOM 2212 O OG . SER A 1 267 ? 10.610 21.744 -14.499 1.00 21.64 ? 267 SER A OG 1
+ATOM 2213 N N . LEU A 1 268 ? 12.371 21.488 -10.401 1.00 13.19 ? 268 LEU A N 1
+ATOM 2214 C CA . LEU A 1 268 ? 12.359 21.248 -8.965 1.00 13.02 ? 268 LEU A CA 1
+ATOM 2215 C C . LEU A 1 268 ? 12.836 22.482 -8.205 1.00 13.76 ? 268 LEU A C 1
+ATOM 2216 O O . LEU A 1 268 ? 12.237 22.854 -7.203 1.00 13.46 ? 268 LEU A O 1
+ATOM 2217 C CB . LEU A 1 268 ? 13.191 20.007 -8.611 1.00 12.54 ? 268 LEU A CB 1
+ATOM 2218 C CG . LEU A 1 268 ? 13.338 19.701 -7.124 1.00 13.38 ? 268 LEU A CG 1
+ATOM 2219 C CD1 . LEU A 1 268 ? 11.961 19.546 -6.450 1.00 14.09 ? 268 LEU A CD1 1
+ATOM 2220 C CD2 . LEU A 1 268 ? 14.098 18.421 -6.934 1.00 13.76 ? 268 LEU A CD2 1
+ATOM 2221 N N . LYS A 1 269 ? 13.869 23.160 -8.705 1.00 12.82 ? 269 LYS A N 1
+ATOM 2222 C CA . LYS A 1 269 ? 14.363 24.389 -8.097 1.00 12.60 ? 269 LYS A CA 1
+ATOM 2223 C C . LYS A 1 269 ? 13.255 25.446 -8.026 1.00 13.34 ? 269 LYS A C 1
+ATOM 2224 O O . LYS A 1 269 ? 13.062 26.038 -6.976 1.00 13.99 ? 269 LYS A O 1
+ATOM 2225 C CB . LYS A 1 269 ? 15.546 24.917 -8.911 1.00 13.63 ? 269 LYS A CB 1
+ATOM 2226 C CG . LYS A 1 269 ? 16.062 26.292 -8.492 1.00 17.21 ? 269 LYS A CG 1
+ATOM 2227 C CD . LYS A 1 269 ? 17.254 26.664 -9.357 1.00 20.23 ? 269 LYS A CD 1
+ATOM 2228 C CE . LYS A 1 269 ? 17.557 28.150 -9.315 1.00 23.68 ? 269 LYS A CE 1
+ATOM 2229 N NZ . LYS A 1 269 ? 18.553 28.518 -10.362 1.00 25.16 ? 269 LYS A NZ 1
+ATOM 2230 N N . GLU A 1 270 ? 12.479 25.616 -9.107 1.00 13.60 ? 270 GLU A N 1
+ATOM 2231 C CA . GLU A 1 270 ? 11.380 26.581 -9.098 1.00 14.67 ? 270 GLU A CA 1
+ATOM 2232 C C . GLU A 1 270 ? 10.288 26.174 -8.115 1.00 15.62 ? 270 GLU A C 1
+ATOM 2233 O O . GLU A 1 270 ? 9.749 27.026 -7.415 1.00 16.25 ? 270 GLU A O 1
+ATOM 2234 C CB . GLU A 1 270 ? 10.813 26.806 -10.505 1.00 17.51 ? 270 GLU A CB 1
+ATOM 2235 C CG . GLU A 1 270 ? 11.804 27.456 -11.453 1.00 24.81 ? 270 GLU A CG 1
+ATOM 2236 C CD . GLU A 1 270 ? 12.368 28.793 -11.016 1.00 32.43 ? 270 GLU A CD 1
+ATOM 2237 O OE1 . GLU A 1 270 ? 11.568 29.730 -10.794 1.00 33.99 ? 270 GLU A OE1 1
+ATOM 2238 O OE2 . GLU A 1 270 ? 13.611 28.907 -10.900 1.00 33.71 ? 270 GLU A OE2 1
+ATOM 2239 N N . LEU A 1 271 ? 9.974 24.877 -8.043 1.00 15.19 ? 271 LEU A N 1
+ATOM 2240 C CA . LEU A 1 271 ? 8.984 24.384 -7.082 1.00 15.27 ? 271 LEU A CA 1
+ATOM 2241 C C . LEU A 1 271 ? 9.434 24.628 -5.646 1.00 15.62 ? 271 LEU A C 1
+ATOM 2242 O O . LEU A 1 271 ? 8.598 24.933 -4.792 1.00 17.11 ? 271 LEU A O 1
+ATOM 2243 C CB . LEU A 1 271 ? 8.749 22.894 -7.289 1.00 15.27 ? 271 LEU A CB 1
+ATOM 2244 C CG . LEU A 1 271 ? 7.915 22.555 -8.510 1.00 16.49 ? 271 LEU A CG 1
+ATOM 2245 C CD1 . LEU A 1 271 ? 7.962 21.084 -8.777 1.00 16.95 ? 271 LEU A CD1 1
+ATOM 2246 C CD2 . LEU A 1 271 ? 6.477 23.030 -8.321 1.00 17.56 ? 271 LEU A CD2 1
+ATOM 2247 N N . LEU A 1 272 ? 10.737 24.490 -5.367 1.00 14.10 ? 272 LEU A N 1
+ATOM 2248 C CA . LEU A 1 272 ? 11.233 24.723 -4.011 1.00 14.76 ? 272 LEU A CA 1
+ATOM 2249 C C . LEU A 1 272 ? 11.164 26.195 -3.655 1.00 16.26 ? 272 LEU A C 1
+ATOM 2250 O O . LEU A 1 272 ? 10.760 26.536 -2.543 1.00 17.01 ? 272 LEU A O 1
+ATOM 2251 C CB . LEU A 1 272 ? 12.669 24.214 -3.869 1.00 14.74 ? 272 LEU A CB 1
+ATOM 2252 C CG . LEU A 1 272 ? 12.797 22.705 -3.843 1.00 16.78 ? 272 LEU A CG 1
+ATOM 2253 C CD1 . LEU A 1 272 ? 14.257 22.274 -3.868 1.00 17.63 ? 272 LEU A CD1 1
+ATOM 2254 C CD2 . LEU A 1 272 ? 12.062 22.119 -2.657 1.00 18.76 ? 272 LEU A CD2 1
+ATOM 2255 N N . GLN A 1 273 ? 11.531 27.061 -4.599 1.00 16.06 ? 273 GLN A N 1
+ATOM 2256 C CA . GLN A 1 273 ? 11.587 28.499 -4.374 1.00 17.33 ? 273 GLN A CA 1
+ATOM 2257 C C . GLN A 1 273 ? 10.240 29.180 -4.375 1.00 19.69 ? 273 GLN A C 1
+ATOM 2258 O O . GLN A 1 273 ? 10.080 30.197 -3.708 1.00 20.97 ? 273 GLN A O 1
+ATOM 2259 C CB . GLN A 1 273 ? 12.515 29.162 -5.409 1.00 17.71 ? 273 GLN A CB 1
+ATOM 2260 C CG . GLN A 1 273 ? 13.968 28.758 -5.252 1.00 19.36 ? 273 GLN A CG 1
+ATOM 2261 C CD . GLN A 1 273 ? 14.860 29.396 -6.286 1.00 22.80 ? 273 GLN A CD 1
+ATOM 2262 O OE1 . GLN A 1 273 ? 14.437 29.745 -7.391 1.00 24.43 ? 273 GLN A OE1 1
+ATOM 2263 N NE2 . GLN A 1 273 ? 16.125 29.546 -5.950 1.00 23.28 ? 273 GLN A NE2 1
+ATOM 2264 N N . ASN A 1 274 ? 9.280 28.656 -5.133 1.00 20.29 ? 274 ASN A N 1
+ATOM 2265 C CA . ASN A 1 274 ? 7.976 29.304 -5.249 1.00 21.83 ? 274 ASN A CA 1
+ATOM 2266 C C . ASN A 1 274 ? 6.801 28.527 -4.690 1.00 22.69 ? 274 ASN A C 1
+ATOM 2267 O O . ASN A 1 274 ? 5.697 29.063 -4.637 1.00 23.59 ? 274 ASN A O 1
+ATOM 2268 C CB . ASN A 1 274 ? 7.716 29.658 -6.695 1.00 23.76 ? 274 ASN A CB 1
+ATOM 2269 C CG . ASN A 1 274 ? 8.780 30.577 -7.217 1.00 29.54 ? 274 ASN A CG 1
+ATOM 2270 O OD1 . ASN A 1 274 ? 8.793 31.778 -6.927 1.00 32.28 ? 274 ASN A OD1 1
+ATOM 2271 N ND2 . ASN A 1 274 ? 9.721 30.023 -7.954 1.00 30.78 ? 274 ASN A ND2 1
+ATOM 2272 N N . GLY A 1 275 ? 7.023 27.287 -4.285 1.00 22.59 ? 275 GLY A N 1
+ATOM 2273 C CA . GLY A 1 275 ? 5.948 26.444 -3.791 1.00 22.92 ? 275 GLY A CA 1
+ATOM 2274 C C . GLY A 1 275 ? 5.080 25.943 -4.929 1.00 23.41 ? 275 GLY A C 1
+ATOM 2275 O O . GLY A 1 275 ? 5.379 26.177 -6.111 1.00 23.66 ? 275 GLY A O 1
+ATOM 2276 N N A MET A 1 276 ? 3.995 25.255 -4.586 0.75 23.76 ? 276 MET A N 1
+ATOM 2277 N N B MET A 1 276 ? 3.999 25.241 -4.587 0.25 23.17 ? 276 MET A N 1
+ATOM 2278 C CA A MET A 1 276 ? 3.106 24.713 -5.607 0.75 24.64 ? 276 MET A CA 1
+ATOM 2279 C CA B MET A 1 276 ? 3.087 24.717 -5.599 0.25 23.44 ? 276 MET A CA 1
+ATOM 2280 C C A MET A 1 276 ? 1.887 25.618 -5.902 0.75 25.05 ? 276 MET A C 1
+ATOM 2281 C C B MET A 1 276 ? 1.968 25.686 -5.984 0.25 24.43 ? 276 MET A C 1
+ATOM 2282 O O A MET A 1 276 ? 1.113 25.299 -6.801 0.75 25.20 ? 276 MET A O 1
+ATOM 2283 O O B MET A 1 276 ? 1.294 25.437 -6.974 0.25 24.50 ? 276 MET A O 1
+ATOM 2284 C CB A MET A 1 276 ? 2.723 23.269 -5.272 0.75 25.92 ? 276 MET A CB 1
+ATOM 2285 C CB B MET A 1 276 ? 2.506 23.358 -5.181 0.25 23.19 ? 276 MET A CB 1
+ATOM 2286 C CG A MET A 1 276 ? 3.943 22.341 -5.362 0.75 28.07 ? 276 MET A CG 1
+ATOM 2287 C CG B MET A 1 276 ? 3.463 22.203 -5.391 0.25 23.17 ? 276 MET A CG 1
+ATOM 2288 S SD A MET A 1 276 ? 3.789 20.735 -4.570 0.75 35.78 ? 276 MET A SD 1
+ATOM 2289 S SD B MET A 1 276 ? 2.590 20.634 -5.587 0.25 19.97 ? 276 MET A SD 1
+ATOM 2290 C CE A MET A 1 276 ? 2.500 20.047 -5.545 0.75 30.19 ? 276 MET A CE 1
+ATOM 2291 C CE B MET A 1 276 ? 3.918 19.512 -5.312 0.25 18.54 ? 276 MET A CE 1
+ATOM 2292 N N . ASN A 1 277 ? 1.774 26.783 -5.227 1.00 24.94 ? 277 ASN A N 1
+ATOM 2293 C CA . ASN A 1 277 ? 0.711 27.772 -5.473 1.00 25.60 ? 277 ASN A CA 1
+ATOM 2294 C C . ASN A 1 277 ? -0.709 27.189 -5.412 1.00 25.41 ? 277 ASN A C 1
+ATOM 2295 O O . ASN A 1 277 ? -1.567 27.570 -6.209 1.00 26.11 ? 277 ASN A O 1
+ATOM 2296 C CB . ASN A 1 277 ? 0.942 28.527 -6.787 1.00 27.55 ? 277 ASN A CB 1
+ATOM 2297 C CG . ASN A 1 277 ? 2.030 29.565 -6.712 1.00 32.36 ? 277 ASN A CG 1
+ATOM 2298 O OD1 . ASN A 1 277 ? 3.087 29.452 -7.353 1.00 34.44 ? 277 ASN A OD1 1
+ATOM 2299 N ND2 . ASN A 1 277 ? 1.795 30.607 -5.933 1.00 32.85 ? 277 ASN A ND2 1
+ATOM 2300 N N . GLY A 1 278 ? -0.939 26.258 -4.495 1.00 24.04 ? 278 GLY A N 1
+ATOM 2301 C CA . GLY A 1 278 ? -2.250 25.630 -4.362 1.00 23.26 ? 278 GLY A CA 1
+ATOM 2302 C C . GLY A 1 278 ? -2.558 24.555 -5.391 1.00 22.48 ? 278 GLY A C 1
+ATOM 2303 O O . GLY A 1 278 ? -3.689 24.070 -5.468 1.00 22.88 ? 278 GLY A O 1
+ATOM 2304 N N A ARG A 1 279 ? -1.553 24.151 -6.167 0.50 21.95 ? 279 ARG A N 1
+ATOM 2305 N N B ARG A 1 279 ? -1.550 24.164 -6.183 0.50 21.71 ? 279 ARG A N 1
+ATOM 2306 C CA A ARG A 1 279 ? -1.722 23.116 -7.173 0.50 21.79 ? 279 ARG A CA 1
+ATOM 2307 C CA B ARG A 1 279 ? -1.691 23.135 -7.207 0.50 21.30 ? 279 ARG A CA 1
+ATOM 2308 C C A ARG A 1 279 ? -1.216 21.759 -6.668 0.50 21.02 ? 279 ARG A C 1
+ATOM 2309 C C B ARG A 1 279 ? -1.203 21.769 -6.683 0.50 20.81 ? 279 ARG A C 1
+ATOM 2310 O O A ARG A 1 279 ? -0.595 21.677 -5.602 0.50 20.83 ? 279 ARG A O 1
+ATOM 2311 O O B ARG A 1 279 ? -0.560 21.694 -5.629 0.50 20.66 ? 279 ARG A O 1
+ATOM 2312 C CB A ARG A 1 279 ? -1.035 23.533 -8.485 0.50 23.35 ? 279 ARG A CB 1
+ATOM 2313 C CB B ARG A 1 279 ? -0.911 23.540 -8.475 0.50 22.14 ? 279 ARG A CB 1
+ATOM 2314 C CG A ARG A 1 279 ? -1.623 24.814 -9.067 0.50 27.22 ? 279 ARG A CG 1
+ATOM 2315 C CG B ARG A 1 279 ? -1.238 24.939 -9.002 0.50 24.89 ? 279 ARG A CG 1
+ATOM 2316 C CD A ARG A 1 279 ? -1.199 25.050 -10.505 0.50 31.04 ? 279 ARG A CD 1
+ATOM 2317 C CD B ARG A 1 279 ? -0.110 25.483 -9.868 0.50 27.42 ? 279 ARG A CD 1
+ATOM 2318 N NE A ARG A 1 279 ? -1.606 23.954 -11.383 0.50 34.59 ? 279 ARG A NE 1
+ATOM 2319 N NE B ARG A 1 279 ? -0.302 26.894 -10.206 0.50 30.09 ? 279 ARG A NE 1
+ATOM 2320 C CZ A ARG A 1 279 ? -2.790 23.867 -11.981 0.50 37.85 ? 279 ARG A CZ 1
+ATOM 2321 C CZ B ARG A 1 279 ? 0.680 27.785 -10.306 0.50 31.90 ? 279 ARG A CZ 1
+ATOM 2322 N NH1 A ARG A 1 279 ? -3.697 24.824 -11.819 0.50 37.97 ? 279 ARG A NH1 1
+ATOM 2323 N NH1 B ARG A 1 279 ? 1.940 27.424 -10.088 0.50 31.04 ? 279 ARG A NH1 1
+ATOM 2324 N NH2 A ARG A 1 279 ? -3.068 22.834 -12.764 0.50 38.37 ? 279 ARG A NH2 1
+ATOM 2325 N NH2 B ARG A 1 279 ? 0.413 29.041 -10.636 0.50 31.90 ? 279 ARG A NH2 1
+ATOM 2326 N N . THR A 1 280 ? -1.531 20.684 -7.398 1.00 20.29 ? 280 THR A N 1
+ATOM 2327 C CA . THR A 1 280 ? -1.107 19.344 -7.010 1.00 19.70 ? 280 THR A CA 1
+ATOM 2328 C C . THR A 1 280 ? -0.346 18.658 -8.148 1.00 18.60 ? 280 THR A C 1
+ATOM 2329 O O . THR A 1 280 ? -0.473 19.032 -9.320 1.00 18.37 ? 280 THR A O 1
+ATOM 2330 C CB . THR A 1 280 ? -2.305 18.475 -6.574 1.00 21.75 ? 280 THR A CB 1
+ATOM 2331 O OG1 . THR A 1 280 ? -3.207 18.341 -7.675 1.00 22.42 ? 280 THR A OG1 1
+ATOM 2332 C CG2 . THR A 1 280 ? -3.016 19.017 -5.348 1.00 22.81 ? 280 THR A CG2 1
+ATOM 2333 N N . ILE A 1 281 ? 0.475 17.669 -7.786 1.00 17.32 ? 281 ILE A N 1
+ATOM 2334 C CA . ILE A 1 281 ? 1.241 16.844 -8.713 1.00 17.17 ? 281 ILE A CA 1
+ATOM 2335 C C . ILE A 1 281 ? 0.971 15.413 -8.307 1.00 17.06 ? 281 ILE A C 1
+ATOM 2336 O O . ILE A 1 281 ? 1.194 15.057 -7.152 1.00 16.72 ? 281 ILE A O 1
+ATOM 2337 C CB . ILE A 1 281 ? 2.749 17.150 -8.631 1.00 17.81 ? 281 ILE A CB 1
+ATOM 2338 C CG1 . ILE A 1 281 ? 3.047 18.602 -9.014 1.00 18.05 ? 281 ILE A CG1 1
+ATOM 2339 C CG2 . ILE A 1 281 ? 3.527 16.160 -9.502 1.00 18.38 ? 281 ILE A CG2 1
+ATOM 2340 C CD1 . ILE A 1 281 ? 4.518 19.020 -8.861 1.00 18.34 ? 281 ILE A CD1 1
+ATOM 2341 N N . LEU A 1 282 ? 0.390 14.603 -9.206 1.00 17.24 ? 282 LEU A N 1
+ATOM 2342 C CA . LEU A 1 282 ? 0.041 13.212 -8.889 1.00 17.35 ? 282 LEU A CA 1
+ATOM 2343 C C . LEU A 1 282 ? -0.763 13.066 -7.587 1.00 18.42 ? 282 LEU A C 1
+ATOM 2344 O O . LEU A 1 282 ? -0.449 12.228 -6.754 1.00 19.49 ? 282 LEU A O 1
+ATOM 2345 C CB . LEU A 1 282 ? 1.267 12.292 -8.890 1.00 16.82 ? 282 LEU A CB 1
+ATOM 2346 C CG . LEU A 1 282 ? 1.936 12.047 -10.240 1.00 17.52 ? 282 LEU A CG 1
+ATOM 2347 C CD1 . LEU A 1 282 ? 3.136 11.159 -10.080 1.00 17.37 ? 282 LEU A CD1 1
+ATOM 2348 C CD2 . LEU A 1 282 ? 0.969 11.447 -11.235 1.00 18.50 ? 282 LEU A CD2 1
+ATOM 2349 N N . GLY A 1 283 ? -1.725 13.970 -7.411 1.00 19.57 ? 283 GLY A N 1
+ATOM 2350 C CA . GLY A 1 283 ? -2.606 13.998 -6.248 1.00 20.20 ? 283 GLY A CA 1
+ATOM 2351 C C . GLY A 1 283 ? -1.975 14.425 -4.940 1.00 20.33 ? 283 GLY A C 1
+ATOM 2352 O O . GLY A 1 283 ? -2.567 14.232 -3.877 1.00 21.64 ? 283 GLY A O 1
+ATOM 2353 N N A SER A 1 284 ? -0.758 14.973 -4.996 0.75 19.07 ? 284 SER A N 1
+ATOM 2354 N N B SER A 1 284 ? -0.757 14.979 -4.998 0.25 19.33 ? 284 SER A N 1
+ATOM 2355 C CA A SER A 1 284 ? -0.061 15.413 -3.798 0.75 18.29 ? 284 SER A CA 1
+ATOM 2356 C CA B SER A 1 284 ? -0.033 15.409 -3.809 0.25 18.82 ? 284 SER A CA 1
+ATOM 2357 C C A SER A 1 284 ? 0.123 16.915 -3.823 0.75 18.11 ? 284 SER A C 1
+ATOM 2358 C C B SER A 1 284 ? 0.197 16.911 -3.813 0.25 18.48 ? 284 SER A C 1
+ATOM 2359 O O A SER A 1 284 ? 0.390 17.488 -4.872 0.75 17.64 ? 284 SER A O 1
+ATOM 2360 O O B SER A 1 284 ? 0.554 17.481 -4.841 0.25 18.38 ? 284 SER A O 1
+ATOM 2361 C CB A SER A 1 284 ? 1.311 14.752 -3.713 0.75 18.83 ? 284 SER A CB 1
+ATOM 2362 C CB B SER A 1 284 ? 1.319 14.705 -3.725 0.25 19.61 ? 284 SER A CB 1
+ATOM 2363 O OG A SER A 1 284 ? 2.022 15.192 -2.566 0.75 20.77 ? 284 SER A OG 1
+ATOM 2364 O OG B SER A 1 284 ? 1.181 13.310 -3.519 0.25 21.27 ? 284 SER A OG 1
+ATOM 2365 N N . ALA A 1 285 ? 0.040 17.547 -2.650 1.00 18.03 ? 285 ALA A N 1
+ATOM 2366 C CA . ALA A 1 285 ? 0.290 18.982 -2.522 1.00 18.74 ? 285 ALA A CA 1
+ATOM 2367 C C . ALA A 1 285 ? 1.728 19.259 -1.985 1.00 18.86 ? 285 ALA A C 1
+ATOM 2368 O O . ALA A 1 285 ? 2.067 20.400 -1.676 1.00 20.19 ? 285 ALA A O 1
+ATOM 2369 C CB . ALA A 1 285 ? -0.755 19.620 -1.623 1.00 19.27 ? 285 ALA A CB 1
+ATOM 2370 N N . LEU A 1 286 ? 2.561 18.233 -1.874 1.00 17.88 ? 286 LEU A N 1
+ATOM 2371 C CA . LEU A 1 286 ? 3.951 18.373 -1.497 1.00 18.08 ? 286 LEU A CA 1
+ATOM 2372 C C . LEU A 1 286 ? 4.832 17.526 -2.431 1.00 17.12 ? 286 LEU A C 1
+ATOM 2373 O O . LEU A 1 286 ? 4.316 16.735 -3.234 1.00 17.43 ? 286 LEU A O 1
+ATOM 2374 C CB . LEU A 1 286 ? 4.191 18.099 -0.005 1.00 19.14 ? 286 LEU A CB 1
+ATOM 2375 C CG . LEU A 1 286 ? 3.662 16.806 0.562 1.00 21.28 ? 286 LEU A CG 1
+ATOM 2376 C CD1 . LEU A 1 286 ? 4.491 15.630 0.105 1.00 22.70 ? 286 LEU A CD1 1
+ATOM 2377 C CD2 . LEU A 1 286 ? 3.721 16.839 2.088 1.00 22.17 ? 286 LEU A CD2 1
+ATOM 2378 N N . LEU A 1 287 ? 6.135 17.757 -2.402 1.00 15.55 ? 287 LEU A N 1
+ATOM 2379 C CA . LEU A 1 287 ? 7.059 17.031 -3.258 1.00 15.39 ? 287 LEU A CA 1
+ATOM 2380 C C . LEU A 1 287 ? 7.339 15.664 -2.641 1.00 15.22 ? 287 LEU A C 1
+ATOM 2381 O O . LEU A 1 287 ? 7.958 15.571 -1.591 1.00 16.81 ? 287 LEU A O 1
+ATOM 2382 C CB . LEU A 1 287 ? 8.323 17.863 -3.459 1.00 16.06 ? 287 LEU A CB 1
+ATOM 2383 C CG . LEU A 1 287 ? 8.026 19.223 -4.104 1.00 18.18 ? 287 LEU A CG 1
+ATOM 2384 C CD1 . LEU A 1 287 ? 9.204 20.138 -3.991 1.00 18.93 ? 287 LEU A CD1 1
+ATOM 2385 C CD2 . LEU A 1 287 ? 7.575 19.068 -5.566 1.00 19.33 ? 287 LEU A CD2 1
+ATOM 2386 N N A GLU A 1 288 ? 6.855 14.602 -3.286 0.50 13.98 ? 288 GLU A N 1
+ATOM 2387 N N B GLU A 1 288 ? 6.866 14.610 -3.293 0.50 14.00 ? 288 GLU A N 1
+ATOM 2388 C CA A GLU A 1 288 ? 6.993 13.231 -2.776 0.50 13.48 ? 288 GLU A CA 1
+ATOM 2389 C CA B GLU A 1 288 ? 6.991 13.233 -2.807 0.50 13.54 ? 288 GLU A CA 1
+ATOM 2390 C C A GLU A 1 288 ? 8.376 12.638 -2.986 0.50 13.16 ? 288 GLU A C 1
+ATOM 2391 C C B GLU A 1 288 ? 8.390 12.654 -2.992 0.50 13.22 ? 288 GLU A C 1
+ATOM 2392 O O A GLU A 1 288 ? 8.883 12.653 -4.105 0.50 13.26 ? 288 GLU A O 1
+ATOM 2393 O O B GLU A 1 288 ? 8.917 12.689 -4.102 0.50 13.37 ? 288 GLU A O 1
+ATOM 2394 C CB A GLU A 1 288 ? 5.916 12.318 -3.382 0.50 14.44 ? 288 GLU A CB 1
+ATOM 2395 C CB B GLU A 1 288 ? 5.938 12.358 -3.504 0.50 14.59 ? 288 GLU A CB 1
+ATOM 2396 C CG A GLU A 1 288 ? 4.495 12.789 -3.115 0.50 16.46 ? 288 GLU A CG 1
+ATOM 2397 C CG B GLU A 1 288 ? 6.026 10.881 -3.187 0.50 16.96 ? 288 GLU A CG 1
+ATOM 2398 C CD A GLU A 1 288 ? 3.946 12.471 -1.736 0.50 20.85 ? 288 GLU A CD 1
+ATOM 2399 C CD B GLU A 1 288 ? 5.638 10.508 -1.773 0.50 19.50 ? 288 GLU A CD 1
+ATOM 2400 O OE1 A GLU A 1 288 ? 4.624 11.747 -0.972 0.50 22.15 ? 288 GLU A OE1 1
+ATOM 2401 O OE1 B GLU A 1 288 ? 6.458 9.855 -1.089 0.50 16.00 ? 288 GLU A OE1 1
+ATOM 2402 O OE2 A GLU A 1 288 ? 2.824 12.931 -1.426 0.50 21.03 ? 288 GLU A OE2 1
+ATOM 2403 O OE2 B GLU A 1 288 ? 4.514 10.867 -1.350 0.50 22.07 ? 288 GLU A OE2 1
+ATOM 2404 N N . ASP A 1 289 ? 8.971 12.078 -1.927 1.00 12.93 ? 289 ASP A N 1
+ATOM 2405 C CA . ASP A 1 289 ? 10.310 11.516 -2.024 1.00 12.60 ? 289 ASP A CA 1
+ATOM 2406 C C . ASP A 1 289 ? 10.423 10.047 -1.666 1.00 13.43 ? 289 ASP A C 1
+ATOM 2407 O O . ASP A 1 289 ? 11.543 9.594 -1.414 1.00 13.88 ? 289 ASP A O 1
+ATOM 2408 C CB . ASP A 1 289 ? 11.323 12.330 -1.215 1.00 12.56 ? 289 ASP A CB 1
+ATOM 2409 C CG . ASP A 1 289 ? 11.288 12.143 0.274 1.00 14.92 ? 289 ASP A CG 1
+ATOM 2410 O OD1 . ASP A 1 289 ? 10.301 11.554 0.778 1.00 14.82 ? 289 ASP A OD1 1
+ATOM 2411 O OD2 . ASP A 1 289 ? 12.243 12.583 0.934 1.00 15.48 ? 289 ASP A OD2 1
+ATOM 2412 N N . GLU A 1 290 ? 9.296 9.306 -1.633 1.00 13.33 ? 290 GLU A N 1
+ATOM 2413 C CA . GLU A 1 290 ? 9.409 7.892 -1.299 1.00 13.90 ? 290 GLU A CA 1
+ATOM 2414 C C . GLU A 1 290 ? 9.082 6.995 -2.504 1.00 14.27 ? 290 GLU A C 1
+ATOM 2415 O O . GLU A 1 290 ? 8.544 5.902 -2.363 1.00 14.58 ? 290 GLU A O 1
+ATOM 2416 C CB . GLU A 1 290 ? 8.658 7.524 -0.006 1.00 14.67 ? 290 GLU A CB 1
+ATOM 2417 C CG . GLU A 1 290 ? 9.218 8.275 1.202 1.00 16.76 ? 290 GLU A CG 1
+ATOM 2418 C CD . GLU A 1 290 ? 8.875 7.717 2.576 1.00 18.56 ? 290 GLU A CD 1
+ATOM 2419 O OE1 . GLU A 1 290 ? 7.986 6.840 2.655 1.00 16.60 ? 290 GLU A OE1 1
+ATOM 2420 O OE2 . GLU A 1 290 ? 9.511 8.133 3.572 1.00 19.92 ? 290 GLU A OE2 1
+ATOM 2421 N N . PHE A 1 291 ? 9.510 7.433 -3.696 1.00 13.63 ? 291 PHE A N 1
+ATOM 2422 C CA . PHE A 1 291 ? 9.546 6.589 -4.879 1.00 14.24 ? 291 PHE A CA 1
+ATOM 2423 C C . PHE A 1 291 ? 10.925 6.730 -5.436 1.00 14.69 ? 291 PHE A C 1
+ATOM 2424 O O . PHE A 1 291 ? 11.307 7.844 -5.781 1.00 15.37 ? 291 PHE A O 1
+ATOM 2425 C CB . PHE A 1 291 ? 8.614 7.038 -5.997 1.00 14.36 ? 291 PHE A CB 1
+ATOM 2426 C CG . PHE A 1 291 ? 7.153 6.969 -5.703 1.00 15.75 ? 291 PHE A CG 1
+ATOM 2427 C CD1 . PHE A 1 291 ? 6.458 5.787 -5.858 1.00 16.87 ? 291 PHE A CD1 1
+ATOM 2428 C CD2 . PHE A 1 291 ? 6.457 8.100 -5.333 1.00 17.27 ? 291 PHE A CD2 1
+ATOM 2429 C CE1 . PHE A 1 291 ? 5.089 5.746 -5.646 1.00 18.29 ? 291 PHE A CE1 1
+ATOM 2430 C CE2 . PHE A 1 291 ? 5.090 8.060 -5.145 1.00 18.48 ? 291 PHE A CE2 1
+ATOM 2431 C CZ . PHE A 1 291 ? 4.414 6.885 -5.307 1.00 18.11 ? 291 PHE A CZ 1
+ATOM 2432 N N . THR A 1 292 ? 11.657 5.637 -5.560 1.00 14.58 ? 292 THR A N 1
+ATOM 2433 C CA . THR A 1 292 ? 12.980 5.663 -6.157 1.00 14.64 ? 292 THR A CA 1
+ATOM 2434 C C . THR A 1 292 ? 12.849 5.681 -7.683 1.00 14.39 ? 292 THR A C 1
+ATOM 2435 O O . THR A 1 292 ? 11.814 5.278 -8.228 1.00 14.19 ? 292 THR A O 1
+ATOM 2436 C CB . THR A 1 292 ? 13.753 4.380 -5.771 1.00 15.84 ? 292 THR A CB 1
+ATOM 2437 O OG1 . THR A 1 292 ? 13.148 3.243 -6.396 1.00 17.07 ? 292 THR A OG1 1
+ATOM 2438 C CG2 . THR A 1 292 ? 13.836 4.168 -4.275 1.00 15.86 ? 292 THR A CG2 1
+ATOM 2439 N N . PRO A 1 293 ? 13.938 5.984 -8.406 1.00 14.84 ? 293 PRO A N 1
+ATOM 2440 C CA . PRO A 1 293 ? 13.897 5.872 -9.875 1.00 14.67 ? 293 PRO A CA 1
+ATOM 2441 C C . PRO A 1 293 ? 13.499 4.455 -10.322 1.00 15.65 ? 293 PRO A C 1
+ATOM 2442 O O . PRO A 1 293 ? 12.761 4.300 -11.296 1.00 16.06 ? 293 PRO A O 1
+ATOM 2443 C CB . PRO A 1 293 ? 15.339 6.206 -10.275 1.00 15.78 ? 293 PRO A CB 1
+ATOM 2444 C CG . PRO A 1 293 ? 15.801 7.141 -9.190 1.00 16.06 ? 293 PRO A CG 1
+ATOM 2445 C CD . PRO A 1 293 ? 15.229 6.536 -7.942 1.00 14.54 ? 293 PRO A CD 1
+ATOM 2446 N N . PHE A 1 294 ? 13.961 3.420 -9.593 1.00 16.05 ? 294 PHE A N 1
+ATOM 2447 C CA A PHE A 1 294 ? 13.614 2.037 -9.947 0.60 17.63 ? 294 PHE A CA 1
+ATOM 2448 C CA B PHE A 1 294 ? 13.625 2.042 -9.943 0.40 17.39 ? 294 PHE A CA 1
+ATOM 2449 C C . PHE A 1 294 ? 12.129 1.806 -9.755 1.00 17.49 ? 294 PHE A C 1
+ATOM 2450 O O . PHE A 1 294 ? 11.509 1.147 -10.587 1.00 18.53 ? 294 PHE A O 1
+ATOM 2451 C CB A PHE A 1 294 ? 14.414 1.007 -9.126 0.60 18.71 ? 294 PHE A CB 1
+ATOM 2452 C CB B PHE A 1 294 ? 14.457 1.057 -9.109 0.40 18.14 ? 294 PHE A CB 1
+ATOM 2453 C CG A PHE A 1 294 ? 15.839 0.729 -9.559 0.60 20.73 ? 294 PHE A CG 1
+ATOM 2454 C CG B PHE A 1 294 ? 14.453 -0.377 -9.584 0.40 19.78 ? 294 PHE A CG 1
+ATOM 2455 C CD1 A PHE A 1 294 ? 16.370 1.325 -10.689 0.60 22.07 ? 294 PHE A CD1 1
+ATOM 2456 C CD1 B PHE A 1 294 ? 14.237 -0.685 -10.916 0.40 21.21 ? 294 PHE A CD1 1
+ATOM 2457 C CD2 A PHE A 1 294 ? 16.668 -0.076 -8.794 0.60 22.36 ? 294 PHE A CD2 1
+ATOM 2458 C CD2 B PHE A 1 294 ? 14.733 -1.411 -8.711 0.40 21.02 ? 294 PHE A CD2 1
+ATOM 2459 C CE1 A PHE A 1 294 ? 17.685 1.092 -11.061 0.60 23.04 ? 294 PHE A CE1 1
+ATOM 2460 C CE1 B PHE A 1 294 ? 14.239 -2.002 -11.348 0.40 22.18 ? 294 PHE A CE1 1
+ATOM 2461 C CE2 A PHE A 1 294 ? 17.988 -0.290 -9.162 0.60 23.26 ? 294 PHE A CE2 1
+ATOM 2462 C CE2 B PHE A 1 294 ? 14.734 -2.729 -9.147 0.40 21.90 ? 294 PHE A CE2 1
+ATOM 2463 C CZ A PHE A 1 294 ? 18.485 0.292 -10.294 0.60 23.11 ? 294 PHE A CZ 1
+ATOM 2464 C CZ B PHE A 1 294 ? 14.485 -3.015 -10.461 0.40 21.80 ? 294 PHE A CZ 1
+ATOM 2465 N N . ASP A 1 295 ? 11.540 2.357 -8.678 1.00 16.66 ? 295 ASP A N 1
+ATOM 2466 C CA . ASP A 1 295 ? 10.103 2.218 -8.410 1.00 16.33 ? 295 ASP A CA 1
+ATOM 2467 C C . ASP A 1 295 ? 9.308 2.848 -9.537 1.00 17.17 ? 295 ASP A C 1
+ATOM 2468 O O . ASP A 1 295 ? 8.307 2.286 -9.970 1.00 18.29 ? 295 ASP A O 1
+ATOM 2469 C CB . ASP A 1 295 ? 9.693 2.913 -7.106 1.00 17.12 ? 295 ASP A CB 1
+ATOM 2470 C CG . ASP A 1 295 ? 10.224 2.304 -5.838 1.00 18.41 ? 295 ASP A CG 1
+ATOM 2471 O OD1 . ASP A 1 295 ? 10.556 1.095 -5.850 1.00 19.16 ? 295 ASP A OD1 1
+ATOM 2472 O OD2 . ASP A 1 295 ? 10.319 3.037 -4.827 1.00 18.01 ? 295 ASP A OD2 1
+ATOM 2473 N N . VAL A 1 296 ? 9.741 4.040 -9.998 1.00 16.16 ? 296 VAL A N 1
+ATOM 2474 C CA . VAL A 1 296 ? 9.047 4.738 -11.073 1.00 16.40 ? 296 VAL A CA 1
+ATOM 2475 C C . VAL A 1 296 ? 9.068 3.925 -12.358 1.00 18.06 ? 296 VAL A C 1
+ATOM 2476 O O . VAL A 1 296 ? 8.017 3.731 -12.959 1.00 19.14 ? 296 VAL A O 1
+ATOM 2477 C CB . VAL A 1 296 ? 9.581 6.179 -11.258 1.00 16.18 ? 296 VAL A CB 1
+ATOM 2478 C CG1 . VAL A 1 296 ? 8.940 6.830 -12.468 1.00 16.59 ? 296 VAL A CG1 1
+ATOM 2479 C CG2 . VAL A 1 296 ? 9.293 7.003 -10.012 1.00 16.05 ? 296 VAL A CG2 1
+ATOM 2480 N N . VAL A 1 297 ? 10.238 3.395 -12.748 1.00 18.39 ? 297 VAL A N 1
+ATOM 2481 C CA . VAL A 1 297 ? 10.337 2.563 -13.952 1.00 19.89 ? 297 VAL A CA 1
+ATOM 2482 C C . VAL A 1 297 ? 9.473 1.298 -13.807 1.00 20.88 ? 297 VAL A C 1
+ATOM 2483 O O . VAL A 1 297 ? 8.737 0.942 -14.739 1.00 21.36 ? 297 VAL A O 1
+ATOM 2484 C CB . VAL A 1 297 ? 11.811 2.192 -14.251 1.00 21.55 ? 297 VAL A CB 1
+ATOM 2485 C CG1 . VAL A 1 297 ? 11.910 1.180 -15.391 1.00 22.49 ? 297 VAL A CG1 1
+ATOM 2486 C CG2 . VAL A 1 297 ? 12.640 3.438 -14.563 1.00 22.68 ? 297 VAL A CG2 1
+ATOM 2487 N N . ARG A 1 298 ? 9.549 0.644 -12.641 1.00 21.24 ? 298 ARG A N 1
+ATOM 2488 C CA . ARG A 1 298 ? 8.807 -0.585 -12.372 1.00 22.55 ? 298 ARG A CA 1
+ATOM 2489 C C . ARG A 1 298 ? 7.308 -0.361 -12.501 1.00 22.93 ? 298 ARG A C 1
+ATOM 2490 O O . ARG A 1 298 ? 6.636 -1.115 -13.208 1.00 22.97 ? 298 ARG A O 1
+ATOM 2491 C CB . ARG A 1 298 ? 9.156 -1.144 -10.976 1.00 25.03 ? 298 ARG A CB 1
+ATOM 2492 C CG . ARG A 1 298 ? 8.689 -2.583 -10.744 1.00 29.79 ? 298 ARG A CG 1
+ATOM 2493 C CD . ARG A 1 298 ? 8.979 -3.085 -9.331 1.00 34.67 ? 298 ARG A CD 1
+ATOM 2494 N NE . ARG A 1 298 ? 10.404 -3.075 -8.999 1.00 39.16 ? 298 ARG A NE 1
+ATOM 2495 C CZ . ARG A 1 298 ? 10.970 -2.244 -8.127 1.00 42.47 ? 298 ARG A CZ 1
+ATOM 2496 N NH1 . ARG A 1 298 ? 12.272 -2.306 -7.894 1.00 43.09 ? 298 ARG A NH1 1
+ATOM 2497 N NH2 . ARG A 1 298 ? 10.237 -1.347 -7.482 1.00 42.21 ? 298 ARG A NH2 1
+ATOM 2498 N N . GLN A 1 299 ? 6.784 0.674 -11.846 1.00 23.07 ? 299 GLN A N 1
+ATOM 2499 C CA . GLN A 1 299 ? 5.354 0.958 -11.884 1.00 23.81 ? 299 GLN A CA 1
+ATOM 2500 C C . GLN A 1 299 ? 4.900 1.427 -13.238 1.00 25.68 ? 299 GLN A C 1
+ATOM 2501 O O . GLN A 1 299 ? 3.853 0.988 -13.714 1.00 26.69 ? 299 GLN A O 1
+ATOM 2502 C CB . GLN A 1 299 ? 4.957 1.970 -10.809 1.00 23.65 ? 299 GLN A CB 1
+ATOM 2503 C CG . GLN A 1 299 ? 3.447 2.122 -10.708 1.00 23.14 ? 299 GLN A CG 1
+ATOM 2504 C CD . GLN A 1 299 ? 2.957 2.977 -9.576 1.00 22.18 ? 299 GLN A CD 1
+ATOM 2505 O OE1 . GLN A 1 299 ? 1.844 3.497 -9.627 1.00 22.38 ? 299 GLN A OE1 1
+ATOM 2506 N NE2 . GLN A 1 299 ? 3.758 3.156 -8.534 1.00 20.10 ? 299 GLN A NE2 1
+ATOM 2507 N N . CYS A 1 300 ? 5.691 2.286 -13.886 1.00 26.06 ? 300 CYS A N 1
+ATOM 2508 C CA . CYS A 1 300 ? 5.337 2.786 -15.204 1.00 27.01 ? 300 CYS A CA 1
+ATOM 2509 C C . CYS A 1 300 ? 5.445 1.714 -16.315 1.00 28.98 ? 300 CYS A C 1
+ATOM 2510 O O . CYS A 1 300 ? 4.855 1.899 -17.375 1.00 29.26 ? 300 CYS A O 1
+ATOM 2511 C CB . CYS A 1 300 ? 6.127 4.045 -15.545 1.00 26.34 ? 300 CYS A CB 1
+ATOM 2512 S SG . CYS A 1 300 ? 5.721 5.471 -14.500 1.00 27.90 ? 300 CYS A SG 1
+ATOM 2513 N N . SER A 1 301 ? 6.132 0.583 -16.063 1.00 30.28 ? 301 SER A N 1
+ATOM 2514 C CA . SER A 1 301 ? 6.245 -0.481 -17.069 1.00 32.04 ? 301 SER A CA 1
+ATOM 2515 C C . SER A 1 301 ? 5.465 -1.768 -16.734 1.00 33.71 ? 301 SER A C 1
+ATOM 2516 O O . SER A 1 301 ? 5.292 -2.617 -17.604 1.00 34.43 ? 301 SER A O 1
+ATOM 2517 C CB . SER A 1 301 ? 7.705 -0.806 -17.369 1.00 33.84 ? 301 SER A CB 1
+ATOM 2518 O OG . SER A 1 301 ? 8.315 -1.500 -16.296 1.00 36.40 ? 301 SER A OG 1
+ATOM 2519 N N . GLY A 1 302 ? 5.019 -1.910 -15.491 1.00 34.12 ? 302 GLY A N 1
+ATOM 2520 C CA . GLY A 1 302 ? 4.222 -3.058 -15.071 1.00 35.05 ? 302 GLY A CA 1
+ATOM 2521 C C . GLY A 1 302 ? 4.997 -4.334 -14.820 1.00 35.61 ? 302 GLY A C 1
+ATOM 2522 O O . GLY A 1 302 ? 4.571 -5.413 -15.243 1.00 36.15 ? 302 GLY A O 1
+ATOM 2523 N N . VAL A 1 303 ? 6.128 -4.228 -14.109 1.00 35.32 ? 303 VAL A N 1
+ATOM 2524 C CA . VAL A 1 303 ? 6.954 -5.389 -13.780 1.00 35.32 ? 303 VAL A CA 1
+ATOM 2525 C C . VAL A 1 303 ? 6.215 -6.275 -12.784 1.00 34.93 ? 303 VAL A C 1
+ATOM 2526 O O . VAL A 1 303 ? 5.658 -5.767 -11.815 1.00 34.71 ? 303 VAL A O 1
+ATOM 2527 C CB . VAL A 1 303 ? 8.320 -4.942 -13.211 1.00 36.13 ? 303 VAL A CB 1
+ATOM 2528 C CG1 . VAL A 1 303 ? 9.179 -6.136 -12.804 1.00 36.86 ? 303 VAL A CG1 1
+ATOM 2529 C CG2 . VAL A 1 303 ? 9.059 -4.069 -14.209 1.00 36.62 ? 303 VAL A CG2 1
+ATOM 2530 N N A THR A 1 304 ? 6.200 -7.599 -13.004 0.50 34.73 ? 304 THR A N 1
+ATOM 2531 N N B THR A 1 304 ? 6.201 -7.585 -13.044 0.50 34.72 ? 304 THR A N 1
+ATOM 2532 C CA A THR A 1 304 ? 5.514 -8.516 -12.093 0.50 34.97 ? 304 THR A CA 1
+ATOM 2533 C CA B THR A 1 304 ? 5.553 -8.566 -12.184 0.50 34.96 ? 304 THR A CA 1
+ATOM 2534 C C A THR A 1 304 ? 6.476 -9.352 -11.246 0.50 35.09 ? 304 THR A C 1
+ATOM 2535 C C B THR A 1 304 ? 6.556 -9.620 -11.706 0.50 35.18 ? 304 THR A C 1
+ATOM 2536 O O A THR A 1 304 ? 6.038 -10.116 -10.384 0.50 34.91 ? 304 THR A O 1
+ATOM 2537 O O B THR A 1 304 ? 7.751 -9.347 -11.597 0.50 35.09 ? 304 THR A O 1
+ATOM 2538 C CB A THR A 1 304 ? 4.532 -9.384 -12.868 0.50 36.14 ? 304 THR A CB 1
+ATOM 2539 C CB B THR A 1 304 ? 4.394 -9.205 -12.939 0.50 35.98 ? 304 THR A CB 1
+ATOM 2540 O OG1 A THR A 1 304 ? 5.255 -10.142 -13.839 0.50 37.13 ? 304 THR A OG1 1
+ATOM 2541 O OG1 B THR A 1 304 ? 4.903 -9.804 -14.134 0.50 36.92 ? 304 THR A OG1 1
+ATOM 2542 C CG2 A THR A 1 304 ? 3.471 -8.559 -13.555 0.50 36.53 ? 304 THR A CG2 1
+ATOM 2543 C CG2 B THR A 1 304 ? 3.329 -8.196 -13.297 0.50 36.25 ? 304 THR A CG2 1
+HETATM 2544 S S . DMS B 2 . ? 6.882 -28.125 21.472 1.00 20.06 ? 401 DMS A S 1
+HETATM 2545 O O . DMS B 2 . ? 7.674 -27.206 22.316 1.00 20.48 ? 401 DMS A O 1
+HETATM 2546 C C1 . DMS B 2 . ? 5.955 -27.138 20.370 1.00 19.79 ? 401 DMS A C1 1
+HETATM 2547 C C2 . DMS B 2 . ? 5.581 -28.752 22.497 1.00 19.86 ? 401 DMS A C2 1
+HETATM 2548 S S . DMS C 2 . ? 7.044 -21.256 28.847 1.00 48.64 ? 402 DMS A S 1
+HETATM 2549 O O . DMS C 2 . ? 6.922 -22.717 28.688 1.00 48.54 ? 402 DMS A O 1
+HETATM 2550 C C1 . DMS C 2 . ? 5.390 -20.729 29.206 1.00 48.61 ? 402 DMS A C1 1
+HETATM 2551 C C2 . DMS C 2 . ? 7.732 -21.050 30.463 1.00 48.75 ? 402 DMS A C2 1
+HETATM 2552 S S . DMS D 2 . ? 6.261 -1.076 -6.323 1.00 29.95 ? 403 DMS A S 1
+HETATM 2553 O O . DMS D 2 . ? 5.958 -2.533 -6.360 1.00 30.71 ? 403 DMS A O 1
+HETATM 2554 C C1 . DMS D 2 . ? 7.022 -0.725 -7.858 1.00 30.37 ? 403 DMS A C1 1
+HETATM 2555 C C2 . DMS D 2 . ? 7.596 -0.894 -5.175 1.00 30.14 ? 403 DMS A C2 1
+HETATM 2556 S S . DMS E 2 . ? 2.371 -18.855 7.984 1.00 36.23 ? 404 DMS A S 1
+HETATM 2557 O O . DMS E 2 . ? 1.975 -20.201 7.546 1.00 36.88 ? 404 DMS A O 1
+HETATM 2558 C C1 . DMS E 2 . ? 3.628 -19.160 9.196 1.00 36.02 ? 404 DMS A C1 1
+HETATM 2559 C C2 . DMS E 2 . ? 1.058 -18.333 9.062 1.00 36.25 ? 404 DMS A C2 1
+HETATM 2560 O O . HOH F 3 . ? 16.168 1.473 -5.859 1.00 46.52 ? 501 HOH A O 1
+HETATM 2561 O O . HOH F 3 . ? 14.078 -19.491 32.277 1.00 41.46 ? 502 HOH A O 1
+HETATM 2562 O O . HOH F 3 . ? 6.880 13.380 21.324 1.00 29.25 ? 503 HOH A O 1
+HETATM 2563 O O . HOH F 3 . ? 13.998 -10.881 31.006 1.00 35.36 ? 504 HOH A O 1
+HETATM 2564 O O . HOH F 3 . ? -0.912 17.057 -19.539 1.00 38.93 ? 505 HOH A O 1
+HETATM 2565 O O . HOH F 3 . ? -3.061 10.895 -16.794 1.00 40.86 ? 506 HOH A O 1
+HETATM 2566 O O . HOH F 3 . ? 6.044 5.803 1.306 1.00 24.97 ? 507 HOH A O 1
+HETATM 2567 O O . HOH F 3 . ? 2.799 4.893 20.226 1.00 34.61 ? 508 HOH A O 1
+HETATM 2568 O O . HOH F 3 . ? 24.406 -5.758 8.993 1.00 17.99 ? 509 HOH A O 1
+HETATM 2569 O O . HOH F 3 . ? 21.426 -20.287 30.771 1.00 23.30 ? 510 HOH A O 1
+HETATM 2570 O O . HOH F 3 . ? 11.397 31.677 -2.156 1.00 25.90 ? 511 HOH A O 1
+HETATM 2571 O O . HOH F 3 . ? 12.195 -27.051 22.943 1.00 19.83 ? 512 HOH A O 1
+HETATM 2572 O O . HOH F 3 . ? 19.756 10.134 -2.112 1.00 30.96 ? 513 HOH A O 1
+HETATM 2573 O O . HOH F 3 . ? 5.478 -17.689 1.918 1.00 19.67 ? 514 HOH A O 1
+HETATM 2574 O O . HOH F 3 . ? 8.621 24.377 -11.854 1.00 26.34 ? 515 HOH A O 1
+HETATM 2575 O O . HOH F 3 . ? 0.090 -17.755 15.613 1.00 35.61 ? 516 HOH A O 1
+HETATM 2576 O O . HOH F 3 . ? 9.022 -26.606 14.754 1.00 40.22 ? 517 HOH A O 1
+HETATM 2577 O O . HOH F 3 . ? 9.601 -23.263 23.053 1.00 21.34 ? 518 HOH A O 1
+HETATM 2578 O O . HOH F 3 . ? 7.168 -26.153 0.208 1.00 33.81 ? 519 HOH A O 1
+HETATM 2579 O O . HOH F 3 . ? 16.939 -5.562 33.520 1.00 37.83 ? 520 HOH A O 1
+HETATM 2580 O O . HOH F 3 . ? 8.175 -31.641 17.026 1.00 31.45 ? 521 HOH A O 1
+HETATM 2581 O O . HOH F 3 . ? 20.485 8.740 25.153 1.00 39.46 ? 522 HOH A O 1
+HETATM 2582 O O . HOH F 3 . ? 6.032 -8.497 8.633 1.00 14.96 ? 523 HOH A O 1
+HETATM 2583 O O . HOH F 3 . ? 13.232 10.946 19.529 1.00 48.19 ? 524 HOH A O 1
+HETATM 2584 O O . HOH F 3 . ? 3.638 22.182 -0.621 1.00 34.15 ? 525 HOH A O 1
+HETATM 2585 O O . HOH F 3 . ? 6.136 4.320 21.727 1.00 40.25 ? 526 HOH A O 1
+HETATM 2586 O O . HOH F 3 . ? 24.549 4.929 18.980 1.00 27.73 ? 527 HOH A O 1
+HETATM 2587 O O . HOH F 3 . ? 21.248 -12.985 34.361 1.00 37.99 ? 528 HOH A O 1
+HETATM 2588 O O . HOH F 3 . ? 4.472 26.774 -8.479 1.00 30.69 ? 529 HOH A O 1
+HETATM 2589 O O . HOH F 3 . ? 16.252 12.230 7.025 1.00 30.97 ? 530 HOH A O 1
+HETATM 2590 O O . HOH F 3 . ? 6.267 8.345 11.973 1.00 33.79 ? 531 HOH A O 1
+HETATM 2591 O O . HOH F 3 . ? 14.837 -9.578 -4.136 1.00 34.69 ? 532 HOH A O 1
+HETATM 2592 O O . HOH F 3 . ? 23.775 -14.714 27.189 1.00 19.51 ? 533 HOH A O 1
+HETATM 2593 O O . HOH F 3 . ? 12.117 31.027 -8.579 1.00 28.22 ? 534 HOH A O 1
+HETATM 2594 O O . HOH F 3 . ? 10.798 -24.784 2.844 1.00 18.90 ? 535 HOH A O 1
+HETATM 2595 O O . HOH F 3 . ? 18.416 -28.970 20.813 1.00 44.66 ? 536 HOH A O 1
+HETATM 2596 O O . HOH F 3 . ? 13.207 23.157 -18.628 1.00 23.28 ? 537 HOH A O 1
+HETATM 2597 O O . HOH F 3 . ? 1.305 22.918 -1.525 1.00 39.57 ? 538 HOH A O 1
+HETATM 2598 O O . HOH F 3 . ? 13.733 -16.538 32.742 1.00 42.72 ? 539 HOH A O 1
+HETATM 2599 O O . HOH F 3 . ? 20.769 -13.106 10.684 1.00 24.31 ? 540 HOH A O 1
+HETATM 2600 O O . HOH F 3 . ? 8.621 5.486 22.418 1.00 37.97 ? 541 HOH A O 1
+HETATM 2601 O O . HOH F 3 . ? 19.369 9.113 0.911 0.50 21.92 ? 542 HOH A O 1
+HETATM 2602 O O . HOH F 3 . ? 20.059 10.278 15.617 1.00 20.33 ? 543 HOH A O 1
+HETATM 2603 O O . HOH F 3 . ? 13.595 0.797 -5.476 1.00 24.59 ? 544 HOH A O 1
+HETATM 2604 O O . HOH F 3 . ? 15.233 18.533 -21.978 1.00 20.38 ? 545 HOH A O 1
+HETATM 2605 O O . HOH F 3 . ? 4.305 7.616 10.196 1.00 32.91 ? 546 HOH A O 1
+HETATM 2606 O O . HOH F 3 . ? 28.704 8.986 -11.711 1.00 37.15 ? 547 HOH A O 1
+HETATM 2607 O O . HOH F 3 . ? 20.309 -18.432 26.843 1.00 19.13 ? 548 HOH A O 1
+HETATM 2608 O O . HOH F 3 . ? -0.916 1.911 13.421 1.00 31.81 ? 549 HOH A O 1
+HETATM 2609 O O . HOH F 3 . ? 22.855 27.060 -0.065 1.00 31.20 ? 550 HOH A O 1
+HETATM 2610 O O . HOH F 3 . ? 14.655 26.081 4.261 1.00 21.96 ? 551 HOH A O 1
+HETATM 2611 O O . HOH F 3 . ? 3.751 4.190 -18.169 1.00 34.28 ? 552 HOH A O 1
+HETATM 2612 O O . HOH F 3 . ? 13.326 -24.508 3.825 1.00 22.78 ? 553 HOH A O 1
+HETATM 2613 O O . HOH F 3 . ? 27.169 26.220 -11.432 1.00 21.90 ? 554 HOH A O 1
+HETATM 2614 O O . HOH F 3 . ? 9.882 19.723 -0.456 1.00 21.00 ? 555 HOH A O 1
+HETATM 2615 O O . HOH F 3 . ? -3.265 28.392 -8.099 1.00 21.52 ? 556 HOH A O 1
+HETATM 2616 O O . HOH F 3 . ? 20.738 21.420 4.165 1.00 27.07 ? 557 HOH A O 1
+HETATM 2617 O O . HOH F 3 . ? 6.867 -23.050 20.986 1.00 15.42 ? 558 HOH A O 1
+HETATM 2618 O O . HOH F 3 . ? 8.877 28.045 -1.387 1.00 22.94 ? 559 HOH A O 1
+HETATM 2619 O O . HOH F 3 . ? 0.113 -1.132 12.039 1.00 27.87 ? 560 HOH A O 1
+HETATM 2620 O O . HOH F 3 . ? 2.365 -8.994 18.707 1.00 22.91 ? 561 HOH A O 1
+HETATM 2621 O O . HOH F 3 . ? 4.775 24.485 -18.488 1.00 38.08 ? 562 HOH A O 1
+HETATM 2622 O O . HOH F 3 . ? 11.512 21.778 -17.020 1.00 21.35 ? 563 HOH A O 1
+HETATM 2623 O O . HOH F 3 . ? -1.260 -19.317 22.131 1.00 37.41 ? 564 HOH A O 1
+HETATM 2624 O O . HOH F 3 . ? 23.016 1.706 15.920 1.00 19.55 ? 565 HOH A O 1
+HETATM 2625 O O . HOH F 3 . ? 22.194 19.573 0.676 1.00 26.37 ? 566 HOH A O 1
+HETATM 2626 O O . HOH F 3 . ? 8.161 -17.907 28.320 1.00 34.19 ? 567 HOH A O 1
+HETATM 2627 O O . HOH F 3 . ? 7.958 3.525 -3.456 1.00 17.12 ? 568 HOH A O 1
+HETATM 2628 O O . HOH F 3 . ? 15.855 -27.834 12.287 1.00 23.48 ? 569 HOH A O 1
+HETATM 2629 O O . HOH F 3 . ? 16.709 28.254 -20.308 1.00 19.84 ? 570 HOH A O 1
+HETATM 2630 O O . HOH F 3 . ? 8.450 15.959 1.017 1.00 29.83 ? 571 HOH A O 1
+HETATM 2631 O O . HOH F 3 . ? 9.777 6.249 5.698 1.00 15.43 ? 572 HOH A O 1
+HETATM 2632 O O . HOH F 3 . ? 17.679 -25.053 30.209 1.00 30.30 ? 573 HOH A O 1
+HETATM 2633 O O . HOH F 3 . ? -5.912 -4.357 9.377 1.00 39.55 ? 574 HOH A O 1
+HETATM 2634 O O . HOH F 3 . ? 25.363 9.442 -4.945 1.00 28.46 ? 575 HOH A O 1
+HETATM 2635 O O . HOH F 3 . ? 16.878 6.559 -3.938 1.00 17.95 ? 576 HOH A O 1
+HETATM 2636 O O . HOH F 3 . ? 12.105 -32.691 16.980 1.00 31.58 ? 577 HOH A O 1
+HETATM 2637 O O . HOH F 3 . ? 12.237 21.928 2.499 1.00 20.92 ? 578 HOH A O 1
+HETATM 2638 O O . HOH F 3 . ? 9.918 -25.725 22.117 1.00 14.76 ? 579 HOH A O 1
+HETATM 2639 O O . HOH F 3 . ? 21.216 28.768 -6.698 1.00 41.88 ? 580 HOH A O 1
+HETATM 2640 O O . HOH F 3 . ? 10.267 17.926 1.520 1.00 26.08 ? 581 HOH A O 1
+HETATM 2641 O O . HOH F 3 . ? 24.873 29.260 -8.891 1.00 23.50 ? 582 HOH A O 1
+HETATM 2642 O O . HOH F 3 . ? 18.869 10.206 13.140 1.00 19.66 ? 583 HOH A O 1
+HETATM 2643 O O . HOH F 3 . ? -1.740 -15.236 2.695 1.00 33.35 ? 584 HOH A O 1
+HETATM 2644 O O . HOH F 3 . ? 10.507 -0.544 -3.024 1.00 21.42 ? 585 HOH A O 1
+HETATM 2645 O O . HOH F 3 . ? 23.489 22.748 -17.286 1.00 16.05 ? 586 HOH A O 1
+HETATM 2646 O O . HOH F 3 . ? 13.322 21.382 -20.851 1.00 26.01 ? 587 HOH A O 1
+HETATM 2647 O O . HOH F 3 . ? 18.541 -8.076 -3.408 1.00 40.63 ? 588 HOH A O 1
+HETATM 2648 O O . HOH F 3 . ? 8.071 3.586 30.056 1.00 37.79 ? 589 HOH A O 1
+HETATM 2649 O O . HOH F 3 . ? -1.477 3.593 -1.801 1.00 42.67 ? 590 HOH A O 1
+HETATM 2650 O O . HOH F 3 . ? 3.602 22.218 -19.191 1.00 32.60 ? 591 HOH A O 1
+HETATM 2651 O O . HOH F 3 . ? 9.993 -17.767 -3.963 1.00 21.80 ? 592 HOH A O 1
+HETATM 2652 O O . HOH F 3 . ? 22.259 16.293 3.670 1.00 37.29 ? 593 HOH A O 1
+HETATM 2653 O O . HOH F 3 . ? 10.599 32.889 -5.240 1.00 50.44 ? 594 HOH A O 1
+HETATM 2654 O O . HOH F 3 . ? 13.521 12.427 17.221 1.00 36.62 ? 595 HOH A O 1
+HETATM 2655 O O . HOH F 3 . ? -3.864 -12.103 2.544 1.00 20.32 ? 596 HOH A O 1
+HETATM 2656 O O . HOH F 3 . ? 26.359 -5.686 17.729 1.00 34.04 ? 597 HOH A O 1
+HETATM 2657 O O . HOH F 3 . ? 0.896 -16.433 2.082 1.00 39.32 ? 598 HOH A O 1
+HETATM 2658 O O . HOH F 3 . ? 28.921 9.379 -15.273 1.00 32.13 ? 599 HOH A O 1
+HETATM 2659 O O . HOH F 3 . ? 24.011 13.123 -1.655 1.00 31.18 ? 600 HOH A O 1
+HETATM 2660 O O . HOH F 3 . ? 21.433 21.717 -18.735 1.00 17.60 ? 601 HOH A O 1
+HETATM 2661 O O . HOH F 3 . ? 1.773 1.863 0.024 1.00 26.63 ? 602 HOH A O 1
+HETATM 2662 O O . HOH F 3 . ? 7.494 -28.340 15.770 1.00 33.19 ? 603 HOH A O 1
+HETATM 2663 O O . HOH F 3 . ? 15.633 -5.640 20.179 1.00 12.60 ? 604 HOH A O 1
+HETATM 2664 O O . HOH F 3 . ? 22.115 9.845 5.153 1.00 29.86 ? 605 HOH A O 1
+HETATM 2665 O O . HOH F 3 . ? 24.327 -8.927 20.642 1.00 20.53 ? 606 HOH A O 1
+HETATM 2666 O O . HOH F 3 . ? 16.826 -18.849 7.693 1.00 18.59 ? 607 HOH A O 1
+HETATM 2667 O O . HOH F 3 . ? 28.679 18.724 -8.356 1.00 35.42 ? 608 HOH A O 1
+HETATM 2668 O O . HOH F 3 . ? 24.424 -0.652 12.999 1.00 27.63 ? 609 HOH A O 1
+HETATM 2669 O O . HOH F 3 . ? -0.724 22.828 -3.129 1.00 39.81 ? 610 HOH A O 1
+HETATM 2670 O O . HOH F 3 . ? 19.959 5.204 -1.851 1.00 27.89 ? 611 HOH A O 1
+HETATM 2671 O O . HOH F 3 . ? 15.062 26.996 -12.204 1.00 18.02 ? 612 HOH A O 1
+HETATM 2672 O O . HOH F 3 . ? 8.199 -28.395 6.565 1.00 25.90 ? 613 HOH A O 1
+HETATM 2673 O O . HOH F 3 . ? 7.788 -24.522 25.639 1.00 18.95 ? 614 HOH A O 1
+HETATM 2674 O O . HOH F 3 . ? 10.042 -5.817 25.008 1.00 36.65 ? 615 HOH A O 1
+HETATM 2675 O O . HOH F 3 . ? 22.116 2.055 5.700 1.00 36.41 ? 616 HOH A O 1
+HETATM 2676 O O . HOH F 3 . ? 3.693 -17.399 20.860 1.00 18.97 ? 617 HOH A O 1
+HETATM 2677 O O . HOH F 3 . ? 26.732 23.577 -4.772 1.00 19.11 ? 618 HOH A O 1
+HETATM 2678 O O . HOH F 3 . ? 9.585 10.091 -4.896 1.00 12.16 ? 619 HOH A O 1
+HETATM 2679 O O . HOH F 3 . ? 1.295 -21.833 9.645 1.00 55.13 ? 620 HOH A O 1
+HETATM 2680 O O . HOH F 3 . ? 22.839 -7.292 34.441 1.00 27.63 ? 621 HOH A O 1
+HETATM 2681 O O . HOH F 3 . ? 18.961 -27.689 9.426 1.00 43.04 ? 622 HOH A O 1
+HETATM 2682 O O . HOH F 3 . ? 21.521 10.599 -17.013 1.00 25.46 ? 623 HOH A O 1
+HETATM 2683 O O . HOH F 3 . ? 13.990 14.918 12.502 1.00 32.85 ? 624 HOH A O 1
+HETATM 2684 O O . HOH F 3 . ? 1.918 -11.990 25.974 1.00 35.35 ? 625 HOH A O 1
+HETATM 2685 O O . HOH F 3 . ? -4.038 -9.431 16.969 1.00 48.81 ? 626 HOH A O 1
+HETATM 2686 O O . HOH F 3 . ? 13.366 19.059 3.371 1.00 28.20 ? 627 HOH A O 1
+HETATM 2687 O O . HOH F 3 . ? 24.678 1.909 12.377 1.00 46.47 ? 628 HOH A O 1
+HETATM 2688 O O . HOH F 3 . ? 14.580 -25.790 26.928 1.00 17.27 ? 629 HOH A O 1
+HETATM 2689 O O . HOH F 3 . ? 15.757 -12.840 31.816 1.00 22.74 ? 630 HOH A O 1
+HETATM 2690 O O . HOH F 3 . ? 14.529 -20.206 0.077 1.00 29.75 ? 631 HOH A O 1
+HETATM 2691 O O . HOH F 3 . ? 10.744 -23.544 0.343 1.00 18.47 ? 632 HOH A O 1
+HETATM 2692 O O . HOH F 3 . ? 2.570 13.675 -20.732 1.00 43.65 ? 633 HOH A O 1
+HETATM 2693 O O . HOH F 3 . ? 5.372 -6.477 21.881 1.00 27.60 ? 634 HOH A O 1
+HETATM 2694 O O . HOH F 3 . ? 3.140 9.142 -21.338 1.00 30.01 ? 635 HOH A O 1
+HETATM 2695 O O . HOH F 3 . ? 19.977 -21.182 28.743 1.00 32.10 ? 636 HOH A O 1
+HETATM 2696 O O . HOH F 3 . ? 7.570 12.013 0.722 1.00 33.53 ? 637 HOH A O 1
+HETATM 2697 O O . HOH F 3 . ? 12.447 11.173 10.477 1.00 26.80 ? 638 HOH A O 1
+HETATM 2698 O O . HOH F 3 . ? 15.757 6.369 -14.440 1.00 24.76 ? 639 HOH A O 1
+HETATM 2699 O O . HOH F 3 . ? 17.547 27.500 -12.889 1.00 19.19 ? 640 HOH A O 1
+HETATM 2700 O O . HOH F 3 . ? 5.057 -17.229 28.359 1.00 47.39 ? 641 HOH A O 1
+HETATM 2701 O O . HOH F 3 . ? -2.486 12.802 -14.220 1.00 42.13 ? 642 HOH A O 1
+HETATM 2702 O O . HOH F 3 . ? -4.994 23.645 -3.052 1.00 32.21 ? 643 HOH A O 1
+HETATM 2703 O O . HOH F 3 . ? -0.389 -15.332 10.266 1.00 36.06 ? 644 HOH A O 1
+HETATM 2704 O O . HOH F 3 . ? 5.665 2.461 -4.750 1.00 17.90 ? 645 HOH A O 1
+HETATM 2705 O O . HOH F 3 . ? 5.266 -27.778 14.491 1.00 36.75 ? 646 HOH A O 1
+HETATM 2706 O O . HOH F 3 . ? 2.594 25.678 -16.824 1.00 30.95 ? 647 HOH A O 1
+HETATM 2707 O O . HOH F 3 . ? 22.547 8.950 -2.317 1.00 43.74 ? 648 HOH A O 1
+HETATM 2708 O O . HOH F 3 . ? 15.056 -5.071 0.319 1.00 20.13 ? 649 HOH A O 1
+HETATM 2709 O O . HOH F 3 . ? 18.804 -7.696 6.107 1.00 16.54 ? 650 HOH A O 1
+HETATM 2710 O O . HOH F 3 . ? 6.258 2.386 -7.542 1.00 22.14 ? 651 HOH A O 1
+HETATM 2711 O O . HOH F 3 . ? 25.440 -15.867 12.089 1.00 45.56 ? 652 HOH A O 1
+HETATM 2712 O O . HOH F 3 . ? 13.858 31.054 -2.000 1.00 31.40 ? 653 HOH A O 1
+HETATM 2713 O O . HOH F 3 . ? 3.992 -22.184 7.072 1.00 17.77 ? 654 HOH A O 1
+HETATM 2714 O O . HOH F 3 . ? 16.781 4.789 30.472 1.00 57.67 ? 655 HOH A O 1
+HETATM 2715 O O . HOH F 3 . ? 14.653 -22.055 31.952 1.00 32.65 ? 656 HOH A O 1
+HETATM 2716 O O . HOH F 3 . ? 13.879 4.396 -20.671 1.00 28.86 ? 657 HOH A O 1
+HETATM 2717 O O . HOH F 3 . ? 27.708 -4.709 14.373 1.00 45.60 ? 658 HOH A O 1
+HETATM 2718 O O . HOH F 3 . ? -2.375 19.163 -11.398 1.00 31.14 ? 659 HOH A O 1
+HETATM 2719 O O . HOH F 3 . ? 9.946 -10.999 28.175 1.00 34.34 ? 660 HOH A O 1
+HETATM 2720 O O . HOH F 3 . ? 16.584 2.526 12.374 1.00 14.44 ? 661 HOH A O 1
+HETATM 2721 O O . HOH F 3 . ? 7.870 23.887 -2.281 1.00 26.01 ? 662 HOH A O 1
+HETATM 2722 O O . HOH F 3 . ? 15.076 11.269 -25.013 1.00 30.97 ? 663 HOH A O 1
+HETATM 2723 O O . HOH F 3 . ? 12.776 -3.174 -5.257 1.00 33.42 ? 664 HOH A O 1
+HETATM 2724 O O . HOH F 3 . ? 17.673 16.856 14.835 1.00 35.96 ? 665 HOH A O 1
+HETATM 2725 O O . HOH F 3 . ? -5.618 24.316 -7.513 1.00 20.87 ? 666 HOH A O 1
+HETATM 2726 O O . HOH F 3 . ? 29.467 15.778 -12.676 1.00 32.03 ? 667 HOH A O 1
+HETATM 2727 O O . HOH F 3 . ? -2.615 16.225 -9.453 1.00 26.89 ? 668 HOH A O 1
+HETATM 2728 O O . HOH F 3 . ? 20.970 6.298 19.867 1.00 27.96 ? 669 HOH A O 1
+HETATM 2729 O O . HOH F 3 . ? 22.051 -18.298 38.812 1.00 31.27 ? 670 HOH A O 1
+HETATM 2730 O O . HOH F 3 . ? 22.550 7.382 -17.399 1.00 24.21 ? 671 HOH A O 1
+HETATM 2731 O O . HOH F 3 . ? 20.505 18.890 3.164 1.00 33.29 ? 672 HOH A O 1
+HETATM 2732 O O . HOH F 3 . ? 21.340 -1.629 20.448 1.00 16.34 ? 673 HOH A O 1
+HETATM 2733 O O . HOH F 3 . ? -0.741 -15.736 14.250 1.00 30.76 ? 674 HOH A O 1
+HETATM 2734 O O . HOH F 3 . ? 23.323 20.417 -1.600 1.00 29.58 ? 675 HOH A O 1
+HETATM 2735 O O . HOH F 3 . ? 1.456 8.663 -6.092 1.00 38.82 ? 676 HOH A O 1
+HETATM 2736 O O . HOH F 3 . ? 17.887 4.741 -6.103 1.00 34.71 ? 677 HOH A O 1
+HETATM 2737 O O . HOH F 3 . ? 14.269 5.280 22.766 1.00 24.58 ? 678 HOH A O 1
+HETATM 2738 O O . HOH F 3 . ? 27.355 20.815 -5.391 1.00 24.25 ? 679 HOH A O 1
+HETATM 2739 O O . HOH F 3 . ? 9.720 -1.209 21.229 1.00 30.93 ? 680 HOH A O 1
+HETATM 2740 O O . HOH F 3 . ? 2.024 11.322 -5.624 1.00 22.74 ? 681 HOH A O 1
+HETATM 2741 O O . HOH F 3 . ? 9.861 24.688 -0.545 1.00 22.75 ? 682 HOH A O 1
+HETATM 2742 O O . HOH F 3 . ? 20.486 -1.656 24.001 1.00 24.64 ? 683 HOH A O 1
+HETATM 2743 O O . HOH F 3 . ? 23.225 2.694 9.309 1.00 22.82 ? 684 HOH A O 1
+HETATM 2744 O O . HOH F 3 . ? 27.418 16.923 -6.933 1.00 31.40 ? 685 HOH A O 1
+HETATM 2745 O O . HOH F 3 . ? 16.157 -27.895 23.992 1.00 21.03 ? 686 HOH A O 1
+HETATM 2746 O O . HOH F 3 . ? 18.371 -16.308 -2.702 1.00 39.26 ? 687 HOH A O 1
+HETATM 2747 O O . HOH F 3 . ? 25.461 -11.702 20.577 1.00 40.43 ? 688 HOH A O 1
+HETATM 2748 O O . HOH F 3 . ? 22.395 -0.560 18.161 1.00 15.98 ? 689 HOH A O 1
+HETATM 2749 O O . HOH F 3 . ? 11.106 -22.190 32.650 1.00 28.72 ? 690 HOH A O 1
+HETATM 2750 O O . HOH F 3 . ? 13.906 15.879 -26.087 1.00 40.25 ? 691 HOH A O 1
+HETATM 2751 O O . HOH F 3 . ? 3.233 28.434 -3.275 1.00 28.74 ? 692 HOH A O 1
+HETATM 2752 O O . HOH F 3 . ? 22.874 -2.369 16.096 1.00 16.71 ? 693 HOH A O 1
+HETATM 2753 O O . HOH F 3 . ? 5.924 -4.719 19.944 1.00 29.98 ? 694 HOH A O 1
+HETATM 2754 O O . HOH F 3 . ? 13.872 17.335 10.417 1.00 36.01 ? 695 HOH A O 1
+HETATM 2755 O O . HOH F 3 . ? -3.730 23.139 -15.560 1.00 97.94 ? 696 HOH A O 1
+HETATM 2756 O O . HOH F 3 . ? 8.299 -10.717 30.288 1.00 47.50 ? 697 HOH A O 1
+HETATM 2757 O O . HOH F 3 . ? 21.543 -1.801 26.438 1.00 47.98 ? 698 HOH A O 1
+HETATM 2758 O O . HOH F 3 . ? 18.028 -23.973 26.108 1.00 19.47 ? 699 HOH A O 1
+HETATM 2759 O O . HOH F 3 . ? 12.908 18.528 -23.180 1.00 41.68 ? 700 HOH A O 1
+HETATM 2760 O O . HOH F 3 . ? 2.949 30.284 -11.274 1.00 37.62 ? 701 HOH A O 1
+HETATM 2761 O O . HOH F 3 . ? 20.081 -20.090 16.613 1.00 22.76 ? 702 HOH A O 1
+HETATM 2762 O O . HOH F 3 . ? 18.378 30.888 -7.178 1.00 34.12 ? 703 HOH A O 1
+HETATM 2763 O O . HOH F 3 . ? 5.351 -31.635 18.500 1.00 40.71 ? 704 HOH A O 1
+HETATM 2764 O O . HOH F 3 . ? 0.701 25.514 -2.225 1.00 36.15 ? 705 HOH A O 1
+HETATM 2765 O O . HOH F 3 . ? 25.191 16.426 -14.367 1.00 24.82 ? 706 HOH A O 1
+HETATM 2766 O O . HOH F 3 . ? 21.234 -13.358 2.280 1.00 27.41 ? 707 HOH A O 1
+HETATM 2767 O O . HOH F 3 . ? 7.239 19.679 -0.526 1.00 19.53 ? 708 HOH A O 1
+HETATM 2768 O O . HOH F 3 . ? 26.231 -10.821 18.148 1.00 29.32 ? 709 HOH A O 1
+HETATM 2769 O O . HOH F 3 . ? 18.272 24.759 5.918 1.00 42.75 ? 710 HOH A O 1
+HETATM 2770 O O . HOH F 3 . ? 23.954 -16.170 21.645 1.00 23.30 ? 711 HOH A O 1
+HETATM 2771 O O . HOH F 3 . ? 10.555 -16.892 30.368 1.00 33.54 ? 712 HOH A O 1
+HETATM 2772 O O . HOH F 3 . ? -3.214 21.063 -9.741 1.00 34.02 ? 713 HOH A O 1
+HETATM 2773 O O . HOH F 3 . ? -2.136 9.260 -10.450 1.00 40.46 ? 714 HOH A O 1
+HETATM 2774 O O . HOH F 3 . ? 11.910 -29.685 8.498 1.00 34.74 ? 715 HOH A O 1
+HETATM 2775 O O . HOH F 3 . ? 1.343 -16.891 12.512 1.00 27.31 ? 716 HOH A O 1
+HETATM 2776 O O . HOH F 3 . ? 13.914 19.690 7.284 1.00 37.82 ? 717 HOH A O 1
+HETATM 2777 O O . HOH F 3 . ? -0.234 16.076 -0.146 0.50 11.47 ? 718 HOH A O 1
+HETATM 2778 O O . HOH F 3 . ? 24.548 -7.687 26.198 1.00 36.32 ? 719 HOH A O 1
+HETATM 2779 O O . HOH F 3 . ? 18.171 27.334 4.952 1.00 53.03 ? 720 HOH A O 1
+HETATM 2780 O O . HOH F 3 . ? 11.863 12.861 14.635 1.00 54.98 ? 721 HOH A O 1
+HETATM 2781 O O . HOH F 3 . ? 19.214 -6.192 32.419 1.00 25.40 ? 722 HOH A O 1
+HETATM 2782 O O . HOH F 3 . ? -0.227 7.570 -3.969 1.00 37.09 ? 723 HOH A O 1
+HETATM 2783 O O . HOH F 3 . ? 19.243 12.398 -3.622 1.00 19.12 ? 724 HOH A O 1
+HETATM 2784 O O . HOH F 3 . ? 23.410 -6.008 1.926 1.00 25.91 ? 725 HOH A O 1
+HETATM 2785 O O . HOH F 3 . ? 7.624 -8.536 -15.424 1.00 46.55 ? 726 HOH A O 1
+HETATM 2786 O O . HOH F 3 . ? 23.169 -8.425 4.161 1.00 50.23 ? 727 HOH A O 1
+HETATM 2787 O O . HOH F 3 . ? 20.967 16.913 -17.778 1.00 17.97 ? 728 HOH A O 1
+HETATM 2788 O O . HOH F 3 . ? 3.435 -8.065 24.643 1.00 37.20 ? 729 HOH A O 1
+HETATM 2789 O O . HOH F 3 . ? 2.421 -19.701 21.721 1.00 19.80 ? 730 HOH A O 1
+HETATM 2790 O O . HOH F 3 . ? 20.354 -26.799 18.082 1.00 35.93 ? 731 HOH A O 1
+HETATM 2791 O O . HOH F 3 . ? 26.885 -9.220 10.443 1.00 44.15 ? 732 HOH A O 1
+HETATM 2792 O O . HOH F 3 . ? 1.564 -8.119 21.531 1.00 37.29 ? 733 HOH A O 1
+HETATM 2793 O O . HOH F 3 . ? 15.456 24.744 7.786 1.00 37.81 ? 734 HOH A O 1
+HETATM 2794 O O . HOH F 3 . ? 27.760 21.772 -11.674 1.00 17.55 ? 735 HOH A O 1
+HETATM 2795 O O . HOH F 3 . ? -5.506 20.181 -8.002 1.00 40.32 ? 736 HOH A O 1
+HETATM 2796 O O . HOH F 3 . ? 11.915 15.221 4.229 1.00 32.50 ? 737 HOH A O 1
+HETATM 2797 O O . HOH F 3 . ? 30.151 25.265 -10.687 1.00 30.25 ? 738 HOH A O 1
+HETATM 2798 O O . HOH F 3 . ? 20.827 -22.801 22.064 1.00 21.95 ? 739 HOH A O 1
+HETATM 2799 O O . HOH F 3 . ? 13.583 -14.012 33.010 1.00 38.07 ? 740 HOH A O 1
+HETATM 2800 O O . HOH F 3 . ? 0.455 1.284 20.771 1.00 47.74 ? 741 HOH A O 1
+HETATM 2801 O O . HOH F 3 . ? -0.514 19.449 -15.740 1.00 36.34 ? 742 HOH A O 1
+HETATM 2802 O O . HOH F 3 . ? 23.836 -4.507 23.876 1.00 50.45 ? 743 HOH A O 1
+HETATM 2803 O O . HOH F 3 . ? 3.878 20.684 -21.337 1.00 32.39 ? 744 HOH A O 1
+HETATM 2804 O O . HOH F 3 . ? 24.290 -15.929 16.833 1.00 38.93 ? 745 HOH A O 1
+HETATM 2805 O O . HOH F 3 . ? 23.201 -5.397 26.412 1.00 24.88 ? 746 HOH A O 1
+HETATM 2806 O O . HOH F 3 . ? 26.273 20.548 -14.032 1.00 22.96 ? 747 HOH A O 1
+HETATM 2807 O O . HOH F 3 . ? 2.975 2.530 24.921 1.00 30.68 ? 748 HOH A O 1
+HETATM 2808 O O . HOH F 3 . ? 10.919 -11.853 30.486 1.00 37.95 ? 749 HOH A O 1
+HETATM 2809 O O . HOH F 3 . ? 20.396 13.586 9.082 1.00 33.87 ? 750 HOH A O 1
+HETATM 2810 O O . HOH F 3 . ? 11.865 4.048 22.653 1.00 33.22 ? 751 HOH A O 1
+HETATM 2811 O O . HOH F 3 . ? 27.729 -7.194 12.023 1.00 36.54 ? 752 HOH A O 1
+HETATM 2812 O O . HOH F 3 . ? 17.618 22.329 9.554 1.00 40.97 ? 753 HOH A O 1
+HETATM 2813 O O . HOH F 3 . ? 8.941 -7.897 -8.369 1.00 32.94 ? 754 HOH A O 1
+HETATM 2814 O O . HOH F 3 . ? 11.761 -29.800 22.589 1.00 19.37 ? 755 HOH A O 1
+HETATM 2815 O O . HOH F 3 . ? 28.635 10.717 -8.101 1.00 30.16 ? 756 HOH A O 1
+HETATM 2816 O O . HOH F 3 . ? 9.498 1.361 21.295 1.00 24.46 ? 757 HOH A O 1
+HETATM 2817 O O . HOH F 3 . ? 9.182 28.999 -17.474 1.00 26.72 ? 758 HOH A O 1
+HETATM 2818 O O . HOH F 3 . ? 16.203 30.204 -2.976 1.00 42.95 ? 759 HOH A O 1
+HETATM 2819 O O . HOH F 3 . ? 11.088 -31.620 10.226 1.00 43.15 ? 760 HOH A O 1
+HETATM 2820 O O . HOH F 3 . ? 20.093 -25.462 22.433 1.00 26.03 ? 761 HOH A O 1
+HETATM 2821 O O . HOH F 3 . ? 28.829 14.538 -8.128 1.00 34.41 ? 762 HOH A O 1
+HETATM 2822 O O . HOH F 3 . ? 3.441 24.795 -1.613 1.00 34.84 ? 763 HOH A O 1
+HETATM 2823 O O . HOH F 3 . ? 20.202 14.527 -19.039 1.00 33.34 ? 764 HOH A O 1
+HETATM 2824 O O . HOH F 3 . ? 0.115 -27.182 17.907 1.00 30.24 ? 765 HOH A O 1
+HETATM 2825 O O . HOH F 3 . ? 1.044 -16.222 23.465 1.00 44.28 ? 766 HOH A O 1
+HETATM 2826 O O . HOH F 3 . ? -2.627 17.627 -15.519 1.00 60.97 ? 767 HOH A O 1
+HETATM 2827 O O . HOH F 3 . ? 16.474 3.496 -7.806 1.00 29.34 ? 768 HOH A O 1
+HETATM 2828 O O . HOH F 3 . ? 24.409 -4.330 16.668 1.00 28.43 ? 769 HOH A O 1
+HETATM 2829 O O . HOH F 3 . ? 16.789 -18.630 -0.780 1.00 27.06 ? 770 HOH A O 1
+HETATM 2830 O O . HOH F 3 . ? 25.012 13.875 -17.225 1.00 25.24 ? 771 HOH A O 1
+HETATM 2831 O O . HOH F 3 . ? 6.492 -8.329 -7.853 1.00 39.75 ? 772 HOH A O 1
+HETATM 2832 O O . HOH F 3 . ? 20.068 -0.155 -1.012 1.00 35.16 ? 773 HOH A O 1
+HETATM 2833 O O . HOH F 3 . ? -0.000 -0.407 -0.000 0.50 24.99 ? 774 HOH A O 1
+HETATM 2834 O O . HOH F 3 . ? 11.274 -2.559 -16.545 1.00 43.12 ? 775 HOH A O 1
+HETATM 2835 O O . HOH F 3 . ? -1.568 6.148 -2.378 1.00 39.83 ? 776 HOH A O 1
+HETATM 2836 O O . HOH F 3 . ? -4.782 26.408 -9.310 1.00 22.16 ? 777 HOH A O 1
+HETATM 2837 O O . HOH F 3 . ? 16.309 -2.605 -2.855 1.00 41.31 ? 778 HOH A O 1
+HETATM 2838 O O . HOH F 3 . ? 30.825 20.967 -5.604 1.00 39.69 ? 779 HOH A O 1
+HETATM 2839 O O . HOH F 3 . ? 15.578 -19.046 34.790 1.00 41.80 ? 780 HOH A O 1
+HETATM 2840 O O . HOH F 3 . ? -2.125 -3.200 18.826 1.00 41.36 ? 781 HOH A O 1
+HETATM 2841 O O . HOH F 3 . ? 23.956 -20.421 20.945 1.00 45.16 ? 782 HOH A O 1
+HETATM 2842 O O . HOH F 3 . ? 12.859 22.637 6.077 1.00 35.21 ? 783 HOH A O 1
+HETATM 2843 O O . HOH F 3 . ? 25.214 -7.886 22.805 1.00 37.18 ? 784 HOH A O 1
+HETATM 2844 O O . HOH F 3 . ? 6.955 -15.138 -8.159 1.00 53.30 ? 785 HOH A O 1
+HETATM 2845 O O . HOH F 3 . ? 26.675 27.198 -8.963 1.00 30.23 ? 786 HOH A O 1
+HETATM 2846 O O . HOH F 3 . ? 5.969 2.060 28.913 1.00 39.92 ? 787 HOH A O 1
+HETATM 2847 O O . HOH F 3 . ? 3.824 -29.082 18.300 1.00 39.98 ? 788 HOH A O 1
+HETATM 2848 O O . HOH F 3 . ? 5.982 -23.035 -1.144 1.00 38.34 ? 789 HOH A O 1
+HETATM 2849 O O . HOH F 3 . ? 2.922 -18.050 1.197 1.00 32.81 ? 790 HOH A O 1
+HETATM 2850 O O . HOH F 3 . ? 21.637 -7.541 6.163 1.00 28.51 ? 791 HOH A O 1
+HETATM 2851 O O . HOH F 3 . ? 20.695 25.668 5.052 1.00 48.77 ? 792 HOH A O 1
+HETATM 2852 O O . HOH F 3 . ? 21.965 -17.907 23.656 1.00 32.28 ? 793 HOH A O 1
+HETATM 2853 O O . HOH F 3 . ? 3.738 9.887 14.440 1.00 38.47 ? 794 HOH A O 1
+HETATM 2854 O O . HOH F 3 . ? 7.546 -34.937 19.762 1.00 35.53 ? 795 HOH A O 1
+HETATM 2855 O O . HOH F 3 . ? 19.252 -11.117 34.347 1.00 37.85 ? 796 HOH A O 1
+HETATM 2856 O O . HOH F 3 . ? 17.203 15.425 -23.516 1.00 36.42 ? 797 HOH A O 1
+HETATM 2857 O O . HOH F 3 . ? 25.973 23.296 -2.028 1.00 29.90 ? 798 HOH A O 1
+HETATM 2858 O O . HOH F 3 . ? 17.194 -10.402 -5.842 1.00 42.68 ? 799 HOH A O 1
+HETATM 2859 O O . HOH F 3 . ? 8.784 -4.353 26.547 1.00 44.39 ? 800 HOH A O 1
+HETATM 2860 O O . HOH F 3 . ? 17.638 -17.925 37.524 1.00 49.93 ? 801 HOH A O 1
+HETATM 2861 O O . HOH F 3 . ? 12.370 32.802 -12.287 1.00 44.37 ? 802 HOH A O 1
+HETATM 2862 O O . HOH F 3 . ? 2.872 -1.757 -11.757 1.00 38.02 ? 803 HOH A O 1
+HETATM 2863 O O . HOH F 3 . ? 20.613 4.079 -5.766 1.00 40.55 ? 804 HOH A O 1
+HETATM 2864 O O . HOH F 3 . ? 14.640 -29.204 9.936 1.00 30.84 ? 805 HOH A O 1
+HETATM 2865 O O . HOH F 3 . ? 17.978 -19.808 33.834 1.00 31.41 ? 806 HOH A O 1
+HETATM 2866 O O . HOH F 3 . ? 15.789 -25.802 6.748 1.00 34.39 ? 807 HOH A O 1
+HETATM 2867 O O . HOH F 3 . ? 5.765 11.051 11.864 1.00 47.77 ? 808 HOH A O 1
+HETATM 2868 O O . HOH F 3 . ? 20.630 8.871 18.299 1.00 34.56 ? 809 HOH A O 1
+HETATM 2869 O O . HOH F 3 . ? 28.704 24.207 -12.425 1.00 28.48 ? 810 HOH A O 1
+HETATM 2870 O O . HOH F 3 . ? 0.105 -17.197 4.667 1.00 37.28 ? 811 HOH A O 1
+HETATM 2871 O O . HOH F 3 . ? 22.401 -22.767 19.930 1.00 34.52 ? 812 HOH A O 1
+HETATM 2872 O O . HOH F 3 . ? 18.717 -18.428 1.379 1.00 41.70 ? 813 HOH A O 1
+HETATM 2873 O O . HOH F 3 . ? 17.792 -22.269 33.181 1.00 42.81 ? 814 HOH A O 1
+HETATM 2874 O O . HOH F 3 . ? 20.668 -22.530 17.546 1.00 24.89 ? 815 HOH A O 1
+HETATM 2875 O O . HOH F 3 . ? 7.721 -5.547 22.694 1.00 46.81 ? 816 HOH A O 1
+HETATM 2876 O O . HOH F 3 . ? 20.766 5.826 -19.089 1.00 39.70 ? 817 HOH A O 1
+HETATM 2877 O O . HOH F 3 . ? 28.111 9.358 -5.026 1.00 37.59 ? 818 HOH A O 1
+HETATM 2878 O O . HOH F 3 . ? 25.908 -14.886 15.182 1.00 37.07 ? 819 HOH A O 1
+HETATM 2879 O O . HOH F 3 . ? 14.701 -6.924 -4.448 1.00 39.83 ? 820 HOH A O 1
+HETATM 2880 O O . HOH F 3 . ? 21.178 6.636 -5.226 1.00 32.30 ? 821 HOH A O 1
+HETATM 2881 O O . HOH F 3 . ? 24.874 10.464 -2.477 1.00 28.16 ? 822 HOH A O 1
+HETATM 2882 O O . HOH F 3 . ? -2.947 28.034 -1.971 1.00 40.10 ? 823 HOH A O 1
+HETATM 2883 O O . HOH F 3 . ? 14.364 20.232 9.961 1.00 64.02 ? 824 HOH A O 1
+HETATM 2884 O O . HOH F 3 . ? 1.998 9.130 -3.466 1.00 43.88 ? 825 HOH A O 1
+HETATM 2885 O O . HOH F 3 . ? 11.115 20.848 -19.436 1.00 28.04 ? 826 HOH A O 1
+HETATM 2886 O O . HOH F 3 . ? 10.569 -34.359 21.224 1.00 30.05 ? 827 HOH A O 1
+HETATM 2887 O O . HOH F 3 . ? 7.992 2.820 22.784 1.00 30.45 ? 828 HOH A O 1
+HETATM 2888 O O . HOH F 3 . ? 23.890 6.960 -5.408 1.00 41.41 ? 829 HOH A O 1
+HETATM 2889 O O . HOH F 3 . ? -4.860 -11.927 5.027 1.00 34.53 ? 830 HOH A O 1
+HETATM 2890 O O . HOH F 3 . ? -5.504 22.417 -9.461 1.00 35.31 ? 831 HOH A O 1
+HETATM 2891 O O . HOH F 3 . ? 21.823 -25.766 20.312 1.00 35.08 ? 832 HOH A O 1
+HETATM 2892 O O . HOH F 3 . ? 24.913 4.376 10.687 1.00 37.92 ? 833 HOH A O 1
+HETATM 2893 O O . HOH F 3 . ? 1.269 20.703 -21.897 1.00 32.97 ? 834 HOH A O 1
+HETATM 2894 O O . HOH F 3 . ? 3.771 11.637 -21.977 1.00 31.92 ? 835 HOH A O 1
+HETATM 2895 O O . HOH F 3 . ? 12.626 24.742 -22.470 1.00 40.86 ? 836 HOH A O 1
+HETATM 2896 O O . HOH F 3 . ? 16.595 -4.924 -1.942 1.00 35.09 ? 837 HOH A O 1
+HETATM 2897 O O . HOH F 3 . ? 11.940 -2.105 -13.997 1.00 81.21 ? 838 HOH A O 1
+HETATM 2898 O O . HOH F 3 . ? 22.261 -14.167 8.754 1.00 42.15 ? 839 HOH A O 1
+HETATM 2899 O O . HOH F 3 . ? 25.901 3.885 16.892 1.00 35.17 ? 840 HOH A O 1
+HETATM 2900 O O . HOH F 3 . ? 6.955 0.869 24.448 1.00 37.90 ? 841 HOH A O 1
+HETATM 2901 O O . HOH F 3 . ? 19.400 7.494 -3.277 1.00 24.50 ? 842 HOH A O 1
+HETATM 2902 O O . HOH F 3 . ? 22.943 -1.301 22.523 1.00 28.74 ? 843 HOH A O 1
+HETATM 2903 O O . HOH F 3 . ? -4.289 9.192 -7.451 1.00 33.71 ? 844 HOH A O 1
+HETATM 2904 O O . HOH F 3 . ? 24.338 2.535 6.965 1.00 50.58 ? 845 HOH A O 1
+HETATM 2905 O O . HOH F 3 . ? 12.482 24.156 3.931 1.00 27.61 ? 846 HOH A O 1
+HETATM 2906 O O . HOH F 3 . ? 13.627 -27.685 25.198 1.00 17.11 ? 847 HOH A O 1
+HETATM 2907 O O . HOH F 3 . ? 21.105 -20.304 14.193 1.00 35.35 ? 848 HOH A O 1
+HETATM 2908 O O . HOH F 3 . ? 22.677 -16.948 26.065 1.00 22.28 ? 849 HOH A O 1
+HETATM 2909 O O . HOH F 3 . ? 8.193 2.892 -22.627 1.00 55.19 ? 850 HOH A O 1
+HETATM 2910 O O . HOH F 3 . ? 17.203 -26.064 27.384 1.00 25.61 ? 851 HOH A O 1
+HETATM 2911 O O . HOH F 3 . ? 6.147 21.871 -1.733 1.00 31.41 ? 852 HOH A O 1
+HETATM 2912 O O . HOH F 3 . ? 20.037 -8.416 33.885 1.00 27.89 ? 853 HOH A O 1
+HETATM 2913 O O . HOH F 3 . ? 15.046 17.762 14.001 1.00 56.06 ? 854 HOH A O 1
+HETATM 2914 O O . HOH F 3 . ? 25.051 -3.698 20.136 1.00 53.04 ? 855 HOH A O 1
+HETATM 2915 O O . HOH F 3 . ? 10.109 25.184 -23.031 1.00 38.82 ? 856 HOH A O 1
+HETATM 2916 O O . HOH F 3 . ? 27.648 -2.076 15.145 1.00 34.17 ? 857 HOH A O 1
+HETATM 2917 O O . HOH F 3 . ? 19.976 14.798 -21.747 1.00 35.44 ? 858 HOH A O 1
+HETATM 2918 O O . HOH F 3 . ? 11.374 -33.896 23.985 1.00 24.95 ? 859 HOH A O 1
+HETATM 2919 O O . HOH F 3 . ? 25.999 20.692 -1.475 1.00 31.16 ? 860 HOH A O 1
+HETATM 2920 O O . HOH F 3 . ? 8.111 -2.686 22.688 1.00 44.34 ? 861 HOH A O 1
+HETATM 2921 O O . HOH F 3 . ? 10.912 0.306 23.988 1.00 62.89 ? 862 HOH A O 1
+HETATM 2922 O O . HOH F 3 . ? 0.810 22.459 -19.140 1.00 42.26 ? 863 HOH A O 1
+HETATM 2923 O O . HOH F 3 . ? 9.569 31.573 -18.134 1.00 44.74 ? 864 HOH A O 1
+HETATM 2924 O O . HOH F 3 . ? 4.943 1.282 26.322 1.00 29.80 ? 865 HOH A O 1
+HETATM 2925 O O . HOH F 3 . ? 8.400 -28.634 3.942 1.00 32.60 ? 866 HOH A O 1
+HETATM 2926 O O . HOH F 3 . ? 13.703 12.434 22.929 1.00 44.31 ? 867 HOH A O 1
+HETATM 2927 O O . HOH F 3 . ? 10.378 -27.381 2.773 1.00 30.68 ? 868 HOH A O 1
+HETATM 2928 O O . HOH F 3 . ? 28.747 25.438 -4.710 1.00 33.95 ? 869 HOH A O 1
+HETATM 2929 O O . HOH F 3 . ? 16.308 -29.927 22.132 1.00 41.46 ? 870 HOH A O 1
+HETATM 2930 O O . HOH F 3 . ? 20.530 -15.652 4.907 1.00 37.96 ? 871 HOH A O 1
+HETATM 2931 O O . HOH F 3 . ? 1.363 -29.462 16.883 1.00 43.05 ? 872 HOH A O 1
+HETATM 2932 O O . HOH F 3 . ? 28.290 -3.921 16.901 1.00 33.06 ? 873 HOH A O 1
+HETATM 2933 O O . HOH F 3 . ? 21.119 -26.362 24.834 1.00 28.95 ? 874 HOH A O 1
+HETATM 2934 O O . HOH F 3 . ? 27.101 14.413 -1.879 1.00 33.91 ? 875 HOH A O 1
+HETATM 2935 O O . HOH F 3 . ? 25.873 21.448 -16.628 1.00 22.36 ? 876 HOH A O 1
+HETATM 2936 O O . HOH F 3 . ? 25.161 31.405 -7.246 1.00 39.01 ? 877 HOH A O 1
+HETATM 2937 O O . HOH F 3 . ? 25.157 -0.742 15.399 1.00 32.15 ? 878 HOH A O 1
+HETATM 2938 O O . HOH F 3 . ? 18.090 -7.289 35.812 1.00 56.43 ? 879 HOH A O 1
+HETATM 2939 O O . HOH F 3 . ? 16.073 13.714 23.421 1.00 31.52 ? 880 HOH A O 1
+HETATM 2940 O O . HOH F 3 . ? 21.892 0.520 24.913 1.00 47.37 ? 881 HOH A O 1
+HETATM 2941 O O . HOH F 3 . ? 10.432 22.183 0.548 1.00 21.18 ? 882 HOH A O 1
+HETATM 2942 O O . HOH F 3 . ? 16.365 -11.946 34.322 1.00 44.91 ? 883 HOH A O 1
+HETATM 2943 O O . HOH F 3 . ? 14.946 -32.152 15.788 1.00 37.75 ? 884 HOH A O 1
+HETATM 2944 O O . HOH F 3 . ? 21.901 12.848 -18.345 1.00 27.03 ? 885 HOH A O 1
+HETATM 2945 O O . HOH F 3 . ? 23.819 16.236 -16.712 1.00 22.25 ? 886 HOH A O 1
+HETATM 2946 O O . HOH F 3 . ? 24.099 18.963 2.615 1.00 30.17 ? 887 HOH A O 1
+HETATM 2947 O O . HOH F 3 . ? 13.977 -31.276 21.409 1.00 26.57 ? 888 HOH A O 1
+HETATM 2948 O O . HOH F 3 . ? 24.747 17.900 -18.867 1.00 37.61 ? 889 HOH A O 1
+HETATM 2949 O O . HOH F 3 . ? 26.570 31.349 -4.896 1.00 34.25 ? 890 HOH A O 1
+HETATM 2950 O O . HOH F 3 . ? 25.523 16.140 -20.792 1.00 39.96 ? 891 HOH A O 1
+#
+loop_
+_atom_site_anisotrop.id
+_atom_site_anisotrop.type_symbol
+_atom_site_anisotrop.pdbx_label_atom_id
+_atom_site_anisotrop.pdbx_label_alt_id
+_atom_site_anisotrop.pdbx_label_comp_id
+_atom_site_anisotrop.pdbx_label_asym_id
+_atom_site_anisotrop.pdbx_label_seq_id
+_atom_site_anisotrop.pdbx_PDB_ins_code
+_atom_site_anisotrop.U[1][1]
+_atom_site_anisotrop.U[2][2]
+_atom_site_anisotrop.U[3][3]
+_atom_site_anisotrop.U[1][2]
+_atom_site_anisotrop.U[1][3]
+_atom_site_anisotrop.U[2][3]
+_atom_site_anisotrop.pdbx_auth_seq_id
+_atom_site_anisotrop.pdbx_auth_comp_id
+_atom_site_anisotrop.pdbx_auth_asym_id
+_atom_site_anisotrop.pdbx_auth_atom_id
+1 N N A SER A 1 ? 0.3790 0.3658 0.2638 -0.1331 -0.1030 0.0674 1 SER A N
+2 N N B SER A 1 ? 0.3647 0.3506 0.2482 -0.1342 -0.1039 0.0678 1 SER A N
+3 C CA A SER A 1 ? 0.3697 0.3711 0.2741 -0.1239 -0.0975 0.0694 1 SER A CA
+4 C CA B SER A 1 ? 0.3548 0.3538 0.2566 -0.1238 -0.0970 0.0677 1 SER A CA
+5 C C A SER A 1 ? 0.3512 0.3620 0.2738 -0.1150 -0.0937 0.0712 1 SER A C
+6 C C B SER A 1 ? 0.3399 0.3488 0.2604 -0.1153 -0.0938 0.0702 1 SER A C
+7 O O A SER A 1 ? 0.3500 0.3592 0.2735 -0.1169 -0.0968 0.0737 1 SER A O
+8 O O B SER A 1 ? 0.3368 0.3447 0.2586 -0.1178 -0.0975 0.0736 1 SER A O
+9 C CB A SER A 1 ? 0.3908 0.4027 0.3042 -0.1293 -0.1027 0.0802 1 SER A CB
+10 C CB B SER A 1 ? 0.3697 0.3791 0.2803 -0.1274 -0.1004 0.0766 1 SER A CB
+11 O OG A SER A 1 ? 0.4343 0.4421 0.3375 -0.1310 -0.1009 0.0760 1 SER A OG
+12 O OG B SER A 1 ? 0.3934 0.4150 0.3207 -0.1305 -0.1062 0.0898 1 SER A OG
+13 N N A GLY A 2 ? 0.3321 0.3515 0.2678 -0.1055 -0.0870 0.0696 2 GLY A N
+14 N N B GLY A 2 ? 0.3248 0.3424 0.2586 -0.1055 -0.0869 0.0684 2 GLY A N
+15 C CA A GLY A 2 ? 0.3196 0.3459 0.2699 -0.0962 -0.0822 0.0700 2 GLY A CA
+16 C CA B GLY A 2 ? 0.3159 0.3411 0.2651 -0.0967 -0.0827 0.0698 2 GLY A CA
+17 C C A GLY A 2 ? 0.3152 0.3338 0.2586 -0.0888 -0.0752 0.0577 2 GLY A C
+18 C C B GLY A 2 ? 0.3152 0.3333 0.2584 -0.0889 -0.0756 0.0578 2 GLY A C
+19 O O A GLY A 2 ? 0.3266 0.3335 0.2538 -0.0916 -0.0748 0.0500 2 GLY A O
+20 O O B GLY A 2 ? 0.3260 0.3323 0.2536 -0.0917 -0.0755 0.0505 2 GLY A O
+21 N N . PHE A 3 ? 0.2972 0.3216 0.2523 -0.0793 -0.0695 0.0563 3 PHE A N
+22 C CA . PHE A 3 ? 0.2893 0.3080 0.2403 -0.0721 -0.0633 0.0461 3 PHE A CA
+23 C C . PHE A 3 ? 0.2801 0.3044 0.2431 -0.0646 -0.0601 0.0477 3 PHE A C
+24 O O . PHE A 3 ? 0.2968 0.3290 0.2718 -0.0601 -0.0580 0.0527 3 PHE A O
+25 C CB . PHE A 3 ? 0.2768 0.2952 0.2263 -0.0688 -0.0591 0.0409 3 PHE A CB
+26 C CG . PHE A 3 ? 0.2827 0.2930 0.2240 -0.0645 -0.0542 0.0307 3 PHE A CG
+27 C CD1 . PHE A 3 ? 0.2957 0.2956 0.2219 -0.0689 -0.0544 0.0255 3 PHE A CD1
+28 C CD2 . PHE A 3 ? 0.2846 0.2969 0.2329 -0.0562 -0.0493 0.0269 3 PHE A CD2
+29 C CE1 . PHE A 3 ? 0.3093 0.3023 0.2298 -0.0646 -0.0492 0.0174 3 PHE A CE1
+30 C CE2 . PHE A 3 ? 0.2909 0.2968 0.2333 -0.0528 -0.0452 0.0189 3 PHE A CE2
+31 C CZ . PHE A 3 ? 0.2995 0.2964 0.2291 -0.0566 -0.0449 0.0146 3 PHE A CZ
+32 N N . ARG A 4 ? 0.2533 0.2727 0.2124 -0.0633 -0.0595 0.0440 4 ARG A N
+33 C CA . ARG A 4 ? 0.2321 0.2556 0.2008 -0.0566 -0.0566 0.0454 4 ARG A CA
+34 C C . ARG A 4 ? 0.2271 0.2449 0.1914 -0.0506 -0.0517 0.0360 4 ARG A C
+35 O O . ARG A 4 ? 0.2404 0.2504 0.1940 -0.0527 -0.0512 0.0292 4 ARG A O
+36 C CB . ARG A 4 ? 0.2469 0.2710 0.2168 -0.0613 -0.0615 0.0515 4 ARG A CB
+37 C CG . ARG A 4 ? 0.2796 0.3131 0.2608 -0.0646 -0.0656 0.0640 4 ARG A CG
+38 C CD . ARG A 4 ? 0.3081 0.3495 0.3037 -0.0561 -0.0610 0.0691 4 ARG A CD
+39 N NE . ARG A 4 ? 0.3468 0.3979 0.3555 -0.0584 -0.0639 0.0826 4 ARG A NE
+40 C CZ . ARG A 4 ? 0.3666 0.4250 0.3888 -0.0513 -0.0594 0.0896 4 ARG A CZ
+41 N NH1 . ARG A 4 ? 0.3673 0.4234 0.3900 -0.0420 -0.0523 0.0836 4 ARG A NH1
+42 N NH2 . ARG A 4 ? 0.3326 0.4003 0.3678 -0.0535 -0.0618 0.1030 4 ARG A NH2
+43 N N A LYS A 5 ? 0.2120 0.2334 0.1844 -0.0433 -0.0480 0.0363 5 LYS A N
+44 N N B LYS A 5 ? 0.2144 0.2357 0.1867 -0.0432 -0.0480 0.0362 5 LYS A N
+45 C CA A LYS A 5 ? 0.2153 0.2320 0.1845 -0.0381 -0.0442 0.0287 5 LYS A CA
+46 C CA B LYS A 5 ? 0.2199 0.2365 0.1890 -0.0379 -0.0441 0.0285 5 LYS A CA
+47 C C A LYS A 5 ? 0.2227 0.2362 0.1884 -0.0413 -0.0467 0.0289 5 LYS A C
+48 C C B LYS A 5 ? 0.2302 0.2435 0.1960 -0.0403 -0.0460 0.0280 5 LYS A C
+49 O O A LYS A 5 ? 0.2236 0.2416 0.1956 -0.0420 -0.0489 0.0356 5 LYS A O
+50 O O B LYS A 5 ? 0.2387 0.2557 0.2110 -0.0380 -0.0461 0.0322 5 LYS A O
+51 C CB A LYS A 5 ? 0.2280 0.2480 0.2048 -0.0301 -0.0401 0.0295 5 LYS A CB
+52 C CB B LYS A 5 ? 0.2315 0.2515 0.2083 -0.0300 -0.0399 0.0293 5 LYS A CB
+53 C CG A LYS A 5 ? 0.2735 0.2887 0.2467 -0.0254 -0.0368 0.0217 5 LYS A CG
+54 C CG B LYS A 5 ? 0.2752 0.2905 0.2486 -0.0252 -0.0367 0.0218 5 LYS A CG
+55 C CD A LYS A 5 ? 0.3187 0.3300 0.2866 -0.0257 -0.0355 0.0155 5 LYS A CD
+56 C CD B LYS A 5 ? 0.3199 0.3310 0.2877 -0.0255 -0.0354 0.0153 5 LYS A CD
+57 C CE A LYS A 5 ? 0.3569 0.3701 0.3282 -0.0227 -0.0339 0.0162 5 LYS A CE
+58 C CE B LYS A 5 ? 0.3559 0.3690 0.3270 -0.0227 -0.0339 0.0160 5 LYS A CE
+59 N NZ A LYS A 5 ? 0.3728 0.3864 0.3481 -0.0165 -0.0312 0.0172 5 LYS A NZ
+60 N NZ B LYS A 5 ? 0.3701 0.3837 0.3454 -0.0165 -0.0312 0.0172 5 LYS A NZ
+61 N N . MET A 6 ? 0.2284 0.2341 0.1838 -0.0444 -0.0468 0.0227 6 MET A N
+62 C CA . MET A 6 ? 0.2335 0.2339 0.1832 -0.0482 -0.0492 0.0221 6 MET A CA
+63 C C . MET A 6 ? 0.2208 0.2164 0.1681 -0.0440 -0.0454 0.0155 6 MET A C
+64 O O . MET A 6 ? 0.2287 0.2206 0.1722 -0.0415 -0.0417 0.0095 6 MET A O
+65 C CB . MET A 6 ? 0.2693 0.2619 0.2066 -0.0561 -0.0522 0.0206 6 MET A CB
+66 C CG . MET A 6 ? 0.3399 0.3251 0.2691 -0.0619 -0.0558 0.0208 6 MET A CG
+67 S SD . MET A 6 ? 0.4425 0.4174 0.3551 -0.0716 -0.0596 0.0200 6 MET A SD
+68 C CE . MET A 6 ? 0.3824 0.3682 0.3041 -0.0757 -0.0652 0.0303 6 MET A CE
+69 N N . ALA A 7 ? 0.2066 0.2027 0.1567 -0.0436 -0.0466 0.0174 7 ALA A N
+70 C CA . ALA A 7 ? 0.2137 0.2054 0.1620 -0.0401 -0.0434 0.0119 7 ALA A CA
+71 C C . ALA A 7 ? 0.2240 0.2060 0.1616 -0.0459 -0.0451 0.0093 7 ALA A C
+72 O O . ALA A 7 ? 0.2328 0.2119 0.1649 -0.0528 -0.0498 0.0128 7 ALA A O
+73 C CB . ALA A 7 ? 0.2122 0.2101 0.1700 -0.0356 -0.0430 0.0154 7 ALA A CB
+74 N N . PHE A 8 ? 0.2275 0.2033 0.1611 -0.0435 -0.0413 0.0035 8 PHE A N
+75 C CA . PHE A 8 ? 0.2512 0.2159 0.1740 -0.0482 -0.0419 0.0008 8 PHE A CA
+76 C C . PHE A 8 ? 0.2471 0.2136 0.1735 -0.0506 -0.0463 0.0055 8 PHE A C
+77 O O . PHE A 8 ? 0.2320 0.2076 0.1699 -0.0462 -0.0464 0.0090 8 PHE A O
+78 C CB . PHE A 8 ? 0.2598 0.2187 0.1802 -0.0438 -0.0357 -0.0056 8 PHE A CB
+79 C CG . PHE A 8 ? 0.2847 0.2396 0.1998 -0.0426 -0.0313 -0.0096 8 PHE A CG
+80 C CD1 . PHE A 8 ? 0.3166 0.2600 0.2176 -0.0474 -0.0304 -0.0122 8 PHE A CD1
+81 C CD2 . PHE A 8 ? 0.2990 0.2610 0.2225 -0.0369 -0.0282 -0.0105 8 PHE A CD2
+82 C CE1 . PHE A 8 ? 0.3331 0.2732 0.2298 -0.0458 -0.0259 -0.0152 8 PHE A CE1
+83 C CE2 . PHE A 8 ? 0.3182 0.2773 0.2381 -0.0358 -0.0244 -0.0134 8 PHE A CE2
+84 C CZ . PHE A 8 ? 0.3277 0.2764 0.2349 -0.0400 -0.0230 -0.0155 8 PHE A CZ
+85 N N . PRO A 9 ? 0.2598 0.2165 0.1755 -0.0577 -0.0500 0.0058 9 PRO A N
+86 C CA . PRO A 9 ? 0.2606 0.2180 0.1797 -0.0604 -0.0544 0.0103 9 PRO A CA
+87 C C . PRO A 9 ? 0.2575 0.2167 0.1833 -0.0537 -0.0498 0.0072 9 PRO A C
+88 O O . PRO A 9 ? 0.2854 0.2383 0.2066 -0.0505 -0.0442 0.0008 9 PRO A O
+89 C CB . PRO A 9 ? 0.2926 0.2349 0.1951 -0.0690 -0.0579 0.0086 9 PRO A CB
+90 C CG . PRO A 9 ? 0.3068 0.2437 0.1989 -0.0719 -0.0570 0.0060 9 PRO A CG
+91 C CD . PRO A 9 ? 0.2731 0.2162 0.1721 -0.0635 -0.0498 0.0018 9 PRO A CD
+92 N N . SER A 10 ? 0.2329 0.2016 0.1705 -0.0510 -0.0516 0.0125 10 SER A N
+93 C CA . SER A 10 ? 0.2194 0.1919 0.1648 -0.0441 -0.0474 0.0103 10 SER A CA
+94 C C . SER A 10 ? 0.2215 0.1881 0.1649 -0.0458 -0.0482 0.0097 10 SER A C
+95 O O . SER A 10 ? 0.2135 0.1831 0.1632 -0.0404 -0.0448 0.0080 10 SER A O
+96 C CB . SER A 10 ? 0.2200 0.2056 0.1788 -0.0388 -0.0475 0.0160 10 SER A CB
+97 O OG . SER A 10 ? 0.2428 0.2330 0.2066 -0.0426 -0.0530 0.0242 10 SER A OG
+98 N N . GLY A 11 ? 0.2295 0.1874 0.1641 -0.0534 -0.0530 0.0111 11 GLY A N
+99 C CA . GLY A 11 ? 0.2298 0.1812 0.1622 -0.0558 -0.0546 0.0111 11 GLY A CA
+100 C C . GLY A 11 ? 0.2268 0.1718 0.1570 -0.0512 -0.0480 0.0044 11 GLY A C
+101 O O . GLY A 11 ? 0.2323 0.1805 0.1699 -0.0483 -0.0473 0.0055 11 GLY A O
+102 N N . LYS A 12 ? 0.2248 0.1612 0.1455 -0.0504 -0.0428 -0.0020 12 LYS A N
+103 C CA . LYS A 12 ? 0.2278 0.1579 0.1471 -0.0461 -0.0359 -0.0075 12 LYS A CA
+104 C C . LYS A 12 ? 0.2202 0.1631 0.1547 -0.0382 -0.0326 -0.0068 12 LYS A C
+105 O O . LYS A 12 ? 0.2276 0.1691 0.1658 -0.0351 -0.0292 -0.0082 12 LYS A O
+106 C CB . LYS A 12 ? 0.2543 0.1739 0.1622 -0.0460 -0.0303 -0.0132 12 LYS A CB
+107 C CG . LYS A 12 ? 0.3209 0.2229 0.2099 -0.0536 -0.0318 -0.0155 12 LYS A CG
+108 C CD . LYS A 12 ? 0.3976 0.2910 0.2756 -0.0533 -0.0264 -0.0200 12 LYS A CD
+109 C CE . LYS A 12 ? 0.4817 0.3558 0.3382 -0.0610 -0.0278 -0.0224 12 LYS A CE
+110 N NZ . LYS A 12 ? 0.5337 0.3937 0.3822 -0.0623 -0.0255 -0.0248 12 LYS A NZ
+111 N N . VAL A 13 ? 0.2016 0.1563 0.1443 -0.0351 -0.0337 -0.0041 13 VAL A N
+112 C CA . VAL A 13 ? 0.1813 0.1466 0.1360 -0.0282 -0.0311 -0.0033 13 VAL A CA
+113 C C . VAL A 13 ? 0.1687 0.1420 0.1324 -0.0272 -0.0345 0.0020 13 VAL A C
+114 O O . VAL A 13 ? 0.1657 0.1433 0.1367 -0.0227 -0.0324 0.0021 13 VAL A O
+115 C CB . VAL A 13 ? 0.1893 0.1613 0.1468 -0.0253 -0.0301 -0.0035 13 VAL A CB
+116 C CG1 . VAL A 13 ? 0.1965 0.1771 0.1637 -0.0189 -0.0280 -0.0028 13 VAL A CG1
+117 C CG2 . VAL A 13 ? 0.2103 0.1748 0.1597 -0.0262 -0.0265 -0.0082 13 VAL A CG2
+118 N N . GLU A 14 ? 0.1675 0.1426 0.1312 -0.0315 -0.0400 0.0072 14 GLU A N
+119 C CA . GLU A 14 ? 0.1621 0.1448 0.1350 -0.0306 -0.0432 0.0135 14 GLU A CA
+120 C C . GLU A 14 ? 0.1768 0.1554 0.1508 -0.0305 -0.0424 0.0123 14 GLU A C
+121 O O . GLU A 14 ? 0.1752 0.1613 0.1585 -0.0261 -0.0416 0.0149 14 GLU A O
+122 C CB . GLU A 14 ? 0.1742 0.1577 0.1464 -0.0368 -0.0496 0.0200 14 GLU A CB
+123 C CG . GLU A 14 ? 0.2071 0.1980 0.1825 -0.0359 -0.0505 0.0238 14 GLU A CG
+124 C CD . GLU A 14 ? 0.2494 0.2399 0.2232 -0.0433 -0.0572 0.0303 14 GLU A CD
+125 O OE1 . GLU A 14 ? 0.2807 0.2738 0.2599 -0.0459 -0.0616 0.0368 14 GLU A OE1
+126 O OE2 . GLU A 14 ? 0.2641 0.2514 0.2313 -0.0469 -0.0584 0.0294 14 GLU A OE2
+127 N N . GLY A 15 ? 0.1868 0.1528 0.1505 -0.0348 -0.0418 0.0079 15 GLY A N
+128 C CA . GLY A 15 ? 0.1869 0.1467 0.1502 -0.0351 -0.0405 0.0063 15 GLY A CA
+129 C C . GLY A 15 ? 0.1802 0.1431 0.1499 -0.0284 -0.0343 0.0031 15 GLY A C
+130 O O . GLY A 15 ? 0.1941 0.1536 0.1659 -0.0278 -0.0328 0.0025 15 GLY A O
+131 N N . CYS A 16 ? 0.1662 0.1350 0.1391 -0.0239 -0.0310 0.0014 16 CYS A N
+132 C CA . CYS A 16 ? 0.1612 0.1338 0.1407 -0.0181 -0.0261 -0.0007 16 CYS A CA
+133 C C . CYS A 16 ? 0.1592 0.1443 0.1489 -0.0133 -0.0270 0.0029 16 CYS A C
+134 O O . CYS A 16 ? 0.1672 0.1557 0.1622 -0.0092 -0.0239 0.0020 16 CYS A O
+135 C CB . CYS A 16 ? 0.1764 0.1450 0.1513 -0.0169 -0.0216 -0.0051 16 CYS A CB
+136 S SG . CYS A 16 ? 0.2316 0.1834 0.1921 -0.0216 -0.0188 -0.0097 16 CYS A SG
+137 N N . MET A 17 ? 0.1526 0.1440 0.1446 -0.0137 -0.0308 0.0074 17 MET A N
+138 C CA . MET A 17 ? 0.1522 0.1534 0.1515 -0.0085 -0.0305 0.0105 17 MET A CA
+139 C C . MET A 17 ? 0.1518 0.1579 0.1587 -0.0065 -0.0311 0.0143 17 MET A C
+140 O O . MET A 17 ? 0.1596 0.1653 0.1680 -0.0094 -0.0341 0.0178 17 MET A O
+141 C CB . MET A 17 ? 0.1531 0.1588 0.1521 -0.0085 -0.0326 0.0140 17 MET A CB
+142 C CG . MET A 17 ? 0.1697 0.1714 0.1618 -0.0104 -0.0321 0.0106 17 MET A CG
+143 S SD . MET A 17 ? 0.1856 0.1854 0.1757 -0.0071 -0.0278 0.0048 17 MET A SD
+144 C CE . MET A 17 ? 0.2009 0.2086 0.1971 -0.0010 -0.0269 0.0074 17 MET A CE
+145 N N . VAL A 18 ? 0.1429 0.1536 0.1543 -0.0018 -0.0287 0.0140 18 VAL A N
+146 C CA . VAL A 18 ? 0.1498 0.1659 0.1684 0.0009 -0.0289 0.0176 18 VAL A CA
+147 C C . VAL A 18 ? 0.1456 0.1680 0.1660 0.0060 -0.0278 0.0197 18 VAL A C
+148 O O . VAL A 18 ? 0.1443 0.1657 0.1602 0.0072 -0.0267 0.0174 18 VAL A O
+149 C CB . VAL A 18 ? 0.1652 0.1787 0.1868 0.0011 -0.0267 0.0150 18 VAL A CB
+150 C CG1 . VAL A 18 ? 0.1808 0.1855 0.1986 -0.0036 -0.0270 0.0128 18 VAL A CG1
+151 C CG2 . VAL A 18 ? 0.1651 0.1782 0.1858 0.0034 -0.0238 0.0115 18 VAL A CG2
+152 N N . GLN A 19 ? 0.1422 0.1701 0.1683 0.0088 -0.0280 0.0241 19 GLN A N
+153 C CA . GLN A 19 ? 0.1465 0.1786 0.1726 0.0138 -0.0264 0.0262 19 GLN A CA
+154 C C . GLN A 19 ? 0.1436 0.1763 0.1715 0.0154 -0.0252 0.0242 19 GLN A C
+155 O O . GLN A 19 ? 0.1405 0.1740 0.1740 0.0142 -0.0255 0.0247 19 GLN A O
+156 C CB . GLN A 19 ? 0.1656 0.2034 0.1970 0.0161 -0.0268 0.0332 19 GLN A CB
+157 C CG . GLN A 19 ? 0.2122 0.2528 0.2420 0.0218 -0.0243 0.0357 19 GLN A CG
+158 C CD . GLN A 19 ? 0.2795 0.3260 0.3160 0.0245 -0.0240 0.0433 19 GLN A CD
+159 O OE1 . GLN A 19 ? 0.2999 0.3499 0.3420 0.0254 -0.0242 0.0455 19 GLN A OE1
+160 N NE2 . GLN A 19 ? 0.2951 0.3434 0.3321 0.0261 -0.0232 0.0481 19 GLN A NE2
+161 N N . VAL A 20 ? 0.1391 0.1710 0.1624 0.0177 -0.0242 0.0225 20 VAL A N
+162 C CA . VAL A 20 ? 0.1480 0.1811 0.1733 0.0187 -0.0239 0.0219 20 VAL A CA
+163 C C . VAL A 20 ? 0.1564 0.1910 0.1775 0.0226 -0.0234 0.0245 20 VAL A C
+164 O O . VAL A 20 ? 0.1651 0.1964 0.1783 0.0241 -0.0228 0.0238 20 VAL A O
+165 C CB . VAL A 20 ? 0.1530 0.1826 0.1763 0.0167 -0.0238 0.0177 20 VAL A CB
+166 C CG1 . VAL A 20 ? 0.1603 0.1924 0.1876 0.0173 -0.0241 0.0188 20 VAL A CG1
+167 C CG2 . VAL A 20 ? 0.1588 0.1853 0.1843 0.0134 -0.0231 0.0150 20 VAL A CG2
+168 N N . THR A 21 ? 0.1601 0.1987 0.1858 0.0244 -0.0234 0.0277 21 THR A N
+169 C CA . THR A 21 ? 0.1782 0.2169 0.1984 0.0281 -0.0225 0.0302 21 THR A CA
+170 C C . THR A 21 ? 0.1897 0.2293 0.2108 0.0274 -0.0239 0.0300 21 THR A C
+171 O O . THR A 21 ? 0.1860 0.2296 0.2163 0.0258 -0.0245 0.0309 21 THR A O
+172 C CB . THR A 21 ? 0.2060 0.2495 0.2307 0.0314 -0.0211 0.0358 21 THR A CB
+173 O OG1 . THR A 21 ? 0.2226 0.2663 0.2481 0.0316 -0.0204 0.0375 21 THR A OG1
+174 C CG2 . THR A 21 ? 0.2269 0.2694 0.2447 0.0358 -0.0192 0.0387 21 THR A CG2
+175 N N . CYS A 22 ? 0.2077 0.2429 0.2189 0.0281 -0.0245 0.0292 22 CYS A N
+176 C CA . CYS A 22 ? 0.2335 0.2695 0.2447 0.0270 -0.0266 0.0302 22 CYS A CA
+177 C C . CYS A 22 ? 0.2710 0.3026 0.2700 0.0302 -0.0258 0.0320 22 CYS A C
+178 O O . CYS A 22 ? 0.2785 0.3027 0.2655 0.0312 -0.0250 0.0301 22 CYS A O
+179 C CB . CYS A 22 ? 0.2364 0.2697 0.2468 0.0230 -0.0292 0.0274 22 CYS A CB
+180 S SG . CYS A 22 ? 0.3129 0.3491 0.3273 0.0205 -0.0326 0.0304 22 CYS A SG
+181 N N . GLY A 23 ? 0.2938 0.3296 0.2959 0.0323 -0.0252 0.0360 23 GLY A N
+182 C CA . GLY A 23 ? 0.3204 0.3516 0.3105 0.0360 -0.0235 0.0383 23 GLY A CA
+183 C C . GLY A 23 ? 0.3405 0.3689 0.3258 0.0405 -0.0191 0.0393 23 GLY A C
+184 O O . GLY A 23 ? 0.3496 0.3845 0.3455 0.0421 -0.0173 0.0419 23 GLY A O
+185 N N . THR A 24 ? 0.3500 0.3684 0.3199 0.0420 -0.0176 0.0372 24 THR A N
+186 C CA . THR A 24 ? 0.3600 0.3750 0.3251 0.0468 -0.0126 0.0387 24 THR A CA
+187 C C . THR A 24 ? 0.3425 0.3554 0.3082 0.0448 -0.0129 0.0352 24 THR A C
+188 O O . THR A 24 ? 0.3580 0.3683 0.3207 0.0484 -0.0090 0.0367 24 THR A O
+189 C CB . THR A 24 ? 0.4144 0.4183 0.3611 0.0508 -0.0092 0.0394 24 THR A CB
+190 O OG1 . THR A 24 ? 0.4539 0.4472 0.3867 0.0473 -0.0122 0.0343 24 THR A OG1
+191 C CG2 . THR A 24 ? 0.4277 0.4329 0.3722 0.0528 -0.0086 0.0431 24 THR A CG2
+192 N N . THR A 25 ? 0.3104 0.3248 0.2808 0.0395 -0.0172 0.0312 25 THR A N
+193 C CA . THR A 25 ? 0.2916 0.3033 0.2612 0.0375 -0.0177 0.0277 25 THR A CA
+194 C C . THR A 25 ? 0.2647 0.2846 0.2487 0.0354 -0.0183 0.0281 25 THR A C
+195 O O . THR A 25 ? 0.2662 0.2913 0.2590 0.0329 -0.0204 0.0281 25 THR A O
+196 C CB . THR A 25 ? 0.3080 0.3144 0.2715 0.0330 -0.0217 0.0233 25 THR A CB
+197 O OG1 . THR A 25 ? 0.3325 0.3293 0.2804 0.0341 -0.0218 0.0229 25 THR A OG1
+198 C CG2 . THR A 25 ? 0.3143 0.3188 0.2782 0.0307 -0.0223 0.0198 25 THR A CG2
+199 N N . THR A 26 ? 0.2504 0.2704 0.2356 0.0365 -0.0163 0.0289 26 THR A N
+200 C CA . THR A 26 ? 0.2337 0.2594 0.2297 0.0337 -0.0176 0.0293 26 THR A CA
+201 C C . THR A 26 ? 0.2166 0.2386 0.2093 0.0312 -0.0182 0.0256 26 THR A C
+202 O O . THR A 26 ? 0.2275 0.2450 0.2130 0.0334 -0.0162 0.0257 26 THR A O
+203 C CB . THR A 26 ? 0.2539 0.2850 0.2569 0.0365 -0.0155 0.0355 26 THR A CB
+204 O OG1 . THR A 26 ? 0.2709 0.3065 0.2788 0.0383 -0.0153 0.0390 26 THR A OG1
+205 C CG2 . THR A 26 ? 0.2595 0.2945 0.2711 0.0327 -0.0176 0.0361 26 THR A CG2
+206 N N . LEU A 27 ? 0.1900 0.2133 0.1877 0.0268 -0.0206 0.0225 27 LEU A N
+207 C CA . LEU A 27 ? 0.1763 0.1967 0.1717 0.0241 -0.0212 0.0193 27 LEU A CA
+208 C C . LEU A 27 ? 0.1629 0.1858 0.1657 0.0201 -0.0227 0.0183 27 LEU A C
+209 O O . LEU A 27 ? 0.1637 0.1902 0.1728 0.0199 -0.0230 0.0208 27 LEU A O
+210 C CB . LEU A 27 ? 0.1762 0.1911 0.1642 0.0230 -0.0222 0.0151 27 LEU A CB
+211 C CG . LEU A 27 ? 0.1771 0.1923 0.1666 0.0215 -0.0240 0.0137 27 LEU A CG
+212 C CD1 . LEU A 27 ? 0.1749 0.1939 0.1740 0.0186 -0.0246 0.0130 27 LEU A CD1
+213 C CD2 . LEU A 27 ? 0.1888 0.1986 0.1711 0.0199 -0.0258 0.0109 27 LEU A CD2
+214 N N . ASN A 28 ? 0.1481 0.1682 0.1488 0.0171 -0.0233 0.0150 28 ASN A N
+215 C CA . ASN A 28 ? 0.1428 0.1628 0.1474 0.0132 -0.0242 0.0138 28 ASN A CA
+216 C C . ASN A 28 ? 0.1380 0.1558 0.1440 0.0112 -0.0240 0.0101 28 ASN A C
+217 O O . ASN A 28 ? 0.1433 0.1598 0.1471 0.0117 -0.0238 0.0082 28 ASN A O
+218 C CB . ASN A 28 ? 0.1590 0.1768 0.1601 0.0110 -0.0247 0.0131 28 ASN A CB
+219 C CG . ASN A 28 ? 0.1851 0.2055 0.1862 0.0134 -0.0244 0.0178 28 ASN A CG
+220 O OD1 . ASN A 28 ? 0.1866 0.2104 0.1926 0.0130 -0.0252 0.0224 28 ASN A OD1
+221 N ND2 . ASN A 28 ? 0.1936 0.2120 0.1895 0.0160 -0.0230 0.0173 28 ASN A ND2
+222 N N . GLY A 29 ? 0.1306 0.1477 0.1402 0.0088 -0.0239 0.0097 29 GLY A N
+223 C CA . GLY A 29 ? 0.1316 0.1457 0.1430 0.0071 -0.0224 0.0068 29 GLY A CA
+224 C C . GLY A 29 ? 0.1363 0.1448 0.1445 0.0035 -0.0219 0.0046 29 GLY A C
+225 O O . GLY A 29 ? 0.1468 0.1545 0.1528 0.0015 -0.0237 0.0059 29 GLY A O
+226 N N . LEU A 30 ? 0.1341 0.1384 0.1416 0.0024 -0.0195 0.0016 30 LEU A N
+227 C CA . LEU A 30 ? 0.1373 0.1342 0.1396 -0.0008 -0.0180 -0.0011 30 LEU A CA
+228 C C . LEU A 30 ? 0.1373 0.1300 0.1426 -0.0011 -0.0150 -0.0017 30 LEU A C
+229 O O . LEU A 30 ? 0.1475 0.1416 0.1582 0.0010 -0.0121 -0.0015 30 LEU A O
+230 C CB . LEU A 30 ? 0.1341 0.1286 0.1331 -0.0010 -0.0162 -0.0037 30 LEU A CB
+231 C CG . LEU A 30 ? 0.1495 0.1355 0.1410 -0.0042 -0.0143 -0.0065 30 LEU A CG
+232 C CD1 . LEU A 30 ? 0.1640 0.1487 0.1493 -0.0073 -0.0180 -0.0060 30 LEU A CD1
+233 C CD2 . LEU A 30 ? 0.1619 0.1464 0.1524 -0.0034 -0.0116 -0.0084 30 LEU A CD2
+234 N N . TRP A 31 ? 0.1360 0.1233 0.1380 -0.0039 -0.0156 -0.0018 31 TRP A N
+235 C CA . TRP A 31 ? 0.1406 0.1227 0.1448 -0.0042 -0.0127 -0.0022 31 TRP A CA
+236 C C . TRP A 31 ? 0.1535 0.1230 0.1484 -0.0069 -0.0091 -0.0060 31 TRP A C
+237 O O . TRP A 31 ? 0.1585 0.1212 0.1440 -0.0111 -0.0114 -0.0072 31 TRP A O
+238 C CB . TRP A 31 ? 0.1435 0.1275 0.1500 -0.0056 -0.0164 0.0007 31 TRP A CB
+239 C CG . TRP A 31 ? 0.1463 0.1244 0.1545 -0.0063 -0.0142 0.0006 31 TRP A CG
+240 C CD1 . TRP A 31 ? 0.1544 0.1298 0.1669 -0.0040 -0.0090 -0.0003 31 TRP A CD1
+241 C CD2 . TRP A 31 ? 0.1473 0.1227 0.1548 -0.0093 -0.0176 0.0027 31 TRP A CD2
+242 N NE1 . TRP A 31 ? 0.1567 0.1268 0.1702 -0.0052 -0.0083 0.0003 31 TRP A NE1
+243 C CE2 . TRP A 31 ? 0.1583 0.1284 0.1687 -0.0086 -0.0139 0.0021 31 TRP A CE2
+244 C CE3 . TRP A 31 ? 0.1574 0.1343 0.1627 -0.0126 -0.0234 0.0056 31 TRP A CE3
+245 C CZ2 . TRP A 31 ? 0.1623 0.1274 0.1721 -0.0115 -0.0162 0.0035 31 TRP A CZ2
+246 C CZ3 . TRP A 31 ? 0.1626 0.1355 0.1682 -0.0157 -0.0261 0.0078 31 TRP A CZ3
+247 C CH2 . TRP A 31 ? 0.1640 0.1305 0.1711 -0.0153 -0.0226 0.0063 31 TRP A CH2
+248 N N . LEU A 32 ? 0.1528 0.1193 0.1501 -0.0046 -0.0033 -0.0072 32 LEU A N
+249 C CA . LEU A 32 ? 0.1720 0.1257 0.1602 -0.0059 0.0020 -0.0106 32 LEU A CA
+250 C C . LEU A 32 ? 0.1779 0.1269 0.1710 -0.0036 0.0080 -0.0101 32 LEU A C
+251 O O . LEU A 32 ? 0.1695 0.1268 0.1746 0.0001 0.0099 -0.0072 32 LEU A O
+252 C CB . LEU A 32 ? 0.1767 0.1319 0.1644 -0.0044 0.0045 -0.0115 32 LEU A CB
+253 C CG . LEU A 32 ? 0.1925 0.1523 0.1759 -0.0062 -0.0006 -0.0120 32 LEU A CG
+254 C CD1 . LEU A 32 ? 0.1900 0.1524 0.1752 -0.0043 0.0018 -0.0122 32 LEU A CD1
+255 C CD2 . LEU A 32 ? 0.2102 0.1605 0.1805 -0.0111 -0.0028 -0.0142 32 LEU A CD2
+256 N N . ASP A 33 ? 0.1908 0.1261 0.1746 -0.0061 0.0105 -0.0124 33 ASP A N
+257 C CA . ASP A 33 ? 0.2009 0.1304 0.1891 -0.0038 0.0166 -0.0117 33 ASP A CA
+258 C C . ASP A 33 ? 0.1946 0.1369 0.1970 -0.0019 0.0130 -0.0076 33 ASP A C
+259 O O . ASP A 33 ? 0.2016 0.1493 0.2037 -0.0042 0.0060 -0.0065 33 ASP A O
+260 C CB . ASP A 33 ? 0.2335 0.1598 0.2250 0.0003 0.0255 -0.0115 33 ASP A CB
+261 C CG . ASP A 33 ? 0.3105 0.2238 0.2874 -0.0013 0.0295 -0.0153 33 ASP A CG
+262 O OD1 . ASP A 33 ? 0.3480 0.2480 0.3097 -0.0056 0.0283 -0.0188 33 ASP A OD1
+263 O OD2 . ASP A 33 ? 0.3265 0.2427 0.3068 0.0015 0.0337 -0.0145 33 ASP A OD2
+264 N N . ASP A 34 ? 0.1764 0.1244 0.1914 0.0022 0.0173 -0.0046 34 ASP A N
+265 C CA . ASP A 34 ? 0.1641 0.1238 0.1917 0.0038 0.0139 -0.0005 34 ASP A CA
+266 C C . ASP A 34 ? 0.1535 0.1277 0.1907 0.0061 0.0110 0.0026 34 ASP A C
+267 O O . ASP A 34 ? 0.1547 0.1379 0.2036 0.0083 0.0105 0.0066 34 ASP A O
+268 C CB . ASP A 34 ? 0.1742 0.1298 0.2092 0.0061 0.0201 0.0014 34 ASP A CB
+269 C CG . ASP A 34 ? 0.2272 0.1819 0.2691 0.0099 0.0282 0.0033 34 ASP A CG
+270 O OD1 . ASP A 34 ? 0.2261 0.1809 0.2648 0.0103 0.0295 0.0023 34 ASP A OD1
+271 O OD2 . ASP A 34 ? 0.2542 0.2083 0.3054 0.0125 0.0334 0.0063 34 ASP A OD2
+272 N N . VAL A 35 ? 0.1421 0.1184 0.1739 0.0053 0.0084 0.0010 35 VAL A N
+273 C CA . VAL A 35 ? 0.1436 0.1316 0.1821 0.0069 0.0051 0.0037 35 VAL A CA
+274 C C . VAL A 35 ? 0.1399 0.1313 0.1715 0.0051 -0.0011 0.0023 35 VAL A C
+275 O O . VAL A 35 ? 0.1499 0.1347 0.1716 0.0027 -0.0017 -0.0008 35 VAL A O
+276 C CB . VAL A 35 ? 0.1601 0.1481 0.2015 0.0084 0.0091 0.0044 35 VAL A CB
+277 C CG1 . VAL A 35 ? 0.1611 0.1599 0.2082 0.0091 0.0045 0.0072 35 VAL A CG1
+278 C CG2 . VAL A 35 ? 0.1679 0.1529 0.2177 0.0107 0.0163 0.0069 35 VAL A CG2
+279 N N . VAL A 36 ? 0.1299 0.1308 0.1664 0.0064 -0.0053 0.0050 36 VAL A N
+280 C CA . VAL A 36 ? 0.1327 0.1371 0.1637 0.0058 -0.0101 0.0046 36 VAL A CA
+281 C C . VAL A 36 ? 0.1263 0.1352 0.1584 0.0070 -0.0112 0.0053 36 VAL A C
+282 O O . VAL A 36 ? 0.1188 0.1327 0.1579 0.0084 -0.0115 0.0082 36 VAL A O
+283 C CB . VAL A 36 ? 0.1401 0.1500 0.1736 0.0065 -0.0136 0.0073 36 VAL A CB
+284 C CG1 . VAL A 36 ? 0.1445 0.1580 0.1732 0.0070 -0.0172 0.0078 36 VAL A CG1
+285 C CG2 . VAL A 36 ? 0.1485 0.1535 0.1807 0.0045 -0.0135 0.0070 36 VAL A CG2
+286 N N . TYR A 37 ? 0.1289 0.1355 0.1541 0.0060 -0.0122 0.0030 37 TYR A N
+287 C CA . TYR A 37 ? 0.1248 0.1341 0.1497 0.0065 -0.0137 0.0034 37 TYR A CA
+288 C C . TYR A 37 ? 0.1305 0.1425 0.1501 0.0071 -0.0177 0.0037 37 TYR A C
+289 O O . TYR A 37 ? 0.1433 0.1537 0.1579 0.0064 -0.0186 0.0027 37 TYR A O
+290 C CB . TYR A 37 ? 0.1259 0.1303 0.1462 0.0052 -0.0117 0.0008 37 TYR A CB
+291 C CG . TYR A 37 ? 0.1381 0.1378 0.1616 0.0052 -0.0062 0.0005 37 TYR A CG
+292 C CD1 . TYR A 37 ? 0.1543 0.1469 0.1734 0.0041 -0.0034 -0.0017 37 TYR A CD1
+293 C CD2 . TYR A 37 ? 0.1499 0.1515 0.1806 0.0063 -0.0038 0.0029 37 TYR A CD2
+294 C CE1 . TYR A 37 ? 0.1709 0.1572 0.1914 0.0046 0.0027 -0.0021 37 TYR A CE1
+295 C CE2 . TYR A 37 ? 0.1620 0.1589 0.1962 0.0072 0.0026 0.0034 37 TYR A CE2
+296 C CZ . TYR A 37 ? 0.1816 0.1701 0.2098 0.0066 0.0062 0.0005 37 TYR A CZ
+297 O OH . TYR A 37 ? 0.2143 0.1962 0.2448 0.0079 0.0135 0.0010 37 TYR A OH
+298 N N . CYS A 38 ? 0.1233 0.1388 0.1439 0.0081 -0.0201 0.0056 38 CYS A N
+299 C CA . CYS A 38 ? 0.1292 0.1452 0.1430 0.0092 -0.0229 0.0058 38 CYS A CA
+300 C C . CYS A 38 ? 0.1335 0.1493 0.1447 0.0091 -0.0254 0.0065 38 CYS A C
+301 O O . CYS A 38 ? 0.1367 0.1541 0.1535 0.0081 -0.0258 0.0082 38 CYS A O
+302 C CB . CYS A 38 ? 0.1355 0.1545 0.1507 0.0110 -0.0234 0.0081 38 CYS A CB
+303 S SG . CYS A 38 ? 0.1562 0.1794 0.1768 0.0121 -0.0247 0.0115 38 CYS A SG
+304 N N . PRO A 39 ? 0.1337 0.1469 0.1360 0.0098 -0.0274 0.0058 39 PRO A N
+305 C CA . PRO A 39 ? 0.1342 0.1442 0.1298 0.0092 -0.0309 0.0063 39 PRO A CA
+306 C C . PRO A 39 ? 0.1415 0.1548 0.1415 0.0092 -0.0323 0.0095 39 PRO A C
+307 O O . PRO A 39 ? 0.1469 0.1622 0.1478 0.0111 -0.0313 0.0107 39 PRO A O
+308 C CB . PRO A 39 ? 0.1438 0.1499 0.1296 0.0112 -0.0305 0.0050 39 PRO A CB
+309 C CG . PRO A 39 ? 0.1467 0.1541 0.1352 0.0113 -0.0279 0.0037 39 PRO A CG
+310 C CD . PRO A 39 ? 0.1321 0.1439 0.1290 0.0113 -0.0265 0.0050 39 PRO A CD
+311 N N . ARG A 40 ? 0.1347 0.1480 0.1365 0.0068 -0.0353 0.0114 40 ARG A N
+312 C CA . ARG A 40 ? 0.1363 0.1522 0.1409 0.0061 -0.0378 0.0151 40 ARG A CA
+313 C C . ARG A 40 ? 0.1631 0.1740 0.1549 0.0073 -0.0400 0.0150 40 ARG A C
+314 O O . ARG A 40 ? 0.1704 0.1833 0.1629 0.0078 -0.0407 0.0175 40 ARG A O
+315 C CB . ARG A 40 ? 0.1380 0.1555 0.1486 0.0025 -0.0411 0.0184 40 ARG A CB
+316 C CG . ARG A 40 ? 0.1592 0.1704 0.1596 0.0001 -0.0455 0.0177 40 ARG A CG
+317 C CD . ARG A 40 ? 0.1588 0.1727 0.1669 -0.0040 -0.0497 0.0227 40 ARG A CD
+318 N NE . ARG A 40 ? 0.1780 0.1853 0.1766 -0.0069 -0.0543 0.0221 40 ARG A NE
+319 C CZ . ARG A 40 ? 0.1952 0.2032 0.1976 -0.0113 -0.0597 0.0268 40 ARG A CZ
+320 N NH1 . ARG A 40 ? 0.1822 0.1977 0.1982 -0.0129 -0.0605 0.0328 40 ARG A NH1
+321 N NH2 . ARG A 40 ? 0.1947 0.1956 0.1873 -0.0143 -0.0643 0.0261 40 ARG A NH2
+322 N N . HIS A 41 ? 0.1708 0.1750 0.1508 0.0084 -0.0397 0.0121 41 HIS A N
+323 C CA . HIS A 41 ? 0.1863 0.1838 0.1525 0.0106 -0.0399 0.0119 41 HIS A CA
+324 C C . HIS A 41 ? 0.1951 0.1958 0.1627 0.0149 -0.0359 0.0129 41 HIS A C
+325 O O . HIS A 41 ? 0.2054 0.2012 0.1629 0.0172 -0.0354 0.0136 41 HIS A O
+326 C CB . HIS A 41 ? 0.1972 0.1853 0.1502 0.0106 -0.0406 0.0091 41 HIS A CB
+327 C CG . HIS A 41 ? 0.2270 0.2150 0.1798 0.0134 -0.0364 0.0069 41 HIS A CG
+328 N ND1 . HIS A 41 ? 0.2661 0.2548 0.2175 0.0176 -0.0323 0.0076 41 HIS A ND1
+329 C CD2 . HIS A 41 ? 0.2370 0.2239 0.1905 0.0124 -0.0360 0.0046 41 HIS A CD2
+330 C CE1 . HIS A 41 ? 0.2654 0.2539 0.2173 0.0188 -0.0298 0.0062 41 HIS A CE1
+331 N NE2 . HIS A 41 ? 0.2544 0.2419 0.2074 0.0157 -0.0320 0.0041 41 HIS A NE2
+332 N N . VAL A 42 ? 0.1822 0.1906 0.1623 0.0156 -0.0336 0.0136 42 VAL A N
+333 C CA . VAL A 42 ? 0.1859 0.1985 0.1696 0.0188 -0.0310 0.0159 42 VAL A CA
+334 C C . VAL A 42 ? 0.1949 0.2082 0.1770 0.0189 -0.0329 0.0189 42 VAL A C
+335 O O . VAL A 42 ? 0.2105 0.2241 0.1898 0.0221 -0.0310 0.0207 42 VAL A O
+336 C CB . VAL A 42 ? 0.1841 0.2034 0.1807 0.0184 -0.0292 0.0161 42 VAL A CB
+337 C CG1 . VAL A 42 ? 0.1795 0.2032 0.1863 0.0160 -0.0303 0.0173 42 VAL A CG1
+338 C CG2 . VAL A 42 ? 0.1914 0.2140 0.1907 0.0215 -0.0268 0.0185 42 VAL A CG2
+339 N N . ILE A 43 ? 0.1867 0.2004 0.1707 0.0153 -0.0367 0.0199 43 ILE A N
+340 C CA . ILE A 43 ? 0.2001 0.2144 0.1822 0.0145 -0.0394 0.0234 43 ILE A CA
+341 C C . ILE A 43 ? 0.2405 0.2444 0.2041 0.0146 -0.0414 0.0228 43 ILE A C
+342 O O . ILE A 43 ? 0.2518 0.2544 0.2107 0.0138 -0.0437 0.0255 43 ILE A O
+343 C CB . ILE A 43 ? 0.1911 0.2105 0.1842 0.0102 -0.0429 0.0260 43 ILE A CB
+344 C CG1 . ILE A 43 ? 0.2007 0.2149 0.1882 0.0061 -0.0472 0.0255 43 ILE A CG1
+345 C CG2 . ILE A 43 ? 0.1891 0.2162 0.1985 0.0106 -0.0396 0.0261 43 ILE A CG2
+346 C CD1 . ILE A 43 ? 0.2105 0.2308 0.2108 0.0020 -0.0504 0.0297 43 ILE A CD1
+347 N N . CYS A 44 ? 0.2667 0.2625 0.2191 0.0156 -0.0403 0.0196 44 CYS A N
+348 C CA . CYS A 44 ? 0.3137 0.2971 0.2464 0.0156 -0.0418 0.0188 44 CYS A CA
+349 C C . CYS A 44 ? 0.3723 0.3510 0.2957 0.0217 -0.0360 0.0186 44 CYS A C
+350 O O . CYS A 44 ? 0.3787 0.3624 0.3097 0.0251 -0.0317 0.0185 44 CYS A O
+351 C CB . CYS A 44 ? 0.3157 0.2911 0.2403 0.0133 -0.0436 0.0155 44 CYS A CB
+352 S SG . CYS A 44 ? 0.3091 0.2889 0.2438 0.0063 -0.0504 0.0168 44 CYS A SG
+353 N N . THR A 45 ? 0.4158 0.3836 0.3217 0.0226 -0.0363 0.0189 45 THR A N
+354 C CA . THR A 45 ? 0.4565 0.4164 0.3498 0.0287 -0.0301 0.0190 45 THR A CA
+355 C C . THR A 45 ? 0.4930 0.4402 0.3723 0.0283 -0.0296 0.0152 45 THR A C
+356 O O . THR A 45 ? 0.4961 0.4420 0.3762 0.0231 -0.0348 0.0130 45 THR A O
+357 C CB . THR A 45 ? 0.4873 0.4397 0.3665 0.0295 -0.0304 0.0212 45 THR A CB
+358 O OG1 . THR A 45 ? 0.5172 0.4565 0.3790 0.0245 -0.0359 0.0193 45 THR A OG1
+359 C CG2 . THR A 45 ? 0.4854 0.4501 0.3785 0.0283 -0.0326 0.0250 45 THR A CG2
+360 N N . SER A 46 ? 0.5146 0.4523 0.3813 0.0340 -0.0232 0.0150 46 SER A N
+361 C CA . SER A 46 ? 0.5392 0.4636 0.3915 0.0340 -0.0223 0.0116 46 SER A CA
+362 C C . SER A 46 ? 0.5572 0.4670 0.3904 0.0286 -0.0286 0.0095 46 SER A C
+363 O O . SER A 46 ? 0.5653 0.4683 0.3928 0.0247 -0.0323 0.0065 46 SER A O
+364 C CB . SER A 46 ? 0.5692 0.4857 0.4118 0.0418 -0.0133 0.0128 46 SER A CB
+365 O OG . SER A 46 ? 0.6206 0.5295 0.4576 0.0423 -0.0115 0.0101 46 SER A OG
+366 N N . GLU A 47 ? 0.5606 0.4662 0.3845 0.0278 -0.0303 0.0114 47 GLU A N
+367 C CA . GLU A 47 ? 0.5733 0.4653 0.3785 0.0217 -0.0373 0.0104 47 GLU A CA
+368 C C . GLU A 47 ? 0.5575 0.4580 0.3755 0.0133 -0.0468 0.0109 47 GLU A C
+369 O O . GLU A 47 ? 0.5721 0.4620 0.3788 0.0078 -0.0527 0.0091 47 GLU A O
+370 C CB . GLU A 47 ? 0.6141 0.5023 0.4093 0.0228 -0.0369 0.0133 47 GLU A CB
+371 C CG . GLU A 47 ? 0.7008 0.5744 0.4757 0.0154 -0.0451 0.0130 47 GLU A CG
+372 C CD . GLU A 47 ? 0.7996 0.6698 0.5645 0.0150 -0.0462 0.0161 47 GLU A CD
+373 O OE1 . GLU A 47 ? 0.8102 0.6928 0.5882 0.0202 -0.0412 0.0191 47 GLU A OE1
+374 O OE2 . GLU A 47 ? 0.8443 0.6991 0.5879 0.0092 -0.0525 0.0159 47 GLU A OE2
+375 N N . ASP A 48 ? 0.5245 0.4437 0.3662 0.0125 -0.0481 0.0136 48 ASP A N
+376 C CA . ASP A 48 ? 0.5032 0.4319 0.3596 0.0056 -0.0555 0.0152 48 ASP A CA
+377 C C . ASP A 48 ? 0.4859 0.4129 0.3449 0.0034 -0.0570 0.0124 48 ASP A C
+378 O O . ASP A 48 ? 0.4853 0.4111 0.3451 -0.0031 -0.0643 0.0134 48 ASP A O
+379 C CB . ASP A 48 ? 0.5029 0.4508 0.3845 0.0067 -0.0541 0.0181 48 ASP A CB
+380 C CG . ASP A 48 ? 0.5549 0.5080 0.4393 0.0072 -0.0546 0.0220 48 ASP A CG
+381 O OD1 . ASP A 48 ? 0.5653 0.5100 0.4362 0.0033 -0.0596 0.0238 48 ASP A OD1
+382 O OD2 . ASP A 48 ? 0.5728 0.5380 0.4728 0.0109 -0.0503 0.0236 48 ASP A OD2
+383 N N . MET A 49 ? 0.4729 0.4001 0.3335 0.0086 -0.0505 0.0095 49 MET A N
+384 C CA . MET A 49 ? 0.4625 0.3892 0.3268 0.0069 -0.0514 0.0069 49 MET A CA
+385 C C . MET A 49 ? 0.4647 0.3753 0.3103 0.0022 -0.0568 0.0051 49 MET A C
+386 O O . MET A 49 ? 0.4547 0.3665 0.3055 -0.0011 -0.0601 0.0043 49 MET A O
+387 C CB . MET A 49 ? 0.4649 0.3936 0.3326 0.0132 -0.0435 0.0048 49 MET A CB
+388 C CG . MET A 49 ? 0.4693 0.4140 0.3572 0.0161 -0.0398 0.0065 49 MET A CG
+389 S SD . MET A 49 ? 0.4666 0.4249 0.3751 0.0107 -0.0446 0.0075 49 MET A SD
+390 C CE . MET A 49 ? 0.3963 0.3518 0.3049 0.0097 -0.0444 0.0042 49 MET A CE
+391 N N . LEU A 50 ? 0.4750 0.3702 0.2988 0.0018 -0.0579 0.0048 50 LEU A N
+392 C CA . LEU A 50 ? 0.4951 0.3727 0.2988 -0.0035 -0.0638 0.0031 50 LEU A CA
+393 C C . LEU A 50 ? 0.4892 0.3714 0.3007 -0.0125 -0.0744 0.0062 50 LEU A C
+394 O O . LEU A 50 ? 0.5008 0.3775 0.3094 -0.0168 -0.0790 0.0053 50 LEU A O
+395 C CB . LEU A 50 ? 0.5188 0.3769 0.2950 -0.0022 -0.0625 0.0021 50 LEU A CB
+396 C CG . LEU A 50 ? 0.5538 0.4051 0.3208 0.0072 -0.0512 -0.0002 50 LEU A CG
+397 C CD1 . LEU A 50 ? 0.5787 0.4107 0.3185 0.0088 -0.0492 -0.0005 50 LEU A CD1
+398 C CD2 . LEU A 50 ? 0.5675 0.4125 0.3316 0.0097 -0.0473 -0.0035 50 LEU A CD2
+399 N N . ASN A 51 ? 0.4655 0.3587 0.2886 -0.0153 -0.0781 0.0107 51 ASN A N
+400 C CA . ASN A 51 ? 0.4505 0.3502 0.2843 -0.0236 -0.0877 0.0154 51 ASN A CA
+401 C C . ASN A 51 ? 0.4106 0.3292 0.2674 -0.0231 -0.0871 0.0201 51 ASN A C
+402 O O . ASN A 51 ? 0.4166 0.3359 0.2718 -0.0268 -0.0920 0.0243 51 ASN A O
+403 C CB . ASN A 51 ? 0.4934 0.3764 0.3050 -0.0310 -0.0968 0.0172 51 ASN A CB
+404 C CG . ASN A 51 ? 0.5408 0.4292 0.3627 -0.0404 -0.1077 0.0232 51 ASN A CG
+405 O OD1 . ASN A 51 ? 0.5517 0.4536 0.3951 -0.0411 -0.1081 0.0253 51 ASN A OD1
+406 N ND2 . ASN A 51 ? 0.5631 0.4408 0.3698 -0.0478 -0.1167 0.0266 51 ASN A ND2
+407 N N . PRO A 52 ? 0.3637 0.2970 0.2411 -0.0183 -0.0808 0.0193 52 PRO A N
+408 C CA . PRO A 52 ? 0.3370 0.2864 0.2345 -0.0171 -0.0792 0.0233 52 PRO A CA
+409 C C . PRO A 52 ? 0.3183 0.2781 0.2333 -0.0231 -0.0854 0.0295 52 PRO A C
+410 O O . PRO A 52 ? 0.3308 0.2919 0.2521 -0.0260 -0.0879 0.0301 52 PRO A O
+411 C CB . PRO A 52 ? 0.3352 0.2934 0.2451 -0.0104 -0.0704 0.0200 52 PRO A CB
+412 C CG . PRO A 52 ? 0.3498 0.3017 0.2544 -0.0104 -0.0698 0.0161 52 PRO A CG
+413 C CD . PRO A 52 ? 0.3524 0.2872 0.2342 -0.0139 -0.0749 0.0150 52 PRO A CD
+414 N N . ASN A 53 ? 0.2904 0.2581 0.2144 -0.0247 -0.0874 0.0346 53 ASN A N
+415 C CA . ASN A 53 ? 0.2714 0.2513 0.2160 -0.0292 -0.0915 0.0417 53 ASN A CA
+416 C C . ASN A 53 ? 0.2561 0.2495 0.2199 -0.0233 -0.0835 0.0415 53 ASN A C
+417 O O . ASN A 53 ? 0.2636 0.2611 0.2298 -0.0214 -0.0818 0.0432 53 ASN A O
+418 C CB . ASN A 53 ? 0.2848 0.2640 0.2268 -0.0357 -0.0999 0.0486 53 ASN A CB
+419 C CG . ASN A 53 ? 0.3101 0.3024 0.2753 -0.0401 -0.1038 0.0571 53 ASN A CG
+420 O OD1 . ASN A 53 ? 0.3120 0.3174 0.2984 -0.0364 -0.0978 0.0589 53 ASN A OD1
+421 N ND2 . ASN A 53 ? 0.3174 0.3058 0.2792 -0.0483 -0.1136 0.0631 53 ASN A ND2
+422 N N . TYR A 54 ? 0.2424 0.2414 0.2180 -0.0206 -0.0786 0.0394 54 TYR A N
+423 C CA . TYR A 54 ? 0.2190 0.2277 0.2090 -0.0151 -0.0706 0.0380 54 TYR A CA
+424 C C . TYR A 54 ? 0.2126 0.2325 0.2207 -0.0161 -0.0708 0.0446 54 TYR A C
+425 O O . TYR A 54 ? 0.2098 0.2340 0.2224 -0.0125 -0.0664 0.0439 54 TYR A O
+426 C CB . TYR A 54 ? 0.1991 0.2092 0.1952 -0.0128 -0.0659 0.0343 54 TYR A CB
+427 C CG . TYR A 54 ? 0.2051 0.2062 0.1857 -0.0098 -0.0634 0.0275 54 TYR A CG
+428 C CD1 . TYR A 54 ? 0.2100 0.2115 0.1881 -0.0046 -0.0576 0.0238 54 TYR A CD1
+429 C CD2 . TYR A 54 ? 0.2146 0.2070 0.1837 -0.0123 -0.0670 0.0256 54 TYR A CD2
+430 C CE1 . TYR A 54 ? 0.2203 0.2145 0.1861 -0.0017 -0.0549 0.0189 54 TYR A CE1
+431 C CE2 . TYR A 54 ? 0.2297 0.2141 0.1858 -0.0093 -0.0641 0.0200 54 TYR A CE2
+432 C CZ . TYR A 54 ? 0.2388 0.2243 0.1935 -0.0039 -0.0578 0.0169 54 TYR A CZ
+433 O OH . TYR A 54 ? 0.2600 0.2383 0.2033 -0.0007 -0.0547 0.0126 54 TYR A OH
+434 N N . GLU A 55 ? 0.2157 0.2401 0.2346 -0.0210 -0.0755 0.0513 55 GLU A N
+435 C CA . GLU A 55 ? 0.2147 0.2503 0.2523 -0.0216 -0.0749 0.0585 55 GLU A CA
+436 C C . GLU A 55 ? 0.2191 0.2544 0.2503 -0.0224 -0.0778 0.0605 55 GLU A C
+437 O O . GLU A 55 ? 0.2158 0.2588 0.2585 -0.0196 -0.0739 0.0625 55 GLU A O
+438 C CB . GLU A 55 ? 0.2489 0.2902 0.3003 -0.0271 -0.0801 0.0674 55 GLU A CB
+439 C CG . GLU A 55 ? 0.3177 0.3632 0.3827 -0.0252 -0.0751 0.0679 55 GLU A CG
+440 C CD . GLU A 55 ? 0.3953 0.4491 0.4783 -0.0201 -0.0658 0.0687 55 GLU A CD
+441 O OE1 . GLU A 55 ? 0.3796 0.4366 0.4658 -0.0173 -0.0623 0.0681 55 GLU A OE1
+442 O OE2 . GLU A 55 ? 0.4443 0.5004 0.5372 -0.0188 -0.0615 0.0697 55 GLU A OE2
+443 N N . ASP A 56 ? 0.2230 0.2482 0.2347 -0.0260 -0.0845 0.0597 56 ASP A N
+444 C CA . ASP A 56 ? 0.2304 0.2538 0.2334 -0.0269 -0.0872 0.0616 56 ASP A CA
+445 C C . ASP A 56 ? 0.2346 0.2569 0.2318 -0.0198 -0.0798 0.0556 56 ASP A C
+446 O O . ASP A 56 ? 0.2434 0.2719 0.2470 -0.0182 -0.0783 0.0583 56 ASP A O
+447 C CB . ASP A 56 ? 0.2578 0.2683 0.2388 -0.0329 -0.0960 0.0623 56 ASP A CB
+448 C CG . ASP A 56 ? 0.3026 0.3156 0.2907 -0.0413 -0.1053 0.0708 56 ASP A CG
+449 O OD1 . ASP A 56 ? 0.2869 0.3134 0.2985 -0.0422 -0.1049 0.0781 56 ASP A OD1
+450 O OD2 . ASP A 56 ? 0.3320 0.3330 0.3023 -0.0470 -0.1130 0.0709 56 ASP A OD2
+451 N N . LEU A 57 ? 0.2342 0.2493 0.2205 -0.0158 -0.0754 0.0482 57 LEU A N
+452 C CA . LEU A 57 ? 0.2381 0.2527 0.2202 -0.0093 -0.0686 0.0437 57 LEU A CA
+453 C C . LEU A 57 ? 0.2260 0.2529 0.2289 -0.0057 -0.0628 0.0448 57 LEU A C
+454 O O . LEU A 57 ? 0.2258 0.2561 0.2308 -0.0021 -0.0595 0.0449 57 LEU A O
+455 C CB . LEU A 57 ? 0.2503 0.2561 0.2198 -0.0060 -0.0651 0.0369 57 LEU A CB
+456 C CG . LEU A 57 ? 0.2895 0.2804 0.2353 -0.0081 -0.0690 0.0346 57 LEU A CG
+457 C CD1 . LEU A 57 ? 0.3054 0.2892 0.2426 -0.0049 -0.0650 0.0287 57 LEU A CD1
+458 C CD2 . LEU A 57 ? 0.3070 0.2920 0.2385 -0.0060 -0.0683 0.0350 57 LEU A CD2
+459 N N . LEU A 58 ? 0.2097 0.2422 0.2272 -0.0068 -0.0616 0.0459 58 LEU A N
+460 C CA . LEU A 58 ? 0.2064 0.2478 0.2414 -0.0036 -0.0557 0.0464 58 LEU A CA
+461 C C . LEU A 58 ? 0.2077 0.2577 0.2561 -0.0045 -0.0564 0.0529 58 LEU A C
+462 O O . LEU A 58 ? 0.2154 0.2705 0.2731 -0.0010 -0.0514 0.0525 58 LEU A O
+463 C CB . LEU A 58 ? 0.2030 0.2459 0.2476 -0.0042 -0.0534 0.0458 58 LEU A CB
+464 C CG . LEU A 58 ? 0.2085 0.2557 0.2651 -0.0005 -0.0460 0.0438 58 LEU A CG
+465 C CD1 . LEU A 58 ? 0.2022 0.2459 0.2502 0.0035 -0.0423 0.0379 58 LEU A CD1
+466 C CD2 . LEU A 58 ? 0.2163 0.2637 0.2805 -0.0013 -0.0438 0.0438 58 LEU A CD2
+467 N N . ILE A 59 ? 0.2065 0.2578 0.2550 -0.0094 -0.0630 0.0590 59 ILE A N
+468 C CA . ILE A 59 ? 0.2165 0.2764 0.2778 -0.0106 -0.0643 0.0661 59 ILE A CA
+469 C C . ILE A 59 ? 0.2255 0.2857 0.2813 -0.0069 -0.0619 0.0643 59 ILE A C
+470 O O . ILE A 59 ? 0.2214 0.2898 0.2908 -0.0055 -0.0597 0.0681 59 ILE A O
+471 C CB . ILE A 59 ? 0.2392 0.2992 0.2986 -0.0174 -0.0732 0.0734 59 ILE A CB
+472 C CG1 . ILE A 59 ? 0.2630 0.3255 0.3329 -0.0213 -0.0757 0.0777 59 ILE A CG1
+473 C CG2 . ILE A 59 ? 0.2463 0.3149 0.3164 -0.0188 -0.0750 0.0808 59 ILE A CG2
+474 C CD1 . ILE A 59 ? 0.2926 0.3538 0.3584 -0.0292 -0.0861 0.0852 59 ILE A CD1
+475 N N . ARG A 60 ? 0.2395 0.2907 0.2757 -0.0051 -0.0622 0.0591 60 ARG A N
+476 C CA . ARG A 60 ? 0.2522 0.3034 0.2828 -0.0012 -0.0596 0.0581 60 ARG A CA
+477 C C . ARG A 60 ? 0.2388 0.2934 0.2769 0.0044 -0.0524 0.0543 60 ARG A C
+478 O O . ARG A 60 ? 0.2522 0.3074 0.2870 0.0080 -0.0500 0.0539 60 ARG A O
+479 C CB . ARG A 60 ? 0.2970 0.3364 0.3034 -0.0011 -0.0620 0.0552 60 ARG A CB
+480 C CG . ARG A 60 ? 0.3633 0.3965 0.3587 -0.0077 -0.0701 0.0585 60 ARG A CG
+481 C CD . ARG A 60 ? 0.4112 0.4515 0.4147 -0.0112 -0.0745 0.0661 60 ARG A CD
+482 N NE . ARG A 60 ? 0.4675 0.5059 0.4695 -0.0189 -0.0830 0.0711 60 ARG A NE
+483 C CZ . ARG A 60 ? 0.4890 0.5351 0.5020 -0.0237 -0.0881 0.0793 60 ARG A CZ
+484 N NH1 . ARG A 60 ? 0.4853 0.5294 0.4970 -0.0313 -0.0964 0.0846 60 ARG A NH1
+485 N NH2 . ARG A 60 ? 0.4813 0.5375 0.5075 -0.0212 -0.0853 0.0830 60 ARG A NH2
+486 N N . LYS A 61 ? 0.2107 0.2668 0.2580 0.0050 -0.0491 0.0517 61 LYS A N
+487 C CA . LYS A 61 ? 0.2015 0.2591 0.2540 0.0092 -0.0432 0.0481 61 LYS A CA
+488 C C . LYS A 61 ? 0.1973 0.2624 0.2687 0.0094 -0.0401 0.0509 61 LYS A C
+489 O O . LYS A 61 ? 0.2081 0.2760 0.2892 0.0068 -0.0408 0.0540 61 LYS A O
+490 C CB . LYS A 61 ? 0.2188 0.2701 0.2642 0.0098 -0.0414 0.0424 61 LYS A CB
+491 C CG . LYS A 61 ? 0.2620 0.3046 0.2885 0.0101 -0.0435 0.0394 61 LYS A CG
+492 C CD . LYS A 61 ? 0.3096 0.3507 0.3275 0.0139 -0.0418 0.0394 61 LYS A CD
+493 C CE . LYS A 61 ? 0.3620 0.3928 0.3608 0.0150 -0.0423 0.0363 61 LYS A CE
+494 N NZ . LYS A 61 ? 0.3994 0.4282 0.3897 0.0193 -0.0397 0.0373 61 LYS A NZ
+495 N N . SER A 62 ? 0.1776 0.2457 0.2545 0.0125 -0.0365 0.0504 62 SER A N
+496 C CA . SER A 62 ? 0.1690 0.2418 0.2617 0.0132 -0.0327 0.0521 62 SER A CA
+497 C C . SER A 62 ? 0.1510 0.2194 0.2419 0.0152 -0.0285 0.0468 62 SER A C
+498 O O . SER A 62 ? 0.1477 0.2118 0.2273 0.0164 -0.0288 0.0431 62 SER A O
+499 C CB . SER A 62 ? 0.2000 0.2793 0.3004 0.0144 -0.0328 0.0566 62 SER A CB
+500 O OG . SER A 62 ? 0.2401 0.3234 0.3417 0.0120 -0.0372 0.0620 62 SER A OG
+501 N N . ASN A 63 ? 0.1426 0.2113 0.2442 0.0155 -0.0244 0.0467 63 ASN A N
+502 C CA . ASN A 63 ? 0.1389 0.2022 0.2378 0.0164 -0.0210 0.0420 63 ASN A CA
+503 C C . ASN A 63 ? 0.1396 0.2029 0.2325 0.0181 -0.0221 0.0410 63 ASN A C
+504 O O . ASN A 63 ? 0.1422 0.2008 0.2270 0.0182 -0.0218 0.0372 63 ASN A O
+505 C CB . ASN A 63 ? 0.1400 0.2028 0.2503 0.0167 -0.0165 0.0429 63 ASN A CB
+506 C CG . ASN A 63 ? 0.1606 0.2220 0.2770 0.0158 -0.0136 0.0440 63 ASN A CG
+507 O OD1 . ASN A 63 ? 0.1610 0.2198 0.2717 0.0147 -0.0145 0.0422 63 ASN A OD1
+508 N ND2 . ASN A 63 ? 0.1556 0.2186 0.2845 0.0164 -0.0096 0.0474 63 ASN A ND2
+509 N N . HIS A 64 ? 0.1366 0.2058 0.2344 0.0194 -0.0233 0.0450 64 HIS A N
+510 C CA . HIS A 64 ? 0.1395 0.2098 0.2337 0.0214 -0.0239 0.0456 64 HIS A CA
+511 C C . HIS A 64 ? 0.1476 0.2159 0.2288 0.0228 -0.0257 0.0445 64 HIS A C
+512 O O . HIS A 64 ? 0.1578 0.2267 0.2361 0.0249 -0.0255 0.0453 64 HIS A O
+513 C CB . HIS A 64 ? 0.1440 0.2214 0.2474 0.0228 -0.0243 0.0507 64 HIS A CB
+514 C CG . HIS A 64 ? 0.1574 0.2393 0.2592 0.0231 -0.0269 0.0545 64 HIS A CG
+515 N ND1 . HIS A 64 ? 0.1694 0.2548 0.2790 0.0213 -0.0277 0.0575 64 HIS A ND1
+516 C CD2 . HIS A 64 ? 0.1738 0.2566 0.2667 0.0250 -0.0286 0.0562 64 HIS A CD2
+517 C CE1 . HIS A 64 ? 0.1754 0.2634 0.2797 0.0213 -0.0308 0.0606 64 HIS A CE1
+518 N NE2 . HIS A 64 ? 0.1810 0.2667 0.2742 0.0237 -0.0311 0.0595 64 HIS A NE2
+519 N N . ASN A 65 ? 0.1421 0.2078 0.2157 0.0217 -0.0274 0.0433 65 ASN A N
+520 C CA . ASN A 65 ? 0.1553 0.2168 0.2150 0.0231 -0.0285 0.0418 65 ASN A CA
+521 C C . ASN A 65 ? 0.1613 0.2173 0.2150 0.0229 -0.0272 0.0373 65 ASN A C
+522 O O . ASN A 65 ? 0.1761 0.2288 0.2198 0.0247 -0.0271 0.0365 65 ASN A O
+523 C CB . ASN A 65 ? 0.1695 0.2287 0.2218 0.0213 -0.0315 0.0422 65 ASN A CB
+524 C CG . ASN A 65 ? 0.2148 0.2782 0.2691 0.0212 -0.0336 0.0470 65 ASN A CG
+525 O OD1 . ASN A 65 ? 0.2319 0.2968 0.2893 0.0182 -0.0363 0.0491 65 ASN A OD1
+526 N ND2 . ASN A 65 ? 0.2177 0.2836 0.2708 0.0243 -0.0325 0.0495 65 ASN A ND2
+527 N N . PHE A 66 ? 0.1497 0.2042 0.2089 0.0208 -0.0259 0.0348 66 PHE A N
+528 C CA . PHE A 66 ? 0.1500 0.1993 0.2036 0.0201 -0.0250 0.0308 66 PHE A CA
+529 C C . PHE A 66 ? 0.1633 0.2130 0.2202 0.0205 -0.0239 0.0311 66 PHE A C
+530 O O . PHE A 66 ? 0.1783 0.2277 0.2423 0.0190 -0.0227 0.0309 66 PHE A O
+531 C CB . PHE A 66 ? 0.1409 0.1871 0.1969 0.0175 -0.0240 0.0280 66 PHE A CB
+532 C CG . PHE A 66 ? 0.1481 0.1940 0.2013 0.0164 -0.0260 0.0284 66 PHE A CG
+533 C CD1 . PHE A 66 ? 0.1628 0.2043 0.2053 0.0161 -0.0275 0.0261 66 PHE A CD1
+534 C CD2 . PHE A 66 ? 0.1524 0.2022 0.2140 0.0153 -0.0266 0.0318 66 PHE A CD2
+535 C CE1 . PHE A 66 ? 0.1717 0.2122 0.2112 0.0143 -0.0302 0.0269 66 PHE A CE1
+536 C CE2 . PHE A 66 ? 0.1617 0.2114 0.2212 0.0134 -0.0295 0.0333 66 PHE A CE2
+537 C CZ . PHE A 66 ? 0.1615 0.2061 0.2093 0.0127 -0.0316 0.0307 66 PHE A CZ
+538 N N . LEU A 67 ? 0.1528 0.2026 0.2045 0.0223 -0.0242 0.0323 67 LEU A N
+539 C CA . LEU A 67 ? 0.1549 0.2058 0.2102 0.0223 -0.0241 0.0341 67 LEU A CA
+540 C C . LEU A 67 ? 0.1556 0.2011 0.2063 0.0197 -0.0242 0.0307 67 LEU A C
+541 O O . LEU A 67 ? 0.1556 0.1989 0.1989 0.0204 -0.0242 0.0295 67 LEU A O
+542 C CB . LEU A 67 ? 0.1694 0.2240 0.2231 0.0259 -0.0240 0.0387 67 LEU A CB
+543 C CG . LEU A 67 ? 0.2040 0.2634 0.2603 0.0286 -0.0238 0.0424 67 LEU A CG
+544 C CD1 . LEU A 67 ? 0.2174 0.2792 0.2706 0.0330 -0.0225 0.0471 67 LEU A CD1
+545 C CD2 . LEU A 67 ? 0.2184 0.2820 0.2861 0.0273 -0.0243 0.0444 67 LEU A CD2
+546 N N . VAL A 68 ? 0.1411 0.1836 0.1954 0.0166 -0.0241 0.0291 68 VAL A N
+547 C CA . VAL A 68 ? 0.1470 0.1832 0.1958 0.0135 -0.0243 0.0257 68 VAL A CA
+548 C C . VAL A 68 ? 0.1559 0.1913 0.2065 0.0113 -0.0262 0.0282 68 VAL A C
+549 O O . VAL A 68 ? 0.1585 0.1941 0.2148 0.0103 -0.0265 0.0298 68 VAL A O
+550 C CB . VAL A 68 ? 0.1612 0.1918 0.2099 0.0114 -0.0221 0.0215 68 VAL A CB
+551 C CG1 . VAL A 68 ? 0.1670 0.1902 0.2084 0.0082 -0.0220 0.0178 68 VAL A CG1
+552 C CG2 . VAL A 68 ? 0.1702 0.2028 0.2190 0.0132 -0.0210 0.0205 68 VAL A CG2
+553 N N . GLN A 69 ? 0.1602 0.1952 0.2065 0.0104 -0.0278 0.0294 69 GLN A N
+554 C CA . GLN A 69 ? 0.1772 0.2122 0.2259 0.0077 -0.0307 0.0333 69 GLN A CA
+555 C C . GLN A 69 ? 0.1946 0.2232 0.2361 0.0033 -0.0323 0.0309 69 GLN A C
+556 O O . GLN A 69 ? 0.1901 0.2187 0.2267 0.0043 -0.0316 0.0296 69 GLN A O
+557 C CB . GLN A 69 ? 0.1963 0.2396 0.2497 0.0114 -0.0313 0.0402 69 GLN A CB
+558 C CG . GLN A 69 ? 0.2373 0.2833 0.2968 0.0091 -0.0347 0.0466 69 GLN A CG
+559 C CD . GLN A 69 ? 0.2773 0.3317 0.3418 0.0139 -0.0339 0.0540 69 GLN A CD
+560 O OE1 . GLN A 69 ? 0.2862 0.3444 0.3514 0.0190 -0.0309 0.0547 69 GLN A OE1
+561 N NE2 . GLN A 69 ? 0.2905 0.3473 0.3582 0.0121 -0.0365 0.0602 69 GLN A NE2
+562 N N . ALA A 70 ? 0.2201 0.2421 0.2599 -0.0017 -0.0344 0.0301 70 ALA A N
+563 C CA . ALA A 70 ? 0.2502 0.2644 0.2818 -0.0071 -0.0366 0.0280 70 ALA A CA
+564 C C . ALA A 70 ? 0.2762 0.2930 0.3110 -0.0104 -0.0418 0.0350 70 ALA A C
+565 O O . ALA A 70 ? 0.2803 0.2952 0.3183 -0.0131 -0.0442 0.0374 70 ALA A O
+566 C CB . ALA A 70 ? 0.2561 0.2590 0.2818 -0.0106 -0.0351 0.0226 70 ALA A CB
+567 N N . GLY A 71 ? 0.2932 0.3155 0.3291 -0.0097 -0.0433 0.0393 71 GLY A N
+568 C CA . GLY A 71 ? 0.3039 0.3312 0.3459 -0.0122 -0.0480 0.0480 71 GLY A CA
+569 C C . GLY A 71 ? 0.3035 0.3394 0.3562 -0.0076 -0.0472 0.0536 71 GLY A C
+570 O O . GLY A 71 ? 0.3133 0.3550 0.3687 -0.0011 -0.0430 0.0534 71 GLY A O
+571 N N A ASN A 72 ? 0.2967 0.3324 0.3544 -0.0112 -0.0512 0.0581 72 ASN A N
+572 N N B ASN A 72 ? 0.2996 0.3356 0.3576 -0.0112 -0.0512 0.0583 72 ASN A N
+573 C CA A ASN A 72 ? 0.2894 0.3333 0.3579 -0.0072 -0.0506 0.0637 72 ASN A CA
+574 C CA B ASN A 72 ? 0.2953 0.3396 0.3641 -0.0070 -0.0505 0.0639 72 ASN A CA
+575 C C A ASN A 72 ? 0.2844 0.3241 0.3527 -0.0065 -0.0484 0.0581 72 ASN A C
+576 C C B ASN A 72 ? 0.2858 0.3261 0.3550 -0.0067 -0.0489 0.0590 72 ASN A C
+577 O O A ASN A 72 ? 0.2848 0.3311 0.3618 -0.0030 -0.0476 0.0620 72 ASN A O
+578 O O B ASN A 72 ? 0.2853 0.3318 0.3635 -0.0041 -0.0489 0.0637 72 ASN A O
+579 C CB A ASN A 72 ? 0.3023 0.3498 0.3786 -0.0113 -0.0566 0.0734 72 ASN A CB
+580 C CB B ASN A 72 ? 0.3169 0.3666 0.3945 -0.0100 -0.0560 0.0746 72 ASN A CB
+581 C CG A ASN A 72 ? 0.3301 0.3891 0.4194 -0.0061 -0.0557 0.0819 72 ASN A CG
+582 C CG B ASN A 72 ? 0.3733 0.4141 0.4471 -0.0192 -0.0627 0.0749 72 ASN A CG
+583 O OD1 A ASN A 72 ? 0.3382 0.4048 0.4309 0.0010 -0.0511 0.0846 72 ASN A OD1
+584 O OD1 B ASN A 72 ? 0.3977 0.4295 0.4666 -0.0221 -0.0629 0.0691 72 ASN A OD1
+585 N ND2 A ASN A 72 ? 0.3352 0.3945 0.4310 -0.0093 -0.0598 0.0863 72 ASN A ND2
+586 N ND2 B ASN A 72 ? 0.3798 0.4222 0.4556 -0.0241 -0.0683 0.0824 72 ASN A ND2
+587 N N A VAL A 73 ? 0.2756 0.3045 0.3347 -0.0096 -0.0471 0.0497 73 VAL A N
+588 N N B VAL A 73 ? 0.2733 0.3034 0.3335 -0.0091 -0.0471 0.0504 73 VAL A N
+589 C CA A VAL A 73 ? 0.2687 0.2933 0.3288 -0.0090 -0.0446 0.0455 73 VAL A CA
+590 C CA B VAL A 73 ? 0.2623 0.2875 0.3231 -0.0089 -0.0448 0.0461 73 VAL A CA
+591 C C A VAL A 73 ? 0.2429 0.2701 0.3030 -0.0034 -0.0389 0.0407 73 VAL A C
+592 C C B VAL A 73 ? 0.2460 0.2730 0.3061 -0.0036 -0.0390 0.0408 73 VAL A C
+593 O O A VAL A 73 ? 0.2341 0.2588 0.2876 -0.0027 -0.0367 0.0363 73 VAL A O
+594 O O B VAL A 73 ? 0.2468 0.2705 0.2999 -0.0032 -0.0369 0.0361 73 VAL A O
+595 C CB A VAL A 73 ? 0.2938 0.3038 0.3449 -0.0155 -0.0460 0.0407 73 VAL A CB
+596 C CB B VAL A 73 ? 0.2769 0.2878 0.3287 -0.0159 -0.0468 0.0418 73 VAL A CB
+597 C CG1 A VAL A 73 ? 0.3138 0.3149 0.3532 -0.0169 -0.0432 0.0334 73 VAL A CG1
+598 C CG1 B VAL A 73 ? 0.2857 0.2897 0.3364 -0.0147 -0.0422 0.0361 73 VAL A CG1
+599 C CG2 A VAL A 73 ? 0.3009 0.3074 0.3558 -0.0147 -0.0435 0.0388 73 VAL A CG2
+600 C CG2 B VAL A 73 ? 0.2809 0.2903 0.3351 -0.0215 -0.0535 0.0482 73 VAL A CG2
+601 N N . GLN A 74 ? 0.2292 0.2618 0.2972 0.0002 -0.0370 0.0423 74 GLN A N
+602 C CA . GLN A 74 ? 0.2079 0.2433 0.2770 0.0046 -0.0327 0.0391 74 GLN A CA
+603 C C . GLN A 74 ? 0.2000 0.2265 0.2658 0.0028 -0.0296 0.0331 74 GLN A C
+604 O O . GLN A 74 ? 0.2053 0.2250 0.2715 -0.0002 -0.0298 0.0324 74 GLN A O
+605 C CB . GLN A 74 ? 0.2017 0.2464 0.2807 0.0086 -0.0322 0.0440 74 GLN A CB
+606 C CG . GLN A 74 ? 0.2025 0.2529 0.2815 0.0135 -0.0293 0.0433 74 GLN A CG
+607 C CD . GLN A 74 ? 0.2277 0.2810 0.3015 0.0159 -0.0294 0.0447 74 GLN A CD
+608 O OE1 . GLN A 74 ? 0.2352 0.2901 0.3093 0.0154 -0.0314 0.0487 74 GLN A OE1
+609 N NE2 . GLN A 74 ? 0.2313 0.2853 0.3008 0.0187 -0.0273 0.0422 74 GLN A NE2
+610 N N . LEU A 75 ? 0.1864 0.2124 0.2489 0.0049 -0.0264 0.0291 75 LEU A N
+611 C CA . LEU A 75 ? 0.1892 0.2081 0.2503 0.0042 -0.0224 0.0246 75 LEU A CA
+612 C C . LEU A 75 ? 0.1778 0.2034 0.2479 0.0079 -0.0199 0.0263 75 LEU A C
+613 O O . LEU A 75 ? 0.1848 0.2187 0.2575 0.0108 -0.0208 0.0287 75 LEU A O
+614 C CB . LEU A 75 ? 0.2020 0.2155 0.2545 0.0034 -0.0207 0.0199 75 LEU A CB
+615 C CG . LEU A 75 ? 0.2354 0.2421 0.2782 -0.0007 -0.0233 0.0183 75 LEU A CG
+616 C CD1 . LEU A 75 ? 0.2468 0.2484 0.2818 -0.0012 -0.0210 0.0136 75 LEU A CD1
+617 C CD2 . LEU A 75 ? 0.2622 0.2593 0.3016 -0.0052 -0.0245 0.0178 75 LEU A CD2
+618 N N . ARG A 76 ? 0.1580 0.1790 0.2321 0.0075 -0.0166 0.0253 76 ARG A N
+619 C CA . ARG A 76 ? 0.1483 0.1758 0.2325 0.0104 -0.0142 0.0278 76 ARG A CA
+620 C C . ARG A 76 ? 0.1556 0.1822 0.2391 0.0115 -0.0110 0.0257 76 ARG A C
+621 O O . ARG A 76 ? 0.1705 0.1882 0.2501 0.0103 -0.0073 0.0224 76 ARG A O
+622 C CB . ARG A 76 ? 0.1542 0.1774 0.2447 0.0098 -0.0118 0.0289 76 ARG A CB
+623 C CG . ARG A 76 ? 0.1544 0.1859 0.2574 0.0127 -0.0099 0.0329 76 ARG A CG
+624 C CD . ARG A 76 ? 0.1620 0.1890 0.2716 0.0122 -0.0073 0.0342 76 ARG A CD
+625 N NE . ARG A 76 ? 0.1758 0.2025 0.2848 0.0104 -0.0115 0.0359 76 ARG A NE
+626 C CZ . ARG A 76 ? 0.1826 0.2198 0.2994 0.0120 -0.0148 0.0409 76 ARG A CZ
+627 N NH1 . ARG A 76 ? 0.1608 0.2087 0.2855 0.0151 -0.0144 0.0443 76 ARG A NH1
+628 N NH2 . ARG A 76 ? 0.1781 0.2151 0.2948 0.0101 -0.0186 0.0432 76 ARG A NH2
+629 N N . VAL A 77 ? 0.1442 0.1795 0.2310 0.0136 -0.0124 0.0281 77 VAL A N
+630 C CA . VAL A 77 ? 0.1462 0.1822 0.2336 0.0142 -0.0106 0.0274 77 VAL A CA
+631 C C . VAL A 77 ? 0.1473 0.1863 0.2465 0.0153 -0.0074 0.0309 77 VAL A C
+632 O O . VAL A 77 ? 0.1462 0.1929 0.2530 0.0164 -0.0091 0.0352 77 VAL A O
+633 C CB . VAL A 77 ? 0.1438 0.1855 0.2267 0.0150 -0.0144 0.0283 77 VAL A CB
+634 C CG1 . VAL A 77 ? 0.1508 0.1931 0.2347 0.0148 -0.0136 0.0284 77 VAL A CG1
+635 C CG2 . VAL A 77 ? 0.1555 0.1939 0.2278 0.0143 -0.0166 0.0254 77 VAL A CG2
+636 N N . ILE A 78 ? 0.1447 0.1776 0.2457 0.0151 -0.0024 0.0296 78 ILE A N
+637 C CA . ILE A 78 ? 0.1458 0.1813 0.2595 0.0165 0.0018 0.0339 78 ILE A CA
+638 C C . ILE A 78 ? 0.1428 0.1822 0.2617 0.0169 0.0029 0.0366 78 ILE A C
+639 O O . ILE A 78 ? 0.1463 0.1887 0.2773 0.0181 0.0065 0.0414 78 ILE A O
+640 C CB . ILE A 78 ? 0.1617 0.1865 0.2757 0.0167 0.0081 0.0319 78 ILE A CB
+641 C CG1 . ILE A 78 ? 0.1846 0.1983 0.2883 0.0159 0.0119 0.0270 78 ILE A CG1
+642 C CG2 . ILE A 78 ? 0.1700 0.1918 0.2805 0.0156 0.0057 0.0305 78 ILE A CG2
+643 C CD1 . ILE A 78 ? 0.2057 0.2061 0.3078 0.0164 0.0196 0.0251 78 ILE A CD1
+644 N N . GLY A 79 ? 0.1401 0.1801 0.2510 0.0159 -0.0006 0.0346 79 GLY A N
+645 C CA . GLY A 79 ? 0.1374 0.1814 0.2527 0.0155 -0.0010 0.0377 79 GLY A CA
+646 C C . GLY A 79 ? 0.1422 0.1855 0.2460 0.0141 -0.0057 0.0345 79 GLY A C
+647 O O . GLY A 79 ? 0.1454 0.1836 0.2384 0.0138 -0.0065 0.0295 79 GLY A O
+648 N N . HIS A 80 ? 0.1366 0.1849 0.2427 0.0130 -0.0091 0.0379 80 HIS A N
+649 C CA . HIS A 80 ? 0.1385 0.1849 0.2335 0.0116 -0.0132 0.0350 80 HIS A CA
+650 C C . HIS A 80 ? 0.1440 0.1931 0.2443 0.0101 -0.0145 0.0390 80 HIS A C
+651 O O . HIS A 80 ? 0.1452 0.2003 0.2570 0.0095 -0.0151 0.0455 80 HIS A O
+652 C CB . HIS A 80 ? 0.1439 0.1924 0.2301 0.0114 -0.0188 0.0341 80 HIS A CB
+653 C CG . HIS A 80 ? 0.1623 0.2172 0.2534 0.0105 -0.0229 0.0397 80 HIS A CG
+654 N ND1 . HIS A 80 ? 0.1682 0.2281 0.2678 0.0115 -0.0222 0.0432 80 HIS A ND1
+655 C CD2 . HIS A 80 ? 0.1778 0.2344 0.2659 0.0082 -0.0280 0.0424 80 HIS A CD2
+656 C CE1 . HIS A 80 ? 0.1764 0.2412 0.2779 0.0098 -0.0268 0.0480 80 HIS A CE1
+657 N NE2 . HIS A 80 ? 0.1818 0.2442 0.2758 0.0076 -0.0306 0.0477 80 HIS A NE2
+658 N N . SER A 81 ? 0.1420 0.1870 0.2347 0.0092 -0.0151 0.0359 81 SER A N
+659 C CA . SER A 81 ? 0.1398 0.1873 0.2373 0.0074 -0.0171 0.0401 81 SER A CA
+660 C C . SER A 81 ? 0.1430 0.1863 0.2279 0.0059 -0.0208 0.0359 81 SER A C
+661 O O . SER A 81 ? 0.1548 0.1929 0.2294 0.0069 -0.0196 0.0299 81 SER A O
+662 C CB . SER A 81 ? 0.1600 0.2070 0.2686 0.0087 -0.0103 0.0429 81 SER A CB
+663 O OG . SER A 81 ? 0.2105 0.2497 0.3114 0.0102 -0.0053 0.0368 81 SER A OG
+664 N N A MET A 82 ? 0.1375 0.1829 0.2230 0.0032 -0.0258 0.0397 82 MET A N
+665 N N B MET A 82 ? 0.1341 0.1796 0.2199 0.0033 -0.0256 0.0397 82 MET A N
+666 C CA A MET A 82 ? 0.1484 0.1893 0.2223 0.0016 -0.0295 0.0362 82 MET A CA
+667 C CA B MET A 82 ? 0.1415 0.1826 0.2160 0.0016 -0.0294 0.0364 82 MET A CA
+668 C C A MET A 82 ? 0.1526 0.1934 0.2328 0.0010 -0.0272 0.0382 82 MET A C
+669 C C B MET A 82 ? 0.1480 0.1888 0.2288 0.0012 -0.0266 0.0382 82 MET A C
+670 O O A MET A 82 ? 0.1586 0.2045 0.2514 -0.0002 -0.0274 0.0453 82 MET A O
+671 O O B MET A 82 ? 0.1511 0.1969 0.2453 0.0005 -0.0257 0.0451 82 MET A O
+672 C CB A MET A 82 ? 0.1567 0.1980 0.2242 -0.0015 -0.0375 0.0388 82 MET A CB
+673 C CB B MET A 82 ? 0.1426 0.1844 0.2116 -0.0017 -0.0375 0.0395 82 MET A CB
+674 C CG A MET A 82 ? 0.1915 0.2267 0.2458 -0.0031 -0.0413 0.0351 82 MET A CG
+675 C CG B MET A 82 ? 0.1675 0.2033 0.2234 -0.0034 -0.0415 0.0359 82 MET A CG
+676 S SD A MET A 82 ? 0.2388 0.2711 0.2825 -0.0073 -0.0506 0.0379 82 MET A SD
+677 S SD B MET A 82 ? 0.1780 0.2095 0.2192 -0.0061 -0.0495 0.0362 82 MET A SD
+678 C CE A MET A 82 ? 0.2376 0.2679 0.2717 -0.0043 -0.0496 0.0344 82 MET A CE
+679 C CE B MET A 82 ? 0.1267 0.1648 0.1803 -0.0108 -0.0552 0.0463 82 MET A CE
+680 N N . GLN A 83 ? 0.1542 0.1897 0.2265 0.0019 -0.0248 0.0327 83 GLN A N
+681 C CA . GLN A 83 ? 0.1533 0.1881 0.2299 0.0016 -0.0223 0.0341 83 GLN A CA
+682 C C . GLN A 83 ? 0.1433 0.1744 0.2080 -0.0004 -0.0275 0.0308 83 GLN A C
+683 O O . GLN A 83 ? 0.1526 0.1789 0.2062 0.0006 -0.0269 0.0245 83 GLN A O
+684 C CB . GLN A 83 ? 0.1894 0.2200 0.2662 0.0045 -0.0140 0.0304 83 GLN A CB
+685 C CG . GLN A 83 ? 0.2466 0.2763 0.3275 0.0046 -0.0109 0.0324 83 GLN A CG
+686 C CD . GLN A 83 ? 0.3106 0.3341 0.3886 0.0072 -0.0026 0.0284 83 GLN A CD
+687 O OE1 . GLN A 83 ? 0.3192 0.3381 0.3906 0.0083 0.0001 0.0235 83 GLN A OE1
+688 N NE2 . GLN A 83 ? 0.3279 0.3504 0.4102 0.0079 0.0015 0.0307 83 GLN A NE2
+689 N N . ASN A 84 ? 0.1329 0.1659 0.1999 -0.0036 -0.0333 0.0354 84 ASN A N
+690 C CA . ASN A 84 ? 0.1351 0.1634 0.1902 -0.0059 -0.0388 0.0327 84 ASN A CA
+691 C C . ASN A 84 ? 0.1344 0.1580 0.1748 -0.0053 -0.0415 0.0273 84 ASN A C
+692 O O . ASN A 84 ? 0.1453 0.1703 0.1853 -0.0060 -0.0442 0.0295 84 ASN A O
+693 C CB . ASN A 84 ? 0.1455 0.1714 0.1997 -0.0050 -0.0352 0.0300 84 ASN A CB
+694 C CG . ASN A 84 ? 0.1817 0.2124 0.2509 -0.0050 -0.0321 0.0365 84 ASN A CG
+695 O OD1 . ASN A 84 ? 0.1987 0.2336 0.2761 -0.0080 -0.0368 0.0437 84 ASN A OD1
+696 N ND2 . ASN A 84 ? 0.1855 0.2154 0.2584 -0.0019 -0.0241 0.0348 84 ASN A ND2
+697 N N . CYS A 85 ? 0.1317 0.1500 0.1611 -0.0038 -0.0400 0.0211 85 CYS A N
+698 C CA . CYS A 85 ? 0.1382 0.1524 0.1553 -0.0026 -0.0414 0.0172 85 CYS A CA
+699 C C . CYS A 85 ? 0.1403 0.1555 0.1577 0.0007 -0.0364 0.0141 85 CYS A C
+700 O O . CYS A 85 ? 0.1484 0.1605 0.1564 0.0022 -0.0366 0.0113 85 CYS A O
+701 C CB . CYS A 85 ? 0.1510 0.1586 0.1558 -0.0033 -0.0439 0.0138 85 CYS A CB
+702 S SG . CYS A 85 ? 0.1812 0.1858 0.1834 -0.0081 -0.0513 0.0176 85 CYS A SG
+703 N N . VAL A 86 ? 0.1354 0.1543 0.1631 0.0017 -0.0318 0.0152 86 VAL A N
+704 C CA A VAL A 86 ? 0.1452 0.1642 0.1728 0.0040 -0.0279 0.0128 86 VAL A CA
+705 C CA B VAL A 86 ? 0.1442 0.1632 0.1719 0.0040 -0.0279 0.0127 86 VAL A CA
+706 C C . VAL A 86 ? 0.1483 0.1718 0.1854 0.0047 -0.0267 0.0163 86 VAL A C
+707 O O . VAL A 86 ? 0.1515 0.1785 0.1978 0.0036 -0.0272 0.0209 86 VAL A O
+708 C CB A VAL A 86 ? 0.1624 0.1787 0.1895 0.0047 -0.0232 0.0093 86 VAL A CB
+709 C CB B VAL A 86 ? 0.1550 0.1713 0.1828 0.0044 -0.0232 0.0096 86 VAL A CB
+710 C CG1 A VAL A 86 ? 0.1797 0.1922 0.1975 0.0041 -0.0245 0.0060 86 VAL A CG1
+711 C CG1 B VAL A 86 ? 0.1607 0.1764 0.1916 0.0057 -0.0188 0.0085 86 VAL A CG1
+712 C CG2 A VAL A 86 ? 0.1683 0.1855 0.2049 0.0046 -0.0191 0.0115 86 VAL A CG2
+713 C CG2 B VAL A 86 ? 0.1676 0.1800 0.1849 0.0042 -0.0245 0.0058 86 VAL A CG2
+714 N N . LEU A 87 ? 0.1444 0.1682 0.1797 0.0063 -0.0256 0.0150 87 LEU A N
+715 C CA . LEU A 87 ? 0.1464 0.1742 0.1906 0.0072 -0.0239 0.0179 87 LEU A CA
+716 C C . LEU A 87 ? 0.1383 0.1635 0.1851 0.0082 -0.0185 0.0155 87 LEU A C
+717 O O . LEU A 87 ? 0.1425 0.1635 0.1819 0.0082 -0.0176 0.0116 87 LEU A O
+718 C CB . LEU A 87 ? 0.1632 0.1927 0.2037 0.0084 -0.0262 0.0185 87 LEU A CB
+719 C CG . LEU A 87 ? 0.1963 0.2262 0.2314 0.0075 -0.0312 0.0207 87 LEU A CG
+720 C CD1 . LEU A 87 ? 0.2043 0.2347 0.2342 0.0095 -0.0320 0.0209 87 LEU A CD1
+721 C CD2 . LEU A 87 ? 0.2162 0.2502 0.2602 0.0053 -0.0333 0.0259 87 LEU A CD2
+722 N N . LYS A 88 ? 0.1328 0.1598 0.1898 0.0087 -0.0150 0.0182 88 LYS A N
+723 C CA . LYS A 88 ? 0.1334 0.1560 0.1921 0.0095 -0.0095 0.0163 88 LYS A CA
+724 C C . LYS A 88 ? 0.1333 0.1590 0.1978 0.0105 -0.0093 0.0185 88 LYS A C
+725 O O . LYS A 88 ? 0.1402 0.1711 0.2146 0.0109 -0.0093 0.0232 88 LYS A O
+726 C CB . LYS A 88 ? 0.1473 0.1683 0.2136 0.0100 -0.0042 0.0184 88 LYS A CB
+727 C CG . LYS A 88 ? 0.2015 0.2189 0.2621 0.0092 -0.0036 0.0161 88 LYS A CG
+728 C CD . LYS A 88 ? 0.2553 0.2703 0.3230 0.0103 0.0028 0.0185 88 LYS A CD
+729 C CE . LYS A 88 ? 0.3066 0.3292 0.3880 0.0106 0.0021 0.0258 88 LYS A CE
+730 N NZ . LYS A 88 ? 0.3299 0.3515 0.4180 0.0116 0.0074 0.0291 88 LYS A NZ
+731 N N . LEU A 89 ? 0.1301 0.1534 0.1893 0.0106 -0.0097 0.0159 89 LEU A N
+732 C CA . LEU A 89 ? 0.1294 0.1554 0.1937 0.0114 -0.0098 0.0179 89 LEU A CA
+733 C C . LEU A 89 ? 0.1356 0.1549 0.2012 0.0113 -0.0048 0.0163 89 LEU A C
+734 O O . LEU A 89 ? 0.1483 0.1607 0.2054 0.0100 -0.0042 0.0125 89 LEU A O
+735 C CB . LEU A 89 ? 0.1331 0.1607 0.1908 0.0116 -0.0137 0.0171 89 LEU A CB
+736 C CG . LEU A 89 ? 0.1403 0.1710 0.1923 0.0120 -0.0178 0.0176 89 LEU A CG
+737 C CD1 . LEU A 89 ? 0.1515 0.1830 0.1976 0.0129 -0.0200 0.0174 89 LEU A CD1
+738 C CD2 . LEU A 89 ? 0.1466 0.1827 0.2044 0.0123 -0.0197 0.0217 89 LEU A CD2
+739 N N . LYS A 90 ? 0.1274 0.1477 0.2030 0.0124 -0.0010 0.0194 90 LYS A N
+740 C CA . LYS A 90 ? 0.1365 0.1485 0.2125 0.0126 0.0046 0.0179 90 LYS A CA
+741 C C . LYS A 90 ? 0.1366 0.1485 0.2118 0.0120 0.0022 0.0178 90 LYS A C
+742 O O . LYS A 90 ? 0.1371 0.1575 0.2191 0.0129 -0.0008 0.0213 90 LYS A O
+743 C CB . LYS A 90 ? 0.1591 0.1726 0.2476 0.0146 0.0101 0.0223 90 LYS A CB
+744 C CG . LYS A 90 ? 0.2237 0.2255 0.3100 0.0152 0.0174 0.0202 90 LYS A CG
+745 C CD . LYS A 90 ? 0.3041 0.3069 0.4037 0.0179 0.0242 0.0252 90 LYS A CD
+746 C CE . LYS A 90 ? 0.3769 0.3655 0.4717 0.0188 0.0320 0.0225 90 LYS A CE
+747 N NZ . LYS A 90 ? 0.4068 0.3943 0.5138 0.0222 0.0407 0.0276 90 LYS A NZ
+748 N N . VAL A 91 ? 0.1419 0.1445 0.2081 0.0102 0.0029 0.0140 91 VAL A N
+749 C CA . VAL A 91 ? 0.1498 0.1516 0.2152 0.0089 0.0001 0.0144 91 VAL A CA
+750 C C . VAL A 91 ? 0.1577 0.1489 0.2230 0.0084 0.0052 0.0133 91 VAL A C
+751 O O . VAL A 91 ? 0.1654 0.1478 0.2276 0.0088 0.0111 0.0113 91 VAL A O
+752 C CB . VAL A 91 ? 0.1528 0.1533 0.2083 0.0064 -0.0051 0.0124 91 VAL A CB
+753 C CG1 . VAL A 91 ? 0.1531 0.1640 0.2097 0.0079 -0.0093 0.0143 91 VAL A CG1
+754 C CG2 . VAL A 91 ? 0.1613 0.1508 0.2049 0.0039 -0.0033 0.0078 91 VAL A CG2
+755 N N . ASP A 92 ? 0.1643 0.1553 0.2322 0.0075 0.0033 0.0149 92 ASP A N
+756 C CA . ASP A 92 ? 0.1792 0.1588 0.2466 0.0069 0.0081 0.0140 92 ASP A CA
+757 C C . ASP A 92 ? 0.1994 0.1631 0.2511 0.0028 0.0081 0.0092 92 ASP A C
+758 O O . ASP A 92 ? 0.2231 0.1741 0.2708 0.0018 0.0121 0.0077 92 ASP A O
+759 C CB . ASP A 92 ? 0.1931 0.1787 0.2710 0.0077 0.0064 0.0181 92 ASP A CB
+760 C CG . ASP A 92 ? 0.2553 0.2417 0.3296 0.0047 -0.0003 0.0188 92 ASP A CG
+761 O OD1 . ASP A 92 ? 0.2611 0.2460 0.3260 0.0022 -0.0045 0.0169 92 ASP A OD1
+762 O OD2 . ASP A 92 ? 0.2915 0.2806 0.3734 0.0049 -0.0014 0.0220 92 ASP A OD2
+763 N N . THR A 93 ? 0.1939 0.1574 0.2361 0.0001 0.0033 0.0071 93 THR A N
+764 C CA . THR A 93 ? 0.2104 0.1596 0.2373 -0.0047 0.0018 0.0033 93 THR A CA
+765 C C . THR A 93 ? 0.2101 0.1555 0.2272 -0.0055 0.0029 -0.0002 93 THR A C
+766 O O . THR A 93 ? 0.2088 0.1651 0.2291 -0.0043 -0.0001 0.0009 93 THR A O
+767 C CB . THR A 93 ? 0.2348 0.1888 0.2611 -0.0082 -0.0067 0.0059 93 THR A CB
+768 O OG1 . THR A 93 ? 0.2512 0.2085 0.2869 -0.0075 -0.0075 0.0093 93 THR A OG1
+769 C CG2 . THR A 93 ? 0.2512 0.1918 0.2621 -0.0145 -0.0103 0.0033 93 THR A CG2
+770 N N . ALA A 94 ? 0.2136 0.1424 0.2181 -0.0075 0.0076 -0.0044 94 ALA A N
+771 C CA . ALA A 94 ? 0.2209 0.1446 0.2147 -0.0087 0.0087 -0.0077 94 ALA A CA
+772 C C . ALA A 94 ? 0.2124 0.1362 0.1976 -0.0140 0.0003 -0.0079 94 ALA A C
+773 O O . ALA A 94 ? 0.2162 0.1342 0.1968 -0.0183 -0.0041 -0.0072 94 ALA A O
+774 C CB . ALA A 94 ? 0.2408 0.1451 0.2218 -0.0095 0.0164 -0.0119 94 ALA A CB
+775 N N . ASN A 95 ? 0.1950 0.1255 0.1786 -0.0141 -0.0022 -0.0083 95 ASN A N
+776 C CA . ASN A 95 ? 0.1934 0.1243 0.1698 -0.0190 -0.0096 -0.0076 95 ASN A CA
+777 C C . ASN A 95 ? 0.2259 0.1381 0.1848 -0.0249 -0.0097 -0.0111 95 ASN A C
+778 O O . ASN A 95 ? 0.2395 0.1421 0.1889 -0.0248 -0.0045 -0.0150 95 ASN A O
+779 C CB . ASN A 95 ? 0.1754 0.1158 0.1533 -0.0175 -0.0111 -0.0075 95 ASN A CB
+780 C CG . ASN A 95 ? 0.1885 0.1314 0.1617 -0.0219 -0.0184 -0.0054 95 ASN A CG
+781 O OD1 . ASN A 95 ? 0.1915 0.1291 0.1601 -0.0268 -0.0232 -0.0037 95 ASN A OD1
+782 N ND2 . ASN A 95 ? 0.1933 0.1446 0.1685 -0.0204 -0.0197 -0.0048 95 ASN A ND2
+783 N N . PRO A 96 ? 0.2378 0.1442 0.1916 -0.0304 -0.0156 -0.0095 96 PRO A N
+784 C CA . PRO A 96 ? 0.2611 0.1476 0.1956 -0.0371 -0.0165 -0.0128 96 PRO A CA
+785 C C . PRO A 96 ? 0.2771 0.1609 0.2007 -0.0411 -0.0196 -0.0140 96 PRO A C
+786 O O . PRO A 96 ? 0.3125 0.1787 0.2182 -0.0458 -0.0185 -0.0178 96 PRO A O
+787 C CB . PRO A 96 ? 0.2739 0.1579 0.2084 -0.0424 -0.0239 -0.0091 96 PRO A CB
+788 C CG . PRO A 96 ? 0.2656 0.1705 0.2179 -0.0394 -0.0285 -0.0032 96 PRO A CG
+789 C CD . PRO A 96 ? 0.2328 0.1500 0.1975 -0.0311 -0.0220 -0.0040 96 PRO A CD
+790 N N A LYS A 97 ? 0.2603 0.1608 0.1938 -0.0391 -0.0232 -0.0109 97 LYS A N
+791 N N B LYS A 97 ? 0.2564 0.1568 0.1898 -0.0392 -0.0232 -0.0109 97 LYS A N
+792 C CA A LYS A 97 ? 0.2636 0.1643 0.1896 -0.0422 -0.0261 -0.0113 97 LYS A CA
+793 C CA B LYS A 97 ? 0.2560 0.1561 0.1815 -0.0424 -0.0262 -0.0113 97 LYS A CA
+794 C C A LYS A 97 ? 0.2614 0.1653 0.1889 -0.0368 -0.0193 -0.0146 97 LYS A C
+795 C C B LYS A 97 ? 0.2585 0.1605 0.1841 -0.0374 -0.0192 -0.0149 97 LYS A C
+796 O O A LYS A 97 ? 0.2606 0.1709 0.1879 -0.0373 -0.0216 -0.0138 97 LYS A O
+797 O O B LYS A 97 ? 0.2598 0.1652 0.1823 -0.0387 -0.0213 -0.0148 97 LYS A O
+798 C CB A LYS A 97 ? 0.2736 0.1897 0.2095 -0.0434 -0.0339 -0.0050 97 LYS A CB
+799 C CB B LYS A 97 ? 0.2533 0.1698 0.1896 -0.0431 -0.0337 -0.0051 97 LYS A CB
+800 C CG A LYS A 97 ? 0.3212 0.2347 0.2559 -0.0497 -0.0418 -0.0003 97 LYS A CG
+801 C CG B LYS A 97 ? 0.2776 0.1946 0.2165 -0.0478 -0.0409 0.0002 97 LYS A CG
+802 C CD A LYS A 97 ? 0.3618 0.2900 0.3060 -0.0508 -0.0487 0.0069 97 LYS A CD
+803 C CD B LYS A 97 ? 0.2981 0.2314 0.2485 -0.0476 -0.0472 0.0074 97 LYS A CD
+804 C CE A LYS A 97 ? 0.4069 0.3352 0.3536 -0.0564 -0.0565 0.0134 97 LYS A CE
+805 C CE B LYS A 97 ? 0.3308 0.2666 0.2870 -0.0513 -0.0538 0.0139 97 LYS A CE
+806 N NZ A LYS A 97 ? 0.4286 0.3624 0.3867 -0.0522 -0.0549 0.0151 97 LYS A NZ
+807 N NZ B LYS A 97 ? 0.3407 0.2934 0.3103 -0.0497 -0.0582 0.0220 97 LYS A NZ
+808 N N . THR A 98 ? 0.2547 0.1549 0.1848 -0.0317 -0.0110 -0.0174 98 THR A N
+809 C CA . THR A 98 ? 0.2542 0.1576 0.1867 -0.0270 -0.0048 -0.0195 98 THR A CA
+810 C C . THR A 98 ? 0.2842 0.1736 0.1997 -0.0305 -0.0026 -0.0232 98 THR A C
+811 O O . THR A 98 ? 0.3148 0.1866 0.2165 -0.0332 0.0009 -0.0263 98 THR A O
+812 C CB . THR A 98 ? 0.2523 0.1549 0.1925 -0.0210 0.0037 -0.0202 98 THR A CB
+813 O OG1 . THR A 98 ? 0.2326 0.1476 0.1878 -0.0181 0.0015 -0.0166 98 THR A OG1
+814 C CG2 . THR A 98 ? 0.2558 0.1638 0.2009 -0.0164 0.0090 -0.0207 98 THR A CG2
+815 N N . PRO A 99 ? 0.2825 0.1788 0.1980 -0.0308 -0.0048 -0.0229 99 PRO A N
+816 C CA . PRO A 99 ? 0.2921 0.1759 0.1916 -0.0340 -0.0026 -0.0262 99 PRO A CA
+817 C C . PRO A 99 ? 0.3000 0.1796 0.2001 -0.0284 0.0075 -0.0286 99 PRO A C
+818 O O . PRO A 99 ? 0.2949 0.1834 0.2093 -0.0225 0.0117 -0.0271 99 PRO A O
+819 C CB . PRO A 99 ? 0.2916 0.1876 0.1950 -0.0354 -0.0086 -0.0239 99 PRO A CB
+820 C CG . PRO A 99 ? 0.2906 0.2044 0.2130 -0.0291 -0.0083 -0.0211 99 PRO A CG
+821 C CD . PRO A 99 ? 0.2660 0.1807 0.1953 -0.0276 -0.0083 -0.0197 99 PRO A CD
+822 N N . LYS A 100 ? 0.3110 0.1775 0.1960 -0.0303 0.0116 -0.0318 100 LYS A N
+823 C CA . LYS A 100 ? 0.3088 0.1736 0.1961 -0.0246 0.0211 -0.0328 100 LYS A CA
+824 C C . LYS A 100 ? 0.2847 0.1688 0.1873 -0.0214 0.0182 -0.0300 100 LYS A C
+825 O O . LYS A 100 ? 0.2856 0.1769 0.1878 -0.0249 0.0106 -0.0290 100 LYS A O
+826 C CB . LYS A 100 ? 0.3518 0.2000 0.2196 -0.0274 0.0254 -0.0363 100 LYS A CB
+827 C CG . LYS A 100 ? 0.4294 0.2549 0.2793 -0.0297 0.0305 -0.0396 100 LYS A CG
+828 C CD . LYS A 100 ? 0.5093 0.3170 0.3371 -0.0332 0.0340 -0.0431 100 LYS A CD
+829 C CE . LYS A 100 ? 0.5777 0.3601 0.3843 -0.0365 0.0383 -0.0468 100 LYS A CE
+830 N NZ . LYS A 100 ? 0.6311 0.3946 0.4134 -0.0404 0.0413 -0.0503 100 LYS A NZ
+831 N N . TYR A 101 ? 0.2722 0.1649 0.1891 -0.0152 0.0233 -0.0279 101 TYR A N
+832 C CA . TYR A 101 ? 0.2629 0.1725 0.1935 -0.0127 0.0198 -0.0252 101 TYR A CA
+833 C C . TYR A 101 ? 0.2697 0.1834 0.2099 -0.0073 0.0267 -0.0232 101 TYR A C
+834 O O . TYR A 101 ? 0.2816 0.1879 0.2224 -0.0042 0.0348 -0.0229 101 TYR A O
+835 C CB . TYR A 101 ? 0.2444 0.1674 0.1873 -0.0121 0.0131 -0.0225 101 TYR A CB
+836 C CG . TYR A 101 ? 0.2390 0.1652 0.1934 -0.0080 0.0170 -0.0204 101 TYR A CG
+837 C CD1 . TYR A 101 ? 0.2457 0.1632 0.1967 -0.0088 0.0191 -0.0212 101 TYR A CD1
+838 C CD2 . TYR A 101 ? 0.2376 0.1754 0.2064 -0.0037 0.0181 -0.0172 101 TYR A CD2
+839 C CE1 . TYR A 101 ? 0.2546 0.1755 0.2170 -0.0049 0.0228 -0.0188 101 TYR A CE1
+840 C CE2 . TYR A 101 ? 0.2398 0.1813 0.2199 -0.0003 0.0212 -0.0144 101 TYR A CE2
+841 C CZ . TYR A 101 ? 0.2577 0.1913 0.2351 -0.0008 0.0236 -0.0152 101 TYR A CZ
+842 O OH . TYR A 101 ? 0.2740 0.2112 0.2629 0.0025 0.0269 -0.0122 101 TYR A OH
+843 N N . LYS A 102 ? 0.2583 0.1839 0.2065 -0.0062 0.0232 -0.0213 102 LYS A N
+844 C CA . LYS A 102 ? 0.2549 0.1875 0.2147 -0.0018 0.0273 -0.0181 102 LYS A CA
+845 C C . LYS A 102 ? 0.2427 0.1902 0.2135 -0.0015 0.0200 -0.0157 102 LYS A C
+846 O O . LYS A 102 ? 0.2472 0.1982 0.2143 -0.0044 0.0132 -0.0169 102 LYS A O
+847 C CB . LYS A 102 ? 0.2879 0.2152 0.2405 -0.0019 0.0314 -0.0190 102 LYS A CB
+848 C CG . LYS A 102 ? 0.3730 0.2843 0.3144 -0.0009 0.0408 -0.0209 102 LYS A CG
+849 C CD . LYS A 102 ? 0.4398 0.3464 0.3730 -0.0013 0.0439 -0.0217 102 LYS A CD
+850 C CE . LYS A 102 ? 0.5043 0.3923 0.4223 -0.0008 0.0534 -0.0241 102 LYS A CE
+851 N NZ . LYS A 102 ? 0.5466 0.4297 0.4550 -0.0015 0.0561 -0.0250 102 LYS A NZ
+852 N N . PHE A 103 ? 0.2279 0.1836 0.2119 0.0018 0.0214 -0.0118 103 PHE A N
+853 C CA . PHE A 103 ? 0.2188 0.1863 0.2111 0.0019 0.0147 -0.0095 103 PHE A CA
+854 C C . PHE A 103 ? 0.2271 0.1966 0.2214 0.0025 0.0161 -0.0080 103 PHE A C
+855 O O . PHE A 103 ? 0.2426 0.2103 0.2420 0.0050 0.0225 -0.0052 103 PHE A O
+856 C CB . PHE A 103 ? 0.2052 0.1803 0.2106 0.0041 0.0140 -0.0053 103 PHE A CB
+857 C CG . PHE A 103 ? 0.1993 0.1748 0.2051 0.0038 0.0119 -0.0060 103 PHE A CG
+858 C CD1 . PHE A 103 ? 0.2018 0.1733 0.1978 0.0012 0.0087 -0.0095 103 PHE A CD1
+859 C CD2 . PHE A 103 ? 0.1970 0.1780 0.2139 0.0057 0.0123 -0.0022 103 PHE A CD2
+860 C CE1 . PHE A 103 ? 0.2043 0.1770 0.2018 0.0010 0.0065 -0.0093 103 PHE A CE1
+861 C CE2 . PHE A 103 ? 0.1998 0.1817 0.2174 0.0055 0.0102 -0.0025 103 PHE A CE2
+862 C CZ . PHE A 103 ? 0.2000 0.1780 0.2082 0.0033 0.0073 -0.0060 103 PHE A CZ
+863 N N . VAL A 104 ? 0.2197 0.1924 0.2100 0.0005 0.0107 -0.0093 104 VAL A N
+864 C CA . VAL A 104 ? 0.2324 0.2076 0.2249 0.0008 0.0110 -0.0077 104 VAL A CA
+865 C C . VAL A 104 ? 0.2271 0.2109 0.2250 0.0002 0.0039 -0.0060 104 VAL A C
+866 O O . VAL A 104 ? 0.2392 0.2249 0.2341 -0.0010 -0.0012 -0.0076 104 VAL A O
+867 C CB . VAL A 104 ? 0.2641 0.2325 0.2449 -0.0012 0.0127 -0.0110 104 VAL A CB
+868 C CG1 . VAL A 104 ? 0.2834 0.2403 0.2554 -0.0011 0.0197 -0.0131 104 VAL A CG1
+869 C CG2 . VAL A 104 ? 0.2852 0.2550 0.2590 -0.0044 0.0060 -0.0136 104 VAL A CG2
+870 N N . ARG A 105 ? 0.2023 0.1904 0.2078 0.0010 0.0037 -0.0024 105 ARG A N
+871 C CA . ARG A 105 ? 0.1946 0.1886 0.2031 -0.0001 -0.0031 -0.0009 105 ARG A CA
+872 C C . ARG A 105 ? 0.2048 0.1975 0.2081 -0.0013 -0.0037 -0.0024 105 ARG A C
+873 O O . ARG A 105 ? 0.2089 0.2009 0.2150 -0.0006 0.0004 -0.0004 105 ARG A O
+874 C CB . ARG A 105 ? 0.1910 0.1905 0.2118 0.0007 -0.0042 0.0050 105 ARG A CB
+875 C CG . ARG A 105 ? 0.1958 0.1989 0.2171 -0.0012 -0.0119 0.0062 105 ARG A CG
+876 C CD . ARG A 105 ? 0.1972 0.2054 0.2298 -0.0016 -0.0147 0.0126 105 ARG A CD
+877 N NE . ARG A 105 ? 0.1998 0.2089 0.2299 -0.0042 -0.0226 0.0133 105 ARG A NE
+878 C CZ . ARG A 105 ? 0.2140 0.2221 0.2387 -0.0051 -0.0276 0.0117 105 ARG A CZ
+879 N NH1 . ARG A 105 ? 0.1863 0.1938 0.2090 -0.0038 -0.0257 0.0096 105 ARG A NH1
+880 N NH2 . ARG A 105 ? 0.2021 0.2088 0.2227 -0.0074 -0.0342 0.0122 105 ARG A NH2
+881 N N . ILE A 106 ? 0.2107 0.2033 0.2069 -0.0030 -0.0083 -0.0053 106 ILE A N
+882 C CA . ILE A 106 ? 0.2279 0.2195 0.2192 -0.0043 -0.0089 -0.0066 106 ILE A CA
+883 C C . ILE A 106 ? 0.2356 0.2311 0.2318 -0.0047 -0.0128 -0.0040 106 ILE A C
+884 O O . ILE A 106 ? 0.2320 0.2302 0.2331 -0.0046 -0.0166 -0.0018 106 ILE A O
+885 C CB . ILE A 106 ? 0.2423 0.2319 0.2246 -0.0060 -0.0113 -0.0099 106 ILE A CB
+886 C CG1 . ILE A 106 ? 0.2423 0.2345 0.2247 -0.0057 -0.0162 -0.0099 106 ILE A CG1
+887 C CG2 . ILE A 106 ? 0.2585 0.2427 0.2345 -0.0068 -0.0076 -0.0122 106 ILE A CG2
+888 C CD1 . ILE A 106 ? 0.2607 0.2523 0.2368 -0.0069 -0.0185 -0.0114 106 ILE A CD1
+889 N N . GLN A 107 ? 0.2470 0.2421 0.2414 -0.0055 -0.0122 -0.0041 107 GLN A N
+890 C CA . GLN A 107 ? 0.2511 0.2492 0.2493 -0.0062 -0.0161 -0.0018 107 GLN A CA
+891 C C . GLN A 107 ? 0.2377 0.2349 0.2291 -0.0075 -0.0206 -0.0044 107 GLN A C
+892 O O . GLN A 107 ? 0.2268 0.2221 0.2116 -0.0080 -0.0196 -0.0072 107 GLN A O
+893 C CB . GLN A 107 ? 0.2947 0.2930 0.2949 -0.0061 -0.0123 -0.0001 107 GLN A CB
+894 C CG . GLN A 107 ? 0.3689 0.3673 0.3760 -0.0041 -0.0061 0.0033 107 GLN A CG
+895 C CD . GLN A 107 ? 0.4527 0.4559 0.4716 -0.0036 -0.0086 0.0088 107 GLN A CD
+896 O OE1 . GLN A 107 ? 0.4809 0.4869 0.5026 -0.0053 -0.0152 0.0106 107 GLN A OE1
+897 N NE2 . GLN A 107 ? 0.4710 0.4747 0.4969 -0.0014 -0.0034 0.0122 107 GLN A NE2
+898 N N . PRO A 108 ? 0.2328 0.2308 0.2256 -0.0082 -0.0254 -0.0030 108 PRO A N
+899 C CA . PRO A 108 ? 0.2328 0.2291 0.2193 -0.0088 -0.0285 -0.0051 108 PRO A CA
+900 C C . PRO A 108 ? 0.2246 0.2212 0.2084 -0.0096 -0.0261 -0.0061 108 PRO A C
+901 O O . PRO A 108 ? 0.2289 0.2269 0.2161 -0.0099 -0.0235 -0.0046 108 PRO A O
+902 C CB . PRO A 108 ? 0.2553 0.2507 0.2435 -0.0098 -0.0334 -0.0030 108 PRO A CB
+903 C CG . PRO A 108 ? 0.2711 0.2697 0.2685 -0.0102 -0.0330 0.0010 108 PRO A CG
+904 C CD . PRO A 108 ? 0.2406 0.2406 0.2409 -0.0088 -0.0284 0.0011 108 PRO A CD
+905 N N . GLY A 109 ? 0.2113 0.2069 0.1895 -0.0099 -0.0266 -0.0079 109 GLY A N
+906 C CA . GLY A 109 ? 0.2149 0.2110 0.1901 -0.0113 -0.0251 -0.0083 109 GLY A CA
+907 C C . GLY A 109 ? 0.2262 0.2210 0.1971 -0.0123 -0.0223 -0.0097 109 GLY A C
+908 O O . GLY A 109 ? 0.2460 0.2407 0.2128 -0.0141 -0.0223 -0.0099 109 GLY A O
+909 N N A GLN A 110 ? 0.2239 0.2173 0.1955 -0.0114 -0.0202 -0.0104 110 GLN A N
+910 N N B GLN A 110 ? 0.2164 0.2097 0.1880 -0.0114 -0.0201 -0.0104 110 GLN A N
+911 C CA A GLN A 110 ? 0.2291 0.2196 0.1955 -0.0126 -0.0179 -0.0118 110 GLN A CA
+912 C CA B GLN A 110 ? 0.2150 0.2054 0.1816 -0.0125 -0.0177 -0.0118 110 GLN A CA
+913 C C A GLN A 110 ? 0.2190 0.2100 0.1832 -0.0129 -0.0203 -0.0120 110 GLN A C
+914 C C B GLN A 110 ? 0.2140 0.2049 0.1782 -0.0129 -0.0202 -0.0120 110 GLN A C
+915 O O A GLN A 110 ? 0.2176 0.2103 0.1844 -0.0110 -0.0224 -0.0114 110 GLN A O
+916 O O B GLN A 110 ? 0.2136 0.2063 0.1806 -0.0110 -0.0223 -0.0114 110 GLN A O
+917 C CB A GLN A 110 ? 0.2570 0.2450 0.2251 -0.0114 -0.0138 -0.0121 110 GLN A CB
+918 C CB B GLN A 110 ? 0.2230 0.2113 0.1920 -0.0111 -0.0139 -0.0120 110 GLN A CB
+919 C CG A GLN A 110 ? 0.3110 0.2983 0.2815 -0.0108 -0.0101 -0.0110 110 GLN A CG
+920 C CG B GLN A 110 ? 0.2436 0.2268 0.2063 -0.0123 -0.0112 -0.0138 110 GLN A CG
+921 C CD A GLN A 110 ? 0.4009 0.3852 0.3643 -0.0131 -0.0084 -0.0118 110 GLN A CD
+922 C CD B GLN A 110 ? 0.2659 0.2445 0.2201 -0.0152 -0.0094 -0.0149 110 GLN A CD
+923 O OE1 A GLN A 110 ? 0.4405 0.4194 0.3954 -0.0150 -0.0065 -0.0137 110 GLN A OE1
+924 O OE1 B GLN A 110 ? 0.2822 0.2600 0.2362 -0.0150 -0.0068 -0.0144 110 GLN A OE1
+925 N NE2 A GLN A 110 ? 0.4069 0.3944 0.3730 -0.0133 -0.0095 -0.0103 110 GLN A NE2
+926 N NE2 B GLN A 110 ? 0.2433 0.2187 0.1903 -0.0181 -0.0110 -0.0158 110 GLN A NE2
+927 N N . THR A 111 ? 0.2128 0.2018 0.1715 -0.0155 -0.0202 -0.0122 111 THR A N
+928 C CA . THR A 111 ? 0.2075 0.1977 0.1651 -0.0162 -0.0225 -0.0111 111 THR A CA
+929 C C . THR A 111 ? 0.2020 0.1891 0.1577 -0.0166 -0.0214 -0.0120 111 THR A C
+930 O O . THR A 111 ? 0.2183 0.2012 0.1718 -0.0169 -0.0183 -0.0138 111 THR A O
+931 C CB . THR A 111 ? 0.2156 0.2063 0.1695 -0.0197 -0.0243 -0.0094 111 THR A CB
+932 O OG1 . THR A 111 ? 0.2302 0.2157 0.1773 -0.0229 -0.0226 -0.0109 111 THR A OG1
+933 C CG2 . THR A 111 ? 0.2132 0.2071 0.1698 -0.0190 -0.0254 -0.0081 111 THR A CG2
+934 N N . PHE A 112 ? 0.1891 0.1782 0.1460 -0.0163 -0.0234 -0.0104 112 PHE A N
+935 C CA . PHE A 112 ? 0.1846 0.1713 0.1403 -0.0170 -0.0231 -0.0107 112 PHE A CA
+936 C C . PHE A 112 ? 0.1805 0.1706 0.1378 -0.0175 -0.0261 -0.0074 112 PHE A C
+937 O O . PHE A 112 ? 0.1779 0.1722 0.1383 -0.0158 -0.0274 -0.0050 112 PHE A O
+938 C CB . PHE A 112 ? 0.1862 0.1730 0.1462 -0.0136 -0.0210 -0.0121 112 PHE A CB
+939 C CG . PHE A 112 ? 0.1824 0.1736 0.1476 -0.0101 -0.0224 -0.0109 112 PHE A CG
+940 C CD1 . PHE A 112 ? 0.1942 0.1864 0.1613 -0.0087 -0.0225 -0.0112 112 PHE A CD1
+941 C CD2 . PHE A 112 ? 0.1852 0.1784 0.1524 -0.0084 -0.0236 -0.0094 112 PHE A CD2
+942 C CE1 . PHE A 112 ? 0.2015 0.1953 0.1709 -0.0061 -0.0241 -0.0105 112 PHE A CE1
+943 C CE2 . PHE A 112 ? 0.1897 0.1848 0.1592 -0.0052 -0.0244 -0.0086 112 PHE A CE2
+944 C CZ . PHE A 112 ? 0.1967 0.1914 0.1664 -0.0043 -0.0248 -0.0094 112 PHE A CZ
+945 N N . SER A 113 ? 0.1742 0.1622 0.1298 -0.0194 -0.0268 -0.0068 113 SER A N
+946 C CA . SER A 113 ? 0.1744 0.1662 0.1331 -0.0198 -0.0296 -0.0025 113 SER A CA
+947 C C . SER A 113 ? 0.1779 0.1720 0.1416 -0.0156 -0.0286 -0.0023 113 SER A C
+948 O O . SER A 113 ? 0.1868 0.1781 0.1502 -0.0147 -0.0266 -0.0053 113 SER A O
+949 C CB . SER A 113 ? 0.1853 0.1730 0.1390 -0.0252 -0.0320 -0.0012 113 SER A CB
+950 O OG . SER A 113 ? 0.2038 0.1885 0.1513 -0.0296 -0.0333 -0.0013 113 SER A OG
+951 N N . VAL A 114 ? 0.1666 0.1656 0.1348 -0.0132 -0.0296 0.0016 114 VAL A N
+952 C CA . VAL A 114 ? 0.1711 0.1722 0.1433 -0.0093 -0.0287 0.0025 114 VAL A CA
+953 C C . VAL A 114 ? 0.1720 0.1758 0.1472 -0.0107 -0.0308 0.0073 114 VAL A C
+954 O O . VAL A 114 ? 0.1727 0.1794 0.1497 -0.0122 -0.0325 0.0121 114 VAL A O
+955 C CB . VAL A 114 ? 0.1719 0.1753 0.1458 -0.0046 -0.0275 0.0034 114 VAL A CB
+956 C CG1 . VAL A 114 ? 0.1736 0.1787 0.1503 -0.0006 -0.0266 0.0052 114 VAL A CG1
+957 C CG2 . VAL A 114 ? 0.1813 0.1819 0.1527 -0.0037 -0.0264 -0.0007 114 VAL A CG2
+958 N N . LEU A 115 ? 0.1646 0.1679 0.1415 -0.0102 -0.0306 0.0070 115 LEU A N
+959 C CA . LEU A 115 ? 0.1630 0.1694 0.1439 -0.0111 -0.0327 0.0122 115 LEU A CA
+960 C C . LEU A 115 ? 0.1635 0.1741 0.1492 -0.0051 -0.0306 0.0143 115 LEU A C
+961 O O . LEU A 115 ? 0.1683 0.1779 0.1546 -0.0029 -0.0292 0.0116 115 LEU A O
+962 C CB . LEU A 115 ? 0.1697 0.1718 0.1487 -0.0147 -0.0340 0.0106 115 LEU A CB
+963 C CG . LEU A 115 ? 0.1872 0.1925 0.1710 -0.0160 -0.0368 0.0165 115 LEU A CG
+964 C CD1 . LEU A 115 ? 0.1973 0.2049 0.1819 -0.0202 -0.0406 0.0224 115 LEU A CD1
+965 C CD2 . LEU A 115 ? 0.1923 0.1921 0.1735 -0.0192 -0.0377 0.0142 115 LEU A CD2
+966 N N A ALA A 116 ? 0.1576 0.1721 0.1462 -0.0022 -0.0299 0.0190 116 ALA A N
+967 N N B ALA A 116 ? 0.1632 0.1778 0.1520 -0.0024 -0.0300 0.0193 116 ALA A N
+968 C CA A ALA A 116 ? 0.1643 0.1809 0.1552 0.0039 -0.0271 0.0210 116 ALA A CA
+969 C CA B ALA A 116 ? 0.1766 0.1938 0.1682 0.0036 -0.0274 0.0220 116 ALA A CA
+970 C C A ALA A 116 ? 0.1638 0.1840 0.1603 0.0043 -0.0280 0.0257 116 ALA A C
+971 C C B ALA A 116 ? 0.1808 0.2010 0.1775 0.0037 -0.0283 0.0256 116 ALA A C
+972 O O A ALA A 116 ? 0.1640 0.1877 0.1651 0.0017 -0.0302 0.0314 116 ALA A O
+973 O O B ALA A 116 ? 0.1837 0.2061 0.1839 -0.0002 -0.0313 0.0298 116 ALA A O
+974 C CB A ALA A 116 ? 0.1721 0.1901 0.1635 0.0074 -0.0249 0.0250 116 ALA A CB
+975 C CB B ALA A 116 ? 0.1826 0.2025 0.1765 0.0062 -0.0258 0.0276 116 ALA A CB
+976 N N A CYS A 117 ? 0.1629 0.1828 0.1597 0.0071 -0.0266 0.0237 117 CYS A N
+977 N N B CYS A 117 ? 0.1817 0.2018 0.1786 0.0076 -0.0264 0.0241 117 CYS A N
+978 C CA A CYS A 117 ? 0.1670 0.1905 0.1694 0.0080 -0.0272 0.0278 117 CYS A CA
+979 C CA B CYS A 117 ? 0.1867 0.2097 0.1886 0.0078 -0.0272 0.0270 117 CYS A CA
+980 C C A CYS A 117 ? 0.1750 0.2001 0.1782 0.0142 -0.0240 0.0300 117 CYS A C
+981 C C B CYS A 117 ? 0.1857 0.2107 0.1888 0.0141 -0.0240 0.0295 117 CYS A C
+982 O O A CYS A 117 ? 0.1758 0.1973 0.1732 0.0170 -0.0218 0.0262 117 CYS A O
+983 O O B CYS A 117 ? 0.1897 0.2112 0.1872 0.0170 -0.0219 0.0258 117 CYS A O
+984 C CB A CYS A 117 ? 0.1751 0.1960 0.1771 0.0049 -0.0287 0.0233 117 CYS A CB
+985 C CB B CYS A 117 ? 0.2039 0.2234 0.2040 0.0047 -0.0284 0.0214 117 CYS A CB
+986 S SG A CYS A 117 ? 0.1800 0.1960 0.1782 -0.0024 -0.0317 0.0203 117 CYS A SG
+987 S SG B CYS A 117 ? 0.2509 0.2722 0.2567 0.0020 -0.0309 0.0245 117 CYS A SG
+988 N N . TYR A 118 ? 0.1791 0.2090 0.1887 0.0158 -0.0239 0.0360 118 TYR A N
+989 C CA . TYR A 118 ? 0.1964 0.2278 0.2067 0.0219 -0.0205 0.0388 118 TYR A CA
+990 C C . TYR A 118 ? 0.2126 0.2481 0.2297 0.0210 -0.0223 0.0416 118 TYR A C
+991 O O . TYR A 118 ? 0.2115 0.2504 0.2348 0.0173 -0.0253 0.0459 118 TYR A O
+992 C CB . TYR A 118 ? 0.2023 0.2361 0.2148 0.0267 -0.0169 0.0462 118 TYR A CB
+993 C CG . TYR A 118 ? 0.2149 0.2438 0.2205 0.0279 -0.0148 0.0434 118 TYR A CG
+994 C CD1 . TYR A 118 ? 0.2294 0.2518 0.2255 0.0318 -0.0117 0.0390 118 TYR A CD1
+995 C CD2 . TYR A 118 ? 0.2263 0.2562 0.2337 0.0240 -0.0169 0.0444 118 TYR A CD2
+996 C CE1 . TYR A 118 ? 0.2428 0.2598 0.2321 0.0323 -0.0102 0.0360 118 TYR A CE1
+997 C CE2 . TYR A 118 ? 0.2393 0.2647 0.2406 0.0246 -0.0153 0.0412 118 TYR A CE2
+998 C CZ . TYR A 118 ? 0.2523 0.2712 0.2448 0.0289 -0.0119 0.0371 118 TYR A CZ
+999 O OH . TYR A 118 ? 0.2759 0.2898 0.2623 0.0292 -0.0107 0.0342 118 TYR A OH
+1000 N N . ASN A 119 ? 0.2222 0.2571 0.2379 0.0235 -0.0211 0.0393 119 ASN A N
+1001 C CA . ASN A 119 ? 0.2341 0.2729 0.2567 0.0229 -0.0226 0.0418 119 ASN A CA
+1002 C C . ASN A 119 ? 0.2266 0.2644 0.2519 0.0164 -0.0266 0.0395 119 ASN A C
+1003 O O . ASN A 119 ? 0.2314 0.2726 0.2635 0.0144 -0.0290 0.0439 119 ASN A O
+1004 C CB . ASN A 119 ? 0.2617 0.3068 0.2918 0.0263 -0.0213 0.0512 119 ASN A CB
+1005 C CG . ASN A 119 ? 0.3308 0.3751 0.3568 0.0333 -0.0160 0.0538 119 ASN A CG
+1006 O OD1 . ASN A 119 ? 0.3668 0.4120 0.3934 0.0362 -0.0133 0.0588 119 ASN A OD1
+1007 N ND2 . ASN A 119 ? 0.3485 0.3905 0.3698 0.0362 -0.0143 0.0508 119 ASN A ND2
+1008 N N . GLY A 120 ? 0.2131 0.2457 0.2328 0.0131 -0.0274 0.0329 120 GLY A N
+1009 C CA . GLY A 120 ? 0.2116 0.2406 0.2310 0.0073 -0.0301 0.0300 120 GLY A CA
+1010 C C . GLY A 120 ? 0.2124 0.2411 0.2323 0.0027 -0.0334 0.0335 120 GLY A C
+1011 O O . GLY A 120 ? 0.2158 0.2400 0.2337 -0.0027 -0.0360 0.0316 120 GLY A O
+1012 N N . SER A 121 ? 0.2081 0.2410 0.2303 0.0045 -0.0332 0.0393 121 SER A N
+1013 C CA . SER A 121 ? 0.2219 0.2559 0.2461 -0.0002 -0.0369 0.0444 121 SER A CA
+1014 C C . SER A 121 ? 0.2273 0.2595 0.2467 -0.0010 -0.0363 0.0428 121 SER A C
+1015 O O . SER A 121 ? 0.2210 0.2548 0.2397 0.0040 -0.0327 0.0432 121 SER A O
+1016 C CB . SER A 121 ? 0.2465 0.2885 0.2805 0.0022 -0.0374 0.0548 121 SER A CB
+1017 O OG . SER A 121 ? 0.2958 0.3397 0.3349 0.0018 -0.0389 0.0568 121 SER A OG
+1018 N N . PRO A 122 ? 0.2413 0.2691 0.2563 -0.0075 -0.0399 0.0411 122 PRO A N
+1019 C CA . PRO A 122 ? 0.2456 0.2719 0.2562 -0.0087 -0.0395 0.0397 122 PRO A CA
+1020 C C . PRO A 122 ? 0.2367 0.2697 0.2538 -0.0069 -0.0395 0.0485 122 PRO A C
+1021 O O . PRO A 122 ? 0.2354 0.2734 0.2600 -0.0088 -0.0424 0.0570 122 PRO A O
+1022 C CB . PRO A 122 ? 0.2727 0.2920 0.2764 -0.0165 -0.0436 0.0364 122 PRO A CB
+1023 C CG . PRO A 122 ? 0.2849 0.2995 0.2868 -0.0178 -0.0438 0.0324 122 PRO A CG
+1024 C CD . PRO A 122 ? 0.2534 0.2757 0.2652 -0.0142 -0.0439 0.0393 122 PRO A CD
+1025 N N . SER A 123 ? 0.2282 0.2613 0.2432 -0.0032 -0.0360 0.0472 123 SER A N
+1026 C CA . SER A 123 ? 0.2331 0.2718 0.2542 -0.0008 -0.0348 0.0555 123 SER A CA
+1027 C C . SER A 123 ? 0.2247 0.2623 0.2433 -0.0052 -0.0369 0.0555 123 SER A C
+1028 O O . SER A 123 ? 0.2283 0.2711 0.2537 -0.0068 -0.0386 0.0643 123 SER A O
+1029 C CB . SER A 123 ? 0.2721 0.3113 0.2931 0.0077 -0.0283 0.0556 123 SER A CB
+1030 O OG . SER A 123 ? 0.3356 0.3686 0.3475 0.0089 -0.0263 0.0467 123 SER A OG
+1031 N N . GLY A 124 ? 0.2063 0.2377 0.2159 -0.0069 -0.0366 0.0466 124 GLY A N
+1032 C CA . GLY A 124 ? 0.2006 0.2308 0.2073 -0.0109 -0.0383 0.0464 124 GLY A CA
+1033 C C . GLY A 124 ? 0.1914 0.2145 0.1884 -0.0130 -0.0381 0.0366 124 GLY A C
+1034 O O . GLY A 124 ? 0.1835 0.2030 0.1769 -0.0105 -0.0358 0.0302 124 GLY A O
+1035 N N . VAL A 125 ? 0.1915 0.2130 0.1850 -0.0177 -0.0403 0.0362 125 VAL A N
+1036 C CA . VAL A 125 ? 0.2046 0.2196 0.1894 -0.0198 -0.0398 0.0280 125 VAL A CA
+1037 C C . VAL A 125 ? 0.2054 0.2216 0.1896 -0.0194 -0.0388 0.0283 125 VAL A C
+1038 O O . VAL A 125 ? 0.2082 0.2289 0.1970 -0.0211 -0.0406 0.0352 125 VAL A O
+1039 C CB . VAL A 125 ? 0.2389 0.2477 0.2169 -0.0270 -0.0434 0.0256 125 VAL A CB
+1040 C CG1 . VAL A 125 ? 0.2575 0.2676 0.2356 -0.0337 -0.0487 0.0322 125 VAL A CG1
+1041 C CG2 . VAL A 125 ? 0.2505 0.2520 0.2196 -0.0278 -0.0413 0.0171 125 VAL A CG2
+1042 N N . TYR A 126 ? 0.2076 0.2204 0.1874 -0.0167 -0.0359 0.0217 126 TYR A N
+1043 C CA . TYR A 126 ? 0.2073 0.2207 0.1864 -0.0161 -0.0349 0.0215 126 TYR A CA
+1044 C C . TYR A 126 ? 0.2039 0.2122 0.1767 -0.0165 -0.0336 0.0139 126 TYR A C
+1045 O O . TYR A 126 ? 0.2102 0.2149 0.1804 -0.0156 -0.0324 0.0092 126 TYR A O
+1046 C CB . TYR A 126 ? 0.2086 0.2252 0.1926 -0.0098 -0.0316 0.0249 126 TYR A CB
+1047 C CG . TYR A 126 ? 0.2180 0.2320 0.2004 -0.0043 -0.0285 0.0209 126 TYR A CG
+1048 C CD1 . TYR A 126 ? 0.2293 0.2390 0.2069 -0.0027 -0.0271 0.0147 126 TYR A CD1
+1049 C CD2 . TYR A 126 ? 0.2334 0.2491 0.2190 -0.0013 -0.0275 0.0237 126 TYR A CD2
+1050 C CE1 . TYR A 126 ? 0.2413 0.2482 0.2168 0.0014 -0.0252 0.0117 126 TYR A CE1
+1051 C CE2 . TYR A 126 ? 0.2452 0.2581 0.2283 0.0033 -0.0250 0.0202 126 TYR A CE2
+1052 C CZ . TYR A 126 ? 0.2542 0.2625 0.2320 0.0043 -0.0241 0.0143 126 TYR A CZ
+1053 O OH . TYR A 126 ? 0.2901 0.2953 0.2649 0.0080 -0.0226 0.0116 126 TYR A OH
+1054 N N A GLN A 127 ? 0.2048 0.2129 0.1759 -0.0181 -0.0338 0.0136 127 GLN A N
+1055 N N B GLN A 127 ? 0.2029 0.2111 0.1743 -0.0174 -0.0334 0.0134 127 GLN A N
+1056 C CA A GLN A 127 ? 0.2100 0.2140 0.1761 -0.0189 -0.0326 0.0078 127 GLN A CA
+1057 C CA B GLN A 127 ? 0.2088 0.2131 0.1755 -0.0177 -0.0321 0.0075 127 GLN A CA
+1058 C C A GLN A 127 ? 0.2180 0.2225 0.1858 -0.0142 -0.0304 0.0061 127 GLN A C
+1059 C C B GLN A 127 ? 0.2144 0.2186 0.1826 -0.0125 -0.0297 0.0055 127 GLN A C
+1060 O O A GLN A 127 ? 0.2180 0.2252 0.1888 -0.0123 -0.0300 0.0097 127 GLN A O
+1061 O O B GLN A 127 ? 0.2147 0.2211 0.1858 -0.0097 -0.0289 0.0088 127 GLN A O
+1062 C CB A GLN A 127 ? 0.2189 0.2223 0.1814 -0.0245 -0.0349 0.0091 127 GLN A CB
+1063 C CB B GLN A 127 ? 0.2260 0.2301 0.1899 -0.0223 -0.0338 0.0085 127 GLN A CB
+1064 C CG A GLN A 127 ? 0.2441 0.2428 0.2006 -0.0261 -0.0336 0.0039 127 GLN A CG
+1065 C CG B GLN A 127 ? 0.2569 0.2563 0.2152 -0.0236 -0.0324 0.0030 127 GLN A CG
+1066 C CD A GLN A 127 ? 0.2576 0.2501 0.2085 -0.0274 -0.0323 -0.0004 127 GLN A CD
+1067 C CD B GLN A 127 ? 0.2674 0.2610 0.2195 -0.0268 -0.0323 0.0000 127 GLN A CD
+1068 O OE1 A GLN A 127 ? 0.2529 0.2441 0.2039 -0.0277 -0.0329 0.0001 127 GLN A OE1
+1069 O OE1 B GLN A 127 ? 0.2729 0.2655 0.2250 -0.0275 -0.0333 0.0010 127 GLN A OE1
+1070 N NE2 A GLN A 127 ? 0.2689 0.2572 0.2154 -0.0278 -0.0299 -0.0043 127 GLN A NE2
+1071 N NE2 B GLN A 127 ? 0.2625 0.2514 0.2090 -0.0283 -0.0305 -0.0036 127 GLN A NE2
+1072 N N A CYS A 128 ? 0.2195 0.2209 0.1853 -0.0124 -0.0288 0.0013 128 CYS A N
+1073 N N B CYS A 128 ? 0.2191 0.2201 0.1851 -0.0114 -0.0285 0.0006 128 CYS A N
+1074 C CA A CYS A 128 ? 0.2236 0.2241 0.1898 -0.0089 -0.0277 -0.0004 128 CYS A CA
+1075 C CA B CYS A 128 ? 0.2279 0.2275 0.1941 -0.0078 -0.0273 -0.0016 128 CYS A CA
+1076 C C A CYS A 128 ? 0.2259 0.2239 0.1904 -0.0099 -0.0272 -0.0044 128 CYS A C
+1077 C C B CYS A 128 ? 0.2284 0.2260 0.1930 -0.0094 -0.0270 -0.0049 128 CYS A C
+1078 O O A CYS A 128 ? 0.2252 0.2219 0.1876 -0.0130 -0.0269 -0.0057 128 CYS A O
+1079 O O B CYS A 128 ? 0.2274 0.2236 0.1902 -0.0123 -0.0266 -0.0063 128 CYS A O
+1080 C CB A CYS A 128 ? 0.2301 0.2299 0.1972 -0.0046 -0.0267 -0.0001 128 CYS A CB
+1081 C CB B CYS A 128 ? 0.2450 0.2435 0.2118 -0.0049 -0.0266 -0.0027 128 CYS A CB
+1082 S SG A CYS A 128 ? 0.2613 0.2596 0.2283 -0.0042 -0.0265 -0.0031 128 CYS A SG
+1083 S SG B CYS A 128 ? 0.3024 0.3023 0.2705 -0.0008 -0.0258 0.0013 128 CYS A SG
+1084 N N . ALA A 129 ? 0.2293 0.2258 0.1942 -0.0075 -0.0270 -0.0059 129 ALA A N
+1085 C CA . ALA A 129 ? 0.2310 0.2263 0.1962 -0.0084 -0.0268 -0.0082 129 ALA A CA
+1086 C C . ALA A 129 ? 0.2206 0.2142 0.1869 -0.0061 -0.0274 -0.0091 129 ALA A C
+1087 O O . ALA A 129 ? 0.2327 0.2246 0.1972 -0.0039 -0.0283 -0.0085 129 ALA A O
+1088 C CB . ALA A 129 ? 0.2348 0.2306 0.1999 -0.0096 -0.0273 -0.0076 129 ALA A CB
+1089 N N . MET A 130 ? 0.2008 0.1942 0.1694 -0.0068 -0.0270 -0.0101 130 MET A N
+1090 C CA . MET A 130 ? 0.1952 0.1873 0.1656 -0.0057 -0.0286 -0.0099 130 MET A CA
+1091 C C . MET A 130 ? 0.2025 0.1933 0.1720 -0.0061 -0.0307 -0.0095 130 MET A C
+1092 O O . MET A 130 ? 0.2061 0.1984 0.1776 -0.0075 -0.0301 -0.0092 130 MET A O
+1093 C CB . MET A 130 ? 0.1989 0.1922 0.1742 -0.0063 -0.0271 -0.0096 130 MET A CB
+1094 C CG . MET A 130 ? 0.2203 0.2135 0.1991 -0.0060 -0.0295 -0.0081 130 MET A CG
+1095 S SD . MET A 130 ? 0.2278 0.2187 0.2031 -0.0045 -0.0322 -0.0081 130 MET A SD
+1096 C CE . MET A 130 ? 0.2113 0.2043 0.1880 -0.0035 -0.0287 -0.0088 130 MET A CE
+1097 N N . ARG A 131 ? 0.2015 0.1887 0.1670 -0.0048 -0.0327 -0.0094 131 ARG A N
+1098 C CA . ARG A 131 ? 0.2027 0.1870 0.1662 -0.0053 -0.0347 -0.0091 131 ARG A CA
+1099 C C . ARG A 131 ? 0.2077 0.1917 0.1747 -0.0072 -0.0374 -0.0082 131 ARG A C
+1100 O O . ARG A 131 ? 0.2090 0.1938 0.1788 -0.0075 -0.0383 -0.0074 131 ARG A O
+1101 C CB . ARG A 131 ? 0.2088 0.1867 0.1650 -0.0032 -0.0355 -0.0094 131 ARG A CB
+1102 C CG . ARG A 131 ? 0.2152 0.1936 0.1693 -0.0008 -0.0325 -0.0088 131 ARG A CG
+1103 C CD . ARG A 131 ? 0.2128 0.1956 0.1700 -0.0015 -0.0307 -0.0075 131 ARG A CD
+1104 N NE . ARG A 131 ? 0.2100 0.1907 0.1667 -0.0024 -0.0319 -0.0075 131 ARG A NE
+1105 C CZ . ARG A 131 ? 0.2081 0.1926 0.1680 -0.0038 -0.0312 -0.0063 131 ARG A CZ
+1106 N NH1 . ARG A 131 ? 0.1936 0.1834 0.1563 -0.0048 -0.0297 -0.0050 131 ARG A NH1
+1107 N NH2 . ARG A 131 ? 0.2013 0.1839 0.1611 -0.0045 -0.0325 -0.0061 131 ARG A NH2
+1108 N N . PRO A 132 ? 0.2112 0.1942 0.1788 -0.0085 -0.0393 -0.0075 132 PRO A N
+1109 C CA . PRO A 132 ? 0.2154 0.1985 0.1874 -0.0105 -0.0426 -0.0054 132 PRO A CA
+1110 C C . PRO A 132 ? 0.2233 0.2010 0.1915 -0.0113 -0.0469 -0.0047 132 PRO A C
+1111 O O . PRO A 132 ? 0.2373 0.2166 0.2109 -0.0134 -0.0498 -0.0019 132 PRO A O
+1112 C CB . PRO A 132 ? 0.2262 0.2083 0.1981 -0.0116 -0.0440 -0.0048 132 PRO A CB
+1113 C CG . PRO A 132 ? 0.2227 0.2079 0.1941 -0.0105 -0.0399 -0.0061 132 PRO A CG
+1114 C CD . PRO A 132 ? 0.2092 0.1921 0.1752 -0.0084 -0.0383 -0.0077 132 PRO A CD
+1115 N N . ASN A 133 ? 0.2123 0.1833 0.1710 -0.0098 -0.0473 -0.0067 133 ASN A N
+1116 C CA . ASN A 133 ? 0.2134 0.1779 0.1661 -0.0109 -0.0513 -0.0062 133 ASN A CA
+1117 C C . ASN A 133 ? 0.2127 0.1806 0.1674 -0.0096 -0.0496 -0.0062 133 ASN A C
+1118 O O . ASN A 133 ? 0.2193 0.1818 0.1678 -0.0099 -0.0521 -0.0061 133 ASN A O
+1119 C CB . ASN A 133 ? 0.2299 0.1833 0.1694 -0.0097 -0.0521 -0.0083 133 ASN A CB
+1120 C CG . ASN A 133 ? 0.2370 0.1903 0.1728 -0.0056 -0.0467 -0.0100 133 ASN A CG
+1121 O OD1 . ASN A 133 ? 0.2231 0.1841 0.1651 -0.0041 -0.0433 -0.0099 133 ASN A OD1
+1122 N ND2 . ASN A 133 ? 0.2540 0.1978 0.1793 -0.0036 -0.0456 -0.0112 133 ASN A ND2
+1123 N N . PHE A 134 ? 0.2034 0.1791 0.1657 -0.0083 -0.0454 -0.0063 134 PHE A N
+1124 C CA . PHE A 134 ? 0.2103 0.1897 0.1760 -0.0072 -0.0434 -0.0060 134 PHE A CA
+1125 C C . PHE A 134 ? 0.2120 0.1882 0.1706 -0.0047 -0.0419 -0.0077 134 PHE A C
+1126 O O . PHE A 134 ? 0.2138 0.1918 0.1740 -0.0040 -0.0414 -0.0072 134 PHE A O
+1127 C CB . PHE A 134 ? 0.2145 0.1952 0.1854 -0.0093 -0.0468 -0.0029 134 PHE A CB
+1128 C CG . PHE A 134 ? 0.2344 0.2200 0.2151 -0.0112 -0.0470 0.0000 134 PHE A CG
+1129 C CD1 . PHE A 134 ? 0.2511 0.2428 0.2400 -0.0101 -0.0422 0.0008 134 PHE A CD1
+1130 C CD2 . PHE A 134 ? 0.2532 0.2365 0.2344 -0.0140 -0.0520 0.0026 134 PHE A CD2
+1131 C CE1 . PHE A 134 ? 0.2621 0.2578 0.2600 -0.0110 -0.0413 0.0042 134 PHE A CE1
+1132 C CE2 . PHE A 134 ? 0.2640 0.2525 0.2556 -0.0153 -0.0519 0.0064 134 PHE A CE2
+1133 C CZ . PHE A 134 ? 0.2594 0.2543 0.2595 -0.0135 -0.0462 0.0073 134 PHE A CZ
+1134 N N . THR A 135 ? 0.2087 0.1810 0.1607 -0.0029 -0.0404 -0.0091 135 THR A N
+1135 C CA . THR A 135 ? 0.2126 0.1833 0.1598 0.0002 -0.0376 -0.0096 135 THR A CA
+1136 C C . THR A 135 ? 0.2102 0.1872 0.1627 0.0010 -0.0340 -0.0095 135 THR A C
+1137 O O . THR A 135 ? 0.2047 0.1852 0.1617 -0.0008 -0.0337 -0.0095 135 THR A O
+1138 C CB . THR A 135 ? 0.2285 0.1900 0.1652 0.0020 -0.0376 -0.0102 135 THR A CB
+1139 O OG1 . THR A 135 ? 0.2442 0.2059 0.1817 0.0019 -0.0365 -0.0103 135 THR A OG1
+1140 C CG2 . THR A 135 ? 0.2325 0.1852 0.1610 0.0002 -0.0420 -0.0105 135 THR A CG2
+1141 N N . ILE A 136 ? 0.2069 0.1849 0.1584 0.0034 -0.0314 -0.0087 136 ILE A N
+1142 C CA . ILE A 136 ? 0.2138 0.1964 0.1688 0.0036 -0.0290 -0.0076 136 ILE A CA
+1143 C C . ILE A 136 ? 0.2215 0.2012 0.1722 0.0069 -0.0267 -0.0057 136 ILE A C
+1144 O O . ILE A 136 ? 0.2221 0.1966 0.1672 0.0095 -0.0262 -0.0057 136 ILE A O
+1145 C CB . ILE A 136 ? 0.2269 0.2151 0.1873 0.0025 -0.0280 -0.0073 136 ILE A CB
+1146 C CG1 . ILE A 136 ? 0.2382 0.2265 0.1980 0.0048 -0.0272 -0.0061 136 ILE A CG1
+1147 C CG2 . ILE A 136 ? 0.2386 0.2284 0.2029 0.0000 -0.0288 -0.0088 136 ILE A CG2
+1148 C CD1 . ILE A 136 ? 0.2465 0.2396 0.2111 0.0037 -0.0262 -0.0052 136 ILE A CD1
+1149 N N A LYS A 137 ? 0.2290 0.2116 0.1822 0.0070 -0.0251 -0.0036 137 LYS A N
+1150 N N B LYS A 137 ? 0.2299 0.2126 0.1832 0.0069 -0.0252 -0.0037 137 LYS A N
+1151 C CA A LYS A 137 ? 0.2450 0.2258 0.1963 0.0107 -0.0221 -0.0004 137 LYS A CA
+1152 C CA B LYS A 137 ? 0.2468 0.2279 0.1985 0.0105 -0.0222 -0.0004 137 LYS A CA
+1153 C C A LYS A 137 ? 0.2452 0.2327 0.2025 0.0107 -0.0210 0.0030 137 LYS A C
+1154 C C B LYS A 137 ? 0.2455 0.2332 0.2030 0.0105 -0.0211 0.0029 137 LYS A C
+1155 O O A LYS A 137 ? 0.2446 0.2372 0.2069 0.0083 -0.0214 0.0052 137 LYS A O
+1156 O O B LYS A 137 ? 0.2441 0.2371 0.2066 0.0080 -0.0216 0.0050 137 LYS A O
+1157 C CB A LYS A 137 ? 0.2776 0.2572 0.2288 0.0108 -0.0211 0.0009 137 LYS A CB
+1158 C CB B LYS A 137 ? 0.2817 0.2627 0.2342 0.0101 -0.0214 0.0010 137 LYS A CB
+1159 C CG A LYS A 137 ? 0.3396 0.3121 0.2850 0.0101 -0.0229 -0.0023 137 LYS A CG
+1160 C CG B LYS A 137 ? 0.3499 0.3238 0.2966 0.0098 -0.0227 -0.0018 137 LYS A CG
+1161 C CD A LYS A 137 ? 0.3939 0.3654 0.3399 0.0102 -0.0218 -0.0008 137 LYS A CD
+1162 C CD B LYS A 137 ? 0.4039 0.3799 0.3538 0.0082 -0.0228 -0.0007 137 LYS A CD
+1163 C CE A LYS A 137 ? 0.4429 0.4061 0.3822 0.0148 -0.0181 0.0008 137 LYS A CE
+1164 C CE B LYS A 137 ? 0.4534 0.4206 0.3967 0.0098 -0.0225 -0.0017 137 LYS A CE
+1165 N NZ A LYS A 137 ? 0.4766 0.4283 0.4051 0.0152 -0.0197 -0.0028 137 LYS A NZ
+1166 N NZ B LYS A 137 ? 0.4711 0.4404 0.4176 0.0067 -0.0246 -0.0024 137 LYS A NZ
+1167 N N . GLY A 138 ? 0.2446 0.2319 0.2013 0.0127 -0.0202 0.0035 138 GLY A N
+1168 C CA . GLY A 138 ? 0.2460 0.2394 0.2086 0.0125 -0.0198 0.0070 138 GLY A CA
+1169 C C . GLY A 138 ? 0.2391 0.2328 0.2027 0.0170 -0.0163 0.0123 138 GLY A C
+1170 O O . GLY A 138 ? 0.2492 0.2386 0.2092 0.0205 -0.0133 0.0139 138 GLY A O
+1171 N N . SER A 139 ? 0.2255 0.2242 0.1942 0.0172 -0.0163 0.0156 139 SER A N
+1172 C CA . SER A 139 ? 0.2291 0.2292 0.2003 0.0218 -0.0127 0.0217 139 SER A CA
+1173 C C . SER A 139 ? 0.2372 0.2384 0.2089 0.0226 -0.0132 0.0213 139 SER A C
+1174 O O . SER A 139 ? 0.2391 0.2458 0.2167 0.0194 -0.0158 0.0224 139 SER A O
+1175 C CB . SER A 139 ? 0.2409 0.2483 0.2211 0.0202 -0.0129 0.0287 139 SER A CB
+1176 O OG . SER A 139 ? 0.2930 0.3033 0.2779 0.0245 -0.0096 0.0358 139 SER A OG
+1177 N N . PHE A 140 ? 0.2317 0.2266 0.1959 0.0262 -0.0113 0.0188 140 PHE A N
+1178 C CA . PHE A 140 ? 0.2400 0.2355 0.2040 0.0268 -0.0120 0.0179 140 PHE A CA
+1179 C C . PHE A 140 ? 0.2721 0.2629 0.2306 0.0328 -0.0076 0.0206 140 PHE A C
+1180 O O . PHE A 140 ? 0.2955 0.2774 0.2439 0.0353 -0.0056 0.0183 140 PHE A O
+1181 C CB . PHE A 140 ? 0.2313 0.2232 0.1906 0.0238 -0.0153 0.0113 140 PHE A CB
+1182 C CG . PHE A 140 ? 0.2256 0.2211 0.1894 0.0184 -0.0188 0.0083 140 PHE A CG
+1183 C CD1 . PHE A 140 ? 0.2344 0.2352 0.2047 0.0157 -0.0205 0.0088 140 PHE A CD1
+1184 C CD2 . PHE A 140 ? 0.2295 0.2219 0.1902 0.0162 -0.0202 0.0049 140 PHE A CD2
+1185 C CE1 . PHE A 140 ? 0.2311 0.2331 0.2036 0.0112 -0.0227 0.0059 140 PHE A CE1
+1186 C CE2 . PHE A 140 ? 0.2363 0.2312 0.2005 0.0118 -0.0225 0.0024 140 PHE A CE2
+1187 C CZ . PHE A 140 ? 0.2268 0.2259 0.1962 0.0095 -0.0234 0.0027 140 PHE A CZ
+1188 N N . LEU A 141 ? 0.2734 0.2692 0.2374 0.0351 -0.0061 0.0253 141 LEU A N
+1189 C CA . LEU A 141 ? 0.2985 0.2898 0.2571 0.0412 -0.0013 0.0283 141 LEU A CA
+1190 C C . LEU A 141 ? 0.3053 0.2961 0.2613 0.0405 -0.0035 0.0254 141 LEU A C
+1191 O O . LEU A 141 ? 0.3014 0.2961 0.2616 0.0356 -0.0082 0.0219 141 LEU A O
+1192 C CB . LEU A 141 ? 0.3101 0.3085 0.2785 0.0446 0.0022 0.0372 141 LEU A CB
+1193 C CG . LEU A 141 ? 0.3488 0.3495 0.3224 0.0453 0.0044 0.0422 141 LEU A CG
+1194 C CD1 . LEU A 141 ? 0.3570 0.3675 0.3437 0.0466 0.0057 0.0518 141 LEU A CD1
+1195 C CD2 . LEU A 141 ? 0.3693 0.3596 0.3325 0.0508 0.0105 0.0421 141 LEU A CD2
+1196 N N . ASN A 142 ? 0.3145 0.3005 0.2638 0.0455 0.0003 0.0273 142 ASN A N
+1197 C CA . ASN A 142 ? 0.3191 0.3055 0.2668 0.0448 -0.0019 0.0255 142 ASN A CA
+1198 C C . ASN A 142 ? 0.2914 0.2895 0.2533 0.0425 -0.0043 0.0287 142 ASN A C
+1199 O O . ASN A 142 ? 0.2891 0.2935 0.2599 0.0439 -0.0025 0.0346 142 ASN A O
+1200 C CB . ASN A 142 ? 0.3638 0.3423 0.3007 0.0507 0.0031 0.0276 142 ASN A CB
+1201 C CG . ASN A 142 ? 0.4614 0.4256 0.3811 0.0514 0.0040 0.0230 142 ASN A CG
+1202 O OD1 . ASN A 142 ? 0.4930 0.4539 0.4085 0.0465 -0.0011 0.0174 142 ASN A OD1
+1203 N ND2 . ASN A 142 ? 0.4901 0.4448 0.3992 0.0576 0.0107 0.0256 142 ASN A ND2
+1204 N N . GLY A 143 ? 0.2679 0.2684 0.2323 0.0383 -0.0087 0.0248 143 GLY A N
+1205 C CA . GLY A 143 ? 0.2418 0.2512 0.2180 0.0354 -0.0114 0.0266 143 GLY A CA
+1206 C C . GLY A 143 ? 0.2132 0.2251 0.1943 0.0298 -0.0149 0.0234 143 GLY A C
+1207 O O . GLY A 143 ? 0.2026 0.2193 0.1911 0.0266 -0.0173 0.0235 143 GLY A O
+1208 N N . SER A 144 ? 0.2005 0.2082 0.1767 0.0286 -0.0150 0.0207 144 SER A N
+1209 C CA . SER A 144 ? 0.1811 0.1906 0.1609 0.0235 -0.0179 0.0178 144 SER A CA
+1210 C C . SER A 144 ? 0.1726 0.1799 0.1508 0.0202 -0.0204 0.0123 144 SER A C
+1211 O O . SER A 144 ? 0.1598 0.1682 0.1408 0.0163 -0.0220 0.0101 144 SER A O
+1212 C CB . SER A 144 ? 0.1922 0.1992 0.1689 0.0234 -0.0170 0.0179 144 SER A CB
+1213 O OG . SER A 144 ? 0.2250 0.2249 0.1925 0.0253 -0.0159 0.0147 144 SER A OG
+1214 N N . CYS A 145 ? 0.1754 0.1797 0.1493 0.0216 -0.0206 0.0107 145 CYS A N
+1215 C CA . CYS A 145 ? 0.1740 0.1774 0.1484 0.0185 -0.0230 0.0069 145 CYS A CA
+1216 C C . CYS A 145 ? 0.1604 0.1686 0.1434 0.0158 -0.0237 0.0069 145 CYS A C
+1217 O O . CYS A 145 ? 0.1619 0.1736 0.1494 0.0167 -0.0232 0.0096 145 CYS A O
+1218 C CB . CYS A 145 ? 0.1941 0.1942 0.1633 0.0197 -0.0239 0.0066 145 CYS A CB
+1219 S SG . CYS A 145 ? 0.2609 0.2515 0.2164 0.0219 -0.0233 0.0055 145 CYS A SG
+1220 N N . GLY A 146 ? 0.1498 0.1572 0.1345 0.0128 -0.0246 0.0039 146 GLY A N
+1221 C CA . GLY A 146 ? 0.1474 0.1568 0.1383 0.0104 -0.0244 0.0034 146 GLY A CA
+1222 C C . GLY A 146 ? 0.1458 0.1546 0.1365 0.0080 -0.0242 0.0030 146 GLY A C
+1223 O O . GLY A 146 ? 0.1578 0.1655 0.1507 0.0055 -0.0237 0.0017 146 GLY A O
+1224 N N . SER A 147 ? 0.1431 0.1517 0.1305 0.0086 -0.0243 0.0043 147 SER A N
+1225 C CA . SER A 147 ? 0.1443 0.1522 0.1310 0.0055 -0.0249 0.0043 147 SER A CA
+1226 C C . SER A 147 ? 0.1516 0.1561 0.1359 0.0031 -0.0246 0.0002 147 SER A C
+1227 O O . SER A 147 ? 0.1480 0.1514 0.1310 0.0044 -0.0243 -0.0015 147 SER A O
+1228 C CB . SER A 147 ? 0.1573 0.1662 0.1420 0.0069 -0.0249 0.0071 147 SER A CB
+1229 O OG . SER A 147 ? 0.1685 0.1807 0.1562 0.0096 -0.0244 0.0120 147 SER A OG
+1230 N N . VAL A 148 ? 0.1463 0.1485 0.1295 -0.0004 -0.0246 -0.0010 148 VAL A N
+1231 C CA . VAL A 148 ? 0.1560 0.1546 0.1370 -0.0022 -0.0233 -0.0044 148 VAL A CA
+1232 C C . VAL A 148 ? 0.1614 0.1581 0.1381 -0.0047 -0.0239 -0.0051 148 VAL A C
+1233 O O . VAL A 148 ? 0.1603 0.1578 0.1356 -0.0065 -0.0256 -0.0028 148 VAL A O
+1234 C CB . VAL A 148 ? 0.1675 0.1627 0.1497 -0.0036 -0.0213 -0.0060 148 VAL A CB
+1235 C CG1 . VAL A 148 ? 0.1651 0.1630 0.1529 -0.0010 -0.0206 -0.0050 148 VAL A CG1
+1236 C CG2 . VAL A 148 ? 0.1812 0.1732 0.1603 -0.0071 -0.0223 -0.0055 148 VAL A CG2
+1237 N N . GLY A 149 ? 0.1641 0.1587 0.1394 -0.0051 -0.0225 -0.0076 149 GLY A N
+1238 C CA . GLY A 149 ? 0.1680 0.1602 0.1390 -0.0076 -0.0224 -0.0087 149 GLY A CA
+1239 C C . GLY A 149 ? 0.1725 0.1592 0.1405 -0.0098 -0.0198 -0.0111 149 GLY A C
+1240 O O . GLY A 149 ? 0.1692 0.1545 0.1400 -0.0084 -0.0172 -0.0121 149 GLY A O
+1241 N N . PHE A 150 ? 0.1703 0.1533 0.1322 -0.0134 -0.0202 -0.0117 150 PHE A N
+1242 C CA . PHE A 150 ? 0.1901 0.1652 0.1460 -0.0157 -0.0172 -0.0141 150 PHE A CA
+1243 C C . PHE A 150 ? 0.2117 0.1828 0.1599 -0.0193 -0.0176 -0.0148 150 PHE A C
+1244 O O . PHE A 150 ? 0.2039 0.1788 0.1519 -0.0209 -0.0211 -0.0128 150 PHE A O
+1245 C CB . PHE A 150 ? 0.1951 0.1662 0.1486 -0.0177 -0.0178 -0.0138 150 PHE A CB
+1246 C CG . PHE A 150 ? 0.2071 0.1797 0.1583 -0.0212 -0.0228 -0.0110 150 PHE A CG
+1247 C CD1 . PHE A 150 ? 0.2157 0.1963 0.1740 -0.0192 -0.0256 -0.0074 150 PHE A CD1
+1248 C CD2 . PHE A 150 ? 0.2264 0.1922 0.1683 -0.0267 -0.0246 -0.0111 150 PHE A CD2
+1249 C CE1 . PHE A 150 ? 0.2266 0.2097 0.1848 -0.0220 -0.0297 -0.0033 150 PHE A CE1
+1250 C CE2 . PHE A 150 ? 0.2366 0.2048 0.1780 -0.0305 -0.0299 -0.0070 150 PHE A CE2
+1251 C CZ . PHE A 150 ? 0.2261 0.2036 0.1767 -0.0279 -0.0322 -0.0028 150 PHE A CZ
+1252 N N . ASN A 151 ? 0.2234 0.1864 0.1650 -0.0206 -0.0137 -0.0174 151 ASN A N
+1253 C CA . ASN A 151 ? 0.2490 0.2054 0.1802 -0.0247 -0.0136 -0.0185 151 ASN A CA
+1254 C C . ASN A 151 ? 0.2759 0.2203 0.1967 -0.0277 -0.0115 -0.0205 151 ASN A C
+1255 O O . ASN A 151 ? 0.2690 0.2107 0.1922 -0.0254 -0.0083 -0.0215 151 ASN A O
+1256 C CB . ASN A 151 ? 0.2598 0.2158 0.1913 -0.0227 -0.0096 -0.0196 151 ASN A CB
+1257 C CG . ASN A 151 ? 0.3002 0.2653 0.2385 -0.0214 -0.0125 -0.0177 151 ASN A CG
+1258 O OD1 . ASN A 151 ? 0.3333 0.2995 0.2679 -0.0243 -0.0154 -0.0168 151 ASN A OD1
+1259 N ND2 . ASN A 151 ? 0.2779 0.2494 0.2257 -0.0172 -0.0122 -0.0169 151 ASN A ND2
+1260 N N . ILE A 152 ? 0.3027 0.2392 0.2112 -0.0333 -0.0133 -0.0211 152 ILE A N
+1261 C CA . ILE A 152 ? 0.3469 0.2691 0.2424 -0.0368 -0.0114 -0.0235 152 ILE A CA
+1262 C C . ILE A 152 ? 0.3883 0.2993 0.2701 -0.0391 -0.0075 -0.0260 152 ILE A C
+1263 O O . ILE A 152 ? 0.3936 0.3075 0.2730 -0.0415 -0.0102 -0.0249 152 ILE A O
+1264 C CB . ILE A 152 ? 0.3603 0.2802 0.2511 -0.0428 -0.0184 -0.0213 152 ILE A CB
+1265 C CG1 . ILE A 152 ? 0.3656 0.2977 0.2707 -0.0401 -0.0221 -0.0178 152 ILE A CG1
+1266 C CG2 . ILE A 152 ? 0.3794 0.2822 0.2552 -0.0466 -0.0163 -0.0242 152 ILE A CG2
+1267 C CD1 . ILE A 152 ? 0.3812 0.3132 0.2845 -0.0455 -0.0290 -0.0141 152 ILE A CD1
+1268 N N . ASP A 153 ? 0.4161 0.3142 0.2891 -0.0379 -0.0005 -0.0292 153 ASP A N
+1269 C CA . ASP A 153 ? 0.4501 0.3347 0.3071 -0.0400 0.0042 -0.0317 153 ASP A CA
+1270 C C . ASP A 153 ? 0.4755 0.3426 0.3155 -0.0448 0.0044 -0.0342 153 ASP A C
+1271 O O . ASP A 153 ? 0.4875 0.3468 0.3264 -0.0416 0.0105 -0.0360 153 ASP A O
+1272 C CB . ASP A 153 ? 0.4891 0.3723 0.3503 -0.0332 0.0141 -0.0327 153 ASP A CB
+1273 C CG . ASP A 153 ? 0.6021 0.4717 0.4468 -0.0348 0.0196 -0.0349 153 ASP A CG
+1274 O OD1 . ASP A 153 ? 0.6244 0.4920 0.4593 -0.0404 0.0145 -0.0348 153 ASP A OD1
+1275 O OD2 . ASP A 153 ? 0.6541 0.5147 0.4955 -0.0303 0.0293 -0.0361 153 ASP A OD2
+1276 N N . TYR A 154 ? 0.4783 0.3395 0.3057 -0.0529 -0.0029 -0.0336 154 TYR A N
+1277 C CA . TYR A 154 ? 0.4970 0.3411 0.3065 -0.0599 -0.0057 -0.0351 154 TYR A CA
+1278 C C . TYR A 154 ? 0.4899 0.3367 0.3080 -0.0589 -0.0080 -0.0341 154 TYR A C
+1279 O O . TYR A 154 ? 0.4925 0.3498 0.3191 -0.0620 -0.0165 -0.0302 154 TYR A O
+1280 C CB . TYR A 154 ? 0.5145 0.3358 0.3015 -0.0610 0.0024 -0.0398 154 TYR A CB
+1281 C CG . TYR A 154 ? 0.5418 0.3431 0.3083 -0.0686 -0.0009 -0.0418 154 TYR A CG
+1282 C CD1 . TYR A 154 ? 0.5593 0.3587 0.3171 -0.0784 -0.0120 -0.0392 154 TYR A CD1
+1283 C CD2 . TYR A 154 ? 0.5632 0.3475 0.3196 -0.0663 0.0070 -0.0455 154 TYR A CD2
+1284 C CE1 . TYR A 154 ? 0.5842 0.3648 0.3230 -0.0863 -0.0162 -0.0403 154 TYR A CE1
+1285 C CE2 . TYR A 154 ? 0.5893 0.3541 0.3262 -0.0736 0.0036 -0.0474 154 TYR A CE2
+1286 C CZ . TYR A 154 ? 0.6066 0.3693 0.3342 -0.0840 -0.0084 -0.0449 154 TYR A CZ
+1287 O OH . TYR A 154 ? 0.6433 0.3857 0.3507 -0.0922 -0.0128 -0.0463 154 TYR A OH
+1288 N N . ASP A 155 ? 0.4819 0.3204 0.2992 -0.0543 -0.0001 -0.0370 155 ASP A N
+1289 C CA . ASP A 155 ? 0.4692 0.3101 0.2947 -0.0533 -0.0020 -0.0360 155 ASP A CA
+1290 C C . ASP A 155 ? 0.4375 0.2920 0.2834 -0.0445 0.0033 -0.0350 155 ASP A C
+1291 O O . ASP A 155 ? 0.4396 0.2961 0.2927 -0.0429 0.0028 -0.0342 155 ASP A O
+1292 C CB . ASP A 155 ? 0.5167 0.3350 0.3233 -0.0570 0.0010 -0.0394 155 ASP A CB
+1293 C CG . ASP A 155 ? 0.5979 0.4010 0.3946 -0.0521 0.0136 -0.0436 155 ASP A CG
+1294 O OD1 . ASP A 155 ? 0.6029 0.4128 0.4064 -0.0465 0.0196 -0.0435 155 ASP A OD1
+1295 O OD2 . ASP A 155 ? 0.6460 0.4298 0.4281 -0.0537 0.0176 -0.0465 155 ASP A OD2
+1296 N N . CYS A 156 ? 0.4061 0.2698 0.2611 -0.0390 0.0078 -0.0346 156 CYS A N
+1297 C CA . CYS A 156 ? 0.3780 0.2540 0.2516 -0.0314 0.0122 -0.0330 156 CYS A CA
+1298 C C . CYS A 156 ? 0.3346 0.2300 0.2241 -0.0297 0.0062 -0.0297 156 CYS A C
+1299 O O . CYS A 156 ? 0.3294 0.2298 0.2191 -0.0301 0.0050 -0.0292 156 CYS A O
+1300 C CB . CYS A 156 ? 0.3957 0.2659 0.2683 -0.0262 0.0226 -0.0343 156 CYS A CB
+1301 S SG . CYS A 156 ? 0.4155 0.3003 0.3114 -0.0177 0.0276 -0.0310 156 CYS A SG
+1302 N N . VAL A 157 ? 0.2993 0.2052 0.2021 -0.0273 0.0034 -0.0275 157 VAL A N
+1303 C CA . VAL A 157 ? 0.2695 0.1921 0.1862 -0.0250 -0.0013 -0.0245 157 VAL A CA
+1304 C C . VAL A 157 ? 0.2462 0.1761 0.1745 -0.0190 0.0035 -0.0237 157 VAL A C
+1305 O O . VAL A 157 ? 0.2416 0.1712 0.1762 -0.0156 0.0077 -0.0233 157 VAL A O
+1306 C CB . VAL A 157 ? 0.2674 0.1973 0.1918 -0.0254 -0.0067 -0.0219 157 VAL A CB
+1307 C CG1 . VAL A 157 ? 0.2624 0.2074 0.1989 -0.0227 -0.0108 -0.0189 157 VAL A CG1
+1308 C CG2 . VAL A 157 ? 0.2831 0.2058 0.1974 -0.0319 -0.0121 -0.0214 157 VAL A CG2
+1309 N N . SER A 158 ? 0.2344 0.1714 0.1665 -0.0178 0.0025 -0.0229 158 SER A N
+1310 C CA . SER A 158 ? 0.2258 0.1707 0.1698 -0.0129 0.0054 -0.0212 158 SER A CA
+1311 C C . SER A 158 ? 0.2111 0.1683 0.1649 -0.0118 -0.0005 -0.0189 158 SER A C
+1312 O O . SER A 158 ? 0.2087 0.1705 0.1618 -0.0132 -0.0047 -0.0183 158 SER A O
+1313 C CB . SER A 158 ? 0.2555 0.1997 0.1973 -0.0125 0.0081 -0.0214 158 SER A CB
+1314 O OG . SER A 158 ? 0.3059 0.2382 0.2392 -0.0122 0.0154 -0.0230 158 SER A OG
+1315 N N . PHE A 159 ? 0.1963 0.1580 0.1587 -0.0092 -0.0006 -0.0174 159 PHE A N
+1316 C CA . PHE A 159 ? 0.1856 0.1572 0.1557 -0.0078 -0.0055 -0.0152 159 PHE A CA
+1317 C C . PHE A 159 ? 0.1799 0.1570 0.1566 -0.0054 -0.0052 -0.0138 159 PHE A C
+1318 O O . PHE A 159 ? 0.1835 0.1603 0.1655 -0.0034 -0.0012 -0.0127 159 PHE A O
+1319 C CB . PHE A 159 ? 0.1763 0.1503 0.1525 -0.0061 -0.0055 -0.0139 159 PHE A CB
+1320 C CG . PHE A 159 ? 0.1674 0.1367 0.1381 -0.0086 -0.0069 -0.0146 159 PHE A CG
+1321 C CD1 . PHE A 159 ? 0.1742 0.1471 0.1436 -0.0104 -0.0121 -0.0133 159 PHE A CD1
+1322 C CD2 . PHE A 159 ? 0.1754 0.1360 0.1424 -0.0094 -0.0028 -0.0160 159 PHE A CD2
+1323 C CE1 . PHE A 159 ? 0.1811 0.1504 0.1468 -0.0132 -0.0142 -0.0128 159 PHE A CE1
+1324 C CE2 . PHE A 159 ? 0.1872 0.1425 0.1485 -0.0125 -0.0050 -0.0164 159 PHE A CE2
+1325 C CZ . PHE A 159 ? 0.1816 0.1420 0.1428 -0.0146 -0.0111 -0.0145 159 PHE A CZ
+1326 N N . CYS A 160 ? 0.1774 0.1596 0.1544 -0.0056 -0.0096 -0.0132 160 CYS A N
+1327 C CA . CYS A 160 ? 0.1816 0.1679 0.1634 -0.0042 -0.0104 -0.0118 160 CYS A CA
+1328 C C . CYS A 160 ? 0.1752 0.1668 0.1604 -0.0030 -0.0148 -0.0103 160 CYS A C
+1329 O O . CYS A 160 ? 0.1811 0.1751 0.1700 -0.0023 -0.0161 -0.0089 160 CYS A O
+1330 C CB . CYS A 160 ? 0.2017 0.1866 0.1789 -0.0058 -0.0105 -0.0128 160 CYS A CB
+1331 S SG . CYS A 160 ? 0.2072 0.1925 0.1776 -0.0081 -0.0147 -0.0136 160 CYS A SG
+1332 N N . TYR A 161 ? 0.1606 0.1533 0.1436 -0.0029 -0.0171 -0.0103 161 TYR A N
+1333 C CA . TYR A 161 ? 0.1578 0.1535 0.1414 -0.0014 -0.0205 -0.0090 161 TYR A CA
+1334 C C . TYR A 161 ? 0.1479 0.1452 0.1326 -0.0001 -0.0212 -0.0080 161 TYR A C
+1335 O O . TYR A 161 ? 0.1466 0.1431 0.1302 -0.0010 -0.0204 -0.0081 161 TYR A O
+1336 C CB . TYR A 161 ? 0.1484 0.1439 0.1270 -0.0019 -0.0224 -0.0094 161 TYR A CB
+1337 C CG . TYR A 161 ? 0.1499 0.1462 0.1268 0.0001 -0.0248 -0.0083 161 TYR A CG
+1338 C CD1 . TYR A 161 ? 0.1642 0.1594 0.1405 0.0004 -0.0266 -0.0082 161 TYR A CD1
+1339 C CD2 . TYR A 161 ? 0.1577 0.1549 0.1328 0.0015 -0.0253 -0.0070 161 TYR A CD2
+1340 C CE1 . TYR A 161 ? 0.1733 0.1666 0.1453 0.0020 -0.0286 -0.0076 161 TYR A CE1
+1341 C CE2 . TYR A 161 ? 0.1680 0.1641 0.1399 0.0039 -0.0263 -0.0060 161 TYR A CE2
+1342 C CZ . TYR A 161 ? 0.1717 0.1649 0.1409 0.0041 -0.0279 -0.0067 161 TYR A CZ
+1343 O OH . TYR A 161 ? 0.1797 0.1693 0.1430 0.0063 -0.0287 -0.0061 161 TYR A OH
+1344 N N . MET A 162 ? 0.1349 0.1341 0.1214 0.0016 -0.0230 -0.0066 162 MET A N
+1345 C CA . MET A 162 ? 0.1393 0.1402 0.1261 0.0032 -0.0238 -0.0051 162 MET A CA
+1346 C C . MET A 162 ? 0.1416 0.1418 0.1238 0.0049 -0.0260 -0.0044 162 MET A C
+1347 O O . MET A 162 ? 0.1424 0.1411 0.1235 0.0045 -0.0277 -0.0045 162 MET A O
+1348 C CB . MET A 162 ? 0.1523 0.1551 0.1451 0.0037 -0.0230 -0.0039 162 MET A CB
+1349 C CG . MET A 162 ? 0.1644 0.1693 0.1574 0.0056 -0.0240 -0.0021 162 MET A CG
+1350 S SD . MET A 162 ? 0.1893 0.1969 0.1903 0.0060 -0.0227 -0.0004 162 MET A SD
+1351 C CE . MET A 162 ? 0.2042 0.2095 0.2055 0.0044 -0.0201 -0.0018 162 MET A CE
+1352 N N . HIS A 163 ? 0.1442 0.1446 0.1233 0.0066 -0.0259 -0.0033 163 HIS A N
+1353 C CA . HIS A 163 ? 0.1463 0.1439 0.1192 0.0088 -0.0267 -0.0027 163 HIS A CA
+1354 C C . HIS A 163 ? 0.1486 0.1451 0.1197 0.0103 -0.0278 -0.0017 163 HIS A C
+1355 O O . HIS A 163 ? 0.1525 0.1519 0.1271 0.0113 -0.0271 -0.0001 163 HIS A O
+1356 C CB . HIS A 163 ? 0.1596 0.1579 0.1309 0.0107 -0.0252 -0.0006 163 HIS A CB
+1357 C CG . HIS A 163 ? 0.1737 0.1674 0.1376 0.0134 -0.0246 -0.0001 163 HIS A CG
+1358 N ND1 . HIS A 163 ? 0.1932 0.1824 0.1522 0.0125 -0.0257 -0.0021 163 HIS A ND1
+1359 C CD2 . HIS A 163 ? 0.1884 0.1803 0.1484 0.0172 -0.0229 0.0023 163 HIS A CD2
+1360 C CE1 . HIS A 163 ? 0.2062 0.1900 0.1576 0.0155 -0.0245 -0.0012 163 HIS A CE1
+1361 N NE2 . HIS A 163 ? 0.2005 0.1855 0.1519 0.0186 -0.0224 0.0014 163 HIS A NE2
+1362 N N . HIS A 164 ? 0.1504 0.1420 0.1151 0.0102 -0.0297 -0.0023 164 HIS A N
+1363 C CA . HIS A 164 ? 0.1691 0.1581 0.1297 0.0109 -0.0315 -0.0012 164 HIS A CA
+1364 C C . HIS A 164 ? 0.1951 0.1761 0.1434 0.0131 -0.0314 -0.0013 164 HIS A C
+1365 O O . HIS A 164 ? 0.2104 0.1892 0.1541 0.0150 -0.0310 -0.0001 164 HIS A O
+1366 C CB . HIS A 164 ? 0.1722 0.1610 0.1352 0.0075 -0.0351 -0.0010 164 HIS A CB
+1367 C CG . HIS A 164 ? 0.1532 0.1487 0.1278 0.0062 -0.0345 0.0001 164 HIS A CG
+1368 N ND1 . HIS A 164 ? 0.1547 0.1526 0.1337 0.0053 -0.0361 0.0025 164 HIS A ND1
+1369 C CD2 . HIS A 164 ? 0.1520 0.1510 0.1338 0.0054 -0.0321 -0.0006 164 HIS A CD2
+1370 C CE1 . HIS A 164 ? 0.1538 0.1568 0.1431 0.0046 -0.0342 0.0033 164 HIS A CE1
+1371 N NE2 . HIS A 164 ? 0.1584 0.1614 0.1487 0.0047 -0.0316 0.0011 164 HIS A NE2
+1372 N N A MET A 165 ? 0.2107 0.1865 0.1532 0.0126 -0.0317 -0.0029 165 MET A N
+1373 N N B MET A 165 ? 0.1993 0.1751 0.1418 0.0126 -0.0317 -0.0029 165 MET A N
+1374 C CA A MET A 165 ? 0.2385 0.2048 0.1679 0.0154 -0.0305 -0.0030 165 MET A CA
+1375 C CA B MET A 165 ? 0.2125 0.1782 0.1414 0.0148 -0.0313 -0.0032 165 MET A CA
+1376 C C A MET A 165 ? 0.2389 0.2011 0.1640 0.0169 -0.0281 -0.0037 165 MET A C
+1377 C C B MET A 165 ? 0.2261 0.1882 0.1511 0.0168 -0.0283 -0.0038 165 MET A C
+1378 O O A MET A 165 ? 0.2340 0.1991 0.1642 0.0146 -0.0292 -0.0048 165 MET A O
+1379 O O B MET A 165 ? 0.2205 0.1856 0.1506 0.0147 -0.0292 -0.0048 165 MET A O
+1380 C CB A MET A 165 ? 0.2700 0.2275 0.1892 0.0129 -0.0348 -0.0039 165 MET A CB
+1381 C CB B MET A 165 ? 0.2153 0.1739 0.1371 0.0111 -0.0364 -0.0044 165 MET A CB
+1382 C CG A MET A 165 ? 0.3156 0.2749 0.2397 0.0085 -0.0389 -0.0047 165 MET A CG
+1383 C CG B MET A 165 ? 0.2179 0.1802 0.1450 0.0075 -0.0407 -0.0030 165 MET A CG
+1384 S SD A MET A 165 ? 0.4189 0.3763 0.3410 0.0048 -0.0446 -0.0030 165 MET A SD
+1385 S SD B MET A 165 ? 0.2343 0.1928 0.1536 0.0091 -0.0411 -0.0013 165 MET A SD
+1386 C CE A MET A 165 ? 0.4248 0.3833 0.3446 0.0084 -0.0417 -0.0014 165 MET A CE
+1387 C CE B MET A 165 ? 0.2937 0.2357 0.1926 0.0073 -0.0447 -0.0026 165 MET A CE
+1388 N N . GLU A 166 ? 0.2493 0.2015 0.1619 0.0199 -0.0262 -0.0036 166 GLU A N
+1389 C CA . GLU A 166 ? 0.2711 0.2172 0.1777 0.0221 -0.0233 -0.0039 166 GLU A CA
+1390 C C . GLU A 166 ? 0.3063 0.2383 0.1974 0.0209 -0.0257 -0.0062 166 GLU A C
+1391 O O . GLU A 166 ? 0.3201 0.2445 0.2007 0.0219 -0.0259 -0.0061 166 GLU A O
+1392 C CB . GLU A 166 ? 0.2977 0.2430 0.2027 0.0279 -0.0169 -0.0007 166 GLU A CB
+1393 C CG . GLU A 166 ? 0.3512 0.2905 0.2515 0.0306 -0.0131 -0.0001 166 GLU A CG
+1394 C CD . GLU A 166 ? 0.4030 0.3466 0.3083 0.0360 -0.0068 0.0049 166 GLU A CD
+1395 O OE1 . GLU A 166 ? 0.4265 0.3640 0.3240 0.0405 -0.0028 0.0068 166 GLU A OE1
+1396 O OE2 . GLU A 166 ? 0.3872 0.3407 0.3047 0.0354 -0.0062 0.0075 166 GLU A OE2
+1397 N N . LEU A 167 ? 0.3244 0.2526 0.2134 0.0184 -0.0279 -0.0079 167 LEU A N
+1398 C CA . LEU A 167 ? 0.3661 0.2796 0.2395 0.0166 -0.0309 -0.0100 167 LEU A CA
+1399 C C . LEU A 167 ? 0.4043 0.3052 0.2639 0.0220 -0.0247 -0.0099 167 LEU A C
+1400 O O . LEU A 167 ? 0.3997 0.3053 0.2653 0.0264 -0.0187 -0.0078 167 LEU A O
+1401 C CB . LEU A 167 ? 0.3754 0.2902 0.2534 0.0124 -0.0348 -0.0113 167 LEU A CB
+1402 C CG . LEU A 167 ? 0.4016 0.3291 0.2946 0.0079 -0.0394 -0.0107 167 LEU A CG
+1403 C CD1 . LEU A 167 ? 0.4176 0.3442 0.3127 0.0040 -0.0432 -0.0114 167 LEU A CD1
+1404 C CD2 . LEU A 167 ? 0.4117 0.3399 0.3045 0.0050 -0.0439 -0.0097 167 LEU A CD2
+1405 N N . PRO A 168 ? 0.4393 0.3232 0.2800 0.0214 -0.0261 -0.0117 168 PRO A N
+1406 C CA . PRO A 168 ? 0.4669 0.3364 0.2926 0.0271 -0.0190 -0.0117 168 PRO A CA
+1407 C C . PRO A 168 ? 0.4820 0.3517 0.3119 0.0298 -0.0144 -0.0111 168 PRO A C
+1408 O O . PRO A 168 ? 0.5059 0.3678 0.3287 0.0360 -0.0067 -0.0095 168 PRO A O
+1409 C CB . PRO A 168 ? 0.4906 0.3403 0.2940 0.0240 -0.0231 -0.0145 168 PRO A CB
+1410 C CG . PRO A 168 ? 0.4903 0.3464 0.2981 0.0179 -0.0313 -0.0145 168 PRO A CG
+1411 C CD . PRO A 168 ? 0.4489 0.3251 0.2801 0.0155 -0.0339 -0.0133 168 PRO A CD
+1412 N N . THR A 169 ? 0.4686 0.3473 0.3103 0.0257 -0.0187 -0.0118 169 THR A N
+1413 C CA . THR A 169 ? 0.4668 0.3475 0.3142 0.0278 -0.0149 -0.0108 169 THR A CA
+1414 C C . THR A 169 ? 0.4478 0.3455 0.3136 0.0302 -0.0111 -0.0070 169 THR A C
+1415 O O . THR A 169 ? 0.4469 0.3484 0.3194 0.0311 -0.0089 -0.0055 169 THR A O
+1416 C CB . THR A 169 ? 0.4914 0.3711 0.3402 0.0222 -0.0211 -0.0131 169 THR A CB
+1417 O OG1 . THR A 169 ? 0.4986 0.3909 0.3595 0.0169 -0.0276 -0.0134 169 THR A OG1
+1418 C CG2 . THR A 169 ? 0.5117 0.3714 0.3405 0.0203 -0.0239 -0.0159 169 THR A CG2
+1419 N N . GLY A 170 ? 0.4288 0.3363 0.3024 0.0310 -0.0107 -0.0052 170 GLY A N
+1420 C CA . GLY A 170 ? 0.4084 0.3306 0.2979 0.0327 -0.0078 -0.0012 170 GLY A CA
+1421 C C . GLY A 170 ? 0.3825 0.3184 0.2863 0.0276 -0.0126 -0.0018 170 GLY A C
+1422 O O . GLY A 170 ? 0.3849 0.3314 0.3003 0.0280 -0.0110 0.0014 170 GLY A O
+1423 N N . VAL A 171 ? 0.3537 0.2884 0.2562 0.0226 -0.0185 -0.0054 171 VAL A N
+1424 C CA . VAL A 171 ? 0.3148 0.2609 0.2295 0.0182 -0.0223 -0.0060 171 VAL A CA
+1425 C C . VAL A 171 ? 0.2636 0.2147 0.1821 0.0166 -0.0248 -0.0064 171 VAL A C
+1426 O O . VAL A 171 ? 0.2655 0.2109 0.1765 0.0180 -0.0248 -0.0066 171 VAL A O
+1427 C CB . VAL A 171 ? 0.3351 0.2792 0.2497 0.0143 -0.0262 -0.0082 171 VAL A CB
+1428 C CG1 . VAL A 171 ? 0.3511 0.2915 0.2636 0.0161 -0.0234 -0.0074 171 VAL A CG1
+1429 C CG2 . VAL A 171 ? 0.3457 0.2805 0.2507 0.0118 -0.0307 -0.0104 171 VAL A CG2
+1430 N N . HIS A 172 ? 0.2320 0.1932 0.1615 0.0137 -0.0265 -0.0064 172 HIS A N
+1431 C CA . HIS A 172 ? 0.2098 0.1766 0.1447 0.0127 -0.0277 -0.0062 172 HIS A CA
+1432 C C . HIS A 172 ? 0.2010 0.1704 0.1405 0.0086 -0.0317 -0.0076 172 HIS A C
+1433 O O . HIS A 172 ? 0.2016 0.1725 0.1443 0.0062 -0.0330 -0.0084 172 HIS A O
+1434 C CB . HIS A 172 ? 0.1986 0.1740 0.1423 0.0134 -0.0251 -0.0041 172 HIS A CB
+1435 C CG . HIS A 172 ? 0.1979 0.1719 0.1392 0.0177 -0.0211 -0.0010 172 HIS A CG
+1436 N ND1 . HIS A 172 ? 0.2129 0.1892 0.1572 0.0184 -0.0190 0.0013 172 HIS A ND1
+1437 C CD2 . HIS A 172 ? 0.2140 0.1836 0.1495 0.0216 -0.0186 0.0006 172 HIS A CD2
+1438 C CE1 . HIS A 172 ? 0.2212 0.1955 0.1633 0.0229 -0.0150 0.0048 172 HIS A CE1
+1439 N NE2 . HIS A 172 ? 0.2297 0.1995 0.1659 0.0252 -0.0143 0.0044 172 HIS A NE2
+1440 N N . ALA A 173 ? 0.1934 0.1642 0.1343 0.0080 -0.0331 -0.0072 173 ALA A N
+1441 C CA . ALA A 173 ? 0.1885 0.1623 0.1353 0.0046 -0.0364 -0.0072 173 ALA A CA
+1442 C C . ALA A 173 ? 0.1771 0.1575 0.1317 0.0048 -0.0352 -0.0061 173 ALA A C
+1443 O O . ALA A 173 ? 0.1781 0.1590 0.1312 0.0072 -0.0336 -0.0053 173 ALA A O
+1444 C CB . ALA A 173 ? 0.1967 0.1635 0.1362 0.0027 -0.0408 -0.0069 173 ALA A CB
+1445 N N . GLY A 174 ? 0.1663 0.1516 0.1295 0.0026 -0.0356 -0.0057 174 GLY A N
+1446 C CA . GLY A 174 ? 0.1590 0.1496 0.1298 0.0028 -0.0340 -0.0047 174 GLY A CA
+1447 C C . GLY A 174 ? 0.1505 0.1445 0.1298 0.0006 -0.0341 -0.0036 174 GLY A C
+1448 O O . GLY A 174 ? 0.1524 0.1453 0.1323 -0.0012 -0.0363 -0.0029 174 GLY A O
+1449 N N . THR A 175 ? 0.1423 0.1401 0.1283 0.0010 -0.0314 -0.0030 175 THR A N
+1450 C CA . THR A 175 ? 0.1365 0.1372 0.1314 -0.0001 -0.0302 -0.0010 175 THR A CA
+1451 C C . THR A 175 ? 0.1378 0.1390 0.1355 0.0001 -0.0256 -0.0025 175 THR A C
+1452 O O . THR A 175 ? 0.1427 0.1426 0.1360 0.0006 -0.0241 -0.0047 175 THR A O
+1453 C CB . THR A 175 ? 0.1438 0.1473 0.1442 0.0003 -0.0307 0.0017 175 THR A CB
+1454 O OG1 . THR A 175 ? 0.1485 0.1530 0.1492 0.0019 -0.0277 0.0004 175 THR A OG1
+1455 C CG2 . THR A 175 ? 0.1331 0.1350 0.1289 -0.0004 -0.0355 0.0032 175 THR A CG2
+1456 N N . ASP A 176 ? 0.1357 0.1384 0.1409 -0.0003 -0.0231 -0.0006 176 ASP A N
+1457 C CA . ASP A 176 ? 0.1402 0.1414 0.1467 0.0002 -0.0177 -0.0019 176 ASP A CA
+1458 C C . ASP A 176 ? 0.1491 0.1512 0.1593 0.0014 -0.0159 -0.0011 176 ASP A C
+1459 O O . ASP A 176 ? 0.1476 0.1524 0.1594 0.0017 -0.0190 0.0005 176 ASP A O
+1460 C CB . ASP A 176 ? 0.1529 0.1542 0.1652 0.0002 -0.0144 0.0002 176 ASP A CB
+1461 C CG . ASP A 176 ? 0.1714 0.1768 0.1944 0.0005 -0.0146 0.0055 176 ASP A CG
+1462 O OD1 . ASP A 176 ? 0.1481 0.1558 0.1743 0.0008 -0.0165 0.0072 176 ASP A OD1
+1463 O OD2 . ASP A 176 ? 0.1979 0.2047 0.2269 0.0004 -0.0132 0.0086 176 ASP A OD2
+1464 N N . LEU A 177 ? 0.1557 0.1549 0.1667 0.0018 -0.0108 -0.0021 177 LEU A N
+1465 C CA . LEU A 177 ? 0.1647 0.1641 0.1791 0.0028 -0.0091 -0.0014 177 LEU A CA
+1466 C C . LEU A 177 ? 0.1765 0.1794 0.2020 0.0040 -0.0071 0.0031 177 LEU A C
+1467 O O . LEU A 177 ? 0.1817 0.1855 0.2115 0.0049 -0.0057 0.0043 177 LEU A O
+1468 C CB . LEU A 177 ? 0.1687 0.1618 0.1774 0.0023 -0.0052 -0.0044 177 LEU A CB
+1469 C CG . LEU A 177 ? 0.1860 0.1781 0.1872 0.0009 -0.0085 -0.0067 177 LEU A CG
+1470 C CD1 . LEU A 177 ? 0.1940 0.1903 0.1990 0.0020 -0.0110 -0.0050 177 LEU A CD1
+1471 C CD2 . LEU A 177 ? 0.2019 0.1950 0.1976 -0.0001 -0.0120 -0.0078 177 LEU A CD2
+1472 N N . GLU A 178 ? 0.1687 0.1743 0.1999 0.0038 -0.0076 0.0064 178 GLU A N
+1473 C CA . GLU A 178 ? 0.1564 0.1671 0.1995 0.0043 -0.0076 0.0123 178 GLU A CA
+1474 C C . GLU A 178 ? 0.1508 0.1657 0.1938 0.0026 -0.0152 0.0143 178 GLU A C
+1475 O O . GLU A 178 ? 0.1516 0.1712 0.2037 0.0020 -0.0171 0.0198 178 GLU A O
+1476 C CB . GLU A 178 ? 0.1777 0.1894 0.2282 0.0047 -0.0044 0.0162 178 GLU A CB
+1477 C CG . GLU A 178 ? 0.2469 0.2527 0.2963 0.0068 0.0043 0.0145 178 GLU A CG
+1478 C CD . GLU A 178 ? 0.3511 0.3573 0.4079 0.0081 0.0092 0.0189 178 GLU A CD
+1479 O OE1 . GLU A 178 ? 0.3485 0.3603 0.4119 0.0068 0.0049 0.0235 178 GLU A OE1
+1480 O OE2 . GLU A 178 ? 0.4024 0.4025 0.4580 0.0103 0.0175 0.0182 178 GLU A OE2
+1481 N N . GLY A 179 ? 0.1512 0.1640 0.1836 0.0018 -0.0194 0.0105 179 GLY A N
+1482 C CA . GLY A 179 ? 0.1460 0.1601 0.1751 0.0006 -0.0257 0.0117 179 GLY A CA
+1483 C C . GLY A 179 ? 0.1411 0.1548 0.1686 -0.0018 -0.0306 0.0136 179 GLY A C
+1484 O O . GLY A 179 ? 0.1464 0.1596 0.1702 -0.0034 -0.0361 0.0151 179 GLY A O
+1485 N N . ASN A 180 ? 0.1351 0.1482 0.1645 -0.0022 -0.0289 0.0137 180 ASN A N
+1486 C CA . ASN A 180 ? 0.1386 0.1510 0.1668 -0.0047 -0.0339 0.0158 180 ASN A CA
+1487 C C . ASN A 180 ? 0.1367 0.1440 0.1525 -0.0048 -0.0357 0.0106 180 ASN A C
+1488 O O . ASN A 180 ? 0.1297 0.1355 0.1425 -0.0035 -0.0318 0.0071 180 ASN A O
+1489 C CB . ASN A 180 ? 0.1521 0.1674 0.1905 -0.0049 -0.0310 0.0197 180 ASN A CB
+1490 C CG . ASN A 180 ? 0.1866 0.2074 0.2390 -0.0049 -0.0296 0.0267 180 ASN A CG
+1491 O OD1 . ASN A 180 ? 0.2108 0.2333 0.2715 -0.0025 -0.0227 0.0285 180 ASN A OD1
+1492 N ND2 . ASN A 180 ? 0.1778 0.2009 0.2326 -0.0074 -0.0358 0.0310 180 ASN A ND2
+1493 N N . PHE A 181 ? 0.1401 0.1438 0.1479 -0.0066 -0.0415 0.0105 181 PHE A N
+1494 C CA . PHE A 181 ? 0.1528 0.1509 0.1490 -0.0063 -0.0427 0.0062 181 PHE A CA
+1495 C C . PHE A 181 ? 0.1580 0.1562 0.1561 -0.0071 -0.0419 0.0060 181 PHE A C
+1496 O O . PHE A 181 ? 0.1538 0.1548 0.1602 -0.0089 -0.0430 0.0100 181 PHE A O
+1497 C CB . PHE A 181 ? 0.1623 0.1544 0.1484 -0.0081 -0.0487 0.0065 181 PHE A CB
+1498 C CG . PHE A 181 ? 0.1681 0.1570 0.1456 -0.0060 -0.0481 0.0043 181 PHE A CG
+1499 C CD1 . PHE A 181 ? 0.1711 0.1620 0.1510 -0.0062 -0.0494 0.0068 181 PHE A CD1
+1500 C CD2 . PHE A 181 ? 0.1768 0.1609 0.1444 -0.0036 -0.0461 0.0005 181 PHE A CD2
+1501 C CE1 . PHE A 181 ? 0.1778 0.1658 0.1498 -0.0040 -0.0486 0.0052 181 PHE A CE1
+1502 C CE2 . PHE A 181 ? 0.1865 0.1678 0.1470 -0.0011 -0.0449 -0.0005 181 PHE A CE2
+1503 C CZ . PHE A 181 ? 0.1834 0.1666 0.1458 -0.0012 -0.0461 0.0017 181 PHE A CZ
+1504 N N . TYR A 182 ? 0.1537 0.1491 0.1449 -0.0058 -0.0398 0.0019 182 TYR A N
+1505 C CA . TYR A 182 ? 0.1648 0.1594 0.1557 -0.0067 -0.0400 0.0014 182 TYR A CA
+1506 C C . TYR A 182 ? 0.1812 0.1704 0.1651 -0.0089 -0.0460 0.0020 182 TYR A C
+1507 O O . TYR A 182 ? 0.1923 0.1761 0.1665 -0.0083 -0.0478 0.0002 182 TYR A O
+1508 C CB . TYR A 182 ? 0.1636 0.1569 0.1491 -0.0050 -0.0364 -0.0026 182 TYR A CB
+1509 C CG . TYR A 182 ? 0.1610 0.1576 0.1518 -0.0041 -0.0312 -0.0031 182 TYR A CG
+1510 C CD1 . TYR A 182 ? 0.1643 0.1626 0.1605 -0.0046 -0.0286 -0.0020 182 TYR A CD1
+1511 C CD2 . TYR A 182 ? 0.1635 0.1606 0.1534 -0.0027 -0.0287 -0.0044 182 TYR A CD2
+1512 C CE1 . TYR A 182 ? 0.1644 0.1631 0.1626 -0.0038 -0.0232 -0.0028 182 TYR A CE1
+1513 C CE2 . TYR A 182 ? 0.1670 0.1648 0.1595 -0.0023 -0.0242 -0.0052 182 TYR A CE2
+1514 C CZ . TYR A 182 ? 0.1702 0.1681 0.1661 -0.0029 -0.0212 -0.0046 182 TYR A CZ
+1515 O OH . TYR A 182 ? 0.1692 0.1653 0.1651 -0.0025 -0.0162 -0.0057 182 TYR A OH
+1516 N N . GLY A 183 ? 0.1830 0.1729 0.1714 -0.0113 -0.0488 0.0049 183 GLY A N
+1517 C CA . GLY A 183 ? 0.2017 0.1853 0.1830 -0.0142 -0.0551 0.0058 183 GLY A CA
+1518 C C . GLY A 183 ? 0.2106 0.1916 0.1898 -0.0167 -0.0605 0.0087 183 GLY A C
+1519 O O . GLY A 183 ? 0.2050 0.1914 0.1923 -0.0166 -0.0597 0.0118 183 GLY A O
+1520 N N . PRO A 184 ? 0.2194 0.1910 0.1864 -0.0190 -0.0659 0.0079 184 PRO A N
+1521 C CA . PRO A 184 ? 0.2234 0.1908 0.1861 -0.0227 -0.0724 0.0112 184 PRO A CA
+1522 C C . PRO A 184 ? 0.2274 0.1897 0.1796 -0.0209 -0.0716 0.0086 184 PRO A C
+1523 O O . PRO A 184 ? 0.2463 0.2028 0.1912 -0.0241 -0.0773 0.0107 184 PRO A O
+1524 C CB . PRO A 184 ? 0.2447 0.2017 0.1965 -0.0264 -0.0787 0.0110 184 PRO A CB
+1525 C CG . PRO A 184 ? 0.2552 0.2077 0.1988 -0.0224 -0.0734 0.0051 184 PRO A CG
+1526 C CD . PRO A 184 ? 0.2274 0.1912 0.1842 -0.0190 -0.0667 0.0046 184 PRO A CD
+1527 N N . PHE A 185 ? 0.2187 0.1827 0.1693 -0.0159 -0.0649 0.0045 185 PHE A N
+1528 C CA . PHE A 185 ? 0.2245 0.1836 0.1649 -0.0134 -0.0632 0.0022 185 PHE A CA
+1529 C C . PHE A 185 ? 0.2280 0.1925 0.1746 -0.0138 -0.0639 0.0052 185 PHE A C
+1530 O O . PHE A 185 ? 0.2167 0.1908 0.1780 -0.0146 -0.0631 0.0084 185 PHE A O
+1531 C CB . PHE A 185 ? 0.2196 0.1798 0.1582 -0.0083 -0.0562 -0.0017 185 PHE A CB
+1532 C CG . PHE A 185 ? 0.2271 0.1816 0.1595 -0.0080 -0.0557 -0.0041 185 PHE A CG
+1533 C CD1 . PHE A 185 ? 0.2458 0.1877 0.1632 -0.0089 -0.0586 -0.0054 185 PHE A CD1
+1534 C CD2 . PHE A 185 ? 0.2299 0.1909 0.1710 -0.0072 -0.0527 -0.0047 185 PHE A CD2
+1535 C CE1 . PHE A 185 ? 0.2512 0.1878 0.1637 -0.0087 -0.0581 -0.0071 185 PHE A CE1
+1536 C CE2 . PHE A 185 ? 0.2336 0.1901 0.1701 -0.0073 -0.0526 -0.0062 185 PHE A CE2
+1537 C CZ . PHE A 185 ? 0.2389 0.1835 0.1617 -0.0078 -0.0552 -0.0074 185 PHE A CZ
+1538 N N . VAL A 186 ? 0.2393 0.1970 0.1744 -0.0134 -0.0652 0.0045 186 VAL A N
+1539 C CA . VAL A 186 ? 0.2422 0.2041 0.1814 -0.0139 -0.0663 0.0074 186 VAL A CA
+1540 C C . VAL A 186 ? 0.2486 0.2085 0.1806 -0.0092 -0.0614 0.0047 186 VAL A C
+1541 O O . VAL A 186 ? 0.2669 0.2189 0.1870 -0.0063 -0.0588 0.0013 186 VAL A O
+1542 C CB . VAL A 186 ? 0.2610 0.2167 0.1934 -0.0196 -0.0747 0.0112 186 VAL A CB
+1543 C CG1 . VAL A 186 ? 0.2715 0.2320 0.2153 -0.0245 -0.0797 0.0160 186 VAL A CG1
+1544 C CG2 . VAL A 186 ? 0.2830 0.2224 0.1930 -0.0204 -0.0773 0.0080 186 VAL A CG2
+1545 N N . ASP A 187 ? 0.2285 0.1956 0.1684 -0.0081 -0.0601 0.0069 187 ASP A N
+1546 C CA . ASP A 187 ? 0.2303 0.1966 0.1651 -0.0037 -0.0557 0.0053 187 ASP A CA
+1547 C C . ASP A 187 ? 0.2549 0.2120 0.1752 -0.0047 -0.0590 0.0061 187 ASP A C
+1548 O O . ASP A 187 ? 0.2531 0.2136 0.1759 -0.0047 -0.0597 0.0085 187 ASP A O
+1549 C CB . ASP A 187 ? 0.2152 0.1930 0.1649 -0.0016 -0.0519 0.0067 187 ASP A CB
+1550 C CG . ASP A 187 ? 0.2089 0.1944 0.1717 -0.0048 -0.0548 0.0111 187 ASP A CG
+1551 O OD1 . ASP A 187 ? 0.2092 0.1923 0.1709 -0.0092 -0.0606 0.0141 187 ASP A OD1
+1552 O OD2 . ASP A 187 ? 0.1961 0.1897 0.1704 -0.0029 -0.0512 0.0121 187 ASP A OD2
+1553 N N . ARG A 188 ? 0.2821 0.2263 0.1859 -0.0057 -0.0611 0.0040 188 ARG A N
+1554 C CA . ARG A 188 ? 0.3215 0.2525 0.2064 -0.0070 -0.0642 0.0040 188 ARG A CA
+1555 C C . ARG A 188 ? 0.3521 0.2702 0.2206 -0.0035 -0.0603 0.0000 188 ARG A C
+1556 O O . ARG A 188 ? 0.3475 0.2648 0.2178 -0.0036 -0.0596 -0.0019 188 ARG A O
+1557 C CB . ARG A 188 ? 0.3562 0.2825 0.2376 -0.0146 -0.0735 0.0070 188 ARG A CB
+1558 C CG . ARG A 188 ? 0.4405 0.3529 0.3017 -0.0173 -0.0780 0.0076 188 ARG A CG
+1559 C CD . ARG A 188 ? 0.5164 0.4237 0.3738 -0.0260 -0.0885 0.0114 188 ARG A CD
+1560 N NE . ARG A 188 ? 0.5940 0.4813 0.4246 -0.0288 -0.0924 0.0099 188 ARG A NE
+1561 C CZ . ARG A 188 ? 0.6437 0.5225 0.4646 -0.0369 -0.1024 0.0134 188 ARG A CZ
+1562 N NH1 . ARG A 188 ? 0.6388 0.5290 0.4771 -0.0431 -0.1096 0.0195 188 ARG A NH1
+1563 N NH2 . ARG A 188 ? 0.6649 0.5232 0.4584 -0.0392 -0.1053 0.0113 188 ARG A NH2
+1564 N N . GLN A 189 ? 0.3850 0.2930 0.2379 -0.0002 -0.0573 -0.0009 189 GLN A N
+1565 C CA . GLN A 189 ? 0.4227 0.3172 0.2593 0.0041 -0.0522 -0.0040 189 GLN A CA
+1566 C C . GLN A 189 ? 0.4583 0.3352 0.2753 -0.0010 -0.0582 -0.0054 189 GLN A C
+1567 O O . GLN A 189 ? 0.4780 0.3414 0.2765 -0.0022 -0.0601 -0.0054 189 GLN A O
+1568 C CB . GLN A 189 ? 0.4560 0.3469 0.2846 0.0103 -0.0454 -0.0036 189 GLN A CB
+1569 C CG . GLN A 189 ? 0.5266 0.4059 0.3421 0.0164 -0.0378 -0.0056 189 GLN A CG
+1570 C CD . GLN A 189 ? 0.6110 0.4864 0.4185 0.0225 -0.0312 -0.0040 189 GLN A CD
+1571 O OE1 . GLN A 189 ? 0.6280 0.5166 0.4490 0.0248 -0.0292 -0.0013 189 GLN A OE1
+1572 N NE2 . GLN A 189 ? 0.6387 0.4950 0.4234 0.0254 -0.0275 -0.0054 189 GLN A NE2
+1573 N N . THR A 190 ? 0.4705 0.3476 0.2918 -0.0045 -0.0618 -0.0063 190 THR A N
+1574 C CA . THR A 190 ? 0.5034 0.3648 0.3086 -0.0104 -0.0687 -0.0071 190 THR A CA
+1575 C C . THR A 190 ? 0.5160 0.3722 0.3190 -0.0089 -0.0662 -0.0100 190 THR A C
+1576 O O . THR A 190 ? 0.5161 0.3828 0.3322 -0.0039 -0.0597 -0.0107 190 THR A O
+1577 C CB . THR A 190 ? 0.5318 0.4010 0.3480 -0.0186 -0.0788 -0.0031 190 THR A CB
+1578 O OG1 . THR A 190 ? 0.5408 0.4293 0.3822 -0.0179 -0.0774 -0.0014 190 THR A OG1
+1579 C CG2 . THR A 190 ? 0.5465 0.4150 0.3586 -0.0220 -0.0835 0.0001 190 THR A CG2
+1580 N N . ALA A 191 ? 0.5262 0.3663 0.3131 -0.0138 -0.0719 -0.0112 191 ALA A N
+1581 C CA . ALA A 191 ? 0.5322 0.3675 0.3178 -0.0132 -0.0705 -0.0134 191 ALA A CA
+1582 C C . ALA A 191 ? 0.5178 0.3715 0.3276 -0.0162 -0.0740 -0.0110 191 ALA A C
+1583 O O . ALA A 191 ? 0.5351 0.3910 0.3496 -0.0232 -0.0828 -0.0080 191 ALA A O
+1584 C CB . ALA A 191 ? 0.5515 0.3644 0.3138 -0.0185 -0.0768 -0.0149 191 ALA A CB
+1585 N N . GLN A 192 ? 0.4838 0.3510 0.3093 -0.0110 -0.0671 -0.0115 192 GLN A N
+1586 C CA . GLN A 192 ? 0.4556 0.3388 0.3022 -0.0128 -0.0686 -0.0098 192 GLN A CA
+1587 C C . GLN A 192 ? 0.4553 0.3366 0.3017 -0.0092 -0.0634 -0.0122 192 GLN A C
+1588 O O . GLN A 192 ? 0.4729 0.3568 0.3204 -0.0031 -0.0556 -0.0134 192 GLN A O
+1589 C CB . GLN A 192 ? 0.4330 0.3339 0.2979 -0.0100 -0.0647 -0.0081 192 GLN A CB
+1590 C CG . GLN A 192 ? 0.4245 0.3272 0.2891 -0.0117 -0.0676 -0.0057 192 GLN A CG
+1591 C CD . GLN A 192 ? 0.3715 0.2920 0.2566 -0.0101 -0.0647 -0.0038 192 GLN A CD
+1592 O OE1 . GLN A 192 ? 0.3411 0.2712 0.2406 -0.0125 -0.0666 -0.0019 192 GLN A OE1
+1593 N NE2 . GLN A 192 ? 0.3545 0.2788 0.2407 -0.0057 -0.0597 -0.0041 192 GLN A NE2
+1594 N N . ALA A 193 ? 0.4362 0.3127 0.2810 -0.0129 -0.0677 -0.0124 193 ALA A N
+1595 C CA . ALA A 193 ? 0.4262 0.3013 0.2715 -0.0096 -0.0629 -0.0143 193 ALA A CA
+1596 C C . ALA A 193 ? 0.4005 0.2918 0.2661 -0.0109 -0.0634 -0.0126 193 ALA A C
+1597 O O . ALA A 193 ? 0.3993 0.2976 0.2745 -0.0157 -0.0693 -0.0099 193 ALA A O
+1598 C CB . ALA A 193 ? 0.4384 0.2947 0.2658 -0.0122 -0.0662 -0.0160 193 ALA A CB
+1599 N N . ALA A 194 ? 0.3784 0.2757 0.2506 -0.0066 -0.0571 -0.0136 194 ALA A N
+1600 C CA . ALA A 194 ? 0.3522 0.2633 0.2414 -0.0076 -0.0568 -0.0123 194 ALA A CA
+1601 C C . ALA A 194 ? 0.3308 0.2368 0.2184 -0.0108 -0.0606 -0.0122 194 ALA A C
+1602 O O . ALA A 194 ? 0.3411 0.2333 0.2150 -0.0104 -0.0607 -0.0139 194 ALA A O
+1603 C CB . ALA A 194 ? 0.3502 0.2696 0.2465 -0.0025 -0.0493 -0.0129 194 ALA A CB
+1604 N N . GLY A 195 ? 0.2987 0.2156 0.2004 -0.0136 -0.0632 -0.0100 195 GLY A N
+1605 C CA . GLY A 195 ? 0.2911 0.2060 0.1945 -0.0164 -0.0665 -0.0092 195 GLY A CA
+1606 C C . GLY A 195 ? 0.2800 0.1973 0.1857 -0.0127 -0.0606 -0.0108 195 GLY A C
+1607 O O . GLY A 195 ? 0.2772 0.1964 0.1819 -0.0082 -0.0544 -0.0122 195 GLY A O
+1608 N N . THR A 196 ? 0.2668 0.1859 0.1776 -0.0148 -0.0627 -0.0097 196 THR A N
+1609 C CA . THR A 196 ? 0.2699 0.1913 0.1834 -0.0121 -0.0581 -0.0105 196 THR A CA
+1610 C C . THR A 196 ? 0.2685 0.2034 0.1931 -0.0095 -0.0527 -0.0101 196 THR A C
+1611 O O . THR A 196 ? 0.2559 0.2007 0.1909 -0.0111 -0.0536 -0.0087 196 THR A O
+1612 C CB . THR A 196 ? 0.2861 0.2086 0.2049 -0.0155 -0.0621 -0.0088 196 THR A CB
+1613 O OG1 . THR A 196 ? 0.3079 0.2169 0.2157 -0.0191 -0.0684 -0.0087 196 THR A OG1
+1614 C CG2 . THR A 196 ? 0.2955 0.2193 0.2161 -0.0131 -0.0578 -0.0092 196 THR A CG2
+1615 N N . ASP A 197 ? 0.2743 0.2089 0.1966 -0.0054 -0.0470 -0.0110 197 ASP A N
+1616 C CA . ASP A 197 ? 0.2719 0.2186 0.2041 -0.0038 -0.0428 -0.0102 197 ASP A CA
+1617 C C . ASP A 197 ? 0.2617 0.2144 0.2013 -0.0050 -0.0423 -0.0090 197 ASP A C
+1618 O O . ASP A 197 ? 0.2930 0.2452 0.2321 -0.0030 -0.0392 -0.0083 197 ASP A O
+1619 C CB . ASP A 197 ? 0.2997 0.2457 0.2285 0.0004 -0.0377 -0.0102 197 ASP A CB
+1620 C CG . ASP A 197 ? 0.3365 0.2940 0.2744 0.0008 -0.0350 -0.0091 197 ASP A CG
+1621 O OD1 . ASP A 197 ? 0.2888 0.2537 0.2342 -0.0018 -0.0366 -0.0090 197 ASP A OD1
+1622 O OD2 . ASP A 197 ? 0.3987 0.3570 0.3357 0.0038 -0.0313 -0.0081 197 ASP A OD2
+1623 N N A THR A 198 ? 0.2387 0.1970 0.1855 -0.0081 -0.0454 -0.0081 198 THR A N
+1624 N N B THR A 198 ? 0.2362 0.1952 0.1834 -0.0080 -0.0451 -0.0081 198 THR A N
+1625 C CA A THR A 198 ? 0.2296 0.1938 0.1834 -0.0094 -0.0450 -0.0068 198 THR A CA
+1626 C CA B THR A 198 ? 0.2258 0.1911 0.1806 -0.0097 -0.0452 -0.0067 198 THR A CA
+1627 C C A THR A 198 ? 0.2161 0.1890 0.1751 -0.0084 -0.0407 -0.0063 198 THR A C
+1628 C C B THR A 198 ? 0.2140 0.1880 0.1741 -0.0088 -0.0409 -0.0063 198 THR A C
+1629 O O A THR A 198 ? 0.2153 0.1908 0.1743 -0.0073 -0.0386 -0.0069 198 THR A O
+1630 O O B THR A 198 ? 0.2128 0.1903 0.1740 -0.0081 -0.0390 -0.0068 198 THR A O
+1631 C CB A THR A 198 ? 0.2460 0.2133 0.2061 -0.0126 -0.0489 -0.0051 198 THR A CB
+1632 C CB B THR A 198 ? 0.2355 0.2043 0.1965 -0.0126 -0.0488 -0.0051 198 THR A CB
+1633 O OG1 A THR A 198 ? 0.2540 0.2270 0.2191 -0.0130 -0.0483 -0.0046 198 THR A OG1
+1634 O OG1 B THR A 198 ? 0.2486 0.2088 0.2041 -0.0145 -0.0540 -0.0048 198 THR A OG1
+1635 C CG2 A THR A 198 ? 0.2543 0.2123 0.2089 -0.0148 -0.0545 -0.0046 198 THR A CG2
+1636 C CG2 B THR A 198 ? 0.2360 0.2113 0.2051 -0.0142 -0.0487 -0.0032 198 THR A CG2
+1637 N N . THR A 199 ? 0.1998 0.1767 0.1627 -0.0091 -0.0398 -0.0051 199 THR A N
+1638 C CA . THR A 199 ? 0.1870 0.1712 0.1538 -0.0093 -0.0367 -0.0041 199 THR A CA
+1639 C C . THR A 199 ? 0.1754 0.1658 0.1475 -0.0115 -0.0366 -0.0039 199 THR A C
+1640 O O . THR A 199 ? 0.1801 0.1711 0.1555 -0.0128 -0.0384 -0.0031 199 THR A O
+1641 C CB . THR A 199 ? 0.2008 0.1857 0.1684 -0.0089 -0.0355 -0.0022 199 THR A CB
+1642 O OG1 . THR A 199 ? 0.2126 0.1907 0.1749 -0.0059 -0.0342 -0.0021 199 THR A OG1
+1643 C CG2 . THR A 199 ? 0.2025 0.1949 0.1736 -0.0100 -0.0333 -0.0004 199 THR A CG2
+1644 N N . ILE A 200 ? 0.1639 0.1580 0.1363 -0.0118 -0.0342 -0.0043 200 ILE A N
+1645 C CA . ILE A 200 ? 0.1650 0.1627 0.1402 -0.0134 -0.0327 -0.0044 200 ILE A CA
+1646 C C . ILE A 200 ? 0.1575 0.1587 0.1338 -0.0153 -0.0318 -0.0030 200 ILE A C
+1647 O O . ILE A 200 ? 0.1543 0.1573 0.1284 -0.0166 -0.0304 -0.0027 200 ILE A O
+1648 C CB . ILE A 200 ? 0.1682 0.1662 0.1412 -0.0132 -0.0306 -0.0057 200 ILE A CB
+1649 C CG1 . ILE A 200 ? 0.1744 0.1693 0.1460 -0.0112 -0.0317 -0.0067 200 ILE A CG1
+1650 C CG2 . ILE A 200 ? 0.1724 0.1717 0.1471 -0.0142 -0.0282 -0.0059 200 ILE A CG2
+1651 C CD1 . ILE A 200 ? 0.1923 0.1873 0.1614 -0.0105 -0.0302 -0.0073 200 ILE A CD1
+1652 N N . THR A 201 ? 0.1548 0.1570 0.1348 -0.0158 -0.0329 -0.0018 201 THR A N
+1653 C CA . THR A 201 ? 0.1566 0.1622 0.1383 -0.0175 -0.0324 -0.0001 201 THR A CA
+1654 C C . THR A 201 ? 0.1622 0.1698 0.1412 -0.0193 -0.0294 -0.0002 201 THR A C
+1655 O O . THR A 201 ? 0.1723 0.1817 0.1493 -0.0212 -0.0293 0.0008 201 THR A O
+1656 C CB . THR A 201 ? 0.1688 0.1753 0.1557 -0.0177 -0.0339 0.0016 201 THR A CB
+1657 O OG1 . THR A 201 ? 0.1778 0.1802 0.1650 -0.0168 -0.0373 0.0015 201 THR A OG1
+1658 C CG2 . THR A 201 ? 0.1775 0.1876 0.1668 -0.0192 -0.0336 0.0037 201 THR A CG2
+1659 N N . VAL A 202 ? 0.1512 0.1577 0.1297 -0.0189 -0.0270 -0.0012 202 VAL A N
+1660 C CA . VAL A 202 ? 0.1608 0.1665 0.1342 -0.0206 -0.0235 -0.0018 202 VAL A CA
+1661 C C . VAL A 202 ? 0.1642 0.1685 0.1313 -0.0225 -0.0241 -0.0028 202 VAL A C
+1662 O O . VAL A 202 ? 0.1653 0.1690 0.1273 -0.0253 -0.0233 -0.0023 202 VAL A O
+1663 C CB . VAL A 202 ? 0.1747 0.1781 0.1485 -0.0192 -0.0197 -0.0024 202 VAL A CB
+1664 C CG1 . VAL A 202 ? 0.1879 0.1889 0.1611 -0.0177 -0.0196 -0.0042 202 VAL A CG1
+1665 C CG2 . VAL A 202 ? 0.1887 0.1892 0.1558 -0.0207 -0.0153 -0.0028 202 VAL A CG2
+1666 N N . ASN A 203 ? 0.1651 0.1688 0.1328 -0.0211 -0.0257 -0.0035 203 ASN A N
+1667 C CA . ASN A 203 ? 0.1648 0.1681 0.1284 -0.0228 -0.0266 -0.0032 203 ASN A CA
+1668 C C . ASN A 203 ? 0.1626 0.1693 0.1276 -0.0244 -0.0287 -0.0002 203 ASN A C
+1669 O O . ASN A 203 ? 0.1657 0.1731 0.1272 -0.0277 -0.0295 0.0015 203 ASN A O
+1670 C CB . ASN A 203 ? 0.1660 0.1681 0.1308 -0.0203 -0.0272 -0.0042 203 ASN A CB
+1671 C CG . ASN A 203 ? 0.1764 0.1755 0.1397 -0.0193 -0.0251 -0.0065 203 ASN A CG
+1672 O OD1 . ASN A 203 ? 0.1717 0.1691 0.1335 -0.0200 -0.0225 -0.0074 203 ASN A OD1
+1673 N ND2 . ASN A 203 ? 0.1763 0.1746 0.1404 -0.0173 -0.0256 -0.0072 203 ASN A ND2
+1674 N N . VAL A 204 ? 0.1532 0.1617 0.1232 -0.0225 -0.0298 0.0010 204 VAL A N
+1675 C CA . VAL A 204 ? 0.1539 0.1657 0.1264 -0.0236 -0.0311 0.0045 204 VAL A CA
+1676 C C . VAL A 204 ? 0.1578 0.1719 0.1285 -0.0274 -0.0312 0.0060 204 VAL A C
+1677 O O . VAL A 204 ? 0.1647 0.1814 0.1347 -0.0304 -0.0325 0.0092 204 VAL A O
+1678 C CB . VAL A 204 ? 0.1605 0.1719 0.1374 -0.0207 -0.0318 0.0051 204 VAL A CB
+1679 C CG1 . VAL A 204 ? 0.1644 0.1793 0.1447 -0.0216 -0.0324 0.0092 204 VAL A CG1
+1680 C CG2 . VAL A 204 ? 0.1563 0.1636 0.1325 -0.0172 -0.0317 0.0037 204 VAL A CG2
+1681 N N . LEU A 205 ? 0.1529 0.1659 0.1227 -0.0275 -0.0297 0.0042 205 LEU A N
+1682 C CA . LEU A 205 ? 0.1534 0.1676 0.1201 -0.0309 -0.0291 0.0055 205 LEU A CA
+1683 C C . LEU A 205 ? 0.1627 0.1739 0.1206 -0.0346 -0.0288 0.0051 205 LEU A C
+1684 O O . LEU A 205 ? 0.1567 0.1691 0.1112 -0.0388 -0.0304 0.0076 205 LEU A O
+1685 C CB . LEU A 205 ? 0.1561 0.1693 0.1238 -0.0295 -0.0266 0.0043 205 LEU A CB
+1686 C CG . LEU A 205 ? 0.1609 0.1772 0.1370 -0.0272 -0.0280 0.0057 205 LEU A CG
+1687 C CD1 . LEU A 205 ? 0.1710 0.1866 0.1501 -0.0253 -0.0259 0.0052 205 LEU A CD1
+1688 C CD2 . LEU A 205 ? 0.1744 0.1949 0.1530 -0.0293 -0.0295 0.0089 205 LEU A CD2
+1689 N N . ALA A 206 ? 0.1654 0.1719 0.1192 -0.0337 -0.0273 0.0021 206 ALA A N
+1690 C CA . ALA A 206 ? 0.1774 0.1791 0.1214 -0.0376 -0.0273 0.0015 206 ALA A CA
+1691 C C . ALA A 206 ? 0.1821 0.1871 0.1269 -0.0409 -0.0315 0.0053 206 ALA A C
+1692 O O . ALA A 206 ? 0.1838 0.1872 0.1217 -0.0462 -0.0334 0.0073 206 ALA A O
+1693 C CB . ALA A 206 ? 0.1854 0.1822 0.1269 -0.0354 -0.0251 -0.0019 206 ALA A CB
+1694 N N . TRP A 207 ? 0.1684 0.1778 0.1215 -0.0378 -0.0327 0.0070 207 TRP A N
+1695 C CA . TRP A 207 ? 0.1712 0.1846 0.1275 -0.0399 -0.0358 0.0120 207 TRP A CA
+1696 C C . TRP A 207 ? 0.1705 0.1890 0.1298 -0.0430 -0.0378 0.0168 207 TRP A C
+1697 O O . TRP A 207 ? 0.1798 0.2004 0.1382 -0.0476 -0.0409 0.0215 207 TRP A O
+1698 C CB . TRP A 207 ? 0.1730 0.1883 0.1366 -0.0347 -0.0352 0.0125 207 TRP A CB
+1699 C CG . TRP A 207 ? 0.1756 0.1960 0.1455 -0.0349 -0.0368 0.0187 207 TRP A CG
+1700 C CD1 . TRP A 207 ? 0.1911 0.2131 0.1617 -0.0369 -0.0387 0.0226 207 TRP A CD1
+1701 C CD2 . TRP A 207 ? 0.1708 0.1951 0.1482 -0.0323 -0.0362 0.0222 207 TRP A CD2
+1702 N NE1 . TRP A 207 ? 0.1926 0.2200 0.1718 -0.0353 -0.0388 0.0290 207 TRP A NE1
+1703 C CE2 . TRP A 207 ? 0.1823 0.2106 0.1652 -0.0322 -0.0369 0.0286 207 TRP A CE2
+1704 C CE3 . TRP A 207 ? 0.1833 0.2076 0.1635 -0.0297 -0.0349 0.0208 207 TRP A CE3
+1705 C CZ2 . TRP A 207 ? 0.1891 0.2210 0.1800 -0.0292 -0.0355 0.0335 207 TRP A CZ2
+1706 C CZ3 . TRP A 207 ? 0.1929 0.2200 0.1800 -0.0272 -0.0341 0.0251 207 TRP A CZ3
+1707 C CH2 . TRP A 207 ? 0.1892 0.2198 0.1814 -0.0268 -0.0340 0.0314 207 TRP A CH2
+1708 N N . LEU A 208 ? 0.1624 0.1825 0.1250 -0.0411 -0.0364 0.0160 208 LEU A N
+1709 C CA . LEU A 208 ? 0.1569 0.1818 0.1222 -0.0441 -0.0381 0.0204 208 LEU A CA
+1710 C C . LEU A 208 ? 0.1709 0.1928 0.1260 -0.0504 -0.0394 0.0206 208 LEU A C
+1711 O O . LEU A 208 ? 0.1774 0.2027 0.1324 -0.0554 -0.0427 0.0258 208 LEU A O
+1712 C CB . LEU A 208 ? 0.1490 0.1754 0.1195 -0.0407 -0.0363 0.0191 208 LEU A CB
+1713 C CG . LEU A 208 ? 0.1641 0.1919 0.1430 -0.0354 -0.0357 0.0196 208 LEU A CG
+1714 C CD1 . LEU A 208 ? 0.1654 0.1935 0.1482 -0.0330 -0.0348 0.0182 208 LEU A CD1
+1715 C CD2 . LEU A 208 ? 0.1647 0.1975 0.1502 -0.0360 -0.0369 0.0260 208 LEU A CD2
+1716 N N . TYR A 209 ? 0.1759 0.1907 0.1216 -0.0505 -0.0369 0.0155 209 TYR A N
+1717 C CA . TYR A 209 ? 0.1880 0.1968 0.1206 -0.0564 -0.0375 0.0150 209 TYR A CA
+1718 C C . TYR A 209 ? 0.2056 0.2126 0.1332 -0.0617 -0.0417 0.0179 209 TYR A C
+1719 O O . TYR A 209 ? 0.2150 0.2212 0.1362 -0.0682 -0.0452 0.0215 209 TYR A O
+1720 C CB . TYR A 209 ? 0.1901 0.1901 0.1135 -0.0545 -0.0327 0.0093 209 TYR A CB
+1721 C CG . TYR A 209 ? 0.1898 0.1909 0.1153 -0.0518 -0.0291 0.0083 209 TYR A CG
+1722 C CD1 . TYR A 209 ? 0.2026 0.2029 0.1217 -0.0557 -0.0292 0.0102 209 TYR A CD1
+1723 C CD2 . TYR A 209 ? 0.1937 0.1964 0.1272 -0.0457 -0.0258 0.0060 209 TYR A CD2
+1724 C CE1 . TYR A 209 ? 0.2103 0.2121 0.1321 -0.0531 -0.0257 0.0100 209 TYR A CE1
+1725 C CE2 . TYR A 209 ? 0.2039 0.2083 0.1406 -0.0434 -0.0229 0.0063 209 TYR A CE2
+1726 C CZ . TYR A 209 ? 0.2111 0.2151 0.1421 -0.0469 -0.0226 0.0082 209 TYR A CZ
+1727 O OH . TYR A 209 ? 0.2235 0.2299 0.1587 -0.0445 -0.0196 0.0092 209 TYR A OH
+1728 N N . ALA A 210 ? 0.2094 0.2161 0.1404 -0.0591 -0.0418 0.0170 210 ALA A N
+1729 C CA . ALA A 210 ? 0.2163 0.2224 0.1447 -0.0640 -0.0463 0.0208 210 ALA A CA
+1730 C C . ALA A 210 ? 0.2209 0.2359 0.1579 -0.0673 -0.0507 0.0291 210 ALA A C
+1731 O O . ALA A 210 ? 0.2286 0.2430 0.1608 -0.0745 -0.0557 0.0340 210 ALA A O
+1732 C CB . ALA A 210 ? 0.2153 0.2215 0.1488 -0.0595 -0.0452 0.0192 210 ALA A CB
+1733 N N . ALA A 211 ? 0.2098 0.2324 0.1593 -0.0624 -0.0491 0.0314 211 ALA A N
+1734 C CA . ALA A 211 ? 0.2048 0.2362 0.1643 -0.0643 -0.0520 0.0398 211 ALA A CA
+1735 C C . ALA A 211 ? 0.2108 0.2428 0.1647 -0.0714 -0.0553 0.0430 211 ALA A C
+1736 O O . ALA A 211 ? 0.2234 0.2590 0.1784 -0.0777 -0.0603 0.0504 211 ALA A O
+1737 C CB . ALA A 211 ? 0.2027 0.2395 0.1745 -0.0571 -0.0485 0.0402 211 ALA A CB
+1738 N N . VAL A 212 ? 0.2063 0.2345 0.1535 -0.0709 -0.0527 0.0380 212 VAL A N
+1739 C CA . VAL A 212 ? 0.2194 0.2472 0.1595 -0.0775 -0.0554 0.0407 212 VAL A CA
+1740 C C . VAL A 212 ? 0.2499 0.2699 0.1751 -0.0858 -0.0596 0.0415 212 VAL A C
+1741 O O . VAL A 212 ? 0.2625 0.2852 0.1860 -0.0933 -0.0650 0.0483 212 VAL A O
+1742 C CB . VAL A 212 ? 0.2233 0.2480 0.1591 -0.0745 -0.0509 0.0353 212 VAL A CB
+1743 C CG1 . VAL A 212 ? 0.2307 0.2533 0.1563 -0.0815 -0.0532 0.0376 212 VAL A CG1
+1744 C CG2 . VAL A 212 ? 0.2217 0.2542 0.1723 -0.0679 -0.0483 0.0360 212 VAL A CG2
+1745 N N . ILE A 213 ? 0.2661 0.2762 0.1805 -0.0851 -0.0576 0.0352 213 ILE A N
+1746 C CA . ILE A 213 ? 0.2989 0.2988 0.1967 -0.0932 -0.0615 0.0351 213 ILE A CA
+1747 C C . ILE A 213 ? 0.3284 0.3341 0.2324 -0.0989 -0.0688 0.0438 213 ILE A C
+1748 O O . ILE A 213 ? 0.3478 0.3505 0.2427 -0.1081 -0.0749 0.0486 213 ILE A O
+1749 C CB . ILE A 213 ? 0.3102 0.2991 0.1982 -0.0898 -0.0572 0.0270 213 ILE A CB
+1750 C CG1 . ILE A 213 ? 0.3208 0.3032 0.2015 -0.0853 -0.0501 0.0200 213 ILE A CG1
+1751 C CG2 . ILE A 213 ? 0.3287 0.3063 0.2006 -0.0978 -0.0616 0.0272 213 ILE A CG2
+1752 C CD1 . ILE A 213 ? 0.3387 0.3140 0.2162 -0.0797 -0.0445 0.0132 213 ILE A CD1
+1753 N N . ASN A 214 ? 0.3286 0.3431 0.2488 -0.0934 -0.0681 0.0468 214 ASN A N
+1754 C CA . ASN A 214 ? 0.3465 0.3677 0.2756 -0.0973 -0.0738 0.0560 214 ASN A CA
+1755 C C . ASN A 214 ? 0.3578 0.3920 0.3022 -0.0985 -0.0764 0.0662 214 ASN A C
+1756 O O . ASN A 214 ? 0.3792 0.4213 0.3358 -0.0992 -0.0794 0.0750 214 ASN A O
+1757 C CB . ASN A 214 ? 0.3592 0.3819 0.2964 -0.0909 -0.0712 0.0545 214 ASN A CB
+1758 C CG . ASN A 214 ? 0.4054 0.4159 0.3279 -0.0923 -0.0708 0.0474 214 ASN A CG
+1759 O OD1 . ASN A 214 ? 0.4375 0.4434 0.3529 -0.0994 -0.0763 0.0505 214 ASN A OD1
+1760 N ND2 . ASN A 214 ? 0.4032 0.4076 0.3206 -0.0863 -0.0645 0.0381 214 ASN A ND2
+1761 N N . GLY A 215 ? 0.3423 0.3787 0.2864 -0.0988 -0.0753 0.0660 215 GLY A N
+1762 C CA . GLY A 215 ? 0.3281 0.3761 0.2856 -0.1007 -0.0778 0.0759 215 GLY A CA
+1763 C C . GLY A 215 ? 0.3001 0.3575 0.2753 -0.0920 -0.0726 0.0778 215 GLY A C
+1764 O O . GLY A 215 ? 0.3024 0.3681 0.2871 -0.0937 -0.0741 0.0852 215 GLY A O
+1765 N N A ASP A 216 ? 0.2803 0.3359 0.2594 -0.0829 -0.0667 0.0714 216 ASP A N
+1766 N N B ASP A 216 ? 0.2847 0.3402 0.2637 -0.0830 -0.0668 0.0714 216 ASP A N
+1767 C CA A ASP A 216 ? 0.2635 0.3253 0.2567 -0.0747 -0.0618 0.0725 216 ASP A CA
+1768 C CA B ASP A 216 ? 0.2724 0.3339 0.2653 -0.0747 -0.0617 0.0722 216 ASP A CA
+1769 C C A ASP A 216 ? 0.2716 0.3305 0.2605 -0.0722 -0.0585 0.0655 216 ASP A C
+1770 C C B ASP A 216 ? 0.2758 0.3346 0.2642 -0.0724 -0.0587 0.0654 216 ASP A C
+1771 O O A ASP A 216 ? 0.2864 0.3380 0.2669 -0.0689 -0.0555 0.0565 216 ASP A O
+1772 O O B ASP A 216 ? 0.2909 0.3421 0.2703 -0.0696 -0.0558 0.0564 216 ASP A O
+1773 C CB A ASP A 216 ? 0.2639 0.3240 0.2621 -0.0669 -0.0575 0.0695 216 ASP A CB
+1774 C CB B ASP A 216 ? 0.2863 0.3457 0.2833 -0.0669 -0.0574 0.0686 216 ASP A CB
+1775 C CG A ASP A 216 ? 0.2835 0.3475 0.2882 -0.0685 -0.0600 0.0774 216 ASP A CG
+1776 C CG B ASP A 216 ? 0.3267 0.3938 0.3393 -0.0629 -0.0559 0.0775 216 ASP A CG
+1777 O OD1 A ASP A 216 ? 0.2790 0.3500 0.2902 -0.0743 -0.0644 0.0877 216 ASP A OD1
+1778 O OD1 B ASP A 216 ? 0.3309 0.4047 0.3535 -0.0626 -0.0554 0.0842 216 ASP A OD1
+1779 O OD2 A ASP A 216 ? 0.2960 0.3567 0.3001 -0.0642 -0.0577 0.0741 216 ASP A OD2
+1780 O OD2 B ASP A 216 ? 0.3469 0.4129 0.3618 -0.0597 -0.0546 0.0781 216 ASP A OD2
+1781 N N . ARG A 217 ? 0.2585 0.3236 0.2534 -0.0740 -0.0594 0.0705 217 ARG A N
+1782 C CA . ARG A 217 ? 0.2453 0.3087 0.2367 -0.0726 -0.0572 0.0655 217 ARG A CA
+1783 C C . ARG A 217 ? 0.2271 0.2973 0.2323 -0.0678 -0.0545 0.0689 217 ARG A C
+1784 O O . ARG A 217 ? 0.2224 0.2927 0.2263 -0.0675 -0.0535 0.0665 217 ARG A O
+1785 C CB . ARG A 217 ? 0.2559 0.3186 0.2373 -0.0814 -0.0615 0.0677 217 ARG A CB
+1786 C CG . ARG A 217 ? 0.2916 0.3465 0.2575 -0.0885 -0.0654 0.0663 217 ARG A CG
+1787 C CD . ARG A 217 ? 0.3143 0.3693 0.2718 -0.0984 -0.0710 0.0717 217 ARG A CD
+1788 N NE . ARG A 217 ? 0.3240 0.3770 0.2753 -0.0983 -0.0686 0.0679 217 ARG A NE
+1789 C CZ . ARG A 217 ? 0.3284 0.3705 0.2620 -0.1002 -0.0669 0.0609 217 ARG A CZ
+1790 N NH1 . ARG A 217 ? 0.3197 0.3610 0.2493 -0.0996 -0.0642 0.0587 217 ARG A NH1
+1791 N NH2 . ARG A 217 ? 0.3159 0.3476 0.2355 -0.1029 -0.0676 0.0567 217 ARG A NH2
+1792 N N . TRP A 218 ? 0.2159 0.2912 0.2339 -0.0640 -0.0532 0.0750 218 TRP A N
+1793 C CA . TRP A 218 ? 0.2071 0.2875 0.2374 -0.0597 -0.0503 0.0788 218 TRP A CA
+1794 C C . TRP A 218 ? 0.2084 0.2834 0.2369 -0.0535 -0.0463 0.0704 218 TRP A C
+1795 O O . TRP A 218 ? 0.2116 0.2896 0.2469 -0.0518 -0.0450 0.0724 218 TRP A O
+1796 C CB . TRP A 218 ? 0.1990 0.2837 0.2422 -0.0556 -0.0480 0.0866 218 TRP A CB
+1797 C CG . TRP A 218 ? 0.1998 0.2781 0.2409 -0.0491 -0.0442 0.0816 218 TRP A CG
+1798 C CD1 . TRP A 218 ? 0.2098 0.2871 0.2488 -0.0499 -0.0453 0.0828 218 TRP A CD1
+1799 C CD2 . TRP A 218 ? 0.2055 0.2774 0.2468 -0.0410 -0.0390 0.0754 218 TRP A CD2
+1800 N NE1 . TRP A 218 ? 0.2152 0.2860 0.2523 -0.0426 -0.0408 0.0770 218 TRP A NE1
+1801 C CE2 . TRP A 218 ? 0.2142 0.2813 0.2523 -0.0373 -0.0370 0.0726 218 TRP A CE2
+1802 C CE3 . TRP A 218 ? 0.2123 0.2814 0.2553 -0.0370 -0.0363 0.0720 218 TRP A CE3
+1803 C CZ2 . TRP A 218 ? 0.2196 0.2788 0.2549 -0.0302 -0.0327 0.0663 218 TRP A CZ2
+1804 C CZ3 . TRP A 218 ? 0.2220 0.2828 0.2621 -0.0302 -0.0323 0.0658 218 TRP A CZ3
+1805 C CH2 . TRP A 218 ? 0.2233 0.2790 0.2592 -0.0270 -0.0306 0.0631 218 TRP A CH2
+1806 N N . PHE A 219 ? 0.2026 0.2700 0.2228 -0.0503 -0.0446 0.0619 219 PHE A N
+1807 C CA . PHE A 219 ? 0.1985 0.2603 0.2170 -0.0448 -0.0415 0.0545 219 PHE A CA
+1808 C C . PHE A 219 ? 0.2102 0.2707 0.2225 -0.0472 -0.0423 0.0502 219 PHE A C
+1809 O O . PHE A 219 ? 0.2134 0.2706 0.2260 -0.0434 -0.0405 0.0455 219 PHE A O
+1810 C CB . PHE A 219 ? 0.1881 0.2429 0.2014 -0.0407 -0.0396 0.0485 219 PHE A CB
+1811 C CG . PHE A 219 ? 0.1796 0.2318 0.1831 -0.0447 -0.0415 0.0455 219 PHE A CG
+1812 C CD1 . PHE A 219 ? 0.1862 0.2342 0.1810 -0.0461 -0.0414 0.0395 219 PHE A CD1
+1813 C CD2 . PHE A 219 ? 0.1759 0.2296 0.1791 -0.0472 -0.0432 0.0495 219 PHE A CD2
+1814 C CE1 . PHE A 219 ? 0.1908 0.2348 0.1755 -0.0497 -0.0425 0.0369 219 PHE A CE1
+1815 C CE2 . PHE A 219 ? 0.1857 0.2356 0.1790 -0.0512 -0.0452 0.0467 219 PHE A CE2
+1816 C CZ . PHE A 219 ? 0.1871 0.2316 0.1705 -0.0526 -0.0447 0.0402 219 PHE A CZ
+1817 N N . LEU A 220 ? 0.2060 0.2687 0.2125 -0.0536 -0.0450 0.0522 220 LEU A N
+1818 C CA . LEU A 220 ? 0.2204 0.2817 0.2208 -0.0556 -0.0448 0.0490 220 LEU A CA
+1819 C C . LEU A 220 ? 0.2291 0.2963 0.2392 -0.0547 -0.0447 0.0528 220 LEU A C
+1820 O O . LEU A 220 ? 0.2333 0.3066 0.2522 -0.0558 -0.0460 0.0597 220 LEU A O
+1821 C CB . LEU A 220 ? 0.2247 0.2850 0.2142 -0.0629 -0.0475 0.0503 220 LEU A CB
+1822 C CG . LEU A 220 ? 0.2373 0.2904 0.2156 -0.0645 -0.0477 0.0463 220 LEU A CG
+1823 C CD1 . LEU A 220 ? 0.2414 0.2915 0.2069 -0.0725 -0.0507 0.0479 220 LEU A CD1
+1824 C CD2 . LEU A 220 ? 0.2467 0.2928 0.2205 -0.0591 -0.0436 0.0381 220 LEU A CD2
+1825 N N . ASN A 221 ? 0.2295 0.2950 0.2392 -0.0523 -0.0430 0.0490 221 ASN A N
+1826 C CA . ASN A 221 ? 0.2248 0.2950 0.2438 -0.0510 -0.0429 0.0521 221 ASN A CA
+1827 C C . ASN A 221 ? 0.2211 0.2925 0.2365 -0.0531 -0.0427 0.0511 221 ASN A C
+1828 O O . ASN A 221 ? 0.2310 0.2986 0.2357 -0.0554 -0.0421 0.0482 221 ASN A O
+1829 C CB . ASN A 221 ? 0.2341 0.3011 0.2598 -0.0448 -0.0412 0.0496 221 ASN A CB
+1830 C CG . ASN A 221 ? 0.2661 0.3267 0.2866 -0.0417 -0.0398 0.0428 221 ASN A CG
+1831 O OD1 . ASN A 221 ? 0.2607 0.3206 0.2763 -0.0430 -0.0393 0.0405 221 ASN A OD1
+1832 N ND2 . ASN A 221 ? 0.2758 0.3312 0.2975 -0.0375 -0.0390 0.0400 221 ASN A ND2
+1833 N N . ARG A 222 ? 0.2057 0.2819 0.2299 -0.0522 -0.0429 0.0542 222 ARG A N
+1834 C CA . ARG A 222 ? 0.2060 0.2843 0.2288 -0.0537 -0.0424 0.0545 222 ARG A CA
+1835 C C . ARG A 222 ? 0.2006 0.2750 0.2238 -0.0493 -0.0403 0.0498 222 ARG A C
+1836 O O . ARG A 222 ? 0.2032 0.2802 0.2280 -0.0496 -0.0395 0.0510 222 ARG A O
+1837 C CB . ARG A 222 ? 0.2137 0.2997 0.2475 -0.0546 -0.0439 0.0607 222 ARG A CB
+1838 C CG . ARG A 222 ? 0.2546 0.3462 0.2899 -0.0595 -0.0463 0.0672 222 ARG A CG
+1839 C CD . ARG A 222 ? 0.2858 0.3854 0.3336 -0.0601 -0.0474 0.0740 222 ARG A CD
+1840 N NE . ARG A 222 ? 0.3103 0.4163 0.3597 -0.0658 -0.0502 0.0815 222 ARG A NE
+1841 C CZ . ARG A 222 ? 0.3500 0.4591 0.3926 -0.0722 -0.0526 0.0845 222 ARG A CZ
+1842 N NH1 . ARG A 222 ? 0.3476 0.4538 0.3813 -0.0730 -0.0515 0.0807 222 ARG A NH1
+1843 N NH2 . ARG A 222 ? 0.3501 0.4649 0.3946 -0.0780 -0.0560 0.0921 222 ARG A NH2
+1844 N N . PHE A 223 ? 0.1880 0.2567 0.2104 -0.0456 -0.0395 0.0453 223 PHE A N
+1845 C CA . PHE A 223 ? 0.1905 0.2561 0.2156 -0.0418 -0.0384 0.0423 223 PHE A CA
+1846 C C . PHE A 223 ? 0.1685 0.2292 0.1855 -0.0409 -0.0360 0.0381 223 PHE A C
+1847 O O . PHE A 223 ? 0.1751 0.2326 0.1831 -0.0425 -0.0350 0.0360 223 PHE A O
+1848 C CB . PHE A 223 ? 0.2060 0.2680 0.2368 -0.0381 -0.0397 0.0409 223 PHE A CB
+1849 C CG . PHE A 223 ? 0.2286 0.2930 0.2664 -0.0380 -0.0409 0.0447 223 PHE A CG
+1850 C CD1 . PHE A 223 ? 0.2419 0.3129 0.2861 -0.0400 -0.0417 0.0496 223 PHE A CD1
+1851 C CD2 . PHE A 223 ? 0.2490 0.3088 0.2870 -0.0355 -0.0406 0.0437 223 PHE A CD2
+1852 C CE1 . PHE A 223 ? 0.2545 0.3277 0.3060 -0.0396 -0.0421 0.0538 223 PHE A CE1
+1853 C CE2 . PHE A 223 ? 0.2631 0.3243 0.3077 -0.0346 -0.0405 0.0478 223 PHE A CE2
+1854 C CZ . PHE A 223 ? 0.2589 0.3269 0.3106 -0.0367 -0.0412 0.0529 223 PHE A CZ
+1855 N N . THR A 224 ? 0.1530 0.2131 0.1741 -0.0383 -0.0350 0.0374 224 THR A N
+1856 C CA . THR A 224 ? 0.1516 0.2071 0.1683 -0.0362 -0.0324 0.0342 224 THR A CA
+1857 C C . THR A 224 ? 0.1523 0.2060 0.1769 -0.0330 -0.0344 0.0335 224 THR A C
+1858 O O . THR A 224 ? 0.1582 0.2130 0.1898 -0.0326 -0.0376 0.0351 224 THR A O
+1859 C CB . THR A 224 ? 0.1613 0.2174 0.1731 -0.0369 -0.0284 0.0352 224 THR A CB
+1860 O OG1 . THR A 224 ? 0.1594 0.2096 0.1648 -0.0351 -0.0251 0.0318 224 THR A OG1
+1861 C CG2 . THR A 224 ? 0.1625 0.2231 0.1837 -0.0353 -0.0280 0.0390 224 THR A CG2
+1862 N N . THR A 225 ? 0.1427 0.1930 0.1656 -0.0310 -0.0327 0.0314 225 THR A N
+1863 C CA . THR A 225 ? 0.1450 0.1933 0.1745 -0.0289 -0.0350 0.0314 225 THR A CA
+1864 C C . THR A 225 ? 0.1455 0.1935 0.1756 -0.0272 -0.0316 0.0321 225 THR A C
+1865 O O . THR A 225 ? 0.1403 0.1888 0.1651 -0.0273 -0.0269 0.0323 225 THR A O
+1866 C CB . THR A 225 ? 0.1737 0.2164 0.2000 -0.0281 -0.0375 0.0279 225 THR A CB
+1867 O OG1 . THR A 225 ? 0.1926 0.2324 0.2239 -0.0269 -0.0407 0.0283 225 THR A OG1
+1868 C CG2 . THR A 225 ? 0.1881 0.2273 0.2060 -0.0277 -0.0349 0.0242 225 THR A CG2
+1869 N N . THR A 226 ? 0.1469 0.1936 0.1834 -0.0257 -0.0339 0.0332 226 THR A N
+1870 C CA . THR A 226 ? 0.1483 0.1950 0.1876 -0.0238 -0.0308 0.0348 226 THR A CA
+1871 C C . THR A 226 ? 0.1535 0.1950 0.1898 -0.0231 -0.0325 0.0314 226 THR A C
+1872 O O . THR A 226 ? 0.1489 0.1869 0.1823 -0.0239 -0.0365 0.0286 226 THR A O
+1873 C CB . THR A 226 ? 0.1692 0.2204 0.2212 -0.0234 -0.0332 0.0409 226 THR A CB
+1874 O OG1 . THR A 226 ? 0.1760 0.2243 0.2318 -0.0246 -0.0401 0.0409 226 THR A OG1
+1875 C CG2 . THR A 226 ? 0.1819 0.2387 0.2379 -0.0240 -0.0320 0.0448 226 THR A CG2
+1876 N N A LEU A 227 ? 0.1551 0.1958 0.1924 -0.0213 -0.0291 0.0321 227 LEU A N
+1877 N N B LEU A 227 ? 0.1515 0.1922 0.1888 -0.0213 -0.0291 0.0321 227 LEU A N
+1878 C CA A LEU A 227 ? 0.1694 0.2059 0.2049 -0.0206 -0.0308 0.0296 227 LEU A CA
+1879 C CA B LEU A 227 ? 0.1621 0.1985 0.1977 -0.0207 -0.0310 0.0295 227 LEU A CA
+1880 C C A LEU A 227 ? 0.1749 0.2099 0.2162 -0.0218 -0.0380 0.0311 227 LEU A C
+1881 C C B LEU A 227 ? 0.1711 0.2060 0.2123 -0.0219 -0.0382 0.0311 227 LEU A C
+1882 O O A LEU A 227 ? 0.1842 0.2140 0.2200 -0.0224 -0.0412 0.0274 227 LEU A O
+1883 O O B LEU A 227 ? 0.1795 0.2093 0.2152 -0.0225 -0.0414 0.0273 227 LEU A O
+1884 C CB A LEU A 227 ? 0.1732 0.2100 0.2112 -0.0183 -0.0254 0.0317 227 LEU A CB
+1885 C CB B LEU A 227 ? 0.1603 0.1969 0.1982 -0.0184 -0.0260 0.0314 227 LEU A CB
+1886 C CG A LEU A 227 ? 0.1952 0.2274 0.2273 -0.0174 -0.0240 0.0278 227 LEU A CG
+1887 C CG B LEU A 227 ? 0.1740 0.2074 0.2019 -0.0174 -0.0192 0.0279 227 LEU A CG
+1888 C CD1 A LEU A 227 ? 0.2069 0.2351 0.2268 -0.0185 -0.0232 0.0217 227 LEU A CD1
+1889 C CD1 B LEU A 227 ? 0.1720 0.2045 0.2030 -0.0146 -0.0141 0.0300 227 LEU A CD1
+1890 C CD2 A LEU A 227 ? 0.1975 0.2297 0.2314 -0.0147 -0.0170 0.0301 227 LEU A CD2
+1891 C CD2 B LEU A 227 ? 0.1864 0.2153 0.2040 -0.0187 -0.0211 0.0218 227 LEU A CD2
+1892 N N . ASN A 228 ? 0.1664 0.2052 0.2179 -0.0225 -0.0408 0.0368 228 ASN A N
+1893 C CA . ASN A 228 ? 0.1596 0.1953 0.2151 -0.0245 -0.0486 0.0386 228 ASN A CA
+1894 C C . ASN A 228 ? 0.1620 0.1930 0.2114 -0.0260 -0.0525 0.0350 228 ASN A C
+1895 O O . ASN A 228 ? 0.1794 0.2032 0.2243 -0.0271 -0.0572 0.0328 228 ASN A O
+1896 C CB . ASN A 228 ? 0.1641 0.2053 0.2327 -0.0253 -0.0510 0.0464 228 ASN A CB
+1897 C CG . ASN A 228 ? 0.2077 0.2526 0.2841 -0.0237 -0.0480 0.0514 228 ASN A CG
+1898 O OD1 . ASN A 228 ? 0.2288 0.2799 0.3169 -0.0233 -0.0473 0.0588 228 ASN A OD1
+1899 N ND2 . ASN A 228 ? 0.2169 0.2585 0.2882 -0.0226 -0.0459 0.0482 228 ASN A ND2
+1900 N N . ASP A 229 ? 0.1556 0.1898 0.2042 -0.0260 -0.0501 0.0347 229 ASP A N
+1901 C CA . ASP A 229 ? 0.1631 0.1932 0.2073 -0.0269 -0.0529 0.0323 229 ASP A CA
+1902 C C . ASP A 229 ? 0.1704 0.1950 0.2044 -0.0259 -0.0513 0.0267 229 ASP A C
+1903 O O . ASP A 229 ? 0.1840 0.2011 0.2132 -0.0261 -0.0544 0.0245 229 ASP A O
+1904 C CB . ASP A 229 ? 0.1876 0.2237 0.2347 -0.0273 -0.0507 0.0342 229 ASP A CB
+1905 C CG . ASP A 229 ? 0.2696 0.3018 0.3131 -0.0278 -0.0525 0.0323 229 ASP A CG
+1906 O OD1 . ASP A 229 ? 0.2930 0.3199 0.3380 -0.0287 -0.0572 0.0331 229 ASP A OD1
+1907 O OD2 . ASP A 229 ? 0.2923 0.3257 0.3308 -0.0273 -0.0492 0.0302 229 ASP A OD2
+1908 N N . PHE A 230 ? 0.1635 0.1907 0.1935 -0.0249 -0.0463 0.0247 230 PHE A N
+1909 C CA . PHE A 230 ? 0.1676 0.1905 0.1891 -0.0240 -0.0449 0.0203 230 PHE A CA
+1910 C C . PHE A 230 ? 0.1813 0.1975 0.2000 -0.0235 -0.0479 0.0184 230 PHE A C
+1911 O O . PHE A 230 ? 0.1952 0.2052 0.2080 -0.0229 -0.0491 0.0157 230 PHE A O
+1912 C CB . PHE A 230 ? 0.1586 0.1845 0.1762 -0.0236 -0.0398 0.0189 230 PHE A CB
+1913 C CG . PHE A 230 ? 0.1754 0.1973 0.1855 -0.0229 -0.0389 0.0150 230 PHE A CG
+1914 C CD1 . PHE A 230 ? 0.1837 0.2056 0.1905 -0.0233 -0.0387 0.0144 230 PHE A CD1
+1915 C CD2 . PHE A 230 ? 0.1914 0.2097 0.1991 -0.0218 -0.0389 0.0129 230 PHE A CD2
+1916 C CE1 . PHE A 230 ? 0.2018 0.2204 0.2030 -0.0225 -0.0380 0.0119 230 PHE A CE1
+1917 C CE2 . PHE A 230 ? 0.2005 0.2151 0.2019 -0.0210 -0.0385 0.0099 230 PHE A CE2
+1918 C CZ . PHE A 230 ? 0.2073 0.2221 0.2056 -0.0212 -0.0379 0.0095 230 PHE A CZ
+1919 N N . ASN A 231 ? 0.1764 0.1935 0.1998 -0.0237 -0.0491 0.0205 231 ASN A N
+1920 C CA . ASN A 231 ? 0.1851 0.1963 0.2061 -0.0239 -0.0525 0.0195 231 ASN A CA
+1921 C C . ASN A 231 ? 0.2076 0.2110 0.2259 -0.0255 -0.0585 0.0195 231 ASN A C
+1922 O O . ASN A 231 ? 0.2219 0.2178 0.2334 -0.0255 -0.0607 0.0170 231 ASN A O
+1923 C CB . ASN A 231 ? 0.1929 0.2078 0.2210 -0.0240 -0.0523 0.0231 231 ASN A CB
+1924 C CG . ASN A 231 ? 0.2152 0.2331 0.2414 -0.0220 -0.0461 0.0213 231 ASN A CG
+1925 O OD1 . ASN A 231 ? 0.2253 0.2409 0.2436 -0.0211 -0.0436 0.0169 231 ASN A OD1
+1926 N ND2 . ASN A 231 ? 0.2279 0.2506 0.2612 -0.0211 -0.0431 0.0250 231 ASN A ND2
+1927 N N . LEU A 232 ? 0.2152 0.2191 0.2374 -0.0267 -0.0609 0.0220 232 LEU A N
+1928 C CA . LEU A 232 ? 0.2396 0.2337 0.2569 -0.0283 -0.0662 0.0214 232 LEU A CA
+1929 C C . LEU A 232 ? 0.2511 0.2382 0.2580 -0.0261 -0.0634 0.0166 232 LEU A C
+1930 O O . LEU A 232 ? 0.2721 0.2482 0.2700 -0.0262 -0.0658 0.0142 232 LEU A O
+1931 C CB . LEU A 232 ? 0.2564 0.2531 0.2805 -0.0298 -0.0684 0.0250 232 LEU A CB
+1932 C CG . LEU A 232 ? 0.2869 0.2897 0.3222 -0.0320 -0.0719 0.0310 232 LEU A CG
+1933 C CD1 . LEU A 232 ? 0.2982 0.3035 0.3398 -0.0333 -0.0739 0.0345 232 LEU A CD1
+1934 C CD2 . LEU A 232 ? 0.3027 0.2980 0.3364 -0.0349 -0.0789 0.0327 232 LEU A CD2
+1935 N N . VAL A 233 ? 0.2402 0.2334 0.2479 -0.0243 -0.0580 0.0157 233 VAL A N
+1936 C CA . VAL A 233 ? 0.2420 0.2309 0.2424 -0.0220 -0.0547 0.0128 233 VAL A CA
+1937 C C . VAL A 233 ? 0.2444 0.2304 0.2386 -0.0206 -0.0531 0.0097 233 VAL A C
+1938 O O . VAL A 233 ? 0.2544 0.2316 0.2405 -0.0190 -0.0528 0.0074 233 VAL A O
+1939 C CB . VAL A 233 ? 0.2538 0.2514 0.2584 -0.0214 -0.0505 0.0142 233 VAL A CB
+1940 C CG1 . VAL A 233 ? 0.2676 0.2618 0.2668 -0.0191 -0.0471 0.0128 233 VAL A CG1
+1941 C CG2 . VAL A 233 ? 0.2610 0.2616 0.2722 -0.0228 -0.0521 0.0175 233 VAL A CG2
+1942 N N . ALA A 234 ? 0.2379 0.2302 0.2354 -0.0209 -0.0520 0.0099 234 ALA A N
+1943 C CA . ALA A 234 ? 0.2521 0.2423 0.2446 -0.0197 -0.0506 0.0073 234 ALA A CA
+1944 C C . ALA A 234 ? 0.2700 0.2501 0.2564 -0.0201 -0.0549 0.0061 234 ALA A C
+1945 O O . ALA A 234 ? 0.2737 0.2472 0.2521 -0.0185 -0.0538 0.0034 234 ALA A O
+1946 C CB . ALA A 234 ? 0.2534 0.2510 0.2511 -0.0201 -0.0488 0.0082 234 ALA A CB
+1947 N N . MET A 235 ? 0.2708 0.2489 0.2605 -0.0227 -0.0599 0.0085 235 MET A N
+1948 C CA . MET A 235 ? 0.2833 0.2506 0.2661 -0.0244 -0.0653 0.0080 235 MET A CA
+1949 C C . MET A 235 ? 0.2748 0.2297 0.2458 -0.0231 -0.0651 0.0050 235 MET A C
+1950 O O . MET A 235 ? 0.2808 0.2267 0.2418 -0.0223 -0.0654 0.0024 235 MET A O
+1951 C CB . MET A 235 ? 0.3132 0.2810 0.3027 -0.0282 -0.0716 0.0124 235 MET A CB
+1952 C CG . MET A 235 ? 0.3926 0.3474 0.3734 -0.0313 -0.0786 0.0124 235 MET A CG
+1953 S SD . MET A 235 ? 0.5622 0.5196 0.5473 -0.0340 -0.0831 0.0157 235 MET A SD
+1954 C CE . MET A 235 ? 0.5082 0.4783 0.5112 -0.0362 -0.0851 0.0231 235 MET A CE
+1955 N N . LYS A 236 ? 0.2583 0.2127 0.2306 -0.0226 -0.0639 0.0057 236 LYS A N
+1956 C CA . LYS A 236 ? 0.2595 0.2016 0.2215 -0.0208 -0.0625 0.0036 236 LYS A CA
+1957 C C . LYS A 236 ? 0.2555 0.1957 0.2112 -0.0167 -0.0566 0.0010 236 LYS A C
+1958 O O . LYS A 236 ? 0.2773 0.2045 0.2214 -0.0149 -0.0556 -0.0012 236 LYS A O
+1959 C CB . LYS A 236 ? 0.2939 0.2384 0.2613 -0.0207 -0.0616 0.0056 236 LYS A CB
+1960 C CG . LYS A 236 ? 0.3727 0.3048 0.3307 -0.0180 -0.0586 0.0042 236 LYS A CG
+1961 C CD . LYS A 236 ? 0.4508 0.3874 0.4161 -0.0177 -0.0569 0.0068 236 LYS A CD
+1962 C CE . LYS A 236 ? 0.5137 0.4397 0.4715 -0.0139 -0.0519 0.0061 236 LYS A CE
+1963 N NZ . LYS A 236 ? 0.5567 0.4634 0.5015 -0.0148 -0.0550 0.0042 236 LYS A NZ
+1964 N N . TYR A 237 ? 0.2267 0.1790 0.1895 -0.0153 -0.0527 0.0015 237 TYR A N
+1965 C CA . TYR A 237 ? 0.2168 0.1692 0.1758 -0.0118 -0.0474 0.0002 237 TYR A CA
+1966 C C . TYR A 237 ? 0.2196 0.1729 0.1759 -0.0114 -0.0473 -0.0016 237 TYR A C
+1967 O O . TYR A 237 ? 0.2282 0.1848 0.1841 -0.0089 -0.0431 -0.0019 237 TYR A O
+1968 C CB . TYR A 237 ? 0.2073 0.1712 0.1748 -0.0110 -0.0433 0.0026 237 TYR A CB
+1969 C CG . TYR A 237 ? 0.2211 0.1826 0.1900 -0.0101 -0.0420 0.0047 237 TYR A CG
+1970 C CD1 . TYR A 237 ? 0.2387 0.1928 0.2023 -0.0065 -0.0377 0.0051 237 TYR A CD1
+1971 C CD2 . TYR A 237 ? 0.2272 0.1928 0.2027 -0.0126 -0.0446 0.0066 237 TYR A CD2
+1972 C CE1 . TYR A 237 ? 0.2503 0.2010 0.2152 -0.0053 -0.0360 0.0073 237 TYR A CE1
+1973 C CE2 . TYR A 237 ? 0.2339 0.1968 0.2108 -0.0118 -0.0434 0.0086 237 TYR A CE2
+1974 C CZ . TYR A 237 ? 0.2574 0.2123 0.2289 -0.0082 -0.0391 0.0089 237 TYR A CZ
+1975 O OH . TYR A 237 ? 0.2769 0.2289 0.2504 -0.0070 -0.0372 0.0114 237 TYR A OH
+1976 N N A ASN A 238 ? 0.2175 0.1685 0.1729 -0.0140 -0.0520 -0.0021 238 ASN A N
+1977 N N B ASN A 238 ? 0.2148 0.1657 0.1700 -0.0140 -0.0520 -0.0021 238 ASN A N
+1978 C CA A ASN A 238 ? 0.2240 0.1759 0.1775 -0.0138 -0.0523 -0.0033 238 ASN A CA
+1979 C CA B ASN A 238 ? 0.2182 0.1701 0.1718 -0.0139 -0.0524 -0.0033 238 ASN A CA
+1980 C C A ASN A 238 ? 0.2143 0.1785 0.1758 -0.0131 -0.0487 -0.0028 238 ASN A C
+1981 C C B ASN A 238 ? 0.2122 0.1765 0.1739 -0.0133 -0.0489 -0.0028 238 ASN A C
+1982 O O A ASN A 238 ? 0.2159 0.1809 0.1749 -0.0112 -0.0459 -0.0041 238 ASN A O
+1983 O O B ASN A 238 ? 0.2144 0.1796 0.1739 -0.0117 -0.0466 -0.0041 238 ASN A O
+1984 C CB A ASN A 238 ? 0.2562 0.1969 0.1976 -0.0112 -0.0506 -0.0057 238 ASN A CB
+1985 C CB B ASN A 238 ? 0.2416 0.1827 0.1832 -0.0114 -0.0508 -0.0057 238 ASN A CB
+1986 C CG A ASN A 238 ? 0.3145 0.2403 0.2451 -0.0126 -0.0546 -0.0066 238 ASN A CG
+1987 C CG B ASN A 238 ? 0.2820 0.2082 0.2124 -0.0131 -0.0554 -0.0067 238 ASN A CG
+1988 O OD1 A ASN A 238 ? 0.3377 0.2533 0.2598 -0.0103 -0.0521 -0.0075 238 ASN A OD1
+1989 O OD1 B ASN A 238 ? 0.2879 0.2122 0.2202 -0.0168 -0.0609 -0.0053 238 ASN A OD1
+1990 N ND2 A ASN A 238 ? 0.3215 0.2452 0.2521 -0.0167 -0.0611 -0.0058 238 ASN A ND2
+1991 N ND2 B ASN A 238 ? 0.2978 0.2124 0.2157 -0.0105 -0.0534 -0.0089 238 ASN A ND2
+1992 N N . TYR A 239 ? 0.2042 0.1771 0.1744 -0.0147 -0.0485 -0.0008 239 TYR A N
+1993 C CA . TYR A 239 ? 0.2014 0.1840 0.1775 -0.0147 -0.0454 -0.0004 239 TYR A CA
+1994 C C . TYR A 239 ? 0.2074 0.1933 0.1890 -0.0165 -0.0474 0.0010 239 TYR A C
+1995 O O . TYR A 239 ? 0.2147 0.1986 0.1987 -0.0183 -0.0514 0.0029 239 TYR A O
+1996 C CB . TYR A 239 ? 0.1953 0.1844 0.1764 -0.0154 -0.0435 0.0014 239 TYR A CB
+1997 C CG . TYR A 239 ? 0.1940 0.1846 0.1730 -0.0140 -0.0401 0.0013 239 TYR A CG
+1998 C CD1 . TYR A 239 ? 0.2026 0.1870 0.1769 -0.0118 -0.0394 0.0012 239 TYR A CD1
+1999 C CD2 . TYR A 239 ? 0.1911 0.1889 0.1728 -0.0151 -0.0376 0.0022 239 TYR A CD2
+2000 C CE1 . TYR A 239 ? 0.2095 0.1964 0.1839 -0.0104 -0.0361 0.0026 239 TYR A CE1
+2001 C CE2 . TYR A 239 ? 0.1965 0.1964 0.1773 -0.0146 -0.0355 0.0034 239 TYR A CE2
+2002 C CZ . TYR A 239 ? 0.2094 0.2047 0.1877 -0.0121 -0.0347 0.0041 239 TYR A CZ
+2003 O OH . TYR A 239 ? 0.2142 0.2126 0.1936 -0.0115 -0.0324 0.0067 239 TYR A OH
+2004 N N A GLU A 240 ? 0.2031 0.1938 0.1870 -0.0160 -0.0446 0.0006 240 GLU A N
+2005 N N B GLU A 240 ? 0.2060 0.1969 0.1900 -0.0160 -0.0446 0.0006 240 GLU A N
+2006 C CA A GLU A 240 ? 0.2106 0.2050 0.2009 -0.0169 -0.0451 0.0028 240 GLU A CA
+2007 C CA B GLU A 240 ? 0.2154 0.2099 0.2058 -0.0169 -0.0450 0.0028 240 GLU A CA
+2008 C C A GLU A 240 ? 0.2090 0.2088 0.2064 -0.0180 -0.0444 0.0058 240 GLU A C
+2009 C C B GLU A 240 ? 0.2113 0.2111 0.2087 -0.0180 -0.0444 0.0058 240 GLU A C
+2010 O O A GLU A 240 ? 0.1989 0.2015 0.1956 -0.0179 -0.0417 0.0053 240 GLU A O
+2011 O O B GLU A 240 ? 0.2011 0.2037 0.1979 -0.0179 -0.0417 0.0053 240 GLU A O
+2012 C CB A GLU A 240 ? 0.2421 0.2394 0.2322 -0.0157 -0.0409 0.0014 240 GLU A CB
+2013 C CB B GLU A 240 ? 0.2550 0.2526 0.2454 -0.0157 -0.0408 0.0015 240 GLU A CB
+2014 C CG A GLU A 240 ? 0.2988 0.2918 0.2839 -0.0147 -0.0418 -0.0006 240 GLU A CG
+2015 C CG B GLU A 240 ? 0.3326 0.3262 0.3190 -0.0149 -0.0418 -0.0001 240 GLU A CG
+2016 C CD A GLU A 240 ? 0.3616 0.3521 0.3489 -0.0158 -0.0460 0.0013 240 GLU A CD
+2017 C CD B GLU A 240 ? 0.4209 0.4175 0.4091 -0.0139 -0.0381 -0.0006 240 GLU A CD
+2018 O OE1 A GLU A 240 ? 0.3622 0.3567 0.3563 -0.0160 -0.0451 0.0038 240 GLU A OE1
+2019 O OE1 B GLU A 240 ? 0.4450 0.4433 0.4308 -0.0135 -0.0343 -0.0022 240 GLU A OE1
+2020 O OE2 A GLU A 240 ? 0.3858 0.3697 0.3677 -0.0165 -0.0502 0.0008 240 GLU A OE2
+2021 O OE2 B GLU A 240 ? 0.4574 0.4543 0.4493 -0.0140 -0.0390 0.0010 240 GLU A OE2
+2022 N N . PRO A 241 ? 0.2153 0.2168 0.2193 -0.0191 -0.0466 0.0092 241 PRO A N
+2023 C CA . PRO A 241 ? 0.2227 0.2298 0.2344 -0.0196 -0.0454 0.0129 241 PRO A CA
+2024 C C . PRO A 241 ? 0.2198 0.2315 0.2320 -0.0182 -0.0387 0.0124 241 PRO A C
+2025 O O . PRO A 241 ? 0.2329 0.2443 0.2441 -0.0171 -0.0359 0.0115 241 PRO A O
+2026 C CB . PRO A 241 ? 0.2383 0.2473 0.2589 -0.0208 -0.0485 0.0182 241 PRO A CB
+2027 C CG . PRO A 241 ? 0.2465 0.2487 0.2620 -0.0222 -0.0542 0.0169 241 PRO A CG
+2028 C CD . PRO A 241 ? 0.2168 0.2155 0.2229 -0.0203 -0.0511 0.0114 241 PRO A CD
+2029 N N . LEU A 242 ? 0.2081 0.2229 0.2211 -0.0185 -0.0365 0.0132 242 LEU A N
+2030 C CA . LEU A 242 ? 0.2160 0.2329 0.2268 -0.0176 -0.0302 0.0127 242 LEU A CA
+2031 C C . LEU A 242 ? 0.2124 0.2329 0.2316 -0.0165 -0.0271 0.0175 242 LEU A C
+2032 O O . LEU A 242 ? 0.2108 0.2343 0.2374 -0.0171 -0.0297 0.0215 242 LEU A O
+2033 C CB . LEU A 242 ? 0.2211 0.2391 0.2274 -0.0188 -0.0292 0.0115 242 LEU A CB
+2034 C CG . LEU A 242 ? 0.2425 0.2597 0.2415 -0.0191 -0.0240 0.0096 242 LEU A CG
+2035 C CD1 . LEU A 242 ? 0.2550 0.2685 0.2468 -0.0192 -0.0238 0.0058 242 LEU A CD1
+2036 C CD2 . LEU A 242 ? 0.2458 0.2652 0.2423 -0.0210 -0.0238 0.0103 242 LEU A CD2
+2037 N N . THR A 243 ? 0.2176 0.2371 0.2353 -0.0148 -0.0216 0.0171 243 THR A N
+2038 C CA . THR A 243 ? 0.2205 0.2427 0.2461 -0.0129 -0.0169 0.0223 243 THR A CA
+2039 C C . THR A 243 ? 0.2288 0.2496 0.2482 -0.0118 -0.0094 0.0215 243 THR A C
+2040 O O . THR A 243 ? 0.2298 0.2470 0.2382 -0.0132 -0.0085 0.0168 243 THR A O
+2041 C CB . THR A 243 ? 0.2302 0.2515 0.2595 -0.0111 -0.0150 0.0234 243 THR A CB
+2042 O OG1 . THR A 243 ? 0.2306 0.2470 0.2500 -0.0103 -0.0103 0.0186 243 THR A OG1
+2043 C CG2 . THR A 243 ? 0.2434 0.2647 0.2764 -0.0127 -0.0225 0.0239 243 THR A CG2
+2044 N N . GLN A 244 ? 0.2287 0.2517 0.2550 -0.0095 -0.0042 0.0267 244 GLN A N
+2045 C CA . GLN A 244 ? 0.2356 0.2551 0.2540 -0.0081 0.0041 0.0261 244 GLN A CA
+2046 C C . GLN A 244 ? 0.2382 0.2500 0.2454 -0.0073 0.0089 0.0213 244 GLN A C
+2047 O O . GLN A 244 ? 0.2468 0.2530 0.2417 -0.0083 0.0125 0.0179 244 GLN A O
+2048 C CB . GLN A 244 ? 0.2529 0.2757 0.2816 -0.0048 0.0101 0.0335 244 GLN A CB
+2049 C CG . GLN A 244 ? 0.3001 0.3180 0.3193 -0.0031 0.0191 0.0332 244 GLN A CG
+2050 C CD . GLN A 244 ? 0.3381 0.3566 0.3501 -0.0062 0.0161 0.0309 244 GLN A CD
+2051 O OE1 . GLN A 244 ? 0.3514 0.3767 0.3719 -0.0076 0.0105 0.0337 244 GLN A OE1
+2052 N NE2 . GLN A 244 ? 0.3302 0.3412 0.3261 -0.0076 0.0196 0.0259 244 GLN A NE2
+2053 N N . ASP A 245 ? 0.2271 0.2384 0.2386 -0.0060 0.0086 0.0214 245 ASP A N
+2054 C CA . ASP A 245 ? 0.2274 0.2313 0.2287 -0.0056 0.0124 0.0166 245 ASP A CA
+2055 C C . ASP A 245 ? 0.2178 0.2185 0.2068 -0.0093 0.0079 0.0104 245 ASP A C
+2056 O O . ASP A 245 ? 0.2251 0.2189 0.2021 -0.0101 0.0116 0.0070 245 ASP A O
+2057 C CB . ASP A 245 ? 0.2592 0.2649 0.2687 -0.0042 0.0107 0.0180 245 ASP A CB
+2058 C CG . ASP A 245 ? 0.3428 0.3489 0.3613 -0.0002 0.0180 0.0237 245 ASP A CG
+2059 O OD1 . ASP A 245 ? 0.3544 0.3601 0.3744 0.0020 0.0244 0.0273 245 ASP A OD1
+2060 O OD2 . ASP A 245 ? 0.3785 0.3852 0.4024 0.0008 0.0174 0.0248 245 ASP A OD2
+2061 N N . HIS A 246 ? 0.2032 0.2084 0.1955 -0.0114 0.0000 0.0096 246 HIS A N
+2062 C CA . HIS A 246 ? 0.2009 0.2041 0.1837 -0.0146 -0.0039 0.0052 246 HIS A CA
+2063 C C . HIS A 246 ? 0.2030 0.2044 0.1775 -0.0167 -0.0019 0.0047 246 HIS A C
+2064 O O . HIS A 246 ? 0.2037 0.2007 0.1676 -0.0192 -0.0020 0.0017 246 HIS A O
+2065 C CB . HIS A 246 ? 0.2012 0.2089 0.1896 -0.0157 -0.0114 0.0055 246 HIS A CB
+2066 C CG . HIS A 246 ? 0.2251 0.2332 0.2186 -0.0144 -0.0143 0.0054 246 HIS A CG
+2067 N ND1 . HIS A 246 ? 0.2381 0.2491 0.2389 -0.0146 -0.0197 0.0075 246 HIS A ND1
+2068 C CD2 . HIS A 246 ? 0.2434 0.2488 0.2352 -0.0134 -0.0129 0.0037 246 HIS A CD2
+2069 C CE1 . HIS A 246 ? 0.2470 0.2568 0.2495 -0.0138 -0.0215 0.0070 246 HIS A CE1
+2070 N NE2 . HIS A 246 ? 0.2537 0.2608 0.2516 -0.0129 -0.0174 0.0048 246 HIS A NE2
+2071 N N . VAL A 247 ? 0.2002 0.2054 0.1801 -0.0161 -0.0010 0.0083 247 VAL A N
+2072 C CA . VAL A 247 ? 0.2044 0.2082 0.1767 -0.0182 0.0010 0.0085 247 VAL A CA
+2073 C C . VAL A 247 ? 0.2190 0.2136 0.1784 -0.0181 0.0082 0.0065 247 VAL A C
+2074 O O . VAL A 247 ? 0.2279 0.2181 0.1753 -0.0215 0.0078 0.0042 247 VAL A O
+2075 C CB . VAL A 247 ? 0.2085 0.2181 0.1902 -0.0168 0.0018 0.0134 247 VAL A CB
+2076 C CG1 . VAL A 247 ? 0.2220 0.2293 0.1947 -0.0186 0.0050 0.0137 247 VAL A CG1
+2077 C CG2 . VAL A 247 ? 0.2124 0.2290 0.2044 -0.0177 -0.0057 0.0150 247 VAL A CG2
+2078 N N . ASP A 248 ? 0.2240 0.2157 0.1861 -0.0143 0.0144 0.0078 248 ASP A N
+2079 C CA . ASP A 248 ? 0.2398 0.2205 0.1885 -0.0134 0.0226 0.0058 248 ASP A CA
+2080 C C . ASP A 248 ? 0.2470 0.2205 0.1838 -0.0164 0.0205 0.0006 248 ASP A C
+2081 O O . ASP A 248 ? 0.2636 0.2275 0.1848 -0.0189 0.0234 -0.0021 248 ASP A O
+2082 C CB . ASP A 248 ? 0.2546 0.2342 0.2111 -0.0081 0.0302 0.0092 248 ASP A CB
+2083 C CG . ASP A 248 ? 0.2938 0.2793 0.2610 -0.0051 0.0336 0.0155 248 ASP A CG
+2084 O OD1 . ASP A 248 ? 0.3003 0.2881 0.2652 -0.0070 0.0318 0.0162 248 ASP A OD1
+2085 O OD2 . ASP A 248 ? 0.3247 0.3128 0.3031 -0.0010 0.0376 0.0200 248 ASP A OD2
+2086 N N . ILE A 249 ? 0.2398 0.2176 0.1835 -0.0165 0.0152 -0.0006 249 ILE A N
+2087 C CA . ILE A 249 ? 0.2522 0.2245 0.1865 -0.0193 0.0126 -0.0048 249 ILE A CA
+2088 C C . ILE A 249 ? 0.2467 0.2183 0.1717 -0.0247 0.0074 -0.0062 249 ILE A C
+2089 O O . ILE A 249 ? 0.2569 0.2212 0.1701 -0.0279 0.0069 -0.0089 249 ILE A O
+2090 C CB . ILE A 249 ? 0.2738 0.2517 0.2187 -0.0177 0.0083 -0.0049 249 ILE A CB
+2091 C CG1 . ILE A 249 ? 0.2886 0.2655 0.2407 -0.0132 0.0136 -0.0033 249 ILE A CG1
+2092 C CG2 . ILE A 249 ? 0.2960 0.2709 0.2335 -0.0209 0.0042 -0.0082 249 ILE A CG2
+2093 C CD1 . ILE A 249 ? 0.3018 0.2864 0.2672 -0.0115 0.0089 -0.0017 249 ILE A CD1
+2094 N N . LEU A 250 ? 0.2261 0.2054 0.1573 -0.0259 0.0032 -0.0039 250 LEU A N
+2095 C CA . LEU A 250 ? 0.2291 0.2096 0.1540 -0.0310 -0.0018 -0.0037 250 LEU A CA
+2096 C C . LEU A 250 ? 0.2518 0.2255 0.1636 -0.0339 0.0017 -0.0036 250 LEU A C
+2097 O O . LEU A 250 ? 0.2569 0.2306 0.1623 -0.0388 -0.0024 -0.0030 250 LEU A O
+2098 C CB . LEU A 250 ? 0.2045 0.1956 0.1420 -0.0306 -0.0071 -0.0010 250 LEU A CB
+2099 C CG . LEU A 250 ? 0.1998 0.1957 0.1467 -0.0288 -0.0113 -0.0014 250 LEU A CG
+2100 C CD1 . LEU A 250 ? 0.1986 0.2022 0.1567 -0.0275 -0.0148 0.0013 250 LEU A CD1
+2101 C CD2 . LEU A 250 ? 0.2085 0.2031 0.1500 -0.0320 -0.0152 -0.0024 250 LEU A CD2
+2102 N N . GLY A 251 ? 0.2570 0.2248 0.1650 -0.0307 0.0094 -0.0036 251 GLY A N
+2103 C CA . GLY A 251 ? 0.2790 0.2382 0.1725 -0.0327 0.0142 -0.0036 251 GLY A CA
+2104 C C . GLY A 251 ? 0.3006 0.2497 0.1753 -0.0393 0.0116 -0.0062 251 GLY A C
+2105 O O . GLY A 251 ? 0.3064 0.2557 0.1743 -0.0440 0.0085 -0.0049 251 GLY A O
+2106 N N . PRO A 252 ? 0.3063 0.2471 0.1729 -0.0404 0.0118 -0.0095 252 PRO A N
+2107 C CA . PRO A 252 ? 0.3173 0.2481 0.1658 -0.0477 0.0081 -0.0113 252 PRO A CA
+2108 C C . PRO A 252 ? 0.3076 0.2475 0.1604 -0.0534 -0.0017 -0.0086 252 PRO A C
+2109 O O . PRO A 252 ? 0.3219 0.2563 0.1613 -0.0599 -0.0047 -0.0078 252 PRO A O
+2110 C CB . PRO A 252 ? 0.3331 0.2562 0.1776 -0.0468 0.0095 -0.0146 252 PRO A CB
+2111 C CG . PRO A 252 ? 0.3405 0.2637 0.1935 -0.0389 0.0180 -0.0148 252 PRO A CG
+2112 C CD . PRO A 252 ? 0.3076 0.2467 0.1802 -0.0356 0.0156 -0.0111 252 PRO A CD
+2113 N N . LEU A 253 ? 0.2874 0.2407 0.1582 -0.0512 -0.0065 -0.0066 253 LEU A N
+2114 C CA . LEU A 253 ? 0.2797 0.2418 0.1560 -0.0557 -0.0145 -0.0031 253 LEU A CA
+2115 C C . LEU A 253 ? 0.2847 0.2525 0.1635 -0.0570 -0.0153 0.0001 253 LEU A C
+2116 O O . LEU A 253 ? 0.2944 0.2644 0.1698 -0.0629 -0.0206 0.0032 253 LEU A O
+2117 C CB . LEU A 253 ? 0.2645 0.2373 0.1577 -0.0522 -0.0181 -0.0020 253 LEU A CB
+2118 C CG . LEU A 253 ? 0.2797 0.2484 0.1705 -0.0525 -0.0193 -0.0040 253 LEU A CG
+2119 C CD1 . LEU A 253 ? 0.2723 0.2503 0.1790 -0.0479 -0.0212 -0.0033 253 LEU A CD1
+2120 C CD2 . LEU A 253 ? 0.3014 0.2666 0.1826 -0.0600 -0.0251 -0.0021 253 LEU A CD2
+2121 N N . SER A 254 ? 0.2804 0.2509 0.1657 -0.0518 -0.0101 0.0001 254 SER A N
+2122 C CA . SER A 254 ? 0.2840 0.2596 0.1720 -0.0525 -0.0100 0.0032 254 SER A CA
+2123 C C . SER A 254 ? 0.3057 0.2704 0.1738 -0.0578 -0.0082 0.0029 254 SER A C
+2124 O O . SER A 254 ? 0.3123 0.2805 0.1782 -0.0624 -0.0119 0.0061 254 SER A O
+2125 C CB . SER A 254 ? 0.2930 0.2724 0.1917 -0.0456 -0.0043 0.0035 254 SER A CB
+2126 O OG . SER A 254 ? 0.3179 0.3022 0.2193 -0.0461 -0.0039 0.0068 254 SER A OG
+2127 N N . ALA A 255 ? 0.3155 0.2664 0.1685 -0.0573 -0.0023 -0.0008 255 ALA A N
+2128 C CA . ALA A 255 ? 0.3400 0.2771 0.1707 -0.0623 0.0002 -0.0017 255 ALA A CA
+2129 C C . ALA A 255 ? 0.3655 0.2991 0.1848 -0.0715 -0.0082 -0.0007 255 ALA A C
+2130 O O . ALA A 255 ? 0.3732 0.3025 0.1802 -0.0774 -0.0103 0.0012 255 ALA A O
+2131 C CB . ALA A 255 ? 0.3488 0.2704 0.1658 -0.0590 0.0091 -0.0060 255 ALA A CB
+2132 N N . GLN A 256 ? 0.3714 0.3069 0.1952 -0.0729 -0.0131 -0.0013 256 GLN A N
+2133 C CA . GLN A 256 ? 0.3882 0.3212 0.2036 -0.0818 -0.0217 0.0009 256 GLN A CA
+2134 C C . GLN A 256 ? 0.3764 0.3230 0.2027 -0.0857 -0.0289 0.0071 256 GLN A C
+2135 O O . GLN A 256 ? 0.3964 0.3390 0.2109 -0.0941 -0.0342 0.0102 256 GLN A O
+2136 C CB . GLN A 256 ? 0.4192 0.3527 0.2398 -0.0813 -0.0246 -0.0004 256 GLN A CB
+2137 C CG . GLN A 256 ? 0.4812 0.4119 0.2938 -0.0905 -0.0335 0.0028 256 GLN A CG
+2138 C CD . GLN A 256 ? 0.5459 0.4792 0.3663 -0.0894 -0.0364 0.0025 256 GLN A CD
+2139 O OE1 . GLN A 256 ? 0.5664 0.4991 0.3928 -0.0825 -0.0312 -0.0015 256 GLN A OE1
+2140 N NE2 . GLN A 256 ? 0.5577 0.4944 0.3791 -0.0964 -0.0450 0.0075 256 GLN A NE2
+2141 N N . THR A 257 ? 0.3374 0.2991 0.1853 -0.0801 -0.0291 0.0093 257 THR A N
+2142 C CA . THR A 257 ? 0.3177 0.2924 0.1780 -0.0828 -0.0352 0.0154 257 THR A CA
+2143 C C . THR A 257 ? 0.3148 0.2937 0.1766 -0.0824 -0.0332 0.0176 257 THR A C
+2144 O O . THR A 257 ? 0.3169 0.3048 0.1857 -0.0860 -0.0382 0.0231 257 THR A O
+2145 C CB . THR A 257 ? 0.3105 0.2976 0.1920 -0.0770 -0.0364 0.0167 257 THR A CB
+2146 O OG1 . THR A 257 ? 0.3100 0.2992 0.1997 -0.0691 -0.0302 0.0135 257 THR A OG1
+2147 C CG2 . THR A 257 ? 0.3140 0.2985 0.1956 -0.0772 -0.0386 0.0155 257 THR A CG2
+2148 N N . GLY A 258 ? 0.3055 0.2787 0.1625 -0.0777 -0.0256 0.0140 258 GLY A N
+2149 C CA . GLY A 258 ? 0.3007 0.2784 0.1606 -0.0763 -0.0230 0.0162 258 GLY A CA
+2150 C C . GLY A 258 ? 0.2790 0.2716 0.1619 -0.0707 -0.0237 0.0188 258 GLY A C
+2151 O O . GLY A 258 ? 0.2760 0.2747 0.1645 -0.0699 -0.0229 0.0217 258 GLY A O
+2152 N N . ILE A 259 ? 0.2544 0.2524 0.1504 -0.0664 -0.0249 0.0176 259 ILE A N
+2153 C CA . ILE A 259 ? 0.2404 0.2499 0.1558 -0.0614 -0.0257 0.0196 259 ILE A CA
+2154 C C . ILE A 259 ? 0.2324 0.2402 0.1529 -0.0544 -0.0200 0.0163 259 ILE A C
+2155 O O . ILE A 259 ? 0.2410 0.2438 0.1594 -0.0521 -0.0183 0.0128 259 ILE A O
+2156 C CB . ILE A 259 ? 0.2472 0.2634 0.1733 -0.0617 -0.0310 0.0216 259 ILE A CB
+2157 C CG1 . ILE A 259 ? 0.2679 0.2870 0.1908 -0.0690 -0.0367 0.0267 259 ILE A CG1
+2158 C CG2 . ILE A 259 ? 0.2428 0.2682 0.1863 -0.0565 -0.0312 0.0231 259 ILE A CG2
+2159 C CD1 . ILE A 259 ? 0.2874 0.3119 0.2193 -0.0695 -0.0411 0.0296 259 ILE A CD1
+2160 N N . ALA A 260 ? 0.2177 0.2297 0.1452 -0.0512 -0.0172 0.0179 260 ALA A N
+2161 C CA . ALA A 260 ? 0.2111 0.2229 0.1457 -0.0449 -0.0123 0.0165 260 ALA A CA
+2162 C C . ALA A 260 ? 0.1974 0.2133 0.1439 -0.0416 -0.0150 0.0154 260 ALA A C
+2163 O O . ALA A 260 ? 0.1930 0.2148 0.1470 -0.0426 -0.0201 0.0169 260 ALA A O
+2164 C CB . ALA A 260 ? 0.2178 0.2359 0.1611 -0.0428 -0.0106 0.0202 260 ALA A CB
+2165 N N . VAL A 261 ? 0.1862 0.1984 0.1340 -0.0375 -0.0114 0.0130 261 VAL A N
+2166 C CA . VAL A 261 ? 0.1849 0.1997 0.1422 -0.0346 -0.0140 0.0118 261 VAL A CA
+2167 C C . VAL A 261 ? 0.1738 0.1965 0.1447 -0.0331 -0.0179 0.0145 261 VAL A C
+2168 O O . VAL A 261 ? 0.1797 0.2045 0.1548 -0.0332 -0.0219 0.0141 261 VAL A O
+2169 C CB . VAL A 261 ? 0.2018 0.2123 0.1596 -0.0306 -0.0094 0.0099 261 VAL A CB
+2170 C CG1 . VAL A 261 ? 0.1959 0.2093 0.1635 -0.0281 -0.0127 0.0092 261 VAL A CG1
+2171 C CG2 . VAL A 261 ? 0.2294 0.2303 0.1728 -0.0321 -0.0058 0.0066 261 VAL A CG2
+2172 N N . LEU A 262 ? 0.1670 0.1935 0.1440 -0.0319 -0.0165 0.0175 262 LEU A N
+2173 C CA . LEU A 262 ? 0.1643 0.1971 0.1536 -0.0308 -0.0205 0.0201 262 LEU A CA
+2174 C C . LEU A 262 ? 0.1622 0.1988 0.1522 -0.0338 -0.0245 0.0217 262 LEU A C
+2175 O O . LEU A 262 ? 0.1616 0.2008 0.1595 -0.0329 -0.0281 0.0226 262 LEU A O
+2176 C CB . LEU A 262 ? 0.1625 0.1988 0.1594 -0.0288 -0.0184 0.0237 262 LEU A CB
+2177 C CG . LEU A 262 ? 0.1797 0.2140 0.1806 -0.0252 -0.0152 0.0239 262 LEU A CG
+2178 C CD1 . LEU A 262 ? 0.1849 0.2233 0.1941 -0.0233 -0.0126 0.0290 262 LEU A CD1
+2179 C CD2 . LEU A 262 ? 0.1798 0.2139 0.1872 -0.0239 -0.0195 0.0228 262 LEU A CD2
+2180 N N . ASP A 263 ? 0.1652 0.2012 0.1467 -0.0376 -0.0240 0.0223 263 ASP A N
+2181 C CA . ASP A 263 ? 0.1578 0.1982 0.1413 -0.0407 -0.0279 0.0249 263 ASP A CA
+2182 C C . ASP A 263 ? 0.1734 0.2122 0.1570 -0.0405 -0.0304 0.0233 263 ASP A C
+2183 O O . ASP A 263 ? 0.1790 0.2213 0.1698 -0.0400 -0.0331 0.0254 263 ASP A O
+2184 C CB . ASP A 263 ? 0.1698 0.2097 0.1437 -0.0457 -0.0277 0.0267 263 ASP A CB
+2185 C CG . ASP A 263 ? 0.1838 0.2253 0.1567 -0.0461 -0.0250 0.0288 263 ASP A CG
+2186 O OD1 . ASP A 263 ? 0.1696 0.2137 0.1512 -0.0423 -0.0234 0.0296 263 ASP A OD1
+2187 O OD2 . ASP A 263 ? 0.2039 0.2440 0.1674 -0.0504 -0.0248 0.0302 263 ASP A OD2
+2188 N N . MET A 264 ? 0.1646 0.1978 0.1403 -0.0405 -0.0289 0.0199 264 MET A N
+2189 C CA . MET A 264 ? 0.1588 0.1907 0.1351 -0.0398 -0.0309 0.0187 264 MET A CA
+2190 C C . MET A 264 ? 0.1625 0.1947 0.1475 -0.0352 -0.0315 0.0177 264 MET A C
+2191 O O . MET A 264 ? 0.1712 0.2041 0.1599 -0.0342 -0.0334 0.0186 264 MET A O
+2192 C CB . MET A 264 ? 0.1777 0.2035 0.1444 -0.0407 -0.0293 0.0155 264 MET A CB
+2193 C CG . MET A 264 ? 0.1885 0.2142 0.1558 -0.0409 -0.0317 0.0157 264 MET A CG
+2194 S SD . MET A 264 ? 0.2095 0.2401 0.1771 -0.0463 -0.0356 0.0214 264 MET A SD
+2195 C CE . MET A 264 ? 0.2483 0.2724 0.2007 -0.0520 -0.0357 0.0202 264 MET A CE
+2196 N N . CYS A 265 ? 0.1567 0.1879 0.1448 -0.0327 -0.0301 0.0165 265 CYS A N
+2197 C CA . CYS A 265 ? 0.1578 0.1883 0.1529 -0.0294 -0.0318 0.0160 265 CYS A CA
+2198 C C . CYS A 265 ? 0.1576 0.1912 0.1591 -0.0295 -0.0343 0.0189 265 CYS A C
+2199 O O . CYS A 265 ? 0.1637 0.1946 0.1675 -0.0276 -0.0360 0.0183 265 CYS A O
+2200 C CB . CYS A 265 ? 0.1574 0.1875 0.1559 -0.0276 -0.0304 0.0160 265 CYS A CB
+2201 S SG . CYS A 265 ? 0.1704 0.1959 0.1636 -0.0262 -0.0268 0.0129 265 CYS A SG
+2202 N N . ALA A 266 ? 0.1530 0.1913 0.1565 -0.0317 -0.0343 0.0220 266 ALA A N
+2203 C CA . ALA A 266 ? 0.1644 0.2059 0.1747 -0.0318 -0.0364 0.0252 266 ALA A CA
+2204 C C . ALA A 266 ? 0.1744 0.2162 0.1842 -0.0323 -0.0370 0.0266 266 ALA A C
+2205 O O . ALA A 266 ? 0.1850 0.2259 0.1996 -0.0305 -0.0379 0.0280 266 ALA A O
+2206 C CB . ALA A 266 ? 0.1742 0.2213 0.1873 -0.0342 -0.0362 0.0287 266 ALA A CB
+2207 N N . SER A 267 ? 0.1711 0.2133 0.1750 -0.0346 -0.0364 0.0266 267 SER A N
+2208 C CA . SER A 267 ? 0.1762 0.2192 0.1808 -0.0350 -0.0370 0.0290 267 SER A CA
+2209 C C . SER A 267 ? 0.1678 0.2053 0.1723 -0.0308 -0.0364 0.0261 267 SER A C
+2210 O O . SER A 267 ? 0.1705 0.2073 0.1788 -0.0287 -0.0360 0.0283 267 SER A O
+2211 C CB . SER A 267 ? 0.2095 0.2533 0.2072 -0.0390 -0.0373 0.0297 267 SER A CB
+2212 O OG . SER A 267 ? 0.2588 0.3075 0.2561 -0.0436 -0.0386 0.0337 267 SER A OG
+2213 N N . LEU A 268 ? 0.1561 0.1892 0.1560 -0.0295 -0.0358 0.0216 268 LEU A N
+2214 C CA . LEU A 268 ? 0.1563 0.1837 0.1548 -0.0260 -0.0354 0.0188 268 LEU A CA
+2215 C C . LEU A 268 ? 0.1657 0.1895 0.1678 -0.0233 -0.0363 0.0187 268 LEU A C
+2216 O O . LEU A 268 ? 0.1637 0.1828 0.1651 -0.0206 -0.0357 0.0187 268 LEU A O
+2217 C CB . LEU A 268 ? 0.1529 0.1770 0.1465 -0.0255 -0.0348 0.0147 268 LEU A CB
+2218 C CG . LEU A 268 ? 0.1661 0.1844 0.1579 -0.0223 -0.0349 0.0118 268 LEU A CG
+2219 C CD1 . LEU A 268 ? 0.1760 0.1930 0.1665 -0.0209 -0.0341 0.0130 268 LEU A CD1
+2220 C CD2 . LEU A 268 ? 0.1727 0.1891 0.1609 -0.0223 -0.0341 0.0087 268 LEU A CD2
+2221 N N . LYS A 269 ? 0.1523 0.1773 0.1577 -0.0241 -0.0375 0.0191 269 LYS A N
+2222 C CA . LYS A 269 ? 0.1498 0.1707 0.1582 -0.0225 -0.0392 0.0194 269 LYS A CA
+2223 C C . LYS A 269 ? 0.1584 0.1790 0.1695 -0.0214 -0.0383 0.0224 269 LYS A C
+2224 O O . LYS A 269 ? 0.1699 0.1828 0.1789 -0.0188 -0.0381 0.0215 269 LYS A O
+2225 C CB . LYS A 269 ? 0.1600 0.1846 0.1732 -0.0242 -0.0407 0.0208 269 LYS A CB
+2226 C CG . LYS A 269 ? 0.2053 0.2261 0.2223 -0.0235 -0.0433 0.0219 269 LYS A CG
+2227 C CD . LYS A 269 ? 0.2400 0.2659 0.2629 -0.0252 -0.0448 0.0241 269 LYS A CD
+2228 C CE . LYS A 269 ? 0.2824 0.3067 0.3105 -0.0255 -0.0474 0.0265 269 LYS A CE
+2229 N NZ . LYS A 269 ? 0.2965 0.3278 0.3318 -0.0272 -0.0484 0.0298 269 LYS A NZ
+2230 N N . GLU A 270 ? 0.1579 0.1859 0.1729 -0.0234 -0.0374 0.0264 270 GLU A N
+2231 C CA . GLU A 270 ? 0.1697 0.1985 0.1891 -0.0223 -0.0360 0.0306 270 GLU A CA
+2232 C C . GLU A 270 ? 0.1841 0.2088 0.2007 -0.0194 -0.0335 0.0309 270 GLU A C
+2233 O O . GLU A 270 ? 0.1935 0.2128 0.2111 -0.0162 -0.0315 0.0324 270 GLU A O
+2234 C CB . GLU A 270 ? 0.2006 0.2393 0.2255 -0.0258 -0.0363 0.0358 270 GLU A CB
+2235 C CG . GLU A 270 ? 0.2905 0.3331 0.3190 -0.0280 -0.0381 0.0365 270 GLU A CG
+2236 C CD . GLU A 270 ? 0.3871 0.4255 0.4198 -0.0259 -0.0388 0.0367 270 GLU A CD
+2237 O OE1 . GLU A 270 ? 0.4059 0.4431 0.4426 -0.0243 -0.0375 0.0400 270 GLU A OE1
+2238 O OE2 . GLU A 270 ? 0.4043 0.4403 0.4364 -0.0260 -0.0407 0.0342 270 GLU A OE2
+2239 N N . LEU A 271 ? 0.1794 0.2056 0.1921 -0.0203 -0.0333 0.0295 271 LEU A N
+2240 C CA . LEU A 271 ? 0.1824 0.2050 0.1928 -0.0174 -0.0309 0.0300 271 LEU A CA
+2241 C C . LEU A 271 ? 0.1924 0.2041 0.1972 -0.0133 -0.0299 0.0258 271 LEU A C
+2242 O O . LEU A 271 ? 0.2133 0.2197 0.2169 -0.0095 -0.0268 0.0273 271 LEU A O
+2243 C CB . LEU A 271 ? 0.1825 0.2083 0.1894 -0.0196 -0.0316 0.0289 271 LEU A CB
+2244 C CG . LEU A 271 ? 0.1939 0.2284 0.2042 -0.0240 -0.0327 0.0340 271 LEU A CG
+2245 C CD1 . LEU A 271 ? 0.2015 0.2366 0.2060 -0.0269 -0.0339 0.0316 271 LEU A CD1
+2246 C CD2 . LEU A 271 ? 0.2042 0.2418 0.2211 -0.0226 -0.0308 0.0409 271 LEU A CD2
+2247 N N . LEU A 272 ? 0.1758 0.1833 0.1766 -0.0139 -0.0325 0.0211 272 LEU A N
+2248 C CA . LEU A 272 ? 0.1901 0.1864 0.1843 -0.0111 -0.0327 0.0173 272 LEU A CA
+2249 C C . LEU A 272 ? 0.2116 0.2007 0.2057 -0.0091 -0.0319 0.0186 272 LEU A C
+2250 O O . LEU A 272 ? 0.2267 0.2053 0.2144 -0.0057 -0.0297 0.0175 272 LEU A O
+2251 C CB . LEU A 272 ? 0.1912 0.1860 0.1829 -0.0130 -0.0362 0.0135 272 LEU A CB
+2252 C CG . LEU A 272 ? 0.2166 0.2148 0.2063 -0.0139 -0.0361 0.0114 272 LEU A CG
+2253 C CD1 . LEU A 272 ? 0.2272 0.2256 0.2170 -0.0157 -0.0389 0.0091 272 LEU A CD1
+2254 C CD2 . LEU A 272 ? 0.2454 0.2379 0.2294 -0.0109 -0.0341 0.0099 272 LEU A CD2
+2255 N N . GLN A 273 ? 0.2054 0.1992 0.2057 -0.0112 -0.0335 0.0209 273 GLN A N
+2256 C CA . GLN A 273 ? 0.2237 0.2105 0.2243 -0.0099 -0.0332 0.0221 273 GLN A CA
+2257 C C . GLN A 273 ? 0.2527 0.2390 0.2565 -0.0068 -0.0283 0.0266 273 GLN A C
+2258 O O . GLN A 273 ? 0.2737 0.2493 0.2739 -0.0040 -0.0263 0.0267 273 GLN A O
+2259 C CB . GLN A 273 ? 0.2243 0.2171 0.2315 -0.0133 -0.0367 0.0234 273 GLN A CB
+2260 C CG . GLN A 273 ? 0.2464 0.2378 0.2515 -0.0156 -0.0413 0.0202 273 GLN A CG
+2261 C CD . GLN A 273 ? 0.2852 0.2832 0.2979 -0.0185 -0.0442 0.0225 273 GLN A CD
+2262 O OE1 . GLN A 273 ? 0.3006 0.3075 0.3202 -0.0196 -0.0430 0.0261 273 GLN A OE1
+2263 N NE2 . GLN A 273 ? 0.2929 0.2871 0.3048 -0.0200 -0.0483 0.0211 273 GLN A NE2
+2264 N N . ASN A 274 ? 0.2545 0.2516 0.2649 -0.0075 -0.0264 0.0309 274 ASN A N
+2265 C CA . ASN A 274 ? 0.2714 0.2704 0.2878 -0.0049 -0.0218 0.0371 274 ASN A CA
+2266 C C . ASN A 274 ? 0.2823 0.2817 0.2981 -0.0020 -0.0178 0.0397 274 ASN A C
+2267 O O . ASN A 274 ? 0.2916 0.2917 0.3129 0.0010 -0.0132 0.0457 274 ASN A O
+2268 C CB . ASN A 274 ? 0.2879 0.2999 0.3149 -0.0086 -0.0232 0.0426 274 ASN A CB
+2269 C CG . ASN A 274 ? 0.3608 0.3720 0.3895 -0.0106 -0.0263 0.0411 274 ASN A CG
+2270 O OD1 . ASN A 274 ? 0.3974 0.4019 0.4271 -0.0083 -0.0247 0.0422 274 ASN A OD1
+2271 N ND2 . ASN A 274 ? 0.3745 0.3917 0.4032 -0.0146 -0.0305 0.0387 274 ASN A ND2
+2272 N N . GLY A 275 ? 0.2828 0.2823 0.2932 -0.0028 -0.0193 0.0359 275 GLY A N
+2273 C CA . GLY A 275 ? 0.2865 0.2874 0.2970 -0.0005 -0.0161 0.0386 275 GLY A CA
+2274 C C . GLY A 275 ? 0.2849 0.2996 0.3049 -0.0041 -0.0171 0.0452 275 GLY A C
+2275 O O . GLY A 275 ? 0.2838 0.3064 0.3087 -0.0085 -0.0203 0.0469 275 GLY A O
+2276 N N A MET A 276 ? 0.2877 0.3051 0.3100 -0.0024 -0.0146 0.0494 276 MET A N
+2277 N N B MET A 276 ? 0.2802 0.2977 0.3025 -0.0025 -0.0147 0.0494 276 MET A N
+2278 C CA A MET A 276 ? 0.2918 0.3217 0.3226 -0.0067 -0.0165 0.0565 276 MET A CA
+2279 C CA B MET A 276 ? 0.2766 0.3065 0.3075 -0.0066 -0.0165 0.0566 276 MET A CA
+2280 C C A MET A 276 ? 0.2913 0.3266 0.3338 -0.0049 -0.0128 0.0668 276 MET A C
+2281 C C B MET A 276 ? 0.2834 0.3188 0.3259 -0.0052 -0.0132 0.0666 276 MET A C
+2282 O O A MET A 276 ? 0.2868 0.3330 0.3374 -0.0092 -0.0151 0.0741 276 MET A O
+2283 O O B MET A 276 ? 0.2781 0.3245 0.3285 -0.0099 -0.0158 0.0734 276 MET A O
+2284 C CB A MET A 276 ? 0.3085 0.3402 0.3362 -0.0077 -0.0176 0.0558 276 MET A CB
+2285 C CB B MET A 276 ? 0.2735 0.3053 0.3025 -0.0070 -0.0168 0.0572 276 MET A CB
+2286 C CG A MET A 276 ? 0.3395 0.3688 0.3581 -0.0109 -0.0218 0.0471 276 MET A CG
+2287 C CG B MET A 276 ? 0.2760 0.3074 0.2968 -0.0110 -0.0214 0.0498 276 MET A CG
+2288 S SD A MET A 276 ? 0.4400 0.4671 0.4525 -0.0105 -0.0223 0.0438 276 MET A SD
+2289 S SD B MET A 276 ? 0.2332 0.2709 0.2548 -0.0145 -0.0237 0.0531 276 MET A SD
+2290 C CE A MET A 276 ? 0.3629 0.4010 0.3831 -0.0152 -0.0244 0.0528 276 MET A CE
+2291 C CE B MET A 276 ? 0.2208 0.2526 0.2310 -0.0159 -0.0263 0.0426 276 MET A CE
+2292 N N . ASN A 277 ? 0.2923 0.3197 0.3354 0.0008 -0.0075 0.0678 277 ASN A N
+2293 C CA . ASN A 277 ? 0.2954 0.3270 0.3503 0.0034 -0.0029 0.0778 277 ASN A CA
+2294 C C . ASN A 277 ? 0.2873 0.3268 0.3515 0.0043 -0.0004 0.0878 277 ASN A C
+2295 O O . ASN A 277 ? 0.2883 0.3383 0.3654 0.0022 -0.0004 0.0980 277 ASN A O
+2296 C CB . ASN A 277 ? 0.3146 0.3549 0.3771 -0.0016 -0.0066 0.0811 277 ASN A CB
+2297 C CG . ASN A 277 ? 0.3801 0.4120 0.4375 -0.0004 -0.0067 0.0749 277 ASN A CG
+2298 O OD1 . ASN A 277 ? 0.4070 0.4407 0.4607 -0.0050 -0.0120 0.0694 277 ASN A OD1
+2299 N ND2 . ASN A 277 ? 0.3897 0.4116 0.4467 0.0058 -0.0005 0.0760 277 ASN A ND2
+2300 N N . GLY A 278 ? 0.2732 0.3084 0.3318 0.0070 0.0013 0.0856 278 GLY A N
+2301 C CA . GLY A 278 ? 0.2576 0.3004 0.3255 0.0080 0.0034 0.0955 278 GLY A CA
+2302 C C . GLY A 278 ? 0.2420 0.2976 0.3147 -0.0003 -0.0042 0.0992 278 GLY A C
+2303 O O . GLY A 278 ? 0.2411 0.3048 0.3234 -0.0011 -0.0039 0.1091 278 GLY A O
+2304 N N A ARG A 279 ? 0.2374 0.2940 0.3026 -0.0066 -0.0109 0.0916 279 ARG A N
+2305 N N B ARG A 279 ? 0.2343 0.2909 0.2996 -0.0067 -0.0110 0.0916 279 ARG A N
+2306 C CA A ARG A 279 ? 0.2322 0.2977 0.2981 -0.0149 -0.0181 0.0936 279 ARG A CA
+2307 C CA B ARG A 279 ? 0.2260 0.2915 0.2918 -0.0151 -0.0183 0.0935 279 ARG A CA
+2308 C C A ARG A 279 ? 0.2276 0.2883 0.2826 -0.0159 -0.0206 0.0856 279 ARG A C
+2309 C C B ARG A 279 ? 0.2250 0.2857 0.2799 -0.0160 -0.0206 0.0856 279 ARG A C
+2310 O O A ARG A 279 ? 0.2311 0.2822 0.2782 -0.0106 -0.0172 0.0780 279 ARG A O
+2311 O O B ARG A 279 ? 0.2290 0.2801 0.2759 -0.0107 -0.0173 0.0778 279 ARG A O
+2312 C CB A ARG A 279 ? 0.2510 0.3206 0.3158 -0.0214 -0.0232 0.0918 279 ARG A CB
+2313 C CB B ARG A 279 ? 0.2362 0.3051 0.2999 -0.0213 -0.0233 0.0907 279 ARG A CB
+2314 C CG A ARG A 279 ? 0.2938 0.3698 0.3709 -0.0211 -0.0214 0.1010 279 ARG A CG
+2315 C CG B ARG A 279 ? 0.2661 0.3395 0.3403 -0.0205 -0.0212 0.0976 279 ARG A CG
+2316 C CD A ARG A 279 ? 0.3399 0.4224 0.4173 -0.0287 -0.0273 0.1016 279 ARG A CD
+2317 C CD B ARG A 279 ? 0.2998 0.3726 0.3693 -0.0240 -0.0245 0.0916 279 ARG A CD
+2318 N NE A ARG A 279 ? 0.3833 0.4723 0.4588 -0.0371 -0.0340 0.1049 279 ARG A NE
+2319 N NE B ARG A 279 ? 0.3295 0.4052 0.4085 -0.0223 -0.0219 0.0973 279 ARG A NE
+2320 C CZ A ARG A 279 ? 0.4179 0.5167 0.5037 -0.0417 -0.0368 0.1170 279 ARG A CZ
+2321 C CZ B ARG A 279 ? 0.3550 0.4260 0.4310 -0.0209 -0.0213 0.0917 279 ARG A CZ
+2322 N NH1 A ARG A 279 ? 0.4125 0.5171 0.5131 -0.0382 -0.0327 0.1276 279 ARG A NH1
+2323 N NH1 B ARG A 279 ? 0.3504 0.4141 0.4149 -0.0210 -0.0232 0.0809 279 ARG A NH1
+2324 N NH2 A ARG A 279 ? 0.4248 0.5272 0.5060 -0.0501 -0.0437 0.1190 279 ARG A NH2
+2325 N NH2 B ARG A 279 ? 0.3509 0.4248 0.4364 -0.0195 -0.0189 0.0976 279 ARG A NH2
+2326 N N . THR A 280 ? 0.2166 0.2832 0.2709 -0.0228 -0.0264 0.0879 280 THR A N
+2327 C CA . THR A 280 ? 0.2139 0.2762 0.2585 -0.0242 -0.0287 0.0810 280 THR A CA
+2328 C C . THR A 280 ? 0.2026 0.2653 0.2386 -0.0320 -0.0349 0.0758 280 THR A C
+2329 O O . THR A 280 ? 0.1972 0.2652 0.2356 -0.0377 -0.0384 0.0798 280 THR A O
+2330 C CB . THR A 280 ? 0.2364 0.3030 0.2869 -0.0242 -0.0288 0.0887 280 THR A CB
+2331 O OG1 . THR A 280 ? 0.2391 0.3154 0.2973 -0.0315 -0.0340 0.0988 280 THR A OG1
+2332 C CG2 . THR A 280 ? 0.2482 0.3129 0.3057 -0.0154 -0.0213 0.0936 280 THR A CG2
+2333 N N . ILE A 281 ? 0.1921 0.2483 0.2175 -0.0321 -0.0358 0.0669 281 ILE A N
+2334 C CA . ILE A 281 ? 0.1942 0.2484 0.2097 -0.0384 -0.0402 0.0613 281 ILE A CA
+2335 C C . ILE A 281 ? 0.1954 0.2471 0.2059 -0.0398 -0.0418 0.0598 281 ILE A C
+2336 O O . ILE A 281 ? 0.1929 0.2404 0.2021 -0.0344 -0.0387 0.0558 281 ILE A O
+2337 C CB . ILE A 281 ? 0.2069 0.2547 0.2150 -0.0359 -0.0385 0.0514 281 ILE A CB
+2338 C CG1 . ILE A 281 ? 0.2075 0.2576 0.2209 -0.0346 -0.0371 0.0531 281 ILE A CG1
+2339 C CG2 . ILE A 281 ? 0.2187 0.2634 0.2162 -0.0414 -0.0415 0.0459 281 ILE A CG2
+2340 C CD1 . ILE A 281 ? 0.2148 0.2592 0.2228 -0.0321 -0.0358 0.0447 281 ILE A CD1
+2341 N N . LEU A 282 ? 0.1976 0.2518 0.2056 -0.0474 -0.0470 0.0638 282 LEU A N
+2342 C CA . LEU A 282 ? 0.2014 0.2530 0.2048 -0.0495 -0.0492 0.0632 282 LEU A CA
+2343 C C . LEU A 282 ? 0.2114 0.2652 0.2233 -0.0435 -0.0461 0.0674 282 LEU A C
+2344 O O . LEU A 282 ? 0.2279 0.2771 0.2354 -0.0406 -0.0446 0.0622 282 LEU A O
+2345 C CB . LEU A 282 ? 0.2020 0.2448 0.1923 -0.0498 -0.0488 0.0523 282 LEU A CB
+2346 C CG . LEU A 282 ? 0.2157 0.2547 0.1952 -0.0564 -0.0518 0.0488 282 LEU A CG
+2347 C CD1 . LEU A 282 ? 0.2203 0.2506 0.1889 -0.0551 -0.0497 0.0390 282 LEU A CD1
+2348 C CD2 . LEU A 282 ? 0.2288 0.2691 0.2051 -0.0654 -0.0580 0.0555 282 LEU A CD2
+2349 N N . GLY A 283 ? 0.2195 0.2802 0.2437 -0.0412 -0.0443 0.0767 283 GLY A N
+2350 C CA . GLY A 283 ? 0.2237 0.2868 0.2570 -0.0349 -0.0402 0.0826 283 GLY A CA
+2351 C C . GLY A 283 ? 0.2283 0.2848 0.2593 -0.0257 -0.0334 0.0759 283 GLY A C
+2352 O O . GLY A 283 ? 0.2436 0.2998 0.2788 -0.0202 -0.0296 0.0791 283 GLY A O
+2353 N N A SER A 284 ? 0.2168 0.2675 0.2403 -0.0242 -0.0321 0.0668 284 SER A N
+2354 N N B SER A 284 ? 0.2200 0.2707 0.2436 -0.0242 -0.0321 0.0669 284 SER A N
+2355 C CA A SER A 284 ? 0.2108 0.2539 0.2303 -0.0166 -0.0269 0.0603 284 SER A CA
+2356 C CA B SER A 284 ? 0.2176 0.2606 0.2369 -0.0167 -0.0270 0.0601 284 SER A CA
+2357 C C A SER A 284 ? 0.2077 0.2497 0.2305 -0.0132 -0.0236 0.0613 284 SER A C
+2358 C C B SER A 284 ? 0.2128 0.2543 0.2350 -0.0132 -0.0236 0.0607 284 SER A C
+2359 O O A SER A 284 ? 0.2003 0.2455 0.2245 -0.0173 -0.0261 0.0621 284 SER A O
+2360 O O B SER A 284 ? 0.2104 0.2546 0.2333 -0.0172 -0.0261 0.0607 284 SER A O
+2361 C CB A SER A 284 ? 0.2234 0.2600 0.2319 -0.0177 -0.0285 0.0493 284 SER A CB
+2362 C CB B SER A 284 ? 0.2334 0.2699 0.2416 -0.0179 -0.0287 0.0492 284 SER A CB
+2363 O OG A SER A 284 ? 0.2520 0.2810 0.2562 -0.0114 -0.0246 0.0435 284 SER A OG
+2364 O OG B SER A 284 ? 0.2558 0.2918 0.2605 -0.0199 -0.0308 0.0477 284 SER A OG
+2365 N N . ALA A 285 ? 0.2088 0.2447 0.2314 -0.0058 -0.0178 0.0607 285 ALA A N
+2366 C CA . ALA A 285 ? 0.2189 0.2508 0.2425 -0.0020 -0.0141 0.0606 285 ALA A CA
+2367 C C . ALA A 285 ? 0.2274 0.2492 0.2400 -0.0003 -0.0142 0.0498 285 ALA A C
+2368 O O . ALA A 285 ? 0.2469 0.2625 0.2578 0.0030 -0.0114 0.0483 285 ALA A O
+2369 C CB . ALA A 285 ? 0.2244 0.2542 0.2537 0.0051 -0.0071 0.0676 285 ALA A CB
+2370 N N . LEU A 286 ? 0.2180 0.2377 0.2235 -0.0026 -0.0174 0.0429 286 LEU A N
+2371 C CA . LEU A 286 ? 0.2259 0.2381 0.2229 -0.0022 -0.0186 0.0342 286 LEU A CA
+2372 C C . LEU A 286 ? 0.2134 0.2293 0.2079 -0.0080 -0.0234 0.0299 286 LEU A C
+2373 O O . LEU A 286 ? 0.2143 0.2366 0.2113 -0.0123 -0.0257 0.0329 286 LEU A O
+2374 C CB . LEU A 286 ? 0.2449 0.2477 0.2345 0.0028 -0.0159 0.0300 286 LEU A CB
+2375 C CG . LEU A 286 ? 0.2717 0.2762 0.2607 0.0035 -0.0156 0.0307 286 LEU A CG
+2376 C CD1 . LEU A 286 ? 0.2898 0.2969 0.2759 -0.0012 -0.0201 0.0258 286 LEU A CD1
+2377 C CD2 . LEU A 286 ? 0.2887 0.2833 0.2704 0.0092 -0.0120 0.0279 286 LEU A CD2
+2378 N N . LEU A 287 ? 0.1966 0.2080 0.1863 -0.0085 -0.0248 0.0238 287 LEU A N
+2379 C CA . LEU A 287 ? 0.1945 0.2084 0.1818 -0.0129 -0.0280 0.0201 287 LEU A CA
+2380 C C . LEU A 287 ? 0.1947 0.2063 0.1774 -0.0127 -0.0283 0.0165 287 LEU A C
+2381 O O . LEU A 287 ? 0.2180 0.2238 0.1970 -0.0098 -0.0277 0.0127 287 LEU A O
+2382 C CB . LEU A 287 ? 0.2044 0.2153 0.1904 -0.0131 -0.0290 0.0166 287 LEU A CB
+2383 C CG . LEU A 287 ? 0.2287 0.2422 0.2198 -0.0134 -0.0287 0.0204 287 LEU A CG
+2384 C CD1 . LEU A 287 ? 0.2400 0.2492 0.2299 -0.0128 -0.0297 0.0172 287 LEU A CD1
+2385 C CD2 . LEU A 287 ? 0.2392 0.2611 0.2341 -0.0183 -0.0304 0.0244 287 LEU A CD2
+2386 N N A GLU A 288 ? 0.1777 0.1933 0.1603 -0.0162 -0.0297 0.0179 288 GLU A N
+2387 N N B GLU A 288 ? 0.1778 0.1935 0.1605 -0.0162 -0.0297 0.0179 288 GLU A N
+2388 C CA A GLU A 288 ? 0.1732 0.1869 0.1521 -0.0162 -0.0299 0.0150 288 GLU A CA
+2389 C CA B GLU A 288 ? 0.1739 0.1877 0.1528 -0.0164 -0.0299 0.0151 288 GLU A CA
+2390 C C A GLU A 288 ? 0.1716 0.1824 0.1461 -0.0175 -0.0305 0.0093 288 GLU A C
+2391 C C B GLU A 288 ? 0.1723 0.1831 0.1468 -0.0175 -0.0305 0.0093 288 GLU A C
+2392 O O A GLU A 288 ? 0.1728 0.1850 0.1461 -0.0209 -0.0314 0.0087 288 GLU A O
+2393 O O B GLU A 288 ? 0.1742 0.1863 0.1476 -0.0208 -0.0314 0.0086 288 GLU A O
+2394 C CB A GLU A 288 ? 0.1836 0.2015 0.1635 -0.0199 -0.0314 0.0192 288 GLU A CB
+2395 C CB B GLU A 288 ? 0.1855 0.2036 0.1653 -0.0203 -0.0316 0.0192 288 GLU A CB
+2396 C CG A GLU A 288 ? 0.2056 0.2277 0.1921 -0.0185 -0.0306 0.0266 288 GLU A CG
+2397 C CG B GLU A 288 ? 0.2176 0.2336 0.1934 -0.0213 -0.0322 0.0166 288 GLU A CG
+2398 C CD A GLU A 288 ? 0.2616 0.2815 0.2492 -0.0134 -0.0280 0.0276 288 GLU A CD
+2399 C CD B GLU A 288 ? 0.2499 0.2642 0.2269 -0.0166 -0.0304 0.0167 288 GLU A CD
+2400 O OE1 A GLU A 288 ? 0.2810 0.2966 0.2640 -0.0115 -0.0275 0.0224 288 GLU A OE1
+2401 O OE1 B GLU A 288 ? 0.2080 0.2184 0.1815 -0.0149 -0.0297 0.0118 288 GLU A OE1
+2402 O OE2 A GLU A 288 ? 0.2609 0.2838 0.2546 -0.0111 -0.0261 0.0343 288 GLU A OE2
+2403 O OE2 B GLU A 288 ? 0.2800 0.2969 0.2618 -0.0145 -0.0293 0.0222 288 GLU A OE2
+2404 N N . ASP A 289 ? 0.1707 0.1775 0.1429 -0.0148 -0.0298 0.0058 289 ASP A N
+2405 C CA . ASP A 289 ? 0.1681 0.1727 0.1380 -0.0155 -0.0300 0.0016 289 ASP A CA
+2406 C C . ASP A 289 ? 0.1799 0.1831 0.1473 -0.0156 -0.0295 -0.0004 289 ASP A C
+2407 O O . ASP A 289 ? 0.1866 0.1876 0.1533 -0.0150 -0.0290 -0.0033 289 ASP A O
+2408 C CB . ASP A 289 ? 0.1686 0.1696 0.1389 -0.0129 -0.0303 -0.0004 289 ASP A CB
+2409 C CG . ASP A 289 ? 0.2007 0.1974 0.1689 -0.0096 -0.0302 -0.0016 289 ASP A CG
+2410 O OD1 . ASP A 289 ? 0.1995 0.1965 0.1670 -0.0083 -0.0291 -0.0004 289 ASP A OD1
+2411 O OD2 . ASP A 289 ? 0.2094 0.2023 0.1766 -0.0086 -0.0313 -0.0034 289 ASP A OD2
+2412 N N . GLU A 290 ? 0.1783 0.1828 0.1452 -0.0165 -0.0297 0.0017 290 GLU A N
+2413 C CA . GLU A 290 ? 0.1869 0.1897 0.1516 -0.0168 -0.0293 -0.0002 290 GLU A CA
+2414 C C . GLU A 290 ? 0.1929 0.1955 0.1537 -0.0215 -0.0299 0.0002 290 GLU A C
+2415 O O . GLU A 290 ? 0.1977 0.1993 0.1568 -0.0227 -0.0304 0.0005 290 GLU A O
+2416 C CB . GLU A 290 ? 0.1961 0.1989 0.1623 -0.0136 -0.0289 0.0010 290 GLU A CB
+2417 C CG . GLU A 290 ? 0.2235 0.2234 0.1899 -0.0094 -0.0282 -0.0005 290 GLU A CG
+2418 C CD . GLU A 290 ? 0.2471 0.2452 0.2128 -0.0061 -0.0274 -0.0005 290 GLU A CD
+2419 O OE1 . GLU A 290 ? 0.2213 0.2215 0.1880 -0.0064 -0.0272 0.0016 290 GLU A OE1
+2420 O OE2 . GLU A 290 ? 0.2664 0.2605 0.2300 -0.0035 -0.0273 -0.0023 290 GLU A OE2
+2421 N N . PHE A 291 ? 0.1857 0.1881 0.1443 -0.0244 -0.0300 -0.0001 291 PHE A N
+2422 C CA . PHE A 291 ? 0.1967 0.1958 0.1484 -0.0288 -0.0300 -0.0010 291 PHE A CA
+2423 C C . PHE A 291 ? 0.2040 0.2004 0.1537 -0.0282 -0.0273 -0.0041 291 PHE A C
+2424 O O . PHE A 291 ? 0.2109 0.2098 0.1633 -0.0278 -0.0274 -0.0032 291 PHE A O
+2425 C CB . PHE A 291 ? 0.1984 0.1994 0.1479 -0.0337 -0.0326 0.0028 291 PHE A CB
+2426 C CG . PHE A 291 ? 0.2136 0.2184 0.1665 -0.0352 -0.0355 0.0079 291 PHE A CG
+2427 C CD1 . PHE A 291 ? 0.2299 0.2323 0.1787 -0.0387 -0.0375 0.0090 291 PHE A CD1
+2428 C CD2 . PHE A 291 ? 0.2284 0.2390 0.1890 -0.0331 -0.0361 0.0122 291 PHE A CD2
+2429 C CE1 . PHE A 291 ? 0.2449 0.2518 0.1984 -0.0404 -0.0406 0.0152 291 PHE A CE1
+2430 C CE2 . PHE A 291 ? 0.2408 0.2556 0.2059 -0.0343 -0.0383 0.0184 291 PHE A CE2
+2431 C CZ . PHE A 291 ? 0.2375 0.2511 0.1997 -0.0380 -0.0407 0.0202 291 PHE A CZ
+2432 N N . THR A 292 ? 0.2058 0.1971 0.1510 -0.0281 -0.0247 -0.0071 292 THR A N
+2433 C CA . THR A 292 ? 0.2080 0.1966 0.1518 -0.0272 -0.0211 -0.0090 292 THR A CA
+2434 C C . THR A 292 ? 0.2090 0.1937 0.1441 -0.0315 -0.0204 -0.0088 292 THR A C
+2435 O O . THR A 292 ? 0.2094 0.1919 0.1380 -0.0358 -0.0229 -0.0077 292 THR A O
+2436 C CB . THR A 292 ? 0.2254 0.2090 0.1675 -0.0252 -0.0175 -0.0115 292 THR A CB
+2437 O OG1 . THR A 292 ? 0.2463 0.2233 0.1789 -0.0286 -0.0170 -0.0126 292 THR A OG1
+2438 C CG2 . THR A 292 ? 0.2222 0.2088 0.1715 -0.0217 -0.0184 -0.0116 292 THR A CG2
+2439 N N . PRO A 293 ? 0.2156 0.1986 0.1496 -0.0306 -0.0169 -0.0094 293 PRO A N
+2440 C CA . PRO A 293 ? 0.2189 0.1964 0.1422 -0.0345 -0.0154 -0.0096 293 PRO A CA
+2441 C C . PRO A 293 ? 0.2387 0.2063 0.1496 -0.0376 -0.0141 -0.0118 293 PRO A C
+2442 O O . PRO A 293 ? 0.2490 0.2119 0.1493 -0.0430 -0.0162 -0.0112 293 PRO A O
+2443 C CB . PRO A 293 ? 0.2324 0.2092 0.1581 -0.0312 -0.0103 -0.0099 293 PRO A CB
+2444 C CG . PRO A 293 ? 0.2285 0.2138 0.1679 -0.0274 -0.0122 -0.0083 293 PRO A CG
+2445 C CD . PRO A 293 ? 0.2079 0.1941 0.1504 -0.0263 -0.0145 -0.0092 293 PRO A CD
+2446 N N . PHE A 294 ? 0.2447 0.2087 0.1564 -0.0347 -0.0111 -0.0139 294 PHE A N
+2447 C CA A PHE A 294 ? 0.2722 0.2257 0.1719 -0.0374 -0.0097 -0.0162 294 PHE A CA
+2448 C CA B PHE A 294 ? 0.2692 0.2227 0.1690 -0.0374 -0.0096 -0.0162 294 PHE A CA
+2449 C C . PHE A 294 ? 0.2707 0.2255 0.1683 -0.0420 -0.0162 -0.0146 294 PHE A C
+2450 O O . PHE A 294 ? 0.2910 0.2372 0.1757 -0.0475 -0.0177 -0.0150 294 PHE A O
+2451 C CB A PHE A 294 ? 0.2858 0.2362 0.1888 -0.0329 -0.0050 -0.0182 294 PHE A CB
+2452 C CB B PHE A 294 ? 0.2783 0.2291 0.1819 -0.0327 -0.0049 -0.0181 294 PHE A CB
+2453 C CG A PHE A 294 ? 0.3135 0.2587 0.2155 -0.0291 0.0029 -0.0192 294 PHE A CG
+2454 C CG B PHE A 294 ? 0.3077 0.2455 0.1983 -0.0345 -0.0013 -0.0209 294 PHE A CG
+2455 C CD1 A PHE A 294 ? 0.3332 0.2756 0.2298 -0.0297 0.0061 -0.0187 294 PHE A CD1
+2456 C CD1 B PHE A 294 ? 0.3351 0.2616 0.2092 -0.0392 0.0000 -0.0222 294 PHE A CD1
+2457 C CD2 A PHE A 294 ? 0.3325 0.2768 0.2404 -0.0247 0.0074 -0.0197 294 PHE A CD2
+2458 C CD2 B PHE A 294 ? 0.3229 0.2587 0.2170 -0.0316 0.0011 -0.0221 294 PHE A CD2
+2459 C CE1 A PHE A 294 ? 0.3467 0.2849 0.2437 -0.0255 0.0141 -0.0185 294 PHE A CE1
+2460 C CE1 B PHE A 294 ? 0.3569 0.2690 0.2170 -0.0411 0.0034 -0.0250 294 PHE A CE1
+2461 C CE2 A PHE A 294 ? 0.3446 0.2853 0.2539 -0.0207 0.0151 -0.0191 294 PHE A CE2
+2462 C CE2 B PHE A 294 ? 0.3424 0.2652 0.2243 -0.0331 0.0047 -0.0246 294 PHE A CE2
+2463 C CZ A PHE A 294 ? 0.3455 0.2831 0.2493 -0.0209 0.0187 -0.0184 294 PHE A CZ
+2464 C CZ B PHE A 294 ? 0.3512 0.2615 0.2156 -0.0379 0.0059 -0.0263 294 PHE A CZ
+2465 N N . ASP A 295 ? 0.2529 0.2177 0.1624 -0.0401 -0.0201 -0.0122 295 ASP A N
+2466 C CA . ASP A 295 ? 0.2476 0.2153 0.1577 -0.0437 -0.0259 -0.0092 295 ASP A CA
+2467 C C . ASP A 295 ? 0.2600 0.2280 0.1646 -0.0496 -0.0298 -0.0060 295 ASP A C
+2468 O O . ASP A 295 ? 0.2774 0.2420 0.1754 -0.0553 -0.0340 -0.0039 295 ASP A O
+2469 C CB . ASP A 295 ? 0.2495 0.2275 0.1733 -0.0396 -0.0279 -0.0067 295 ASP A CB
+2470 C CG . ASP A 295 ? 0.2638 0.2425 0.1933 -0.0346 -0.0256 -0.0088 295 ASP A CG
+2471 O OD1 . ASP A 295 ? 0.2773 0.2493 0.2015 -0.0349 -0.0234 -0.0113 295 ASP A OD1
+2472 O OD2 . ASP A 295 ? 0.2535 0.2386 0.1922 -0.0306 -0.0260 -0.0078 295 ASP A OD2
+2473 N N . VAL A 296 ? 0.2445 0.2169 0.1525 -0.0487 -0.0290 -0.0051 296 VAL A N
+2474 C CA . VAL A 296 ? 0.2485 0.2222 0.1524 -0.0542 -0.0327 -0.0016 296 VAL A CA
+2475 C C . VAL A 296 ? 0.2792 0.2410 0.1658 -0.0602 -0.0325 -0.0033 296 VAL A C
+2476 O O . VAL A 296 ? 0.2957 0.2555 0.1759 -0.0670 -0.0378 0.0000 296 VAL A O
+2477 C CB . VAL A 296 ? 0.2406 0.2216 0.1524 -0.0515 -0.0316 -0.0003 296 VAL A CB
+2478 C CG1 . VAL A 296 ? 0.2471 0.2291 0.1541 -0.0575 -0.0351 0.0035 296 VAL A CG1
+2479 C CG2 . VAL A 296 ? 0.2309 0.2216 0.1572 -0.0468 -0.0328 0.0019 296 VAL A CG2
+2480 N N . VAL A 297 ? 0.2892 0.2421 0.1676 -0.0579 -0.0263 -0.0080 297 VAL A N
+2481 C CA . VAL A 297 ? 0.3194 0.2578 0.1784 -0.0631 -0.0248 -0.0103 297 VAL A CA
+2482 C C . VAL A 297 ? 0.3375 0.2679 0.1878 -0.0677 -0.0283 -0.0106 297 VAL A C
+2483 O O . VAL A 297 ? 0.3512 0.2732 0.1873 -0.0755 -0.0325 -0.0093 297 VAL A O
+2484 C CB . VAL A 297 ? 0.3451 0.2753 0.1985 -0.0581 -0.0158 -0.0147 297 VAL A CB
+2485 C CG1 . VAL A 297 ? 0.3705 0.2827 0.2015 -0.0628 -0.0129 -0.0176 297 VAL A CG1
+2486 C CG2 . VAL A 297 ? 0.3543 0.2919 0.2157 -0.0545 -0.0128 -0.0135 297 VAL A CG2
+2487 N N . ARG A 298 ? 0.3385 0.2714 0.1970 -0.0634 -0.0271 -0.0119 298 ARG A N
+2488 C CA . ARG A 298 ? 0.3595 0.2855 0.2117 -0.0670 -0.0301 -0.0122 298 ARG A CA
+2489 C C . ARG A 298 ? 0.3621 0.2932 0.2158 -0.0738 -0.0391 -0.0063 298 ARG A C
+2490 O O . ARG A 298 ? 0.3706 0.2916 0.2105 -0.0814 -0.0433 -0.0054 298 ARG A O
+2491 C CB . ARG A 298 ? 0.3855 0.3161 0.2494 -0.0605 -0.0274 -0.0137 298 ARG A CB
+2492 C CG . ARG A 298 ? 0.4514 0.3728 0.3077 -0.0632 -0.0286 -0.0150 298 ARG A CG
+2493 C CD . ARG A 298 ? 0.5071 0.4343 0.3760 -0.0568 -0.0263 -0.0159 298 ARG A CD
+2494 N NE . ARG A 298 ? 0.5627 0.4894 0.4357 -0.0499 -0.0184 -0.0195 298 ARG A NE
+2495 C CZ . ARG A 298 ? 0.5959 0.5340 0.4836 -0.0439 -0.0169 -0.0186 298 ARG A CZ
+2496 N NH1 . ARG A 298 ? 0.6028 0.5401 0.4942 -0.0386 -0.0104 -0.0208 298 ARG A NH1
+2497 N NH2 . ARG A 298 ? 0.5851 0.5349 0.4837 -0.0434 -0.0218 -0.0151 298 ARG A NH2
+2498 N N . GLN A 299 ? 0.3535 0.2995 0.2235 -0.0715 -0.0421 -0.0016 299 GLN A N
+2499 C CA . GLN A 299 ? 0.3590 0.3118 0.2339 -0.0770 -0.0499 0.0056 299 GLN A CA
+2500 C C . GLN A 299 ? 0.3870 0.3366 0.2520 -0.0848 -0.0542 0.0088 299 GLN A C
+2501 O O . GLN A 299 ? 0.4029 0.3494 0.2619 -0.0928 -0.0611 0.0134 299 GLN A O
+2502 C CB . GLN A 299 ? 0.3452 0.3136 0.2398 -0.0713 -0.0503 0.0098 299 GLN A CB
+2503 C CG . GLN A 299 ? 0.3338 0.3097 0.2356 -0.0760 -0.0573 0.0184 299 GLN A CG
+2504 C CD . GLN A 299 ? 0.3113 0.3003 0.2311 -0.0699 -0.0567 0.0229 299 GLN A CD
+2505 O OE1 . GLN A 299 ? 0.3085 0.3054 0.2364 -0.0726 -0.0610 0.0310 299 GLN A OE1
+2506 N NE2 . GLN A 299 ? 0.2821 0.2734 0.2084 -0.0618 -0.0513 0.0185 299 GLN A NE2
+2507 N N . CYS A 300 ? 0.3924 0.3424 0.2554 -0.0831 -0.0507 0.0068 300 CYS A N
+2508 C CA . CYS A 300 ? 0.4087 0.3556 0.2619 -0.0905 -0.0545 0.0098 300 CYS A CA
+2509 C C . CYS A 300 ? 0.4480 0.3763 0.2769 -0.0979 -0.0552 0.0065 300 CYS A C
+2510 O O . CYS A 300 ? 0.4564 0.3806 0.2748 -0.1063 -0.0607 0.0101 300 CYS A O
+2511 C CB . CYS A 300 ? 0.3963 0.3494 0.2550 -0.0864 -0.0505 0.0091 300 CYS A CB
+2512 S SG . CYS A 300 ? 0.4013 0.3739 0.2849 -0.0804 -0.0515 0.0145 300 CYS A SG
+2513 N N . SER A 301 ? 0.4716 0.3880 0.2911 -0.0951 -0.0500 0.0001 301 SER A N
+2514 C CA . SER A 301 ? 0.5089 0.4050 0.3035 -0.1017 -0.0498 -0.0035 301 SER A CA
+2515 C C . SER A 301 ? 0.5350 0.4229 0.3229 -0.1066 -0.0546 -0.0031 301 SER A C
+2516 O O . SER A 301 ? 0.5574 0.4275 0.3234 -0.1139 -0.0565 -0.0050 301 SER A O
+2517 C CB . SER A 301 ? 0.5388 0.4236 0.3234 -0.0957 -0.0391 -0.0109 301 SER A CB
+2518 O OG . SER A 301 ? 0.5687 0.4535 0.3609 -0.0883 -0.0335 -0.0146 301 SER A OG
+2519 N N . GLY A 302 ? 0.5305 0.4300 0.3361 -0.1026 -0.0563 -0.0006 302 GLY A N
+2520 C CA . GLY A 302 ? 0.5449 0.4392 0.3475 -0.1069 -0.0613 0.0010 302 GLY A CA
+2521 C C . GLY A 302 ? 0.5606 0.4402 0.3523 -0.1038 -0.0550 -0.0062 302 GLY A C
+2522 O O . GLY A 302 ? 0.5777 0.4425 0.3534 -0.1106 -0.0585 -0.0070 302 GLY A O
+2523 N N . VAL A 303 ? 0.5526 0.4361 0.3534 -0.0937 -0.0459 -0.0110 303 VAL A N
+2524 C CA . VAL A 303 ? 0.5589 0.4304 0.3526 -0.0896 -0.0389 -0.0171 303 VAL A CA
+2525 C C . VAL A 303 ? 0.5504 0.4249 0.3518 -0.0901 -0.0431 -0.0151 303 VAL A C
+2526 O O . VAL A 303 ? 0.5357 0.4270 0.3563 -0.0873 -0.0466 -0.0105 303 VAL A O
+2527 C CB . VAL A 303 ? 0.5633 0.4412 0.3684 -0.0789 -0.0291 -0.0207 303 VAL A CB
+2528 C CG1 . VAL A 303 ? 0.5777 0.4448 0.3782 -0.0742 -0.0215 -0.0257 303 VAL A CG1
+2529 C CG2 . VAL A 303 ? 0.5724 0.4479 0.3709 -0.0782 -0.0248 -0.0220 303 VAL A CG2
+2530 N N A THR A 304 ? 0.5584 0.4163 0.3449 -0.0934 -0.0424 -0.0183 304 THR A N
+2531 N N B THR A 304 ? 0.5585 0.4161 0.3445 -0.0936 -0.0424 -0.0183 304 THR A N
+2532 C CA A THR A 304 ? 0.5583 0.4185 0.3519 -0.0940 -0.0464 -0.0162 304 THR A CA
+2533 C CA B THR A 304 ? 0.5595 0.4178 0.3510 -0.0944 -0.0461 -0.0167 304 THR A CA
+2534 C C A THR A 304 ? 0.5592 0.4165 0.3575 -0.0859 -0.0379 -0.0212 304 THR A C
+2535 C C B THR A 304 ? 0.5665 0.4152 0.3551 -0.0881 -0.0372 -0.0228 304 THR A C
+2536 O O A THR A 304 ? 0.5537 0.4136 0.3592 -0.0853 -0.0403 -0.0199 304 THR A O
+2537 O O B THR A 304 ? 0.5641 0.4134 0.3558 -0.0806 -0.0281 -0.0266 304 THR A O
+2538 C CB A THR A 304 ? 0.5841 0.4294 0.3596 -0.1053 -0.0545 -0.0143 304 THR A CB
+2539 C CB B THR A 304 ? 0.5814 0.4283 0.3575 -0.1062 -0.0558 -0.0133 304 THR A CB
+2540 O OG1 A THR A 304 ? 0.6127 0.4346 0.3633 -0.1078 -0.0490 -0.0209 304 THR A OG1
+2541 O OG1 B THR A 304 ? 0.6100 0.4336 0.3593 -0.1110 -0.0526 -0.0187 304 THR A OG1
+2542 C CG2 A THR A 304 ? 0.5871 0.4386 0.3622 -0.1137 -0.0643 -0.0073 304 THR A CG2
+2543 C CG2 B THR A 304 ? 0.5784 0.4376 0.3615 -0.1123 -0.0651 -0.0054 304 THR A CG2
+2544 S S . DMS B . ? 0.2030 0.2530 0.3059 0.0142 -0.0223 0.0422 401 DMS A S
+2545 O O . DMS B . ? 0.2067 0.2623 0.3090 0.0170 -0.0213 0.0422 401 DMS A O
+2546 C C1 . DMS B . ? 0.2054 0.2497 0.2971 0.0117 -0.0247 0.0398 401 DMS A C1
+2547 C C2 . DMS B . ? 0.1948 0.2540 0.3057 0.0159 -0.0255 0.0493 401 DMS A C2
+2548 S S . DMS C . ? 0.5726 0.6429 0.6328 0.0331 -0.0250 0.0516 402 DMS A S
+2549 O O . DMS C . ? 0.5645 0.6411 0.6389 0.0324 -0.0251 0.0544 402 DMS A O
+2550 C C1 . DMS C . ? 0.5741 0.6444 0.6284 0.0381 -0.0224 0.0551 402 DMS A C1
+2551 C C2 . DMS C . ? 0.5761 0.6466 0.6296 0.0338 -0.0265 0.0540 402 DMS A C2
+2552 S S . DMS D . ? 0.4191 0.3868 0.3321 -0.0512 -0.0390 -0.0011 403 DMS A S
+2553 O O . DMS D . ? 0.4341 0.3934 0.3396 -0.0547 -0.0404 -0.0021 403 DMS A O
+2554 C C1 . DMS D . ? 0.4314 0.3907 0.3317 -0.0546 -0.0369 -0.0043 403 DMS A C1
+2555 C C2 . DMS D . ? 0.4176 0.3886 0.3391 -0.0424 -0.0329 -0.0054 403 DMS A C2
+2556 S S . DMS E . ? 0.4677 0.4488 0.4601 -0.0274 -0.0432 0.0179 404 DMS A S
+2557 O O . DMS E . ? 0.4800 0.4523 0.4688 -0.0326 -0.0462 0.0186 404 DMS A O
+2558 C C1 . DMS E . ? 0.4613 0.4467 0.4607 -0.0200 -0.0367 0.0144 404 DMS A C1
+2559 C C2 . DMS E . ? 0.4585 0.4549 0.4639 -0.0243 -0.0465 0.0272 404 DMS A C2
+#
+loop_
+_pdbx_poly_seq_scheme.asym_id
+_pdbx_poly_seq_scheme.entity_id
+_pdbx_poly_seq_scheme.seq_id
+_pdbx_poly_seq_scheme.mon_id
+_pdbx_poly_seq_scheme.ndb_seq_num
+_pdbx_poly_seq_scheme.pdb_seq_num
+_pdbx_poly_seq_scheme.auth_seq_num
+_pdbx_poly_seq_scheme.pdb_mon_id
+_pdbx_poly_seq_scheme.auth_mon_id
+_pdbx_poly_seq_scheme.pdb_strand_id
+_pdbx_poly_seq_scheme.pdb_ins_code
+_pdbx_poly_seq_scheme.hetero
+A 1 1 SER 1 1 1 SER SER A . n
+A 1 2 GLY 2 2 2 GLY GLY A . n
+A 1 3 PHE 3 3 3 PHE PHE A . n
+A 1 4 ARG 4 4 4 ARG ARG A . n
+A 1 5 LYS 5 5 5 LYS LYS A . n
+A 1 6 MET 6 6 6 MET MET A . n
+A 1 7 ALA 7 7 7 ALA ALA A . n
+A 1 8 PHE 8 8 8 PHE PHE A . n
+A 1 9 PRO 9 9 9 PRO PRO A . n
+A 1 10 SER 10 10 10 SER SER A . n
+A 1 11 GLY 11 11 11 GLY GLY A . n
+A 1 12 LYS 12 12 12 LYS LYS A . n
+A 1 13 VAL 13 13 13 VAL VAL A . n
+A 1 14 GLU 14 14 14 GLU GLU A . n
+A 1 15 GLY 15 15 15 GLY GLY A . n
+A 1 16 CYS 16 16 16 CYS CYS A . n
+A 1 17 MET 17 17 17 MET MET A . n
+A 1 18 VAL 18 18 18 VAL VAL A . n
+A 1 19 GLN 19 19 19 GLN GLN A . n
+A 1 20 VAL 20 20 20 VAL VAL A . n
+A 1 21 THR 21 21 21 THR THR A . n
+A 1 22 CYS 22 22 22 CYS CYS A . n
+A 1 23 GLY 23 23 23 GLY GLY A . n
+A 1 24 THR 24 24 24 THR THR A . n
+A 1 25 THR 25 25 25 THR THR A . n
+A 1 26 THR 26 26 26 THR THR A . n
+A 1 27 LEU 27 27 27 LEU LEU A . n
+A 1 28 ASN 28 28 28 ASN ASN A . n
+A 1 29 GLY 29 29 29 GLY GLY A . n
+A 1 30 LEU 30 30 30 LEU LEU A . n
+A 1 31 TRP 31 31 31 TRP TRP A . n
+A 1 32 LEU 32 32 32 LEU LEU A . n
+A 1 33 ASP 33 33 33 ASP ASP A . n
+A 1 34 ASP 34 34 34 ASP ASP A . n
+A 1 35 VAL 35 35 35 VAL VAL A . n
+A 1 36 VAL 36 36 36 VAL VAL A . n
+A 1 37 TYR 37 37 37 TYR TYR A . n
+A 1 38 CYS 38 38 38 CYS CYS A . n
+A 1 39 PRO 39 39 39 PRO PRO A . n
+A 1 40 ARG 40 40 40 ARG ARG A . n
+A 1 41 HIS 41 41 41 HIS HIS A . n
+A 1 42 VAL 42 42 42 VAL VAL A . n
+A 1 43 ILE 43 43 43 ILE ILE A . n
+A 1 44 CYS 44 44 44 CYS CYS A . n
+A 1 45 THR 45 45 45 THR THR A . n
+A 1 46 SER 46 46 46 SER SER A . n
+A 1 47 GLU 47 47 47 GLU GLU A . n
+A 1 48 ASP 48 48 48 ASP ASP A . n
+A 1 49 MET 49 49 49 MET MET A . n
+A 1 50 LEU 50 50 50 LEU LEU A . n
+A 1 51 ASN 51 51 51 ASN ASN A . n
+A 1 52 PRO 52 52 52 PRO PRO A . n
+A 1 53 ASN 53 53 53 ASN ASN A . n
+A 1 54 TYR 54 54 54 TYR TYR A . n
+A 1 55 GLU 55 55 55 GLU GLU A . n
+A 1 56 ASP 56 56 56 ASP ASP A . n
+A 1 57 LEU 57 57 57 LEU LEU A . n
+A 1 58 LEU 58 58 58 LEU LEU A . n
+A 1 59 ILE 59 59 59 ILE ILE A . n
+A 1 60 ARG 60 60 60 ARG ARG A . n
+A 1 61 LYS 61 61 61 LYS LYS A . n
+A 1 62 SER 62 62 62 SER SER A . n
+A 1 63 ASN 63 63 63 ASN ASN A . n
+A 1 64 HIS 64 64 64 HIS HIS A . n
+A 1 65 ASN 65 65 65 ASN ASN A . n
+A 1 66 PHE 66 66 66 PHE PHE A . n
+A 1 67 LEU 67 67 67 LEU LEU A . n
+A 1 68 VAL 68 68 68 VAL VAL A . n
+A 1 69 GLN 69 69 69 GLN GLN A . n
+A 1 70 ALA 70 70 70 ALA ALA A . n
+A 1 71 GLY 71 71 71 GLY GLY A . n
+A 1 72 ASN 72 72 72 ASN ASN A . n
+A 1 73 VAL 73 73 73 VAL VAL A . n
+A 1 74 GLN 74 74 74 GLN GLN A . n
+A 1 75 LEU 75 75 75 LEU LEU A . n
+A 1 76 ARG 76 76 76 ARG ARG A . n
+A 1 77 VAL 77 77 77 VAL VAL A . n
+A 1 78 ILE 78 78 78 ILE ILE A . n
+A 1 79 GLY 79 79 79 GLY GLY A . n
+A 1 80 HIS 80 80 80 HIS HIS A . n
+A 1 81 SER 81 81 81 SER SER A . n
+A 1 82 MET 82 82 82 MET MET A . n
+A 1 83 GLN 83 83 83 GLN GLN A . n
+A 1 84 ASN 84 84 84 ASN ASN A . n
+A 1 85 CYS 85 85 85 CYS CYS A . n
+A 1 86 VAL 86 86 86 VAL VAL A . n
+A 1 87 LEU 87 87 87 LEU LEU A . n
+A 1 88 LYS 88 88 88 LYS LYS A . n
+A 1 89 LEU 89 89 89 LEU LEU A . n
+A 1 90 LYS 90 90 90 LYS LYS A . n
+A 1 91 VAL 91 91 91 VAL VAL A . n
+A 1 92 ASP 92 92 92 ASP ASP A . n
+A 1 93 THR 93 93 93 THR THR A . n
+A 1 94 ALA 94 94 94 ALA ALA A . n
+A 1 95 ASN 95 95 95 ASN ASN A . n
+A 1 96 PRO 96 96 96 PRO PRO A . n
+A 1 97 LYS 97 97 97 LYS LYS A . n
+A 1 98 THR 98 98 98 THR THR A . n
+A 1 99 PRO 99 99 99 PRO PRO A . n
+A 1 100 LYS 100 100 100 LYS LYS A . n
+A 1 101 TYR 101 101 101 TYR TYR A . n
+A 1 102 LYS 102 102 102 LYS LYS A . n
+A 1 103 PHE 103 103 103 PHE PHE A . n
+A 1 104 VAL 104 104 104 VAL VAL A . n
+A 1 105 ARG 105 105 105 ARG ARG A . n
+A 1 106 ILE 106 106 106 ILE ILE A . n
+A 1 107 GLN 107 107 107 GLN GLN A . n
+A 1 108 PRO 108 108 108 PRO PRO A . n
+A 1 109 GLY 109 109 109 GLY GLY A . n
+A 1 110 GLN 110 110 110 GLN GLN A . n
+A 1 111 THR 111 111 111 THR THR A . n
+A 1 112 PHE 112 112 112 PHE PHE A . n
+A 1 113 SER 113 113 113 SER SER A . n
+A 1 114 VAL 114 114 114 VAL VAL A . n
+A 1 115 LEU 115 115 115 LEU LEU A . n
+A 1 116 ALA 116 116 116 ALA ALA A . n
+A 1 117 CYS 117 117 117 CYS CYS A . n
+A 1 118 TYR 118 118 118 TYR TYR A . n
+A 1 119 ASN 119 119 119 ASN ASN A . n
+A 1 120 GLY 120 120 120 GLY GLY A . n
+A 1 121 SER 121 121 121 SER SER A . n
+A 1 122 PRO 122 122 122 PRO PRO A . n
+A 1 123 SER 123 123 123 SER SER A . n
+A 1 124 GLY 124 124 124 GLY GLY A . n
+A 1 125 VAL 125 125 125 VAL VAL A . n
+A 1 126 TYR 126 126 126 TYR TYR A . n
+A 1 127 GLN 127 127 127 GLN GLN A . n
+A 1 128 CYS 128 128 128 CYS CYS A . n
+A 1 129 ALA 129 129 129 ALA ALA A . n
+A 1 130 MET 130 130 130 MET MET A . n
+A 1 131 ARG 131 131 131 ARG ARG A . n
+A 1 132 PRO 132 132 132 PRO PRO A . n
+A 1 133 ASN 133 133 133 ASN ASN A . n
+A 1 134 PHE 134 134 134 PHE PHE A . n
+A 1 135 THR 135 135 135 THR THR A . n
+A 1 136 ILE 136 136 136 ILE ILE A . n
+A 1 137 LYS 137 137 137 LYS LYS A . n
+A 1 138 GLY 138 138 138 GLY GLY A . n
+A 1 139 SER 139 139 139 SER SER A . n
+A 1 140 PHE 140 140 140 PHE PHE A . n
+A 1 141 LEU 141 141 141 LEU LEU A . n
+A 1 142 ASN 142 142 142 ASN ASN A . n
+A 1 143 GLY 143 143 143 GLY GLY A . n
+A 1 144 SER 144 144 144 SER SER A . n
+A 1 145 CYS 145 145 145 CYS CYS A . n
+A 1 146 GLY 146 146 146 GLY GLY A . n
+A 1 147 SER 147 147 147 SER SER A . n
+A 1 148 VAL 148 148 148 VAL VAL A . n
+A 1 149 GLY 149 149 149 GLY GLY A . n
+A 1 150 PHE 150 150 150 PHE PHE A . n
+A 1 151 ASN 151 151 151 ASN ASN A . n
+A 1 152 ILE 152 152 152 ILE ILE A . n
+A 1 153 ASP 153 153 153 ASP ASP A . n
+A 1 154 TYR 154 154 154 TYR TYR A . n
+A 1 155 ASP 155 155 155 ASP ASP A . n
+A 1 156 CYS 156 156 156 CYS CYS A . n
+A 1 157 VAL 157 157 157 VAL VAL A . n
+A 1 158 SER 158 158 158 SER SER A . n
+A 1 159 PHE 159 159 159 PHE PHE A . n
+A 1 160 CYS 160 160 160 CYS CYS A . n
+A 1 161 TYR 161 161 161 TYR TYR A . n
+A 1 162 MET 162 162 162 MET MET A . n
+A 1 163 HIS 163 163 163 HIS HIS A . n
+A 1 164 HIS 164 164 164 HIS HIS A . n
+A 1 165 MET 165 165 165 MET MET A . n
+A 1 166 GLU 166 166 166 GLU GLU A . n
+A 1 167 LEU 167 167 167 LEU LEU A . n
+A 1 168 PRO 168 168 168 PRO PRO A . n
+A 1 169 THR 169 169 169 THR THR A . n
+A 1 170 GLY 170 170 170 GLY GLY A . n
+A 1 171 VAL 171 171 171 VAL VAL A . n
+A 1 172 HIS 172 172 172 HIS HIS A . n
+A 1 173 ALA 173 173 173 ALA ALA A . n
+A 1 174 GLY 174 174 174 GLY GLY A . n
+A 1 175 THR 175 175 175 THR THR A . n
+A 1 176 ASP 176 176 176 ASP ASP A . n
+A 1 177 LEU 177 177 177 LEU LEU A . n
+A 1 178 GLU 178 178 178 GLU GLU A . n
+A 1 179 GLY 179 179 179 GLY GLY A . n
+A 1 180 ASN 180 180 180 ASN ASN A . n
+A 1 181 PHE 181 181 181 PHE PHE A . n
+A 1 182 TYR 182 182 182 TYR TYR A . n
+A 1 183 GLY 183 183 183 GLY GLY A . n
+A 1 184 PRO 184 184 184 PRO PRO A . n
+A 1 185 PHE 185 185 185 PHE PHE A . n
+A 1 186 VAL 186 186 186 VAL VAL A . n
+A 1 187 ASP 187 187 187 ASP ASP A . n
+A 1 188 ARG 188 188 188 ARG ARG A . n
+A 1 189 GLN 189 189 189 GLN GLN A . n
+A 1 190 THR 190 190 190 THR THR A . n
+A 1 191 ALA 191 191 191 ALA ALA A . n
+A 1 192 GLN 192 192 192 GLN GLN A . n
+A 1 193 ALA 193 193 193 ALA ALA A . n
+A 1 194 ALA 194 194 194 ALA ALA A . n
+A 1 195 GLY 195 195 195 GLY GLY A . n
+A 1 196 THR 196 196 196 THR THR A . n
+A 1 197 ASP 197 197 197 ASP ASP A . n
+A 1 198 THR 198 198 198 THR THR A . n
+A 1 199 THR 199 199 199 THR THR A . n
+A 1 200 ILE 200 200 200 ILE ILE A . n
+A 1 201 THR 201 201 201 THR THR A . n
+A 1 202 VAL 202 202 202 VAL VAL A . n
+A 1 203 ASN 203 203 203 ASN ASN A . n
+A 1 204 VAL 204 204 204 VAL VAL A . n
+A 1 205 LEU 205 205 205 LEU LEU A . n
+A 1 206 ALA 206 206 206 ALA ALA A . n
+A 1 207 TRP 207 207 207 TRP TRP A . n
+A 1 208 LEU 208 208 208 LEU LEU A . n
+A 1 209 TYR 209 209 209 TYR TYR A . n
+A 1 210 ALA 210 210 210 ALA ALA A . n
+A 1 211 ALA 211 211 211 ALA ALA A . n
+A 1 212 VAL 212 212 212 VAL VAL A . n
+A 1 213 ILE 213 213 213 ILE ILE A . n
+A 1 214 ASN 214 214 214 ASN ASN A . n
+A 1 215 GLY 215 215 215 GLY GLY A . n
+A 1 216 ASP 216 216 216 ASP ASP A . n
+A 1 217 ARG 217 217 217 ARG ARG A . n
+A 1 218 TRP 218 218 218 TRP TRP A . n
+A 1 219 PHE 219 219 219 PHE PHE A . n
+A 1 220 LEU 220 220 220 LEU LEU A . n
+A 1 221 ASN 221 221 221 ASN ASN A . n
+A 1 222 ARG 222 222 222 ARG ARG A . n
+A 1 223 PHE 223 223 223 PHE PHE A . n
+A 1 224 THR 224 224 224 THR THR A . n
+A 1 225 THR 225 225 225 THR THR A . n
+A 1 226 THR 226 226 226 THR THR A . n
+A 1 227 LEU 227 227 227 LEU LEU A . n
+A 1 228 ASN 228 228 228 ASN ASN A . n
+A 1 229 ASP 229 229 229 ASP ASP A . n
+A 1 230 PHE 230 230 230 PHE PHE A . n
+A 1 231 ASN 231 231 231 ASN ASN A . n
+A 1 232 LEU 232 232 232 LEU LEU A . n
+A 1 233 VAL 233 233 233 VAL VAL A . n
+A 1 234 ALA 234 234 234 ALA ALA A . n
+A 1 235 MET 235 235 235 MET MET A . n
+A 1 236 LYS 236 236 236 LYS LYS A . n
+A 1 237 TYR 237 237 237 TYR TYR A . n
+A 1 238 ASN 238 238 238 ASN ASN A . n
+A 1 239 TYR 239 239 239 TYR TYR A . n
+A 1 240 GLU 240 240 240 GLU GLU A . n
+A 1 241 PRO 241 241 241 PRO PRO A . n
+A 1 242 LEU 242 242 242 LEU LEU A . n
+A 1 243 THR 243 243 243 THR THR A . n
+A 1 244 GLN 244 244 244 GLN GLN A . n
+A 1 245 ASP 245 245 245 ASP ASP A . n
+A 1 246 HIS 246 246 246 HIS HIS A . n
+A 1 247 VAL 247 247 247 VAL VAL A . n
+A 1 248 ASP 248 248 248 ASP ASP A . n
+A 1 249 ILE 249 249 249 ILE ILE A . n
+A 1 250 LEU 250 250 250 LEU LEU A . n
+A 1 251 GLY 251 251 251 GLY GLY A . n
+A 1 252 PRO 252 252 252 PRO PRO A . n
+A 1 253 LEU 253 253 253 LEU LEU A . n
+A 1 254 SER 254 254 254 SER SER A . n
+A 1 255 ALA 255 255 255 ALA ALA A . n
+A 1 256 GLN 256 256 256 GLN GLN A . n
+A 1 257 THR 257 257 257 THR THR A . n
+A 1 258 GLY 258 258 258 GLY GLY A . n
+A 1 259 ILE 259 259 259 ILE ILE A . n
+A 1 260 ALA 260 260 260 ALA ALA A . n
+A 1 261 VAL 261 261 261 VAL VAL A . n
+A 1 262 LEU 262 262 262 LEU LEU A . n
+A 1 263 ASP 263 263 263 ASP ASP A . n
+A 1 264 MET 264 264 264 MET MET A . n
+A 1 265 CYS 265 265 265 CYS CYS A . n
+A 1 266 ALA 266 266 266 ALA ALA A . n
+A 1 267 SER 267 267 267 SER SER A . n
+A 1 268 LEU 268 268 268 LEU LEU A . n
+A 1 269 LYS 269 269 269 LYS LYS A . n
+A 1 270 GLU 270 270 270 GLU GLU A . n
+A 1 271 LEU 271 271 271 LEU LEU A . n
+A 1 272 LEU 272 272 272 LEU LEU A . n
+A 1 273 GLN 273 273 273 GLN GLN A . n
+A 1 274 ASN 274 274 274 ASN ASN A . n
+A 1 275 GLY 275 275 275 GLY GLY A . n
+A 1 276 MET 276 276 276 MET MET A . n
+A 1 277 ASN 277 277 277 ASN ASN A . n
+A 1 278 GLY 278 278 278 GLY GLY A . n
+A 1 279 ARG 279 279 279 ARG ARG A . n
+A 1 280 THR 280 280 280 THR THR A . n
+A 1 281 ILE 281 281 281 ILE ILE A . n
+A 1 282 LEU 282 282 282 LEU LEU A . n
+A 1 283 GLY 283 283 283 GLY GLY A . n
+A 1 284 SER 284 284 284 SER SER A . n
+A 1 285 ALA 285 285 285 ALA ALA A . n
+A 1 286 LEU 286 286 286 LEU LEU A . n
+A 1 287 LEU 287 287 287 LEU LEU A . n
+A 1 288 GLU 288 288 288 GLU GLU A . n
+A 1 289 ASP 289 289 289 ASP ASP A . n
+A 1 290 GLU 290 290 290 GLU GLU A . n
+A 1 291 PHE 291 291 291 PHE PHE A . n
+A 1 292 THR 292 292 292 THR THR A . n
+A 1 293 PRO 293 293 293 PRO PRO A . n
+A 1 294 PHE 294 294 294 PHE PHE A . n
+A 1 295 ASP 295 295 295 ASP ASP A . n
+A 1 296 VAL 296 296 296 VAL VAL A . n
+A 1 297 VAL 297 297 297 VAL VAL A . n
+A 1 298 ARG 298 298 298 ARG ARG A . n
+A 1 299 GLN 299 299 299 GLN GLN A . n
+A 1 300 CYS 300 300 300 CYS CYS A . n
+A 1 301 SER 301 301 301 SER SER A . n
+A 1 302 GLY 302 302 302 GLY GLY A . n
+A 1 303 VAL 303 303 303 VAL VAL A . n
+A 1 304 THR 304 304 304 THR THR A . n
+A 1 305 PHE 305 305 ? ? ? A . n
+A 1 306 GLN 306 306 ? ? ? A . n
+#
+loop_
+_pdbx_nonpoly_scheme.asym_id
+_pdbx_nonpoly_scheme.entity_id
+_pdbx_nonpoly_scheme.mon_id
+_pdbx_nonpoly_scheme.ndb_seq_num
+_pdbx_nonpoly_scheme.pdb_seq_num
+_pdbx_nonpoly_scheme.auth_seq_num
+_pdbx_nonpoly_scheme.pdb_mon_id
+_pdbx_nonpoly_scheme.auth_mon_id
+_pdbx_nonpoly_scheme.pdb_strand_id
+_pdbx_nonpoly_scheme.pdb_ins_code
+B 2 DMS 1 401 401 DMS DMS A .
+C 2 DMS 1 402 501 DMS DMS A .
+D 2 DMS 1 403 601 DMS DMS A .
+E 2 DMS 1 404 701 DMS DMS A .
+F 3 HOH 1 501 374 HOH HOH A .
+F 3 HOH 2 502 340 HOH HOH A .
+F 3 HOH 3 503 119 HOH HOH A .
+F 3 HOH 4 504 199 HOH HOH A .
+F 3 HOH 5 505 165 HOH HOH A .
+F 3 HOH 6 506 275 HOH HOH A .
+F 3 HOH 7 507 112 HOH HOH A .
+F 3 HOH 8 508 162 HOH HOH A .
+F 3 HOH 9 509 66 HOH HOH A .
+F 3 HOH 10 510 25 HOH HOH A .
+F 3 HOH 11 511 132 HOH HOH A .
+F 3 HOH 12 512 35 HOH HOH A .
+F 3 HOH 13 513 345 HOH HOH A .
+F 3 HOH 14 514 29 HOH HOH A .
+F 3 HOH 15 515 99 HOH HOH A .
+F 3 HOH 16 516 129 HOH HOH A .
+F 3 HOH 17 517 212 HOH HOH A .
+F 3 HOH 18 518 93 HOH HOH A .
+F 3 HOH 19 519 327 HOH HOH A .
+F 3 HOH 20 520 120 HOH HOH A .
+F 3 HOH 21 521 155 HOH HOH A .
+F 3 HOH 22 522 373 HOH HOH A .
+F 3 HOH 23 523 9 HOH HOH A .
+F 3 HOH 24 524 335 HOH HOH A .
+F 3 HOH 25 525 243 HOH HOH A .
+F 3 HOH 26 526 358 HOH HOH A .
+F 3 HOH 27 527 97 HOH HOH A .
+F 3 HOH 28 528 264 HOH HOH A .
+F 3 HOH 29 529 137 HOH HOH A .
+F 3 HOH 30 530 352 HOH HOH A .
+F 3 HOH 31 531 151 HOH HOH A .
+F 3 HOH 32 532 256 HOH HOH A .
+F 3 HOH 33 533 48 HOH HOH A .
+F 3 HOH 34 534 107 HOH HOH A .
+F 3 HOH 35 535 40 HOH HOH A .
+F 3 HOH 36 536 313 HOH HOH A .
+F 3 HOH 37 537 34 HOH HOH A .
+F 3 HOH 38 538 277 HOH HOH A .
+F 3 HOH 39 539 332 HOH HOH A .
+F 3 HOH 40 540 73 HOH HOH A .
+F 3 HOH 41 541 198 HOH HOH A .
+F 3 HOH 42 542 251 HOH HOH A .
+F 3 HOH 43 543 38 HOH HOH A .
+F 3 HOH 44 544 55 HOH HOH A .
+F 3 HOH 45 545 63 HOH HOH A .
+F 3 HOH 46 546 247 HOH HOH A .
+F 3 HOH 47 547 248 HOH HOH A .
+F 3 HOH 48 548 44 HOH HOH A .
+F 3 HOH 49 549 178 HOH HOH A .
+F 3 HOH 50 550 154 HOH HOH A .
+F 3 HOH 51 551 76 HOH HOH A .
+F 3 HOH 52 552 242 HOH HOH A .
+F 3 HOH 53 553 67 HOH HOH A .
+F 3 HOH 54 554 104 HOH HOH A .
+F 3 HOH 55 555 30 HOH HOH A .
+F 3 HOH 56 556 157 HOH HOH A .
+F 3 HOH 57 557 33 HOH HOH A .
+F 3 HOH 58 558 1 HOH HOH A .
+F 3 HOH 59 559 80 HOH HOH A .
+F 3 HOH 60 560 77 HOH HOH A .
+F 3 HOH 61 561 53 HOH HOH A .
+F 3 HOH 62 562 179 HOH HOH A .
+F 3 HOH 63 563 56 HOH HOH A .
+F 3 HOH 64 564 319 HOH HOH A .
+F 3 HOH 65 565 21 HOH HOH A .
+F 3 HOH 66 566 181 HOH HOH A .
+F 3 HOH 67 567 208 HOH HOH A .
+F 3 HOH 68 568 3 HOH HOH A .
+F 3 HOH 69 569 45 HOH HOH A .
+F 3 HOH 70 570 82 HOH HOH A .
+F 3 HOH 71 571 183 HOH HOH A .
+F 3 HOH 72 572 20 HOH HOH A .
+F 3 HOH 73 573 182 HOH HOH A .
+F 3 HOH 74 574 390 HOH HOH A .
+F 3 HOH 75 575 177 HOH HOH A .
+F 3 HOH 76 576 24 HOH HOH A .
+F 3 HOH 77 577 244 HOH HOH A .
+F 3 HOH 78 578 116 HOH HOH A .
+F 3 HOH 79 579 7 HOH HOH A .
+F 3 HOH 80 580 241 HOH HOH A .
+F 3 HOH 81 581 159 HOH HOH A .
+F 3 HOH 82 582 347 HOH HOH A .
+F 3 HOH 83 583 113 HOH HOH A .
+F 3 HOH 84 584 142 HOH HOH A .
+F 3 HOH 85 585 12 HOH HOH A .
+F 3 HOH 86 586 10 HOH HOH A .
+F 3 HOH 87 587 186 HOH HOH A .
+F 3 HOH 88 588 266 HOH HOH A .
+F 3 HOH 89 589 349 HOH HOH A .
+F 3 HOH 90 590 175 HOH HOH A .
+F 3 HOH 91 591 184 HOH HOH A .
+F 3 HOH 92 592 42 HOH HOH A .
+F 3 HOH 93 593 294 HOH HOH A .
+F 3 HOH 94 594 304 HOH HOH A .
+F 3 HOH 95 595 274 HOH HOH A .
+F 3 HOH 96 596 26 HOH HOH A .
+F 3 HOH 97 597 169 HOH HOH A .
+F 3 HOH 98 598 368 HOH HOH A .
+F 3 HOH 99 599 189 HOH HOH A .
+F 3 HOH 100 600 105 HOH HOH A .
+F 3 HOH 101 601 19 HOH HOH A .
+F 3 HOH 102 602 259 HOH HOH A .
+F 3 HOH 103 603 357 HOH HOH A .
+F 3 HOH 104 604 6 HOH HOH A .
+F 3 HOH 105 605 170 HOH HOH A .
+F 3 HOH 106 606 58 HOH HOH A .
+F 3 HOH 107 607 65 HOH HOH A .
+F 3 HOH 108 608 361 HOH HOH A .
+F 3 HOH 109 609 94 HOH HOH A .
+F 3 HOH 110 610 236 HOH HOH A .
+F 3 HOH 111 611 163 HOH HOH A .
+F 3 HOH 112 612 86 HOH HOH A .
+F 3 HOH 113 613 31 HOH HOH A .
+F 3 HOH 114 614 27 HOH HOH A .
+F 3 HOH 115 615 326 HOH HOH A .
+F 3 HOH 116 616 306 HOH HOH A .
+F 3 HOH 117 617 43 HOH HOH A .
+F 3 HOH 118 618 92 HOH HOH A .
+F 3 HOH 119 619 4 HOH HOH A .
+F 3 HOH 120 620 272 HOH HOH A .
+F 3 HOH 121 621 168 HOH HOH A .
+F 3 HOH 122 622 342 HOH HOH A .
+F 3 HOH 123 623 117 HOH HOH A .
+F 3 HOH 124 624 263 HOH HOH A .
+F 3 HOH 125 625 289 HOH HOH A .
+F 3 HOH 126 626 171 HOH HOH A .
+F 3 HOH 127 627 69 HOH HOH A .
+F 3 HOH 128 628 269 HOH HOH A .
+F 3 HOH 129 629 5 HOH HOH A .
+F 3 HOH 130 630 68 HOH HOH A .
+F 3 HOH 131 631 87 HOH HOH A .
+F 3 HOH 132 632 89 HOH HOH A .
+F 3 HOH 133 633 351 HOH HOH A .
+F 3 HOH 134 634 172 HOH HOH A .
+F 3 HOH 135 635 230 HOH HOH A .
+F 3 HOH 136 636 54 HOH HOH A .
+F 3 HOH 137 637 118 HOH HOH A .
+F 3 HOH 138 638 60 HOH HOH A .
+F 3 HOH 139 639 106 HOH HOH A .
+F 3 HOH 140 640 79 HOH HOH A .
+F 3 HOH 141 641 185 HOH HOH A .
+F 3 HOH 142 642 381 HOH HOH A .
+F 3 HOH 143 643 298 HOH HOH A .
+F 3 HOH 144 644 295 HOH HOH A .
+F 3 HOH 145 645 17 HOH HOH A .
+F 3 HOH 146 646 164 HOH HOH A .
+F 3 HOH 147 647 204 HOH HOH A .
+F 3 HOH 148 648 310 HOH HOH A .
+F 3 HOH 149 649 11 HOH HOH A .
+F 3 HOH 150 650 15 HOH HOH A .
+F 3 HOH 151 651 28 HOH HOH A .
+F 3 HOH 152 652 392 HOH HOH A .
+F 3 HOH 153 653 246 HOH HOH A .
+F 3 HOH 154 654 37 HOH HOH A .
+F 3 HOH 155 655 309 HOH HOH A .
+F 3 HOH 156 656 200 HOH HOH A .
+F 3 HOH 157 657 130 HOH HOH A .
+F 3 HOH 158 658 285 HOH HOH A .
+F 3 HOH 159 659 83 HOH HOH A .
+F 3 HOH 160 660 102 HOH HOH A .
+F 3 HOH 161 661 62 HOH HOH A .
+F 3 HOH 162 662 101 HOH HOH A .
+F 3 HOH 163 663 176 HOH HOH A .
+F 3 HOH 164 664 325 HOH HOH A .
+F 3 HOH 165 665 234 HOH HOH A .
+F 3 HOH 166 666 52 HOH HOH A .
+F 3 HOH 167 667 88 HOH HOH A .
+F 3 HOH 168 668 72 HOH HOH A .
+F 3 HOH 169 669 128 HOH HOH A .
+F 3 HOH 170 670 228 HOH HOH A .
+F 3 HOH 171 671 145 HOH HOH A .
+F 3 HOH 172 672 173 HOH HOH A .
+F 3 HOH 173 673 18 HOH HOH A .
+F 3 HOH 174 674 125 HOH HOH A .
+F 3 HOH 175 675 152 HOH HOH A .
+F 3 HOH 176 676 299 HOH HOH A .
+F 3 HOH 177 677 240 HOH HOH A .
+F 3 HOH 178 678 111 HOH HOH A .
+F 3 HOH 179 679 61 HOH HOH A .
+F 3 HOH 180 680 203 HOH HOH A .
+F 3 HOH 181 681 100 HOH HOH A .
+F 3 HOH 182 682 156 HOH HOH A .
+F 3 HOH 183 683 71 HOH HOH A .
+F 3 HOH 184 684 59 HOH HOH A .
+F 3 HOH 185 685 133 HOH HOH A .
+F 3 HOH 186 686 64 HOH HOH A .
+F 3 HOH 187 687 127 HOH HOH A .
+F 3 HOH 188 688 386 HOH HOH A .
+F 3 HOH 189 689 14 HOH HOH A .
+F 3 HOH 190 690 78 HOH HOH A .
+F 3 HOH 191 691 344 HOH HOH A .
+F 3 HOH 192 692 131 HOH HOH A .
+F 3 HOH 193 693 2 HOH HOH A .
+F 3 HOH 194 694 135 HOH HOH A .
+F 3 HOH 195 695 239 HOH HOH A .
+F 3 HOH 196 696 276 HOH HOH A .
+F 3 HOH 197 697 328 HOH HOH A .
+F 3 HOH 198 698 213 HOH HOH A .
+F 3 HOH 199 699 32 HOH HOH A .
+F 3 HOH 200 700 360 HOH HOH A .
+F 3 HOH 201 701 201 HOH HOH A .
+F 3 HOH 202 702 136 HOH HOH A .
+F 3 HOH 203 703 153 HOH HOH A .
+F 3 HOH 204 704 379 HOH HOH A .
+F 3 HOH 205 705 166 HOH HOH A .
+F 3 HOH 206 706 84 HOH HOH A .
+F 3 HOH 207 707 75 HOH HOH A .
+F 3 HOH 208 708 231 HOH HOH A .
+F 3 HOH 209 709 187 HOH HOH A .
+F 3 HOH 210 710 290 HOH HOH A .
+F 3 HOH 211 711 96 HOH HOH A .
+F 3 HOH 212 712 211 HOH HOH A .
+F 3 HOH 213 713 150 HOH HOH A .
+F 3 HOH 214 714 267 HOH HOH A .
+F 3 HOH 215 715 260 HOH HOH A .
+F 3 HOH 216 716 103 HOH HOH A .
+F 3 HOH 217 717 232 HOH HOH A .
+F 3 HOH 218 718 8 HOH HOH A .
+F 3 HOH 219 719 126 HOH HOH A .
+F 3 HOH 220 720 330 HOH HOH A .
+F 3 HOH 221 721 385 HOH HOH A .
+F 3 HOH 222 722 188 HOH HOH A .
+F 3 HOH 223 723 217 HOH HOH A .
+F 3 HOH 224 724 47 HOH HOH A .
+F 3 HOH 225 725 81 HOH HOH A .
+F 3 HOH 226 726 329 HOH HOH A .
+F 3 HOH 227 727 388 HOH HOH A .
+F 3 HOH 228 728 51 HOH HOH A .
+F 3 HOH 229 729 95 HOH HOH A .
+F 3 HOH 230 730 13 HOH HOH A .
+F 3 HOH 231 731 197 HOH HOH A .
+F 3 HOH 232 732 296 HOH HOH A .
+F 3 HOH 233 733 235 HOH HOH A .
+F 3 HOH 234 734 148 HOH HOH A .
+F 3 HOH 235 735 22 HOH HOH A .
+F 3 HOH 236 736 268 HOH HOH A .
+F 3 HOH 237 737 193 HOH HOH A .
+F 3 HOH 238 738 261 HOH HOH A .
+F 3 HOH 239 739 23 HOH HOH A .
+F 3 HOH 240 740 308 HOH HOH A .
+F 3 HOH 241 741 265 HOH HOH A .
+F 3 HOH 242 742 146 HOH HOH A .
+F 3 HOH 243 743 339 HOH HOH A .
+F 3 HOH 244 744 252 HOH HOH A .
+F 3 HOH 245 745 262 HOH HOH A .
+F 3 HOH 246 746 16 HOH HOH A .
+F 3 HOH 247 747 57 HOH HOH A .
+F 3 HOH 248 748 143 HOH HOH A .
+F 3 HOH 249 749 206 HOH HOH A .
+F 3 HOH 250 750 139 HOH HOH A .
+F 3 HOH 251 751 297 HOH HOH A .
+F 3 HOH 252 752 123 HOH HOH A .
+F 3 HOH 253 753 286 HOH HOH A .
+F 3 HOH 254 754 237 HOH HOH A .
+F 3 HOH 255 755 219 HOH HOH A .
+F 3 HOH 256 756 109 HOH HOH A .
+F 3 HOH 257 757 36 HOH HOH A .
+F 3 HOH 258 758 144 HOH HOH A .
+F 3 HOH 259 759 312 HOH HOH A .
+F 3 HOH 260 760 291 HOH HOH A .
+F 3 HOH 261 761 110 HOH HOH A .
+F 3 HOH 262 762 233 HOH HOH A .
+F 3 HOH 263 763 245 HOH HOH A .
+F 3 HOH 264 764 149 HOH HOH A .
+F 3 HOH 265 765 194 HOH HOH A .
+F 3 HOH 266 766 370 HOH HOH A .
+F 3 HOH 267 767 389 HOH HOH A .
+F 3 HOH 268 768 39 HOH HOH A .
+F 3 HOH 269 769 91 HOH HOH A .
+F 3 HOH 270 770 138 HOH HOH A .
+F 3 HOH 271 771 50 HOH HOH A .
+F 3 HOH 272 772 140 HOH HOH A .
+F 3 HOH 273 773 46 HOH HOH A .
+F 3 HOH 274 774 250 HOH HOH A .
+F 3 HOH 275 775 270 HOH HOH A .
+F 3 HOH 276 776 353 HOH HOH A .
+F 3 HOH 277 777 249 HOH HOH A .
+F 3 HOH 278 778 322 HOH HOH A .
+F 3 HOH 279 779 336 HOH HOH A .
+F 3 HOH 280 780 192 HOH HOH A .
+F 3 HOH 281 781 315 HOH HOH A .
+F 3 HOH 282 782 377 HOH HOH A .
+F 3 HOH 283 783 284 HOH HOH A .
+F 3 HOH 284 784 300 HOH HOH A .
+F 3 HOH 285 785 320 HOH HOH A .
+F 3 HOH 286 786 121 HOH HOH A .
+F 3 HOH 287 787 271 HOH HOH A .
+F 3 HOH 288 788 371 HOH HOH A .
+F 3 HOH 289 789 257 HOH HOH A .
+F 3 HOH 290 790 318 HOH HOH A .
+F 3 HOH 291 791 74 HOH HOH A .
+F 3 HOH 292 792 341 HOH HOH A .
+F 3 HOH 293 793 238 HOH HOH A .
+F 3 HOH 294 794 365 HOH HOH A .
+F 3 HOH 295 795 215 HOH HOH A .
+F 3 HOH 296 796 366 HOH HOH A .
+F 3 HOH 297 797 356 HOH HOH A .
+F 3 HOH 298 798 214 HOH HOH A .
+F 3 HOH 299 799 311 HOH HOH A .
+F 3 HOH 300 800 331 HOH HOH A .
+F 3 HOH 301 801 307 HOH HOH A .
+F 3 HOH 302 802 387 HOH HOH A .
+F 3 HOH 303 803 280 HOH HOH A .
+F 3 HOH 304 804 305 HOH HOH A .
+F 3 HOH 305 805 167 HOH HOH A .
+F 3 HOH 306 806 220 HOH HOH A .
+F 3 HOH 307 807 255 HOH HOH A .
+F 3 HOH 308 808 314 HOH HOH A .
+F 3 HOH 309 809 202 HOH HOH A .
+F 3 HOH 310 810 191 HOH HOH A .
+F 3 HOH 311 811 303 HOH HOH A .
+F 3 HOH 312 812 346 HOH HOH A .
+F 3 HOH 313 813 334 HOH HOH A .
+F 3 HOH 314 814 364 HOH HOH A .
+F 3 HOH 315 815 221 HOH HOH A .
+F 3 HOH 316 816 378 HOH HOH A .
+F 3 HOH 317 817 287 HOH HOH A .
+F 3 HOH 318 818 293 HOH HOH A .
+F 3 HOH 319 819 362 HOH HOH A .
+F 3 HOH 320 820 384 HOH HOH A .
+F 3 HOH 321 821 273 HOH HOH A .
+F 3 HOH 322 822 174 HOH HOH A .
+F 3 HOH 323 823 301 HOH HOH A .
+F 3 HOH 324 824 317 HOH HOH A .
+F 3 HOH 325 825 372 HOH HOH A .
+F 3 HOH 326 826 180 HOH HOH A .
+F 3 HOH 327 827 253 HOH HOH A .
+F 3 HOH 328 828 161 HOH HOH A .
+F 3 HOH 329 829 288 HOH HOH A .
+F 3 HOH 330 830 190 HOH HOH A .
+F 3 HOH 331 831 355 HOH HOH A .
+F 3 HOH 332 832 278 HOH HOH A .
+F 3 HOH 333 833 391 HOH HOH A .
+F 3 HOH 334 834 226 HOH HOH A .
+F 3 HOH 335 835 258 HOH HOH A .
+F 3 HOH 336 836 227 HOH HOH A .
+F 3 HOH 337 837 147 HOH HOH A .
+F 3 HOH 338 838 323 HOH HOH A .
+F 3 HOH 339 839 369 HOH HOH A .
+F 3 HOH 340 840 354 HOH HOH A .
+F 3 HOH 341 841 205 HOH HOH A .
+F 3 HOH 342 842 108 HOH HOH A .
+F 3 HOH 343 843 122 HOH HOH A .
+F 3 HOH 344 844 229 HOH HOH A .
+F 3 HOH 345 845 363 HOH HOH A .
+F 3 HOH 346 846 158 HOH HOH A .
+F 3 HOH 347 847 90 HOH HOH A .
+F 3 HOH 348 848 210 HOH HOH A .
+F 3 HOH 349 849 49 HOH HOH A .
+F 3 HOH 350 850 338 HOH HOH A .
+F 3 HOH 351 851 124 HOH HOH A .
+F 3 HOH 352 852 218 HOH HOH A .
+F 3 HOH 353 853 160 HOH HOH A .
+F 3 HOH 354 854 333 HOH HOH A .
+F 3 HOH 355 855 223 HOH HOH A .
+F 3 HOH 356 856 207 HOH HOH A .
+F 3 HOH 357 857 343 HOH HOH A .
+F 3 HOH 358 858 282 HOH HOH A .
+F 3 HOH 359 859 41 HOH HOH A .
+F 3 HOH 360 860 225 HOH HOH A .
+F 3 HOH 361 861 383 HOH HOH A .
+F 3 HOH 362 862 216 HOH HOH A .
+F 3 HOH 363 863 337 HOH HOH A .
+F 3 HOH 364 864 380 HOH HOH A .
+F 3 HOH 365 865 254 HOH HOH A .
+F 3 HOH 366 866 292 HOH HOH A .
+F 3 HOH 367 867 376 HOH HOH A .
+F 3 HOH 368 868 70 HOH HOH A .
+F 3 HOH 369 869 209 HOH HOH A .
+F 3 HOH 370 870 134 HOH HOH A .
+F 3 HOH 371 871 281 HOH HOH A .
+F 3 HOH 372 872 382 HOH HOH A .
+F 3 HOH 373 873 350 HOH HOH A .
+F 3 HOH 374 874 141 HOH HOH A .
+F 3 HOH 375 875 195 HOH HOH A .
+F 3 HOH 376 876 114 HOH HOH A .
+F 3 HOH 377 877 316 HOH HOH A .
+F 3 HOH 378 878 359 HOH HOH A .
+F 3 HOH 379 879 324 HOH HOH A .
+F 3 HOH 380 880 279 HOH HOH A .
+F 3 HOH 381 881 367 HOH HOH A .
+F 3 HOH 382 882 98 HOH HOH A .
+F 3 HOH 383 883 375 HOH HOH A .
+F 3 HOH 384 884 302 HOH HOH A .
+F 3 HOH 385 885 348 HOH HOH A .
+F 3 HOH 386 886 115 HOH HOH A .
+F 3 HOH 387 887 196 HOH HOH A .
+F 3 HOH 388 888 224 HOH HOH A .
+F 3 HOH 389 889 222 HOH HOH A .
+F 3 HOH 390 890 283 HOH HOH A .
+F 3 HOH 391 891 321 HOH HOH A .
+#
+_pdbx_struct_assembly.id 1
+_pdbx_struct_assembly.details author_and_software_defined_assembly
+_pdbx_struct_assembly.method_details PISA
+_pdbx_struct_assembly.oligomeric_details dimeric
+_pdbx_struct_assembly.oligomeric_count 2
+#
+_pdbx_struct_assembly_gen.assembly_id 1
+_pdbx_struct_assembly_gen.oper_expression 1,2
+_pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F
+#
+loop_
+_pdbx_struct_assembly_prop.biol_id
+_pdbx_struct_assembly_prop.type
+_pdbx_struct_assembly_prop.value
+_pdbx_struct_assembly_prop.details
+1 'ABSA (A^2)' 4410 ?
+1 MORE -8 ?
+1 'SSA (A^2)' 25910 ?
+#
+loop_
+_pdbx_struct_oper_list.id
+_pdbx_struct_oper_list.type
+_pdbx_struct_oper_list.name
+_pdbx_struct_oper_list.symmetry_operation
+_pdbx_struct_oper_list.matrix[1][1]
+_pdbx_struct_oper_list.matrix[1][2]
+_pdbx_struct_oper_list.matrix[1][3]
+_pdbx_struct_oper_list.vector[1]
+_pdbx_struct_oper_list.matrix[2][1]
+_pdbx_struct_oper_list.matrix[2][2]
+_pdbx_struct_oper_list.matrix[2][3]
+_pdbx_struct_oper_list.vector[2]
+_pdbx_struct_oper_list.matrix[3][1]
+_pdbx_struct_oper_list.matrix[3][2]
+_pdbx_struct_oper_list.matrix[3][3]
+_pdbx_struct_oper_list.vector[3]
+1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000
+0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000
+2 'crystal symmetry operation' 2_555 -x,y,-z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000
+0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000
+#
+_pdbx_struct_special_symmetry.id 1
+_pdbx_struct_special_symmetry.PDB_model_num 1
+_pdbx_struct_special_symmetry.auth_asym_id A
+_pdbx_struct_special_symmetry.auth_comp_id HOH
+_pdbx_struct_special_symmetry.auth_seq_id 774
+_pdbx_struct_special_symmetry.PDB_ins_code ?
+_pdbx_struct_special_symmetry.label_asym_id F
+_pdbx_struct_special_symmetry.label_comp_id HOH
+_pdbx_struct_special_symmetry.label_seq_id .
+#
+_pdbx_audit_revision_history.ordinal 1
+_pdbx_audit_revision_history.data_content_type 'Structure model'
+_pdbx_audit_revision_history.major_revision 1
+_pdbx_audit_revision_history.minor_revision 0
+_pdbx_audit_revision_history.revision_date 2020-03-11
+#
+_pdbx_audit_revision_details.ordinal 1
+_pdbx_audit_revision_details.revision_ordinal 1
+_pdbx_audit_revision_details.data_content_type 'Structure model'
+_pdbx_audit_revision_details.provider repository
+_pdbx_audit_revision_details.type 'Initial release'
+_pdbx_audit_revision_details.description ?
+_pdbx_audit_revision_details.details ?
+#
+_pdbx_refine_tls.id 1
+_pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION'
+_pdbx_refine_tls.details ?
+_pdbx_refine_tls.method refined
+_pdbx_refine_tls.origin_x 11.7561
+_pdbx_refine_tls.origin_y 0.8392
+_pdbx_refine_tls.origin_z 4.6891
+_pdbx_refine_tls.T[1][1] -0.0121
+_pdbx_refine_tls.T[1][1]_esd ?
+_pdbx_refine_tls.T[1][2] -0.0060
+_pdbx_refine_tls.T[1][2]_esd ?
+_pdbx_refine_tls.T[1][3] -0.0248
+_pdbx_refine_tls.T[1][3]_esd ?
+_pdbx_refine_tls.T[2][2] -0.0177
+_pdbx_refine_tls.T[2][2]_esd ?
+_pdbx_refine_tls.T[2][3] -0.0095
+_pdbx_refine_tls.T[2][3]_esd ?
+_pdbx_refine_tls.T[3][3] -0.0441
+_pdbx_refine_tls.T[3][3]_esd ?
+_pdbx_refine_tls.L[1][1] 0.3373
+_pdbx_refine_tls.L[1][1]_esd ?
+_pdbx_refine_tls.L[1][2] 0.1417
+_pdbx_refine_tls.L[1][2]_esd ?
+_pdbx_refine_tls.L[1][3] -0.0841
+_pdbx_refine_tls.L[1][3]_esd ?
+_pdbx_refine_tls.L[2][2] 0.9615
+_pdbx_refine_tls.L[2][2]_esd ?
+_pdbx_refine_tls.L[2][3] -0.7793
+_pdbx_refine_tls.L[2][3]_esd ?
+_pdbx_refine_tls.L[3][3] 0.4899
+_pdbx_refine_tls.L[3][3]_esd ?
+_pdbx_refine_tls.S[1][1] -0.0543
+_pdbx_refine_tls.S[1][1]_esd ?
+_pdbx_refine_tls.S[1][2] 0.0192
+_pdbx_refine_tls.S[1][2]_esd ?
+_pdbx_refine_tls.S[1][3] -0.0247
+_pdbx_refine_tls.S[1][3]_esd ?
+_pdbx_refine_tls.S[2][1] -0.0315
+_pdbx_refine_tls.S[2][1]_esd ?
+_pdbx_refine_tls.S[2][2] 0.0611
+_pdbx_refine_tls.S[2][2]_esd ?
+_pdbx_refine_tls.S[2][3] -0.0331
+_pdbx_refine_tls.S[2][3]_esd ?
+_pdbx_refine_tls.S[3][1] 0.0069
+_pdbx_refine_tls.S[3][1]_esd ?
+_pdbx_refine_tls.S[3][2] -0.0231
+_pdbx_refine_tls.S[3][2]_esd ?
+_pdbx_refine_tls.S[3][3] -0.0068
+_pdbx_refine_tls.S[3][3]_esd ?
+#
+_pdbx_refine_tls_group.id 1
+_pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION'
+_pdbx_refine_tls_group.refine_tls_id 1
+_pdbx_refine_tls_group.beg_label_asym_id ?
+_pdbx_refine_tls_group.beg_label_seq_id ?
+_pdbx_refine_tls_group.beg_auth_asym_id A
+_pdbx_refine_tls_group.beg_auth_seq_id 1
+_pdbx_refine_tls_group.end_label_asym_id ?
+_pdbx_refine_tls_group.end_label_seq_id ?
+_pdbx_refine_tls_group.end_auth_asym_id A
+_pdbx_refine_tls_group.end_auth_seq_id 304
+_pdbx_refine_tls_group.selection ?
+_pdbx_refine_tls_group.selection_details '{ A|* }'
+#
+_pdbx_phasing_MR.entry_id 6Y84
+_pdbx_phasing_MR.method_rotation ?
+_pdbx_phasing_MR.method_translation ?
+_pdbx_phasing_MR.model_details ?
+_pdbx_phasing_MR.R_factor ?
+_pdbx_phasing_MR.R_rigid_body 0.468
+_pdbx_phasing_MR.correlation_coeff_Fo_to_Fc ?
+_pdbx_phasing_MR.correlation_coeff_Io_to_Ic ?
+_pdbx_phasing_MR.d_res_high_rotation 54.910
+_pdbx_phasing_MR.d_res_low_rotation 1.740
+_pdbx_phasing_MR.d_res_high_translation ?
+_pdbx_phasing_MR.d_res_low_translation ?
+_pdbx_phasing_MR.packing ?
+_pdbx_phasing_MR.reflns_percent_rotation ?
+_pdbx_phasing_MR.reflns_percent_translation ?
+_pdbx_phasing_MR.sigma_F_rotation ?
+_pdbx_phasing_MR.sigma_F_translation ?
+_pdbx_phasing_MR.sigma_I_rotation ?
+_pdbx_phasing_MR.sigma_I_translation ?
+#
+_phasing.method MR
+#
+loop_
+_software.citation_id
+_software.classification
+_software.compiler_name
+_software.compiler_version
+_software.contact_author
+_software.contact_author_email
+_software.date
+_software.description
+_software.dependencies
+_software.hardware
+_software.language
+_software.location
+_software.mods
+_software.name
+_software.os
+_software.os_version
+_software.type
+_software.version
+_software.pdbx_ordinal
+? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.4 1
+? phasing ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? . 2
+? refinement ? ? ? ? ? ? ? ? ? ? ? BUSTER ? ? ? . 3
+? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25 4
+? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS ? ? ? . 5
+? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2 ? ? ? . 6
+? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot ? ? ? . 7
+? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 7.0.078 8
+#
+_pdbx_entry_details.entry_id 6Y84
+_pdbx_entry_details.has_ligand_of_interest N
+_pdbx_entry_details.compound_details ?
+_pdbx_entry_details.source_details ?
+_pdbx_entry_details.nonpolymer_details ?
+_pdbx_entry_details.sequence_details ?
+#
+loop_
+_pdbx_validate_torsion.id
+_pdbx_validate_torsion.PDB_model_num
+_pdbx_validate_torsion.auth_comp_id
+_pdbx_validate_torsion.auth_asym_id
+_pdbx_validate_torsion.auth_seq_id
+_pdbx_validate_torsion.PDB_ins_code
+_pdbx_validate_torsion.label_alt_id
+_pdbx_validate_torsion.phi
+_pdbx_validate_torsion.psi
+1 1 ASP A 33 ? ? 57.52 -132.67
+2 1 ASN A 51 ? ? -154.49 69.76
+3 1 ASN A 84 ? ? 56.10 -119.94
+4 1 TYR A 154 ? ? 58.72 -89.93
+#
+loop_
+_pdbx_distant_solvent_atoms.id
+_pdbx_distant_solvent_atoms.PDB_model_num
+_pdbx_distant_solvent_atoms.auth_atom_id
+_pdbx_distant_solvent_atoms.label_alt_id
+_pdbx_distant_solvent_atoms.auth_asym_id
+_pdbx_distant_solvent_atoms.auth_comp_id
+_pdbx_distant_solvent_atoms.auth_seq_id
+_pdbx_distant_solvent_atoms.PDB_ins_code
+_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance
+_pdbx_distant_solvent_atoms.neighbor_ligand_distance
+1 1 O ? A HOH 889 ? 6.51 .
+2 1 O ? A HOH 890 ? 6.68 .
+3 1 O ? A HOH 891 ? 7.12 .
+#
+loop_
+_pdbx_unobs_or_zero_occ_residues.id
+_pdbx_unobs_or_zero_occ_residues.PDB_model_num
+_pdbx_unobs_or_zero_occ_residues.polymer_flag
+_pdbx_unobs_or_zero_occ_residues.occupancy_flag
+_pdbx_unobs_or_zero_occ_residues.auth_asym_id
+_pdbx_unobs_or_zero_occ_residues.auth_comp_id
+_pdbx_unobs_or_zero_occ_residues.auth_seq_id
+_pdbx_unobs_or_zero_occ_residues.PDB_ins_code
+_pdbx_unobs_or_zero_occ_residues.label_asym_id
+_pdbx_unobs_or_zero_occ_residues.label_comp_id
+_pdbx_unobs_or_zero_occ_residues.label_seq_id
+1 1 Y 1 A PHE 305 ? A PHE 305
+2 1 Y 1 A GLN 306 ? A GLN 306
+#
+loop_
+_pdbx_entity_nonpoly.entity_id
+_pdbx_entity_nonpoly.name
+_pdbx_entity_nonpoly.comp_id
+2 'DIMETHYL SULFOXIDE' DMS
+3 water HOH
+#
+loop_
+_pdbx_struct_assembly_auth_evidence.id
+_pdbx_struct_assembly_auth_evidence.assembly_id
+_pdbx_struct_assembly_auth_evidence.experimental_support
+_pdbx_struct_assembly_auth_evidence.details
+1 1 homology ?
+2 1 'gel filtration' ?
+#
diff --git a/Docking/Target/6y84.pdb b/Docking/Target/6y84.pdb
new file mode 100755
index 0000000..d00410f
--- /dev/null
+++ b/Docking/Target/6y84.pdb
@@ -0,0 +1,5934 @@
+HEADER VIRAL PROTEIN 03-MAR-20 6Y84
+TITLE COVID-19 MAIN PROTEASE WITH UNLIGANDED ACTIVE SITE (2019-NCOV,
+TITLE 2 CORONAVIRUS DISEASE 2019, SARS-COV-2)
+COMPND MOL_ID: 1;
+COMPND 2 MOLECULE: NON-STRUCTURAL POLYPROTEIN 1AB;
+COMPND 3 CHAIN: A;
+COMPND 4 ENGINEERED: YES
+SOURCE MOL_ID: 1;
+SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS
+SOURCE 3 2;
+SOURCE 4 ORGANISM_TAXID: 2697049;
+SOURCE 5 STRAIN: COVID-19;
+SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
+SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
+KEYWDS PROTEASE, CYSTEINE PROTEASE, VIRAL PROTEIN
+EXPDTA X-RAY DIFFRACTION
+AUTHOR C.D.OWEN,P.LUKACIK,C.M.STRAIN-DAMERELL,A.DOUANGAMATH,A.J.POWELL,
+AUTHOR 2 D.FEARON,J.BRANDAO-NETO,A.D.CRAWSHAW,D.ARAGAO,M.WILLIAMS,R.FLAIG,
+AUTHOR 3 D.HALL,K.MCAAULEY,D.I.STUART,F.VON DELFT,M.A.WALSH
+REVDAT 1 11-MAR-20 6Y84 0
+JRNL AUTH C.D.OWEN,P.LUKACIK,C.M.STRAIN-DAMERELL,A.DOUANGAMATH,
+JRNL AUTH 2 A.J.POWELL,D.FEARON,J.BRANDAO-NETO,A.D.CRAWSHAW,D.ARAGAO,
+JRNL AUTH 3 M.WILLIAMS,R.FLAIG,D.HALL,K.MCAAULEY,D.I.STUART,F.VON DELFT,
+JRNL AUTH 4 M.A.WALSH
+JRNL TITL COVID-19 MAIN PROTEASE WITH UNLIGANDED ACTIVE SITE
+JRNL REF TO BE PUBLISHED
+JRNL REFN
+REMARK 2
+REMARK 2 RESOLUTION. 1.39 ANGSTROMS.
+REMARK 3
+REMARK 3 REFINEMENT.
+REMARK 3 PROGRAM : BUSTER
+REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
+REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
+REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
+REMARK 3
+REMARK 3 DATA USED IN REFINEMENT.
+REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.39
+REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.93
+REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
+REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
+REMARK 3 NUMBER OF REFLECTIONS : 50331
+REMARK 3
+REMARK 3 FIT TO DATA USED IN REFINEMENT.
+REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
+REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
+REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
+REMARK 3 R VALUE (WORKING SET) : 0.178
+REMARK 3 FREE R VALUE : 0.200
+REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
+REMARK 3 FREE R VALUE TEST SET COUNT : 2498
+REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
+REMARK 3
+REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
+REMARK 3 TOTAL NUMBER OF BINS USED : 51
+REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.39
+REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.40
+REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.99
+REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1007
+REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2107
+REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 941
+REMARK 3 BIN R VALUE (WORKING SET) : 0.2109
+REMARK 3 BIN FREE R VALUE : 0.2075
+REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.55
+REMARK 3 BIN FREE R VALUE TEST SET COUNT : 66
+REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
+REMARK 3
+REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
+REMARK 3 PROTEIN ATOMS : 2347
+REMARK 3 NUCLEIC ACID ATOMS : 0
+REMARK 3 HETEROGEN ATOMS : 16
+REMARK 3 SOLVENT ATOMS : 391
+REMARK 3
+REMARK 3 B VALUES.
+REMARK 3 FROM WILSON PLOT (A**2) : 17.33
+REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.00
+REMARK 3 OVERALL ANISOTROPIC B VALUE.
+REMARK 3 B11 (A**2) : -3.78090
+REMARK 3 B22 (A**2) : 0.69780
+REMARK 3 B33 (A**2) : 3.08310
+REMARK 3 B12 (A**2) : 0.00000
+REMARK 3 B13 (A**2) : 0.04220
+REMARK 3 B23 (A**2) : 0.00000
+REMARK 3
+REMARK 3 ESTIMATED COORDINATE ERROR.
+REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.190
+REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.074
+REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.071
+REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.069
+REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.068
+REMARK 3
+REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
+REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
+REMARK 3
+REMARK 3 CORRELATION COEFFICIENTS.
+REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
+REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
+REMARK 3
+REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
+REMARK 3 TERM COUNT WEIGHT FUNCTION.
+REMARK 3 BOND LENGTHS : 2628 ; 2.000 ; HARMONIC
+REMARK 3 BOND ANGLES : 3595 ; 2.000 ; HARMONIC
+REMARK 3 TORSION ANGLES : 909 ; 2.000 ; SINUSOIDAL
+REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
+REMARK 3 GENERAL PLANES : 466 ; 5.000 ; HARMONIC
+REMARK 3 ISOTROPIC THERMAL FACTORS : 2628 ; 10.000 ; HARMONIC
+REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
+REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
+REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
+REMARK 3 CHIRAL IMPROPER TORSION : 340 ; 5.000 ; SEMIHARMONIC
+REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
+REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
+REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
+REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
+REMARK 3 IDEAL-DIST CONTACT TERM : 3017 ; 4.000 ; SEMIHARMONIC
+REMARK 3
+REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
+REMARK 3 BOND LENGTHS (A) : 0.007
+REMARK 3 BOND ANGLES (DEGREES) : 0.98
+REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.92
+REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.64
+REMARK 3
+REMARK 3 TLS DETAILS
+REMARK 3 NUMBER OF TLS GROUPS : 1
+REMARK 3
+REMARK 3 TLS GROUP : 1
+REMARK 3 SELECTION: { A|* }
+REMARK 3 ORIGIN FOR THE GROUP (A): 11.7561 0.8392 4.6891
+REMARK 3 T TENSOR
+REMARK 3 T11: -0.0121 T22: -0.0177
+REMARK 3 T33: -0.0441 T12: -0.0060
+REMARK 3 T13: -0.0248 T23: -0.0095
+REMARK 3 L TENSOR
+REMARK 3 L11: 0.3373 L22: 0.9615
+REMARK 3 L33: 0.4899 L12: 0.1417
+REMARK 3 L13: -0.0841 L23: -0.7793
+REMARK 3 S TENSOR
+REMARK 3 S11: -0.0543 S12: 0.0192 S13: -0.0247
+REMARK 3 S21: -0.0315 S22: 0.0611 S23: -0.0331
+REMARK 3 S31: 0.0069 S32: -0.0231 S33: -0.0068
+REMARK 3
+REMARK 3 OTHER REFINEMENT REMARKS: NULL
+REMARK 4
+REMARK 4 6Y84 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
+REMARK 100
+REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAR-20.
+REMARK 100 THE DEPOSITION ID IS D_1292107053.
+REMARK 200
+REMARK 200 EXPERIMENTAL DETAILS
+REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
+REMARK 200 DATE OF DATA COLLECTION : 24-FEB-20
+REMARK 200 TEMPERATURE (KELVIN) : 100
+REMARK 200 PH : 6.5
+REMARK 200 NUMBER OF CRYSTALS USED : 1
+REMARK 200
+REMARK 200 SYNCHROTRON (Y/N) : Y
+REMARK 200 RADIATION SOURCE : DIAMOND
+REMARK 200 BEAMLINE : I04-1
+REMARK 200 X-RAY GENERATOR MODEL : NULL
+REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
+REMARK 200 WAVELENGTH OR RANGE (A) : 0.9126
+REMARK 200 MONOCHROMATOR : NULL
+REMARK 200 OPTICS : NULL
+REMARK 200
+REMARK 200 DETECTOR TYPE : PIXEL
+REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
+REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS, XIA2
+REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
+REMARK 200
+REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50348
+REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
+REMARK 200 RESOLUTION RANGE LOW (A) : 54.930
+REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
+REMARK 200
+REMARK 200 OVERALL.
+REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
+REMARK 200 DATA REDUNDANCY : 3.600
+REMARK 200 R MERGE (I) : 0.05900
+REMARK 200 R SYM (I) : NULL
+REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
+REMARK 200
+REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
+REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
+REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.41
+REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7
+REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
+REMARK 200 R MERGE FOR SHELL (I) : 0.92900
+REMARK 200 R SYM FOR SHELL (I) : NULL
+REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
+REMARK 200
+REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
+REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
+REMARK 200 SOFTWARE USED: MOLREP
+REMARK 200 STARTING MODEL: 6LU7
+REMARK 200
+REMARK 200 REMARK: NULL
+REMARK 280
+REMARK 280 CRYSTAL
+REMARK 280 SOLVENT CONTENT, VS (%): 35.89
+REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
+REMARK 280
+REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 5% DMSO, 0.1M MES PH
+REMARK 280 6.5. 0.15 MICROLITRE PROTEIN + 0.3 MICROLITRE RESERVOIR + 0.05
+REMARK 280 MICROLITRE SEED STOCK, VAPOR DIFFUSION, SITTING DROP,
+REMARK 280 TEMPERATURE 293K
+REMARK 290
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
+REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
+REMARK 290
+REMARK 290 SYMOP SYMMETRY
+REMARK 290 NNNMMM OPERATOR
+REMARK 290 1555 X,Y,Z
+REMARK 290 2555 -X,Y,-Z
+REMARK 290 3555 X+1/2,Y+1/2,Z
+REMARK 290 4555 -X+1/2,Y+1/2,-Z
+REMARK 290
+REMARK 290 WHERE NNN -> OPERATOR NUMBER
+REMARK 290 MMM -> TRANSLATION VECTOR
+REMARK 290
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
+REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
+REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
+REMARK 290 RELATED MOLECULES.
+REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
+REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
+REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
+REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
+REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
+REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
+REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 56.40600
+REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.47450
+REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
+REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.40600
+REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.47450
+REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
+REMARK 290
+REMARK 290 REMARK: NULL
+REMARK 300
+REMARK 300 BIOMOLECULE: 1
+REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
+REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
+REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
+REMARK 300 BURIED SURFACE AREA.
+REMARK 350
+REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
+REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
+REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
+REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
+REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
+REMARK 350
+REMARK 350 BIOMOLECULE: 1
+REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
+REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
+REMARK 350 SOFTWARE USED: PISA
+REMARK 350 TOTAL BURIED SURFACE AREA: 4410 ANGSTROM**2
+REMARK 350 SURFACE AREA OF THE COMPLEX: 25910 ANGSTROM**2
+REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
+REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
+REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
+REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
+REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
+REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
+REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
+REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
+REMARK 375
+REMARK 375 SPECIAL POSITION
+REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
+REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
+REMARK 375 POSITIONS.
+REMARK 375
+REMARK 375 ATOM RES CSSEQI
+REMARK 375 HOH A 774 LIES ON A SPECIAL POSITION.
+REMARK 465
+REMARK 465 MISSING RESIDUES
+REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
+REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
+REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
+REMARK 465
+REMARK 465 M RES C SSSEQI
+REMARK 465 PHE A 305
+REMARK 465 GLN A 306
+REMARK 500
+REMARK 500 GEOMETRY AND STEREOCHEMISTRY
+REMARK 500 SUBTOPIC: TORSION ANGLES
+REMARK 500
+REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
+REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
+REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
+REMARK 500
+REMARK 500 STANDARD TABLE:
+REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
+REMARK 500
+REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
+REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
+REMARK 500
+REMARK 500 M RES CSSEQI PSI PHI
+REMARK 500 ASP A 33 -132.67 57.52
+REMARK 500 ASN A 51 69.76 -154.49
+REMARK 500 ASN A 84 -119.94 56.10
+REMARK 500 TYR A 154 -89.93 58.72
+REMARK 500
+REMARK 500 REMARK: NULL
+REMARK 525
+REMARK 525 SOLVENT
+REMARK 525
+REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
+REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
+REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
+REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
+REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
+REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
+REMARK 525 NUMBER; I=INSERTION CODE):
+REMARK 525
+REMARK 525 M RES CSSEQI
+REMARK 525 HOH A 889 DISTANCE = 6.51 ANGSTROMS
+REMARK 525 HOH A 890 DISTANCE = 6.68 ANGSTROMS
+REMARK 525 HOH A 891 DISTANCE = 7.12 ANGSTROMS
+REMARK 800
+REMARK 800 SITE
+REMARK 800 SITE_IDENTIFIER: AC1
+REMARK 800 EVIDENCE_CODE: SOFTWARE
+REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 401
+REMARK 800
+REMARK 800 SITE_IDENTIFIER: AC2
+REMARK 800 EVIDENCE_CODE: SOFTWARE
+REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402
+REMARK 800
+REMARK 800 SITE_IDENTIFIER: AC3
+REMARK 800 EVIDENCE_CODE: SOFTWARE
+REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403
+REMARK 800
+REMARK 800 SITE_IDENTIFIER: AC4
+REMARK 800 EVIDENCE_CODE: SOFTWARE
+REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 404
+DBREF 6Y84 A 1 306 PDB 6Y84 6Y84 1 306
+SEQRES 1 A 306 SER GLY PHE ARG LYS MET ALA PHE PRO SER GLY LYS VAL
+SEQRES 2 A 306 GLU GLY CYS MET VAL GLN VAL THR CYS GLY THR THR THR
+SEQRES 3 A 306 LEU ASN GLY LEU TRP LEU ASP ASP VAL VAL TYR CYS PRO
+SEQRES 4 A 306 ARG HIS VAL ILE CYS THR SER GLU ASP MET LEU ASN PRO
+SEQRES 5 A 306 ASN TYR GLU ASP LEU LEU ILE ARG LYS SER ASN HIS ASN
+SEQRES 6 A 306 PHE LEU VAL GLN ALA GLY ASN VAL GLN LEU ARG VAL ILE
+SEQRES 7 A 306 GLY HIS SER MET GLN ASN CYS VAL LEU LYS LEU LYS VAL
+SEQRES 8 A 306 ASP THR ALA ASN PRO LYS THR PRO LYS TYR LYS PHE VAL
+SEQRES 9 A 306 ARG ILE GLN PRO GLY GLN THR PHE SER VAL LEU ALA CYS
+SEQRES 10 A 306 TYR ASN GLY SER PRO SER GLY VAL TYR GLN CYS ALA MET
+SEQRES 11 A 306 ARG PRO ASN PHE THR ILE LYS GLY SER PHE LEU ASN GLY
+SEQRES 12 A 306 SER CYS GLY SER VAL GLY PHE ASN ILE ASP TYR ASP CYS
+SEQRES 13 A 306 VAL SER PHE CYS TYR MET HIS HIS MET GLU LEU PRO THR
+SEQRES 14 A 306 GLY VAL HIS ALA GLY THR ASP LEU GLU GLY ASN PHE TYR
+SEQRES 15 A 306 GLY PRO PHE VAL ASP ARG GLN THR ALA GLN ALA ALA GLY
+SEQRES 16 A 306 THR ASP THR THR ILE THR VAL ASN VAL LEU ALA TRP LEU
+SEQRES 17 A 306 TYR ALA ALA VAL ILE ASN GLY ASP ARG TRP PHE LEU ASN
+SEQRES 18 A 306 ARG PHE THR THR THR LEU ASN ASP PHE ASN LEU VAL ALA
+SEQRES 19 A 306 MET LYS TYR ASN TYR GLU PRO LEU THR GLN ASP HIS VAL
+SEQRES 20 A 306 ASP ILE LEU GLY PRO LEU SER ALA GLN THR GLY ILE ALA
+SEQRES 21 A 306 VAL LEU ASP MET CYS ALA SER LEU LYS GLU LEU LEU GLN
+SEQRES 22 A 306 ASN GLY MET ASN GLY ARG THR ILE LEU GLY SER ALA LEU
+SEQRES 23 A 306 LEU GLU ASP GLU PHE THR PRO PHE ASP VAL VAL ARG GLN
+SEQRES 24 A 306 CYS SER GLY VAL THR PHE GLN
+HET DMS A 401 4
+HET DMS A 402 4
+HET DMS A 403 4
+HET DMS A 404 4
+HETNAM DMS DIMETHYL SULFOXIDE
+FORMUL 2 DMS 4(C2 H6 O S)
+FORMUL 6 HOH *391(H2 O)
+HELIX 1 AA1 SER A 10 GLY A 15 1 6
+HELIX 2 AA2 HIS A 41 CYS A 44 5 4
+HELIX 3 AA3 GLU A 47 ASN A 51 5 5
+HELIX 4 AA4 ASN A 53 ARG A 60 1 8
+HELIX 5 AA5 LYS A 61 HIS A 64 5 4
+HELIX 6 AA6 ILE A 200 ASN A 214 1 15
+HELIX 7 AA7 THR A 226 TYR A 237 1 12
+HELIX 8 AA8 THR A 243 LEU A 250 1 8
+HELIX 9 AA9 LEU A 250 GLY A 258 1 9
+HELIX 10 AB1 ALA A 260 GLY A 275 1 16
+HELIX 11 AB2 THR A 292 GLY A 302 1 11
+SHEET 1 AA1 7 VAL A 73 LEU A 75 0
+SHEET 2 AA1 7 PHE A 66 ALA A 70 -1 N VAL A 68 O LEU A 75
+SHEET 3 AA1 7 MET A 17 CYS A 22 -1 N GLN A 19 O GLN A 69
+SHEET 4 AA1 7 THR A 25 LEU A 32 -1 O LEU A 27 N VAL A 20
+SHEET 5 AA1 7 VAL A 35 PRO A 39 -1 O TYR A 37 N LEU A 30
+SHEET 6 AA1 7 VAL A 86 VAL A 91 -1 O LEU A 87 N CYS A 38
+SHEET 7 AA1 7 VAL A 77 GLN A 83 -1 N SER A 81 O LYS A 88
+SHEET 1 AA2 5 LYS A 100 PHE A 103 0
+SHEET 2 AA2 5 CYS A 156 GLU A 166 1 O VAL A 157 N LYS A 100
+SHEET 3 AA2 5 VAL A 148 ASP A 153 -1 N ASN A 151 O SER A 158
+SHEET 4 AA2 5 THR A 111 TYR A 118 -1 N SER A 113 O PHE A 150
+SHEET 5 AA2 5 SER A 121 ALA A 129 -1 O SER A 123 N ALA A 116
+SHEET 1 AA3 3 LYS A 100 PHE A 103 0
+SHEET 2 AA3 3 CYS A 156 GLU A 166 1 O VAL A 157 N LYS A 100
+SHEET 3 AA3 3 HIS A 172 THR A 175 -1 O ALA A 173 N MET A 165
+SITE 1 AC1 8 GLN A 74 LEU A 75 ARG A 76 PHE A 223
+SITE 2 AC1 8 THR A 224 ASP A 263 HOH A 570 HOH A 579
+SITE 1 AC2 2 HIS A 64 ASN A 65
+SITE 1 AC3 6 MET A 6 PHE A 8 SER A 123 GLN A 127
+SITE 2 AC3 6 ASP A 295 ARG A 298
+SITE 1 AC4 5 GLY A 15 MET A 17 LYS A 97 HOH A 620
+SITE 2 AC4 5 HOH A 654
+CRYST1 112.812 52.949 44.631 90.00 103.16 90.00 C 1 2 1 4
+ORIGX1 1.000000 0.000000 0.000000 0.00000
+ORIGX2 0.000000 1.000000 0.000000 0.00000
+ORIGX3 0.000000 0.000000 1.000000 0.00000
+SCALE1 0.008864 0.000000 0.002073 0.00000
+SCALE2 0.000000 0.018886 0.000000 0.00000
+SCALE3 0.000000 0.000000 0.023010 0.00000
+ATOM 1 N ASER A 1 -2.185 4.397 -17.079 0.50 26.55 N
+ANISOU 1 N ASER A 1 3790 3658 2638 -1331 -1030 674 N
+ATOM 2 N BSER A 1 -2.224 4.310 -17.137 0.50 25.36 N
+ANISOU 2 N BSER A 1 3647 3506 2482 -1342 -1039 678 N
+ATOM 3 CA ASER A 1 -2.021 5.695 -16.438 0.50 26.71 C
+ANISOU 3 CA ASER A 1 3697 3711 2741 -1239 -975 694 C
+ATOM 4 CA BSER A 1 -1.882 5.526 -16.417 0.50 25.40 C
+ANISOU 4 CA BSER A 1 3548 3538 2566 -1238 -970 677 C
+ATOM 5 C ASER A 1 -2.350 5.650 -14.945 0.50 25.98 C
+ANISOU 5 C ASER A 1 3512 3620 2738 -1150 -937 712 C
+ATOM 6 C BSER A 1 -2.298 5.476 -14.933 0.50 24.98 C
+ANISOU 6 C BSER A 1 3399 3488 2604 -1153 -938 702 C
+ATOM 7 O ASER A 1 -2.957 4.696 -14.446 0.50 25.86 O
+ANISOU 7 O ASER A 1 3500 3592 2735 -1169 -968 737 O
+ATOM 8 O BSER A 1 -2.988 4.551 -14.492 0.50 24.74 O
+ANISOU 8 O BSER A 1 3368 3447 2586 -1178 -975 736 O
+ATOM 9 CB ASER A 1 -2.819 6.777 -17.164 0.50 28.89 C
+ANISOU 9 CB ASER A 1 3908 4027 3042 -1293 -1027 802 C
+ATOM 10 CB BSER A 1 -2.440 6.757 -17.134 0.50 27.08 C
+ANISOU 10 CB BSER A 1 3697 3791 2803 -1274 -1004 766 C
+ATOM 11 OG ASER A 1 -2.052 7.417 -18.170 0.50 31.95 O
+ANISOU 11 OG ASER A 1 4343 4421 3375 -1310 -1009 760 O
+ATOM 12 OG BSER A 1 -3.797 7.000 -16.801 0.50 29.72 O
+ANISOU 12 OG BSER A 1 3934 4150 3207 -1305 -1062 898 O
+ATOM 13 N AGLY A 2 -1.917 6.679 -14.240 0.50 25.04 N
+ANISOU 13 N AGLY A 2 3321 3515 2678 -1055 -870 696 N
+ATOM 14 N BGLY A 2 -1.852 6.467 -14.178 0.50 24.37 N
+ANISOU 14 N BGLY A 2 3248 3424 2586 -1055 -869 684 N
+ATOM 15 CA AGLY A 2 -2.078 6.745 -12.803 0.50 24.62 C
+ANISOU 15 CA AGLY A 2 3196 3459 2699 -962 -822 700 C
+ATOM 16 CA BGLY A 2 -2.122 6.541 -12.756 0.50 24.27 C
+ANISOU 16 CA BGLY A 2 3159 3411 2651 -967 -827 698 C
+ATOM 17 C AGLY A 2 -0.786 6.340 -12.129 0.50 23.89 C
+ANISOU 17 C AGLY A 2 3152 3338 2586 -888 -752 577 C
+ATOM 18 C BGLY A 2 -0.877 6.134 -12.010 0.50 23.87 C
+ANISOU 18 C BGLY A 2 3152 3333 2584 -889 -756 578 C
+ATOM 19 O AGLY A 2 -0.004 5.553 -12.671 0.50 24.05 O
+ANISOU 19 O AGLY A 2 3266 3335 2538 -916 -748 500 O
+ATOM 20 O BGLY A 2 -0.206 5.169 -12.398 0.50 24.00 O
+ANISOU 20 O BGLY A 2 3260 3323 2536 -917 -755 505 O
+ATOM 21 N PHE A 3 -0.560 6.863 -10.941 1.00 22.93 N
+ANISOU 21 N PHE A 3 2972 3216 2523 -793 -695 563 N
+ATOM 22 CA PHE A 3 0.639 6.585 -10.184 1.00 22.04 C
+ANISOU 22 CA PHE A 3 2893 3080 2403 -721 -633 461 C
+ATOM 23 C PHE A 3 0.290 6.604 -8.729 1.00 21.78 C
+ANISOU 23 C PHE A 3 2801 3044 2431 -646 -601 477 C
+ATOM 24 O PHE A 3 -0.157 7.619 -8.198 1.00 23.62 O
+ANISOU 24 O PHE A 3 2968 3290 2718 -601 -580 527 O
+ATOM 25 CB PHE A 3 1.732 7.609 -10.538 1.00 21.01 C
+ANISOU 25 CB PHE A 3 2768 2952 2263 -688 -591 409 C
+ATOM 26 CG PHE A 3 3.117 7.084 -10.258 1.00 21.05 C
+ANISOU 26 CG PHE A 3 2827 2930 2240 -645 -542 307 C
+ATOM 27 CD1 PHE A 3 3.724 6.190 -11.120 1.00 21.40 C
+ANISOU 27 CD1 PHE A 3 2957 2956 2219 -689 -544 255 C
+ATOM 28 CD2 PHE A 3 3.799 7.464 -9.122 1.00 21.44 C
+ANISOU 28 CD2 PHE A 3 2846 2969 2329 -562 -493 269 C
+ATOM 29 CE1 PHE A 3 4.993 5.696 -10.852 1.00 22.14 C
+ANISOU 29 CE1 PHE A 3 3093 3023 2298 -646 -492 174 C
+ATOM 30 CE2 PHE A 3 5.075 6.985 -8.870 1.00 21.61 C
+ANISOU 30 CE2 PHE A 3 2909 2968 2333 -528 -452 189 C
+ATOM 31 CZ PHE A 3 5.652 6.081 -9.717 1.00 21.71 C
+ANISOU 31 CZ PHE A 3 2995 2964 2291 -566 -449 146 C
+ATOM 32 N ARG A 4 0.443 5.457 -8.087 1.00 19.43 N
+ANISOU 32 N ARG A 4 2533 2727 2124 -633 -595 440 N
+ATOM 33 CA ARG A 4 0.091 5.280 -6.693 1.00 18.12 C
+ANISOU 33 CA ARG A 4 2321 2556 2008 -566 -566 454 C
+ATOM 34 C ARG A 4 1.257 4.818 -5.846 1.00 17.46 C
+ANISOU 34 C ARG A 4 2271 2449 1914 -506 -517 360 C
+ATOM 35 O ARG A 4 2.173 4.183 -6.358 1.00 18.03 O
+ANISOU 35 O ARG A 4 2404 2504 1940 -527 -512 292 O
+ATOM 36 CB ARG A 4 -0.984 4.179 -6.615 1.00 19.34 C
+ANISOU 36 CB ARG A 4 2469 2710 2168 -613 -615 515 C
+ATOM 37 CG ARG A 4 -2.389 4.693 -6.846 1.00 22.46 C
+ANISOU 37 CG ARG A 4 2796 3131 2608 -646 -656 640 C
+ATOM 38 CD ARG A 4 -2.962 5.187 -5.525 1.00 25.30 C
+ANISOU 38 CD ARG A 4 3081 3495 3037 -561 -610 691 C
+ATOM 39 NE ARG A 4 -4.352 5.630 -5.666 1.00 28.96 N
+ANISOU 39 NE ARG A 4 3468 3979 3555 -584 -639 826 N
+ATOM 40 CZ ARG A 4 -5.041 6.254 -4.713 1.00 31.07 C
+ANISOU 40 CZ ARG A 4 3666 4250 3888 -513 -594 896 C
+ATOM 41 NH1 ARG A 4 -4.479 6.508 -3.538 1.00 31.07 N
+ANISOU 41 NH1 ARG A 4 3673 4234 3900 -420 -523 836 N
+ATOM 42 NH2 ARG A 4 -6.295 6.632 -4.932 1.00 28.97 N
+ANISOU 42 NH2 ARG A 4 3326 4003 3678 -535 -618 1030 N
+ATOM 43 N ALYS A 5 1.185 5.069 -4.531 0.50 16.58 N
+ANISOU 43 N ALYS A 5 2120 2334 1844 -433 -480 363 N
+ATOM 44 N BLYS A 5 1.202 5.059 -4.523 0.50 16.76 N
+ANISOU 44 N BLYS A 5 2144 2357 1867 -432 -480 362 N
+ATOM 45 CA ALYS A 5 2.185 4.556 -3.613 0.50 16.63 C
+ANISOU 45 CA ALYS A 5 2153 2320 1845 -381 -442 287 C
+ATOM 46 CA BLYS A 5 2.235 4.584 -3.597 0.50 16.99 C
+ANISOU 46 CA BLYS A 5 2199 2365 1890 -379 -441 285 C
+ATOM 47 C ALYS A 5 1.841 3.080 -3.508 0.50 17.04 C
+ANISOU 47 C ALYS A 5 2227 2362 1884 -413 -467 289 C
+ATOM 48 C BLYS A 5 1.980 3.098 -3.369 0.50 17.63 C
+ANISOU 48 C BLYS A 5 2302 2435 1960 -403 -460 280 C
+ATOM 49 O ALYS A 5 0.747 2.726 -3.077 0.50 17.39 O
+ANISOU 49 O ALYS A 5 2236 2416 1956 -420 -489 356 O
+ATOM 50 O BLYS A 5 1.203 2.711 -2.496 0.50 18.57 O
+ANISOU 50 O BLYS A 5 2387 2557 2110 -380 -461 322 O
+ATOM 51 CB ALYS A 5 2.120 5.253 -2.246 0.50 17.92 C
+ANISOU 51 CB ALYS A 5 2280 2480 2048 -301 -401 295 C
+ATOM 52 CB BLYS A 5 2.196 5.363 -2.273 0.50 18.19 C
+ANISOU 52 CB BLYS A 5 2315 2515 2083 -300 -399 293 C
+ATOM 53 CG ALYS A 5 3.300 4.911 -1.342 0.50 21.29 C
+ANISOU 53 CG ALYS A 5 2735 2887 2467 -254 -368 217 C
+ATOM 54 CG BLYS A 5 3.332 5.005 -1.326 0.50 21.43 C
+ANISOU 54 CG BLYS A 5 2752 2905 2486 -252 -367 218 C
+ATOM 55 CD ALYS A 5 4.637 5.388 -1.894 0.50 24.62 C
+ANISOU 55 CD ALYS A 5 3187 3300 2866 -257 -355 155 C
+ATOM 56 CD BLYS A 5 4.694 5.391 -1.868 0.50 24.70 C
+ANISOU 56 CD BLYS A 5 3199 3310 2877 -255 -354 153 C
+ATOM 57 CE ALYS A 5 4.810 6.884 -1.795 0.50 27.77 C
+ANISOU 57 CE ALYS A 5 3569 3701 3282 -227 -339 162 C
+ATOM 58 CE BLYS A 5 4.925 6.879 -1.800 0.50 27.68 C
+ANISOU 58 CE BLYS A 5 3559 3690 3270 -227 -339 160 C
+ATOM 59 NZ ALYS A 5 4.611 7.386 -0.415 0.50 29.14 N
+ANISOU 59 NZ ALYS A 5 3728 3864 3481 -165 -312 172 N
+ATOM 60 NZ BLYS A 5 4.633 7.433 -0.457 0.50 28.93 N
+ANISOU 60 NZ BLYS A 5 3701 3837 3454 -165 -312 172 N
+ATOM 61 N MET A 6 2.663 2.273 -4.148 1.00 17.01 N
+ANISOU 61 N MET A 6 2284 2341 1838 -444 -468 227 N
+ATOM 62 CA MET A 6 2.427 0.855 -4.239 1.00 17.12 C
+ANISOU 62 CA MET A 6 2335 2339 1832 -482 -492 221 C
+ATOM 63 C MET A 6 3.367 0.015 -3.454 1.00 15.93 C
+ANISOU 63 C MET A 6 2208 2164 1681 -440 -454 155 C
+ATOM 64 O MET A 6 4.570 0.202 -3.547 1.00 16.36 O
+ANISOU 64 O MET A 6 2287 2206 1722 -415 -417 95 O
+ATOM 65 CB MET A 6 2.580 0.517 -5.725 1.00 19.42 C
+ANISOU 65 CB MET A 6 2693 2619 2066 -561 -522 206 C
+ATOM 66 CG MET A 6 2.137 -0.836 -6.077 1.00 24.58 C
+ANISOU 66 CG MET A 6 3399 3251 2691 -619 -558 208 C
+ATOM 67 SD MET A 6 2.195 -0.979 -7.868 1.00 31.98 S
+ANISOU 67 SD MET A 6 4425 4174 3551 -716 -596 200 S
+ATOM 68 CE MET A 6 0.949 0.182 -8.339 1.00 27.76 C
+ANISOU 68 CE MET A 6 3824 3682 3041 -757 -652 303 C
+ATOM 69 N ALA A 7 2.820 -0.956 -2.733 1.00 14.89 N
+ANISOU 69 N ALA A 7 2066 2027 1567 -436 -466 174 N
+ATOM 70 CA ALA A 7 3.639 -1.900 -1.989 1.00 15.29 C
+ANISOU 70 CA ALA A 7 2137 2054 1620 -401 -434 119 C
+ATOM 71 C ALA A 7 3.744 -3.190 -2.803 1.00 15.57 C
+ANISOU 71 C ALA A 7 2240 2060 1616 -459 -451 93 C
+ATOM 72 O ALA A 7 2.963 -3.405 -3.734 1.00 16.04 O
+ANISOU 72 O ALA A 7 2328 2119 1649 -528 -498 128 O
+ATOM 73 CB ALA A 7 3.006 -2.185 -0.630 1.00 15.59 C
+ANISOU 73 CB ALA A 7 2122 2101 1700 -356 -430 154 C
+ATOM 74 N PHE A 8 4.742 -4.010 -2.521 1.00 15.58 N
+ANISOU 74 N PHE A 8 2275 2033 1611 -435 -413 35 N
+ATOM 75 CA PHE A 8 4.868 -5.305 -3.172 1.00 16.87 C
+ANISOU 75 CA PHE A 8 2512 2159 1740 -482 -419 8 C
+ATOM 76 C PHE A 8 3.750 -6.202 -2.661 1.00 16.69 C
+ANISOU 76 C PHE A 8 2471 2136 1735 -506 -463 55 C
+ATOM 77 O PHE A 8 3.298 -6.088 -1.511 1.00 16.04 O
+ANISOU 77 O PHE A 8 2320 2076 1699 -462 -464 90 O
+ATOM 78 CB PHE A 8 6.222 -5.940 -2.834 1.00 17.33 C
+ANISOU 78 CB PHE A 8 2598 2187 1802 -438 -357 -56 C
+ATOM 79 CG PHE A 8 7.358 -5.313 -3.588 1.00 19.06 C
+ANISOU 79 CG PHE A 8 2847 2396 1998 -426 -313 -96 C
+ATOM 80 CD1 PHE A 8 7.607 -5.651 -4.907 1.00 20.90 C
+ANISOU 80 CD1 PHE A 8 3166 2600 2176 -474 -304 -122 C
+ATOM 81 CD2 PHE A 8 8.164 -4.366 -2.990 1.00 20.60 C
+ANISOU 81 CD2 PHE A 8 2990 2610 2225 -369 -282 -105 C
+ATOM 82 CE1 PHE A 8 8.640 -5.049 -5.607 1.00 22.00 C
+ANISOU 82 CE1 PHE A 8 3331 2732 2298 -458 -259 -152 C
+ATOM 83 CE2 PHE A 8 9.209 -3.787 -3.685 1.00 21.94 C
+ANISOU 83 CE2 PHE A 8 3182 2773 2381 -358 -244 -134 C
+ATOM 84 CZ PHE A 8 9.433 -4.123 -4.991 1.00 22.08 C
+ANISOU 84 CZ PHE A 8 3277 2764 2349 -400 -230 -155 C
+ATOM 85 N PRO A 9 3.322 -7.176 -3.489 1.00 17.15 N
+ANISOU 85 N PRO A 9 2598 2165 1755 -577 -500 58 N
+ATOM 86 CA PRO A 9 2.348 -8.173 -3.002 1.00 17.33 C
+ANISOU 86 CA PRO A 9 2606 2180 1797 -604 -544 103 C
+ATOM 87 C PRO A 9 2.939 -8.881 -1.771 1.00 17.30 C
+ANISOU 87 C PRO A 9 2575 2167 1833 -537 -498 72 C
+ATOM 88 O PRO A 9 4.125 -9.203 -1.771 1.00 19.22 O
+ANISOU 88 O PRO A 9 2854 2383 2066 -505 -442 8 O
+ATOM 89 CB PRO A 9 2.198 -9.124 -4.195 1.00 19.02 C
+ANISOU 89 CB PRO A 9 2926 2349 1951 -690 -579 86 C
+ATOM 90 CG PRO A 9 2.667 -8.338 -5.372 1.00 19.72 C
+ANISOU 90 CG PRO A 9 3068 2437 1989 -719 -570 60 C
+ATOM 91 CD PRO A 9 3.768 -7.478 -4.860 1.00 17.41 C
+ANISOU 91 CD PRO A 9 2731 2162 1721 -635 -498 18 C
+ATOM 92 N SER A 10 2.170 -8.982 -0.714 1.00 15.92 N
+ANISOU 92 N SER A 10 2329 2016 1705 -510 -516 125 N
+ATOM 93 CA SER A 10 2.701 -9.448 0.569 1.00 15.16 C
+ANISOU 93 CA SER A 10 2194 1919 1648 -441 -474 103 C
+ATOM 94 C SER A 10 2.612 -10.944 0.842 1.00 15.12 C
+ANISOU 94 C SER A 10 2215 1881 1649 -458 -482 97 C
+ATOM 95 O SER A 10 3.100 -11.378 1.869 1.00 14.73 O
+ANISOU 95 O SER A 10 2135 1831 1632 -404 -448 80 O
+ATOM 96 CB SER A 10 2.029 -8.690 1.705 1.00 15.91 C
+ANISOU 96 CB SER A 10 2200 2056 1788 -388 -475 160 C
+ATOM 97 OG SER A 10 0.623 -8.864 1.658 1.00 17.96 O
+ANISOU 97 OG SER A 10 2428 2330 2066 -426 -530 242 O
+ATOM 98 N GLY A 11 2.001 -11.708 -0.041 1.00 15.29 N
+ANISOU 98 N GLY A 11 2295 1874 1641 -534 -530 111 N
+ATOM 99 CA GLY A 11 1.797 -13.135 0.179 1.00 15.09 C
+ANISOU 99 CA GLY A 11 2298 1812 1622 -558 -546 111 C
+ATOM 100 C GLY A 11 3.008 -13.943 0.596 1.00 14.62 C
+ANISOU 100 C GLY A 11 2268 1718 1570 -512 -480 44 C
+ATOM 101 O GLY A 11 2.943 -14.731 1.548 1.00 15.34 O
+ANISOU 101 O GLY A 11 2323 1805 1699 -483 -473 55 O
+ATOM 102 N LYS A 12 4.126 -13.735 -0.106 1.00 13.99 N
+ANISOU 102 N LYS A 12 2248 1612 1455 -504 -428 -20 N
+ATOM 103 CA LYS A 12 5.345 -14.487 0.193 1.00 14.02 C
+ANISOU 103 CA LYS A 12 2278 1579 1471 -461 -359 -75 C
+ATOM 104 C LYS A 12 5.831 -14.217 1.613 1.00 14.16 C
+ANISOU 104 C LYS A 12 2202 1631 1547 -382 -326 -68 C
+ATOM 105 O LYS A 12 6.375 -15.110 2.261 1.00 14.81 O
+ANISOU 105 O LYS A 12 2276 1691 1658 -351 -292 -82 O
+ATOM 106 CB LYS A 12 6.449 -14.195 -0.821 1.00 15.54 C
+ANISOU 106 CB LYS A 12 2543 1739 1622 -460 -303 -132 C
+ATOM 107 CG LYS A 12 6.209 -14.833 -2.180 1.00 19.84 C
+ANISOU 107 CG LYS A 12 3209 2229 2099 -536 -318 -155 C
+ATOM 108 CD LYS A 12 7.166 -14.268 -3.223 1.00 25.38 C
+ANISOU 108 CD LYS A 12 3976 2910 2756 -533 -264 -200 C
+ATOM 109 CE LYS A 12 6.905 -14.864 -4.589 1.00 30.94 C
+ANISOU 109 CE LYS A 12 4817 3558 3382 -610 -278 -224 C
+ATOM 110 NZ LYS A 12 7.019 -16.342 -4.559 1.00 34.47 N
+ANISOU 110 NZ LYS A 12 5337 3937 3822 -623 -255 -248 N
+ATOM 111 N VAL A 13 5.605 -12.996 2.114 1.00 13.22 N
+ANISOU 111 N VAL A 13 2016 1563 1443 -351 -337 -41 N
+ATOM 112 CA VAL A 13 6.032 -12.646 3.468 1.00 12.21 C
+ANISOU 112 CA VAL A 13 1813 1466 1360 -282 -311 -33 C
+ATOM 113 C VAL A 13 5.000 -13.074 4.500 1.00 11.66 C
+ANISOU 113 C VAL A 13 1687 1420 1324 -272 -345 20 C
+ATOM 114 O VAL A 13 5.364 -13.520 5.588 1.00 11.73 O
+ANISOU 114 O VAL A 13 1657 1433 1367 -227 -324 21 O
+ATOM 115 CB VAL A 13 6.355 -11.145 3.551 1.00 13.09 C
+ANISOU 115 CB VAL A 13 1893 1613 1468 -253 -301 -35 C
+ATOM 116 CG1 VAL A 13 6.822 -10.761 4.950 1.00 14.14 C
+ANISOU 116 CG1 VAL A 13 1965 1771 1637 -189 -280 -28 C
+ATOM 117 CG2 VAL A 13 7.411 -10.784 2.519 1.00 14.34 C
+ANISOU 117 CG2 VAL A 13 2103 1748 1597 -262 -265 -82 C
+ATOM 118 N GLU A 14 3.701 -13.021 4.159 1.00 11.62 N
+ANISOU 118 N GLU A 14 1675 1426 1312 -315 -400 72 N
+ATOM 119 CA GLU A 14 2.641 -13.473 5.068 1.00 11.63 C
+ANISOU 119 CA GLU A 14 1621 1448 1350 -306 -432 135 C
+ATOM 120 C GLU A 14 2.876 -14.916 5.521 1.00 12.71 C
+ANISOU 120 C GLU A 14 1768 1554 1508 -305 -424 123 C
+ATOM 121 O GLU A 14 2.716 -15.224 6.703 1.00 13.03 O
+ANISOU 121 O GLU A 14 1752 1613 1585 -261 -416 149 O
+ATOM 122 CB GLU A 14 1.275 -13.399 4.373 1.00 12.59 C
+ANISOU 122 CB GLU A 14 1742 1577 1464 -368 -496 200 C
+ATOM 123 CG GLU A 14 0.756 -11.988 4.211 1.00 15.46 C
+ANISOU 123 CG GLU A 14 2071 1980 1825 -359 -505 238 C
+ATOM 124 CD GLU A 14 -0.445 -11.950 3.292 1.00 18.75 C
+ANISOU 124 CD GLU A 14 2494 2399 2232 -433 -572 303 C
+ATOM 125 OE1 GLU A 14 -1.417 -12.694 3.553 1.00 21.44 O
+ANISOU 125 OE1 GLU A 14 2807 2738 2599 -459 -616 368 O
+ATOM 126 OE2 GLU A 14 -0.390 -11.204 2.289 1.00 19.65 O
+ANISOU 126 OE2 GLU A 14 2641 2514 2313 -469 -584 294 O
+ATOM 127 N GLY A 15 3.357 -15.745 4.598 1.00 12.90 N
+ANISOU 127 N GLY A 15 1868 1528 1505 -348 -418 79 N
+ATOM 128 CA GLY A 15 3.649 -17.145 4.878 1.00 12.73 C
+ANISOU 128 CA GLY A 15 1869 1467 1502 -351 -405 63 C
+ATOM 129 C GLY A 15 4.818 -17.392 5.810 1.00 12.45 C
+ANISOU 129 C GLY A 15 1802 1431 1499 -284 -343 31 C
+ATOM 130 O GLY A 15 5.068 -18.532 6.200 1.00 13.52 O
+ANISOU 130 O GLY A 15 1941 1536 1659 -278 -328 25 O
+ATOM 131 N CYS A 16 5.547 -16.341 6.161 1.00 11.59 N
+ANISOU 131 N CYS A 16 1662 1350 1391 -239 -310 14 N
+ATOM 132 CA CYS A 16 6.690 -16.411 7.064 1.00 11.47 C
+ANISOU 132 CA CYS A 16 1612 1338 1407 -181 -261 -7 C
+ATOM 133 C CYS A 16 6.412 -15.838 8.439 1.00 11.91 C
+ANISOU 133 C CYS A 16 1592 1443 1489 -133 -270 29 C
+ATOM 134 O CYS A 16 7.299 -15.910 9.283 1.00 12.77 O
+ANISOU 134 O CYS A 16 1672 1557 1622 -92 -239 20 O
+ATOM 135 CB CYS A 16 7.899 -15.722 6.446 1.00 12.44 C
+ANISOU 135 CB CYS A 16 1764 1450 1513 -169 -216 -51 C
+ATOM 136 SG CYS A 16 8.356 -16.342 4.810 1.00 15.98 S
+ANISOU 136 SG CYS A 16 2316 1834 1921 -216 -188 -97 S
+ATOM 137 N MET A 17 5.240 -15.226 8.673 1.00 11.61 N
+ANISOU 137 N MET A 17 1526 1440 1446 -137 -308 74 N
+ATOM 138 CA MET A 17 5.017 -14.567 9.953 1.00 12.03 C
+ANISOU 138 CA MET A 17 1522 1534 1515 -85 -305 105 C
+ATOM 139 C MET A 17 4.535 -15.499 11.022 1.00 12.33 C
+ANISOU 139 C MET A 17 1518 1579 1587 -65 -311 143 C
+ATOM 140 O MET A 17 3.618 -16.266 10.806 1.00 12.97 O
+ANISOU 140 O MET A 17 1596 1653 1680 -94 -341 178 O
+ATOM 141 CB MET A 17 4.077 -13.372 9.816 1.00 12.21 C
+ANISOU 141 CB MET A 17 1531 1588 1521 -85 -326 140 C
+ATOM 142 CG MET A 17 4.535 -12.353 8.787 1.00 13.24 C
+ANISOU 142 CG MET A 17 1697 1714 1618 -104 -321 106 C
+ATOM 143 SD MET A 17 6.217 -11.703 9.005 1.00 14.39 S
+ANISOU 143 SD MET A 17 1856 1854 1757 -71 -278 48 S
+ATOM 144 CE MET A 17 6.158 -11.181 10.754 1.00 15.96 C
+ANISOU 144 CE MET A 17 2009 2086 1971 -10 -269 74 C
+ATOM 145 N VAL A 18 5.186 -15.438 12.176 1.00 11.86 N
+ANISOU 145 N VAL A 18 1429 1536 1543 -18 -287 140 N
+ATOM 146 CA VAL A 18 4.849 -16.234 13.343 1.00 12.74 C
+ANISOU 146 CA VAL A 18 1498 1659 1684 9 -289 176 C
+ATOM 147 C VAL A 18 4.775 -15.312 14.559 1.00 12.62 C
+ANISOU 147 C VAL A 18 1456 1680 1660 60 -278 197 C
+ATOM 148 O VAL A 18 5.220 -14.160 14.518 1.00 12.38 O
+ANISOU 148 O VAL A 18 1443 1657 1602 72 -267 174 O
+ATOM 149 CB VAL A 18 5.882 -17.373 13.576 1.00 13.97 C
+ANISOU 149 CB VAL A 18 1652 1787 1868 11 -267 150 C
+ATOM 150 CG1 VAL A 18 5.917 -18.341 12.404 1.00 14.87 C
+ANISOU 150 CG1 VAL A 18 1808 1855 1986 -36 -270 128 C
+ATOM 151 CG2 VAL A 18 7.262 -16.802 13.868 1.00 13.93 C
+ANISOU 151 CG2 VAL A 18 1651 1782 1858 34 -238 115 C
+ATOM 152 N GLN A 19 4.185 -15.818 15.633 1.00 12.65 N
+ANISOU 152 N GLN A 19 1422 1701 1683 88 -280 241 N
+ATOM 153 CA GLN A 19 4.107 -15.113 16.896 1.00 13.10 C
+ANISOU 153 CA GLN A 19 1465 1786 1726 138 -264 262 C
+ATOM 154 C GLN A 19 5.221 -15.641 17.802 1.00 12.93 C
+ANISOU 154 C GLN A 19 1436 1763 1715 154 -252 242 C
+ATOM 155 O GLN A 19 5.433 -16.850 17.868 1.00 12.86 O
+ANISOU 155 O GLN A 19 1405 1740 1740 142 -255 247 O
+ATOM 156 CB GLN A 19 2.735 -15.376 17.520 1.00 14.90 C
+ANISOU 156 CB GLN A 19 1656 2034 1970 161 -268 332 C
+ATOM 157 CG GLN A 19 2.552 -14.741 18.881 1.00 18.61 C
+ANISOU 157 CG GLN A 19 2122 2528 2420 218 -243 357 C
+ATOM 158 CD GLN A 19 1.293 -15.237 19.530 1.00 24.25 C
+ANISOU 158 CD GLN A 19 2795 3260 3160 245 -240 433 C
+ATOM 159 OE1 GLN A 19 1.285 -16.257 20.224 1.00 26.10 O
+ANISOU 159 OE1 GLN A 19 2999 3499 3420 254 -242 455 O
+ATOM 160 NE2 GLN A 19 0.206 -14.527 19.326 1.00 25.55 N
+ANISOU 160 NE2 GLN A 19 2951 3434 3321 261 -232 481 N
+ATOM 161 N VAL A 20 5.940 -14.742 18.500 1.00 12.43 N
+ANISOU 161 N VAL A 20 1391 1710 1624 177 -242 225 N
+ATOM 162 CA VAL A 20 6.962 -15.171 19.450 1.00 13.22 C
+ANISOU 162 CA VAL A 20 1480 1811 1733 187 -239 219 C
+ATOM 163 C VAL A 20 6.631 -14.580 20.807 1.00 13.82 C
+ANISOU 163 C VAL A 20 1564 1910 1775 226 -234 245 C
+ATOM 164 O VAL A 20 6.435 -13.367 20.921 1.00 14.21 O
+ANISOU 164 O VAL A 20 1651 1964 1783 241 -228 238 O
+ATOM 165 CB VAL A 20 8.405 -14.806 19.036 1.00 13.47 C
+ANISOU 165 CB VAL A 20 1530 1826 1763 167 -238 177 C
+ATOM 166 CG1 VAL A 20 9.408 -15.330 20.066 1.00 14.22 C
+ANISOU 166 CG1 VAL A 20 1603 1924 1876 173 -241 188 C
+ATOM 167 CG2 VAL A 20 8.731 -15.348 17.650 1.00 13.91 C
+ANISOU 167 CG2 VAL A 20 1588 1853 1843 134 -231 150 C
+ATOM 168 N THR A 21 6.537 -15.429 21.823 1.00 14.34 N
+ANISOU 168 N THR A 21 1601 1987 1858 244 -234 277 N
+ATOM 169 CA THR A 21 6.264 -14.970 23.174 1.00 15.62 C
+ANISOU 169 CA THR A 21 1782 2169 1984 281 -225 302 C
+ATOM 170 C THR A 21 7.382 -15.417 24.085 1.00 16.58 C
+ANISOU 170 C THR A 21 1897 2293 2108 274 -239 300 C
+ATOM 171 O THR A 21 7.797 -16.567 24.035 1.00 16.63 O
+ANISOU 171 O THR A 21 1860 2296 2163 258 -245 309 O
+ATOM 172 CB THR A 21 4.920 -15.534 23.681 1.00 18.06 C
+ANISOU 172 CB THR A 21 2060 2495 2307 314 -211 358 C
+ATOM 173 OG1 THR A 21 3.855 -15.130 22.823 1.00 19.40 O
+ANISOU 173 OG1 THR A 21 2226 2663 2481 316 -204 375 O
+ATOM 174 CG2 THR A 21 4.614 -15.109 25.110 1.00 19.50 C
+ANISOU 174 CG2 THR A 21 2269 2694 2447 358 -192 387 C
+ATOM 175 N CYS A 22 7.882 -14.511 24.909 1.00 17.62 N
+ANISOU 175 N CYS A 22 2077 2429 2189 281 -245 292 N
+ATOM 176 CA CYS A 22 8.866 -14.862 25.915 1.00 19.68 C
+ANISOU 176 CA CYS A 22 2335 2695 2447 270 -266 302 C
+ATOM 177 C CYS A 22 8.353 -14.192 27.181 1.00 22.21 C
+ANISOU 177 C CYS A 22 2710 3026 2700 302 -258 320 C
+ATOM 178 O CYS A 22 8.185 -12.976 27.221 1.00 22.29 O
+ANISOU 178 O CYS A 22 2785 3027 2655 312 -250 301 O
+ATOM 179 CB CYS A 22 10.273 -14.403 25.535 1.00 19.81 C
+ANISOU 179 CB CYS A 22 2364 2697 2468 230 -292 274 C
+ATOM 180 SG CYS A 22 11.574 -15.049 26.614 1.00 26.04 S
+ANISOU 180 SG CYS A 22 3129 3491 3273 205 -326 304 S
+ATOM 181 N GLY A 23 7.977 -15.014 28.151 1.00 24.20 N
+ANISOU 181 N GLY A 23 2938 3296 2959 323 -252 360 N
+ATOM 182 CA GLY A 23 7.401 -14.541 29.403 1.00 25.86 C
+ANISOU 182 CA GLY A 23 3204 3516 3105 360 -235 383 C
+ATOM 183 C GLY A 23 6.078 -13.859 29.141 1.00 27.25 C
+ANISOU 183 C GLY A 23 3405 3689 3258 405 -191 393 C
+ATOM 184 O GLY A 23 5.164 -14.465 28.577 1.00 28.42 O
+ANISOU 184 O GLY A 23 3496 3845 3455 421 -173 419 O
+ATOM 185 N THR A 24 6.013 -12.564 29.424 1.00 27.33 N
+ANISOU 185 N THR A 24 3500 3684 3199 420 -176 372 N
+ATOM 186 CA THR A 24 4.800 -11.787 29.185 1.00 27.90 C
+ANISOU 186 CA THR A 24 3600 3750 3251 468 -126 387 C
+ATOM 187 C THR A 24 4.849 -10.946 27.898 1.00 26.48 C
+ANISOU 187 C THR A 24 3425 3554 3082 448 -129 352 C
+ATOM 188 O THR A 24 3.899 -10.223 27.618 1.00 27.56 O
+ANISOU 188 O THR A 24 3580 3683 3207 484 -90 367 O
+ATOM 189 CB THR A 24 4.514 -10.899 30.395 1.00 31.42 C
+ANISOU 189 CB THR A 24 4144 4183 3611 508 -92 394 C
+ATOM 190 OG1 THR A 24 5.534 -9.903 30.499 1.00 33.89 O
+ANISOU 190 OG1 THR A 24 4539 4472 3867 473 -122 343 O
+ATOM 191 CG2 THR A 24 4.440 -11.691 31.681 1.00 32.45 C
+ANISOU 191 CG2 THR A 24 4277 4329 3722 528 -86 431 C
+ATOM 192 N THR A 25 5.938 -11.023 27.128 1.00 24.11 N
+ANISOU 192 N THR A 25 3104 3248 2808 395 -172 312 N
+ATOM 193 CA THR A 25 6.082 -10.214 25.922 1.00 22.53 C
+ANISOU 193 CA THR A 25 2916 3033 2612 375 -177 277 C
+ATOM 194 C THR A 25 5.755 -11.009 24.671 1.00 21.00 C
+ANISOU 194 C THR A 25 2647 2846 2487 354 -183 281 C
+ATOM 195 O THR A 25 6.304 -12.083 24.490 1.00 21.49 O
+ANISOU 195 O THR A 25 2662 2913 2590 329 -204 281 O
+ATOM 196 CB THR A 25 7.503 -9.662 25.850 1.00 23.52 C
+ANISOU 196 CB THR A 25 3080 3144 2715 330 -217 233 C
+ATOM 197 OG1 THR A 25 7.752 -8.858 27.011 1.00 24.80 O
+ANISOU 197 OG1 THR A 25 3325 3293 2804 341 -218 229 O
+ATOM 198 CG2 THR A 25 7.756 -8.862 24.584 1.00 23.98 C
+ANISOU 198 CG2 THR A 25 3143 3188 2782 307 -223 198 C
+ATOM 199 N THR A 26 4.880 -10.486 23.817 1.00 19.91 N
+ANISOU 199 N THR A 26 2504 2704 2356 365 -163 289 N
+ATOM 200 CA THR A 26 4.539 -11.124 22.554 1.00 19.02 C
+ANISOU 200 CA THR A 26 2337 2594 2297 337 -176 293 C
+ATOM 201 C THR A 26 4.814 -10.164 21.401 1.00 17.49 C
+ANISOU 201 C THR A 26 2166 2386 2093 312 -182 256 C
+ATOM 202 O THR A 26 4.376 -9.013 21.413 1.00 18.04 O
+ANISOU 202 O THR A 26 2275 2450 2130 334 -162 257 O
+ATOM 203 CB THR A 26 3.074 -11.584 22.541 1.00 20.95 C
+ANISOU 203 CB THR A 26 2539 2850 2569 365 -155 355 C
+ATOM 204 OG1 THR A 26 2.900 -12.636 23.488 1.00 22.53 O
+ANISOU 204 OG1 THR A 26 2709 3065 2788 383 -153 390 O
+ATOM 205 CG2 THR A 26 2.634 -12.069 21.182 1.00 21.72 C
+ANISOU 205 CG2 THR A 26 2595 2945 2711 327 -176 361 C
+ATOM 206 N LEU A 27 5.539 -10.637 20.411 1.00 15.55 N
+ANISOU 206 N LEU A 27 1900 2133 1877 268 -206 225 N
+ATOM 207 CA LEU A 27 5.787 -9.858 19.200 1.00 14.34 C
+ANISOU 207 CA LEU A 27 1763 1967 1717 241 -212 193 C
+ATOM 208 C LEU A 27 5.841 -10.794 17.990 1.00 13.54 C
+ANISOU 208 C LEU A 27 1629 1858 1657 201 -227 183 C
+ATOM 209 O LEU A 27 5.400 -11.943 18.087 1.00 13.86 O
+ANISOU 209 O LEU A 27 1637 1902 1728 199 -230 208 O
+ATOM 210 CB LEU A 27 7.007 -8.909 19.344 1.00 13.99 C
+ANISOU 210 CB LEU A 27 1762 1911 1642 230 -222 151 C
+ATOM 211 CG LEU A 27 8.263 -9.503 19.968 1.00 14.11 C
+ANISOU 211 CG LEU A 27 1771 1923 1666 215 -240 137 C
+ATOM 212 CD1 LEU A 27 8.801 -10.671 19.161 1.00 14.29 C
+ANISOU 212 CD1 LEU A 27 1749 1939 1740 186 -246 130 C
+ATOM 213 CD2 LEU A 27 9.349 -8.450 20.127 1.00 14.70 C
+ANISOU 213 CD2 LEU A 27 1888 1986 1711 199 -258 109 C
+ATOM 214 N ASN A 28 6.313 -10.302 16.845 1.00 12.24 N
+ANISOU 214 N ASN A 28 1481 1682 1488 171 -233 150 N
+ATOM 215 CA ASN A 28 6.346 -11.091 15.631 1.00 11.92 C
+ANISOU 215 CA ASN A 28 1428 1628 1474 132 -242 138 C
+ATOM 216 C ASN A 28 7.714 -11.653 15.355 1.00 11.52 C
+ANISOU 216 C ASN A 28 1380 1558 1440 112 -240 101 C
+ATOM 217 O ASN A 28 8.725 -11.066 15.710 1.00 11.85 O
+ANISOU 217 O ASN A 28 1433 1598 1471 117 -238 82 O
+ATOM 218 CB ASN A 28 5.884 -10.259 14.427 1.00 13.05 C
+ANISOU 218 CB ASN A 28 1590 1768 1601 110 -247 131 C
+ATOM 219 CG ASN A 28 4.569 -9.595 14.702 1.00 15.18 C
+ANISOU 219 CG ASN A 28 1851 2055 1862 134 -244 178 C
+ATOM 220 OD1 ASN A 28 3.512 -10.223 14.621 1.00 15.52 O
+ANISOU 220 OD1 ASN A 28 1866 2104 1926 130 -252 224 O
+ATOM 221 ND2 ASN A 28 4.620 -8.331 15.068 1.00 15.66 N
+ANISOU 221 ND2 ASN A 28 1936 2120 1895 160 -230 173 N
+ATOM 222 N GLY A 29 7.713 -12.775 14.686 1.00 11.02 N
+ANISOU 222 N GLY A 29 1306 1477 1402 88 -239 97 N
+ATOM 223 CA GLY A 29 8.925 -13.411 14.219 1.00 11.06 C
+ANISOU 223 CA GLY A 29 1316 1457 1430 71 -224 68 C
+ATOM 224 C GLY A 29 8.812 -13.718 12.738 1.00 11.20 C
+ANISOU 224 C GLY A 29 1363 1448 1445 35 -219 46 C
+ATOM 225 O GLY A 29 7.714 -13.803 12.179 1.00 11.95 O
+ANISOU 225 O GLY A 29 1468 1545 1528 15 -237 59 O
+ATOM 226 N LEU A 30 9.956 -13.877 12.090 1.00 10.90 N
+ANISOU 226 N LEU A 30 1341 1384 1416 24 -195 16 N
+ATOM 227 CA LEU A 30 10.046 -14.190 10.667 1.00 10.82 C
+ANISOU 227 CA LEU A 30 1373 1342 1396 -8 -180 -11 C
+ATOM 228 C LEU A 30 10.616 -15.606 10.560 1.00 10.79 C
+ANISOU 228 C LEU A 30 1373 1300 1426 -11 -150 -17 C
+ATOM 229 O LEU A 30 11.740 -15.840 11.002 1.00 11.77 O
+ANISOU 229 O LEU A 30 1475 1416 1582 10 -121 -15 O
+ATOM 230 CB LEU A 30 10.994 -13.195 9.995 1.00 10.42 C
+ANISOU 230 CB LEU A 30 1341 1286 1331 -10 -162 -37 C
+ATOM 231 CG LEU A 30 11.086 -13.328 8.477 1.00 11.21 C
+ANISOU 231 CG LEU A 30 1495 1355 1410 -42 -143 -65 C
+ATOM 232 CD1 LEU A 30 9.784 -12.894 7.816 1.00 12.16 C
+ANISOU 232 CD1 LEU A 30 1640 1487 1493 -73 -180 -60 C
+ATOM 233 CD2 LEU A 30 12.245 -12.507 7.952 1.00 12.12 C
+ANISOU 233 CD2 LEU A 30 1619 1464 1524 -34 -116 -84 C
+ATOM 234 N TRP A 31 9.866 -16.535 9.979 1.00 10.46 N
+ANISOU 234 N TRP A 31 1360 1233 1380 -39 -156 -18 N
+ATOM 235 CA TRP A 31 10.255 -17.943 9.908 1.00 10.74 C
+ANISOU 235 CA TRP A 31 1406 1227 1448 -42 -127 -22 C
+ATOM 236 C TRP A 31 10.711 -18.287 8.502 1.00 11.18 C
+ANISOU 236 C TRP A 31 1535 1230 1484 -69 -91 -60 C
+ATOM 237 O TRP A 31 9.923 -18.273 7.553 1.00 11.15 O
+ANISOU 237 O TRP A 31 1585 1212 1440 -111 -114 -72 O
+ATOM 238 CB TRP A 31 9.054 -18.777 10.353 1.00 11.08 C
+ANISOU 238 CB TRP A 31 1435 1275 1500 -56 -164 7 C
+ATOM 239 CG TRP A 31 9.218 -20.262 10.334 1.00 11.19 C
+ANISOU 239 CG TRP A 31 1463 1244 1545 -63 -142 6 C
+ATOM 240 CD1 TRP A 31 10.371 -20.974 10.511 1.00 11.87 C
+ANISOU 240 CD1 TRP A 31 1544 1298 1669 -40 -90 -3 C
+ATOM 241 CD2 TRP A 31 8.153 -21.221 10.295 1.00 11.18 C
+ANISOU 241 CD2 TRP A 31 1473 1227 1548 -93 -176 27 C
+ATOM 242 NE1 TRP A 31 10.090 -22.323 10.513 1.00 11.94 N
+ANISOU 242 NE1 TRP A 31 1567 1268 1702 -52 -83 3 N
+ATOM 243 CE2 TRP A 31 8.734 -22.499 10.412 1.00 11.98 C
+ANISOU 243 CE2 TRP A 31 1583 1284 1687 -86 -139 21 C
+ATOM 244 CE3 TRP A 31 6.763 -21.123 10.121 1.00 11.96 C
+ANISOU 244 CE3 TRP A 31 1574 1343 1627 -126 -234 56 C
+ATOM 245 CZ2 TRP A 31 7.976 -23.673 10.353 1.00 12.16 C
+ANISOU 245 CZ2 TRP A 31 1623 1274 1721 -115 -162 35 C
+ATOM 246 CZ3 TRP A 31 6.013 -22.284 10.075 1.00 12.27 C
+ANISOU 246 CZ3 TRP A 31 1626 1355 1682 -157 -261 78 C
+ATOM 247 CH2 TRP A 31 6.621 -23.544 10.169 1.00 12.25 C
+ANISOU 247 CH2 TRP A 31 1640 1305 1711 -153 -226 63 C
+ATOM 248 N LEU A 32 12.025 -18.505 8.356 1.00 11.11 N
+ANISOU 248 N LEU A 32 1528 1193 1501 -46 -33 -72 N
+ATOM 249 CA LEU A 32 12.646 -18.808 7.060 1.00 12.05 C
+ANISOU 249 CA LEU A 32 1720 1257 1602 -59 20 -106 C
+ATOM 250 C LEU A 32 13.464 -20.041 7.259 1.00 12.52 C
+ANISOU 250 C LEU A 32 1779 1269 1710 -36 80 -101 C
+ATOM 251 O LEU A 32 14.277 -20.097 8.192 1.00 12.39 O
+ANISOU 251 O LEU A 32 1695 1268 1746 1 99 -72 O
+ATOM 252 CB LEU A 32 13.563 -17.678 6.627 1.00 12.45 C
+ANISOU 252 CB LEU A 32 1767 1319 1644 -44 45 -115 C
+ATOM 253 CG LEU A 32 12.892 -16.342 6.393 1.00 13.71 C
+ANISOU 253 CG LEU A 32 1925 1523 1759 -62 -6 -120 C
+ATOM 254 CD1 LEU A 32 13.907 -15.285 6.173 1.00 13.62 C
+ANISOU 254 CD1 LEU A 32 1900 1524 1752 -43 18 -122 C
+ATOM 255 CD2 LEU A 32 11.959 -16.400 5.210 1.00 14.51 C
+ANISOU 255 CD2 LEU A 32 2102 1605 1805 -111 -28 -142 C
+ATOM 256 N ASP A 33 13.193 -21.093 6.468 1.00 12.93 N
+ANISOU 256 N ASP A 33 1908 1261 1746 -61 105 -124 N
+ATOM 257 CA ASP A 33 13.854 -22.381 6.675 1.00 13.70 C
+ANISOU 257 CA ASP A 33 2009 1304 1891 -38 166 -117 C
+ATOM 258 C ASP A 33 13.561 -22.852 8.132 1.00 13.91 C
+ANISOU 258 C ASP A 33 1946 1369 1970 -19 130 -76 C
+ATOM 259 O ASP A 33 12.412 -22.706 8.557 1.00 14.60 O
+ANISOU 259 O ASP A 33 2016 1493 2037 -42 60 -65 O
+ATOM 260 CB ASP A 33 15.356 -22.306 6.311 1.00 16.27 C
+ANISOU 260 CB ASP A 33 2335 1598 2250 3 255 -115 C
+ATOM 261 CG ASP A 33 15.597 -21.887 4.883 1.00 21.63 C
+ANISOU 261 CG ASP A 33 3105 2238 2874 -13 295 -153 C
+ATOM 262 OD1 ASP A 33 14.817 -22.304 4.008 1.00 23.84 O
+ANISOU 262 OD1 ASP A 33 3480 2480 3097 -56 283 -188 O
+ATOM 263 OD2 ASP A 33 16.574 -21.142 4.642 1.00 23.06 O
+ANISOU 263 OD2 ASP A 33 3265 2427 3068 15 337 -145 O
+ATOM 264 N ASP A 34 14.549 -23.299 8.901 1.00 12.95 N
+ANISOU 264 N ASP A 34 1764 1244 1914 22 173 -46 N
+ATOM 265 CA ASP A 34 14.306 -23.727 10.265 1.00 12.62 C
+ANISOU 265 CA ASP A 34 1641 1238 1917 38 139 -5 C
+ATOM 266 C ASP A 34 14.745 -22.702 11.278 1.00 12.42 C
+ANISOU 266 C ASP A 34 1535 1277 1907 61 110 26 C
+ATOM 267 O ASP A 34 15.104 -23.073 12.395 1.00 13.06 O
+ANISOU 267 O ASP A 34 1547 1379 2036 83 105 66 O
+ATOM 268 CB ASP A 34 14.988 -25.077 10.522 1.00 13.51 C
+ANISOU 268 CB ASP A 34 1742 1298 2092 61 201 14 C
+ATOM 269 CG ASP A 34 16.497 -25.078 10.331 1.00 17.85 C
+ANISOU 269 CG ASP A 34 2272 1819 2691 99 282 33 C
+ATOM 270 OD1 ASP A 34 17.037 -24.076 9.798 1.00 17.68 O
+ANISOU 270 OD1 ASP A 34 2261 1809 2648 103 295 23 O
+ATOM 271 OD2 ASP A 34 17.138 -26.087 10.709 1.00 20.21 O
+ANISOU 271 OD2 ASP A 34 2542 2083 3054 125 334 63 O
+ATOM 272 N VAL A 35 14.689 -21.404 10.928 1.00 11.43 N
+ANISOU 272 N VAL A 35 1421 1184 1739 53 84 10 N
+ATOM 273 CA VAL A 35 15.074 -20.358 11.868 1.00 12.04 C
+ANISOU 273 CA VAL A 35 1436 1316 1821 69 51 37 C
+ATOM 274 C VAL A 35 13.987 -19.307 11.950 1.00 11.65 C
+ANISOU 274 C VAL A 35 1399 1313 1715 51 -11 23 C
+ATOM 275 O VAL A 35 13.400 -18.939 10.930 1.00 12.01 O
+ANISOU 275 O VAL A 35 1499 1347 1716 27 -17 -8 O
+ATOM 276 CB VAL A 35 16.424 -19.702 11.481 1.00 13.42 C
+ANISOU 276 CB VAL A 35 1601 1481 2015 84 91 44 C
+ATOM 277 CG1 VAL A 35 16.824 -18.604 12.473 1.00 13.93 C
+ANISOU 277 CG1 VAL A 35 1611 1599 2082 91 45 72 C
+ATOM 278 CG2 VAL A 35 17.519 -20.750 11.384 1.00 14.17 C
+ANISOU 278 CG2 VAL A 35 1679 1529 2177 107 163 69 C
+ATOM 279 N VAL A 36 13.699 -18.861 13.164 1.00 11.24 N
+ANISOU 279 N VAL A 36 1299 1308 1664 64 -53 50 N
+ATOM 280 CA VAL A 36 12.775 -17.774 13.408 1.00 11.41 C
+ANISOU 280 CA VAL A 36 1327 1371 1637 58 -101 46 C
+ATOM 281 C VAL A 36 13.589 -16.584 13.895 1.00 11.05 C
+ANISOU 281 C VAL A 36 1263 1352 1584 70 -112 53 C
+ATOM 282 O VAL A 36 14.339 -16.704 14.855 1.00 10.78 O
+ANISOU 282 O VAL A 36 1188 1327 1579 84 -115 82 O
+ATOM 283 CB VAL A 36 11.676 -18.169 14.404 1.00 12.20 C
+ANISOU 283 CB VAL A 36 1401 1500 1736 65 -136 73 C
+ATOM 284 CG1 VAL A 36 10.833 -16.957 14.781 1.00 12.52 C
+ANISOU 284 CG1 VAL A 36 1445 1580 1732 70 -172 78 C
+ATOM 285 CG2 VAL A 36 10.810 -19.281 13.826 1.00 12.70 C
+ANISOU 285 CG2 VAL A 36 1485 1535 1807 45 -135 70 C
+ATOM 286 N TYR A 37 13.465 -15.444 13.220 1.00 11.02 N
+ANISOU 286 N TYR A 37 1289 1355 1541 60 -122 30 N
+ATOM 287 CA TYR A 37 14.205 -14.229 13.566 1.00 10.75 C
+ANISOU 287 CA TYR A 37 1248 1341 1497 65 -137 34 C
+ATOM 288 C TYR A 37 13.256 -13.286 14.257 1.00 11.13 C
+ANISOU 288 C TYR A 37 1305 1425 1501 71 -177 37 C
+ATOM 289 O TYR A 37 12.130 -13.095 13.787 1.00 11.97 O
+ANISOU 289 O TYR A 37 1433 1537 1579 64 -186 27 O
+ATOM 290 CB TYR A 37 14.693 -13.529 12.285 1.00 10.59 C
+ANISOU 290 CB TYR A 37 1259 1303 1462 52 -117 8 C
+ATOM 291 CG TYR A 37 15.597 -14.400 11.453 1.00 11.51 C
+ANISOU 291 CG TYR A 37 1381 1378 1616 52 -62 5 C
+ATOM 292 CD1 TYR A 37 15.076 -15.318 10.558 1.00 12.49 C
+ANISOU 292 CD1 TYR A 37 1543 1469 1734 41 -34 -17 C
+ATOM 293 CD2 TYR A 37 16.974 -14.306 11.565 1.00 12.68 C
+ANISOU 293 CD2 TYR A 37 1499 1515 1806 63 -38 29 C
+ATOM 294 CE1 TYR A 37 15.904 -16.163 9.830 1.00 13.67 C
+ANISOU 294 CE1 TYR A 37 1709 1572 1914 46 27 -21 C
+ATOM 295 CE2 TYR A 37 17.814 -15.115 10.809 1.00 13.61 C
+ANISOU 295 CE2 TYR A 37 1620 1589 1962 72 26 34 C
+ATOM 296 CZ TYR A 37 17.275 -16.032 9.932 1.00 14.78 C
+ANISOU 296 CZ TYR A 37 1816 1701 2098 66 62 5 C
+ATOM 297 OH TYR A 37 18.101 -16.885 9.229 1.00 17.25 O
+ANISOU 297 OH TYR A 37 2143 1962 2448 79 135 10 O
+ATOM 298 N CYS A 38 13.677 -12.713 15.375 1.00 10.69 N
+ANISOU 298 N CYS A 38 1233 1388 1439 81 -201 56 N
+ATOM 299 CA CYS A 38 12.825 -11.757 16.071 1.00 10.98 C
+ANISOU 299 CA CYS A 38 1292 1452 1430 92 -229 58 C
+ATOM 300 C CYS A 38 13.672 -10.755 16.841 1.00 11.25 C
+ANISOU 300 C CYS A 38 1335 1493 1447 91 -254 65 C
+ATOM 301 O CYS A 38 14.846 -11.012 17.094 1.00 11.69 O
+ANISOU 301 O CYS A 38 1367 1541 1535 81 -258 82 O
+ATOM 302 CB CYS A 38 11.815 -12.484 16.958 1.00 11.60 C
+ANISOU 302 CB CYS A 38 1355 1545 1507 110 -234 81 C
+ATOM 303 SG CYS A 38 12.515 -13.143 18.487 1.00 13.48 S
+ANISOU 303 SG CYS A 38 1562 1794 1768 121 -247 115 S
+ATOM 304 N PRO A 39 13.111 -9.604 17.244 1.00 10.96 N
+ANISOU 304 N PRO A 39 1337 1469 1360 98 -274 58 N
+ATOM 305 CA PRO A 39 13.899 -8.651 18.033 1.00 10.74 C
+ANISOU 305 CA PRO A 39 1342 1442 1298 92 -309 63 C
+ATOM 306 C PRO A 39 14.331 -9.281 19.350 1.00 11.52 C
+ANISOU 306 C PRO A 39 1415 1548 1415 92 -323 95 C
+ATOM 307 O PRO A 39 13.544 -9.987 19.992 1.00 12.03 O
+ANISOU 307 O PRO A 39 1469 1622 1478 111 -313 107 O
+ATOM 308 CB PRO A 39 12.903 -7.512 18.282 1.00 11.14 C
+ANISOU 308 CB PRO A 39 1438 1499 1296 112 -305 50 C
+ATOM 309 CG PRO A 39 11.956 -7.602 17.126 1.00 11.48 C
+ANISOU 309 CG PRO A 39 1467 1541 1352 113 -279 37 C
+ATOM 310 CD PRO A 39 11.753 -9.084 16.998 1.00 10.66 C
+ANISOU 310 CD PRO A 39 1321 1439 1290 113 -265 50 C
+ATOM 311 N ARG A 40 15.581 -9.024 19.762 1.00 11.03 N
+ANISOU 311 N ARG A 40 1347 1480 1365 68 -353 114 N
+ATOM 312 CA ARG A 40 16.049 -9.593 21.020 1.00 11.30 C
+ANISOU 312 CA ARG A 40 1363 1522 1409 61 -378 151 C
+ATOM 313 C ARG A 40 15.284 -9.013 22.218 1.00 12.95 C
+ANISOU 313 C ARG A 40 1631 1740 1549 73 -400 150 C
+ATOM 314 O ARG A 40 15.228 -9.680 23.250 1.00 13.60 O
+ANISOU 314 O ARG A 40 1704 1833 1629 78 -407 175 O
+ATOM 315 CB ARG A 40 17.549 -9.444 21.184 1.00 11.64 C
+ANISOU 315 CB ARG A 40 1380 1555 1486 25 -411 184 C
+ATOM 316 CG ARG A 40 17.977 -8.012 21.332 1.00 12.88 C
+ANISOU 316 CG ARG A 40 1592 1704 1596 1 -455 177 C
+ATOM 317 CD ARG A 40 19.457 -7.968 21.572 1.00 13.12 C
+ANISOU 317 CD ARG A 40 1588 1727 1669 -40 -497 227 C
+ATOM 318 NE ARG A 40 19.935 -6.599 21.666 1.00 14.21 N
+ANISOU 318 NE ARG A 40 1780 1853 1766 -69 -543 221 N
+ATOM 319 CZ ARG A 40 21.174 -6.261 21.996 1.00 15.68 C
+ANISOU 319 CZ ARG A 40 1952 2032 1976 -113 -597 268 C
+ATOM 320 NH1 ARG A 40 22.082 -7.197 22.248 1.00 15.22 N
+ANISOU 320 NH1 ARG A 40 1822 1977 1982 -129 -605 328 N
+ATOM 321 NH2 ARG A 40 21.519 -4.983 22.070 1.00 15.20 N
+ANISOU 321 NH2 ARG A 40 1947 1956 1873 -143 -643 261 N
+ATOM 322 N HIS A 41 14.628 -7.836 22.073 1.00 13.07 N
+ANISOU 322 N HIS A 41 1708 1750 1508 84 -397 121 N
+ATOM 323 CA HIS A 41 13.892 -7.269 23.196 1.00 13.76 C
+ANISOU 323 CA HIS A 41 1863 1838 1525 106 -399 119 C
+ATOM 324 C HIS A 41 12.612 -8.048 23.529 1.00 14.57 C
+ANISOU 324 C HIS A 41 1951 1958 1627 149 -359 129 C
+ATOM 325 O HIS A 41 11.970 -7.700 24.519 1.00 14.99 O
+ANISOU 325 O HIS A 41 2054 2012 1629 172 -354 136 O
+ATOM 326 CB HIS A 41 13.651 -5.754 23.097 1.00 14.02 C
+ANISOU 326 CB HIS A 41 1972 1853 1502 106 -406 91 C
+ATOM 327 CG HIS A 41 12.654 -5.295 22.083 1.00 16.36 C
+ANISOU 327 CG HIS A 41 2270 2150 1798 134 -364 69 C
+ATOM 328 ND1 HIS A 41 11.296 -5.507 22.253 1.00 19.44 N
+ANISOU 328 ND1 HIS A 41 2661 2548 2175 176 -323 76 N
+ATOM 329 CD2 HIS A 41 12.838 -4.516 20.993 1.00 17.15 C
+ANISOU 329 CD2 HIS A 41 2370 2239 1905 124 -360 46 C
+ATOM 330 CE1 HIS A 41 10.708 -4.914 21.223 1.00 19.39 C
+ANISOU 330 CE1 HIS A 41 2654 2539 2173 188 -298 62 C
+ATOM 331 NE2 HIS A 41 11.596 -4.303 20.441 1.00 18.52 N
+ANISOU 331 NE2 HIS A 41 2544 2419 2074 157 -320 41 N
+ATOM 332 N VAL A 42 12.320 -9.175 22.827 1.00 14.08 N
+ANISOU 332 N VAL A 42 1822 1906 1623 156 -336 136 N
+ATOM 333 CA VAL A 42 11.239 -10.064 23.272 1.00 14.58 C
+ANISOU 333 CA VAL A 42 1859 1985 1696 188 -310 159 C
+ATOM 334 C VAL A 42 11.547 -10.606 24.697 1.00 15.27 C
+ANISOU 334 C VAL A 42 1949 2082 1770 189 -329 189 C
+ATOM 335 O VAL A 42 10.628 -10.903 25.447 1.00 16.44 O
+ANISOU 335 O VAL A 42 2105 2241 1898 221 -310 207 O
+ATOM 336 CB VAL A 42 10.982 -11.221 22.276 1.00 14.96 C
+ANISOU 336 CB VAL A 42 1841 2034 1807 184 -292 161 C
+ATOM 337 CG1 VAL A 42 12.125 -12.225 22.274 1.00 14.97 C
+ANISOU 337 CG1 VAL A 42 1795 2032 1863 160 -303 173 C
+ATOM 338 CG2 VAL A 42 9.651 -11.914 22.559 1.00 15.69 C
+ANISOU 338 CG2 VAL A 42 1914 2140 1907 215 -268 185 C
+ATOM 339 N ILE A 43 12.839 -10.667 25.091 1.00 14.68 N
+ANISOU 339 N ILE A 43 1867 2004 1707 153 -367 199 N
+ATOM 340 CA ILE A 43 13.211 -11.149 26.424 1.00 15.70 C
+ANISOU 340 CA ILE A 43 2001 2144 1822 145 -394 234 C
+ATOM 341 C ILE A 43 13.082 -10.078 27.518 1.00 18.13 C
+ANISOU 341 C ILE A 43 2405 2444 2041 146 -414 228 C
+ATOM 342 O ILE A 43 13.347 -10.366 28.682 1.00 18.87 O
+ANISOU 342 O ILE A 43 2518 2544 2107 138 -437 255 O
+ATOM 343 CB ILE A 43 14.635 -11.767 26.406 1.00 15.42 C
+ANISOU 343 CB ILE A 43 1911 2105 1842 102 -429 260 C
+ATOM 344 CG1 ILE A 43 15.718 -10.687 26.276 1.00 15.89 C
+ANISOU 344 CG1 ILE A 43 2007 2149 1882 61 -472 255 C
+ATOM 345 CG2 ILE A 43 14.757 -12.817 25.294 1.00 15.89 C
+ANISOU 345 CG2 ILE A 43 1891 2162 1985 106 -396 261 C
+ATOM 346 CD1 ILE A 43 17.155 -11.214 26.301 1.00 17.16 C
+ANISOU 346 CD1 ILE A 43 2105 2308 2108 20 -504 297 C
+ATOM 347 N CYS A 44 12.700 -8.851 27.161 1.00 19.70 N
+ANISOU 347 N CYS A 44 2667 2625 2191 156 -403 196 N
+ATOM 348 CA CYS A 44 12.587 -7.761 28.109 1.00 22.56 C
+ANISOU 348 CA CYS A 44 3137 2971 2464 156 -418 188 C
+ATOM 349 C CYS A 44 11.166 -7.545 28.562 1.00 26.82 C
+ANISOU 349 C CYS A 44 3723 3510 2957 217 -360 186 C
+ATOM 350 O CYS A 44 10.221 -7.737 27.806 1.00 27.66 O
+ANISOU 350 O CYS A 44 3787 3624 3097 251 -317 185 O
+ATOM 351 CB CYS A 44 13.121 -6.476 27.485 1.00 22.30 C
+ANISOU 351 CB CYS A 44 3157 2911 2403 133 -436 155 C
+ATOM 352 SG CYS A 44 14.871 -6.530 27.050 1.00 22.16 S
+ANISOU 352 SG CYS A 44 3091 2889 2438 63 -504 168 S
+ATOM 353 N THR A 45 11.039 -7.011 29.755 1.00 29.51 N
+ANISOU 353 N THR A 45 4158 3836 3217 226 -363 189 N
+ATOM 354 CA THR A 45 9.787 -6.494 30.270 1.00 32.18 C
+ANISOU 354 CA THR A 45 4565 4164 3498 287 -301 190 C
+ATOM 355 C THR A 45 9.827 -4.970 29.895 1.00 34.36 C
+ANISOU 355 C THR A 45 4930 4402 3723 283 -296 152 C
+ATOM 356 O THR A 45 10.846 -4.488 29.368 1.00 34.59 O
+ANISOU 356 O THR A 45 4961 4420 3762 231 -348 130 O
+ATOM 357 CB THR A 45 9.740 -6.707 31.794 1.00 34.04 C
+ANISOU 357 CB THR A 45 4873 4397 3665 295 -304 212 C
+ATOM 358 OG1 THR A 45 10.699 -5.849 32.419 1.00 35.60 O
+ANISOU 358 OG1 THR A 45 5172 4565 3790 245 -359 193 O
+ATOM 359 CG2 THR A 45 10.010 -8.155 32.194 1.00 34.58 C
+ANISOU 359 CG2 THR A 45 4854 4501 3785 283 -326 250 C
+ATOM 360 N SER A 46 8.754 -4.205 30.188 1.00 35.48 N
+ANISOU 360 N SER A 46 5146 4523 3813 340 -232 150 N
+ATOM 361 CA SER A 46 8.778 -2.760 29.936 1.00 36.69 C
+ANISOU 361 CA SER A 46 5392 4636 3915 340 -223 116 C
+ATOM 362 C SER A 46 9.855 -2.090 30.824 1.00 37.23 C
+ANISOU 362 C SER A 46 5572 4670 3904 286 -286 95 C
+ATOM 363 O SER A 46 10.511 -1.144 30.383 1.00 37.54 O
+ANISOU 363 O SER A 46 5653 4683 3928 247 -323 65 O
+ATOM 364 CB SER A 46 7.409 -2.137 30.185 1.00 38.60 C
+ANISOU 364 CB SER A 46 5692 4857 4118 418 -133 128 C
+ATOM 365 OG SER A 46 7.293 -0.915 29.474 1.00 42.31 O
+ANISOU 365 OG SER A 46 6206 5295 4576 423 -115 101 O
+ATOM 366 N GLU A 47 10.064 -2.620 32.051 1.00 37.15 N
+ANISOU 366 N GLU A 47 5606 4662 3845 278 -303 114 N
+ATOM 367 CA GLU A 47 11.067 -2.151 33.007 1.00 37.30 C
+ANISOU 367 CA GLU A 47 5733 4653 3785 217 -373 104 C
+ATOM 368 C GLU A 47 12.485 -2.408 32.486 1.00 36.61 C
+ANISOU 368 C GLU A 47 5575 4580 3755 133 -468 109 C
+ATOM 369 O GLU A 47 13.323 -1.506 32.541 1.00 37.19 O
+ANISOU 369 O GLU A 47 5721 4620 3788 78 -527 91 O
+ATOM 370 CB GLU A 47 10.871 -2.832 34.379 1.00 40.16 C
+ANISOU 370 CB GLU A 47 6141 5023 4093 228 -369 133 C
+ATOM 371 CG GLU A 47 11.899 -2.401 35.412 1.00 46.08 C
+ANISOU 371 CG GLU A 47 7008 5744 4757 154 -451 130 C
+ATOM 372 CD GLU A 47 11.871 -3.137 36.739 1.00 53.53 C
+ANISOU 372 CD GLU A 47 7996 6698 5645 150 -462 161 C
+ATOM 373 OE1 GLU A 47 11.167 -4.168 36.840 1.00 55.04 O
+ANISOU 373 OE1 GLU A 47 8102 6928 5882 202 -412 191 O
+ATOM 374 OE2 GLU A 47 12.559 -2.680 37.681 1.00 56.09 O
+ANISOU 374 OE2 GLU A 47 8443 6991 5879 92 -525 159 O
+ATOM 375 N ASP A 48 12.752 -3.629 31.971 1.00 35.12 N
+ANISOU 375 N ASP A 48 5245 4437 3662 125 -481 136 N
+ATOM 376 CA ASP A 48 14.071 -3.994 31.442 1.00 34.07 C
+ANISOU 376 CA ASP A 48 5032 4319 3596 56 -555 152 C
+ATOM 377 C ASP A 48 14.517 -3.050 30.338 1.00 32.73 C
+ANISOU 377 C ASP A 48 4859 4129 3449 34 -570 124 C
+ATOM 378 O ASP A 48 15.695 -2.736 30.268 1.00 32.68 O
+ANISOU 378 O ASP A 48 4853 4111 3451 -31 -643 134 O
+ATOM 379 CB ASP A 48 14.089 -5.430 30.884 1.00 35.22 C
+ANISOU 379 CB ASP A 48 5029 4508 3845 67 -541 181 C
+ATOM 380 CG ASP A 48 14.024 -6.544 31.907 1.00 39.53 C
+ANISOU 380 CG ASP A 48 5549 5080 4393 72 -546 220 C
+ATOM 381 OD1 ASP A 48 14.540 -6.353 33.029 1.00 39.78 O
+ANISOU 381 OD1 ASP A 48 5653 5100 4362 33 -596 238 O
+ATOM 382 OD2 ASP A 48 13.467 -7.614 31.581 1.00 41.68 O
+ANISOU 382 OD2 ASP A 48 5728 5380 4728 109 -503 236 O
+ATOM 383 N MET A 49 13.587 -2.587 29.486 1.00 31.75 N
+ANISOU 383 N MET A 49 4729 4001 3335 86 -505 95 N
+ATOM 384 CA MET A 49 13.915 -1.698 28.369 1.00 31.02 C
+ANISOU 384 CA MET A 49 4625 3892 3268 69 -514 69 C
+ATOM 385 C MET A 49 14.627 -0.405 28.761 1.00 30.28 C
+ANISOU 385 C MET A 49 4647 3753 3103 22 -568 51 C
+ATOM 386 O MET A 49 15.313 0.164 27.924 1.00 29.65 O
+ANISOU 386 O MET A 49 4547 3665 3055 -11 -601 43 O
+ATOM 387 CB MET A 49 12.679 -1.384 27.513 1.00 31.35 C
+ANISOU 387 CB MET A 49 4649 3936 3326 132 -435 48 C
+ATOM 388 CG MET A 49 12.174 -2.572 26.724 1.00 32.65 C
+ANISOU 388 CG MET A 49 4693 4140 3572 161 -398 65 C
+ATOM 389 SD MET A 49 13.436 -3.315 25.650 1.00 33.34 S
+ANISOU 389 SD MET A 49 4666 4249 3751 107 -446 75 S
+ATOM 390 CE MET A 49 13.560 -2.060 24.368 1.00 27.71 C
+ANISOU 390 CE MET A 49 3963 3518 3049 97 -444 42 C
+ATOM 391 N LEU A 50 14.493 0.050 30.009 1.00 30.11 N
+ANISOU 391 N LEU A 50 4750 3702 2988 18 -579 48 N
+ATOM 392 CA LEU A 50 15.162 1.274 30.453 1.00 30.70 C
+ANISOU 392 CA LEU A 50 4951 3727 2988 -35 -638 31 C
+ATOM 393 C LEU A 50 16.689 1.159 30.403 1.00 30.56 C
+ANISOU 393 C LEU A 50 4892 3714 3007 -125 -744 62 C
+ATOM 394 O LEU A 50 17.345 2.089 29.955 1.00 31.26 O
+ANISOU 394 O LEU A 50 5008 3775 3094 -168 -790 53 O
+ATOM 395 CB LEU A 50 14.682 1.683 31.851 1.00 31.34 C
+ANISOU 395 CB LEU A 50 5188 3769 2950 -22 -625 21 C
+ATOM 396 CG LEU A 50 13.191 1.988 31.949 1.00 33.68 C
+ANISOU 396 CG LEU A 50 5538 4051 3208 72 -512 -2 C
+ATOM 397 CD1 LEU A 50 12.778 2.229 33.387 1.00 34.43 C
+ANISOU 397 CD1 LEU A 50 5787 4107 3185 88 -492 -5 C
+ATOM 398 CD2 LEU A 50 12.806 3.173 31.059 1.00 34.52 C
+ANISOU 398 CD2 LEU A 50 5675 4125 3316 97 -473 -35 C
+ATOM 399 N ASN A 51 17.251 0.022 30.820 1.00 29.29 N
+ANISOU 399 N ASN A 51 4655 3587 2886 -153 -781 107 N
+ATOM 400 CA ASN A 51 18.701 -0.204 30.771 1.00 28.56 C
+ANISOU 400 CA ASN A 51 4505 3502 2843 -236 -877 154 C
+ATOM 401 C ASN A 51 18.964 -1.718 30.692 1.00 26.51 C
+ANISOU 401 C ASN A 51 4106 3292 2674 -231 -871 201 C
+ATOM 402 O ASN A 51 19.400 -2.327 31.674 1.00 26.96 O
+ANISOU 402 O ASN A 51 4166 3359 2718 -268 -920 243 O
+ATOM 403 CB ASN A 51 19.381 0.398 32.009 1.00 30.92 C
+ANISOU 403 CB ASN A 51 4934 3764 3050 -310 -968 172 C
+ATOM 404 CG ASN A 51 20.892 0.388 31.942 1.00 35.07 C
+ANISOU 404 CG ASN A 51 5408 4292 3627 -404 -1077 232 C
+ATOM 405 OD1 ASN A 51 21.493 0.225 30.873 1.00 36.86 O
+ANISOU 405 OD1 ASN A 51 5517 4536 3951 -411 -1081 253 O
+ATOM 406 ND2 ASN A 51 21.539 0.567 33.085 1.00 36.16 N
+ANISOU 406 ND2 ASN A 51 5631 4408 3698 -478 -1167 266 N
+ATOM 407 N PRO A 52 18.640 -2.362 29.557 1.00 23.74 N
+ANISOU 407 N PRO A 52 3637 2970 2411 -183 -808 193 N
+ATOM 408 CA PRO A 52 18.791 -3.824 29.494 1.00 22.58 C
+ANISOU 408 CA PRO A 52 3370 2864 2345 -171 -792 233 C
+ATOM 409 C PRO A 52 20.203 -4.339 29.261 1.00 21.84 C
+ANISOU 409 C PRO A 52 3183 2781 2333 -231 -854 295 C
+ATOM 410 O PRO A 52 20.938 -3.775 28.461 1.00 23.02 O
+ANISOU 410 O PRO A 52 3308 2919 2521 -260 -879 301 O
+ATOM 411 CB PRO A 52 17.858 -4.228 28.347 1.00 23.00 C
+ANISOU 411 CB PRO A 52 3352 2934 2451 -104 -704 200 C
+ATOM 412 CG PRO A 52 17.799 -3.012 27.462 1.00 23.84 C
+ANISOU 412 CG PRO A 52 3498 3017 2544 -104 -698 161 C
+ATOM 413 CD PRO A 52 18.087 -1.804 28.306 1.00 23.00 C
+ANISOU 413 CD PRO A 52 3524 2872 2342 -139 -749 150 C
+ATOM 414 N ASN A 53 20.579 -5.426 29.948 1.00 20.08 N
+ANISOU 414 N ASN A 53 2904 2581 2144 -247 -874 346 N
+ATOM 415 CA ASN A 53 21.843 -6.098 29.676 1.00 19.44 C
+ANISOU 415 CA ASN A 53 2714 2513 2160 -292 -915 417 C
+ATOM 416 C ASN A 53 21.378 -7.382 29.004 1.00 19.09 C
+ANISOU 416 C ASN A 53 2561 2495 2199 -233 -835 415 C
+ATOM 417 O ASN A 53 20.976 -8.328 29.682 1.00 19.86 O
+ANISOU 417 O ASN A 53 2636 2611 2298 -214 -818 432 O
+ATOM 418 CB ASN A 53 22.650 -6.418 30.934 1.00 20.41 C
+ANISOU 418 CB ASN A 53 2848 2640 2268 -357 -999 486 C
+ATOM 419 CG ASN A 53 24.001 -6.990 30.569 1.00 23.36 C
+ANISOU 419 CG ASN A 53 3101 3024 2753 -401 -1038 571 C
+ATOM 420 OD1 ASN A 53 24.112 -7.970 29.818 1.00 24.42 O
+ANISOU 420 OD1 ASN A 53 3120 3174 2984 -364 -978 589 O
+ATOM 421 ND2 ASN A 53 25.063 -6.397 31.086 1.00 23.75 N
+ANISOU 421 ND2 ASN A 53 3174 3058 2792 -483 -1136 631 N
+ATOM 422 N TYR A 54 21.348 -7.382 27.684 1.00 18.47 N
+ANISOU 422 N TYR A 54 2424 2414 2180 -206 -786 394 N
+ATOM 423 CA TYR A 54 20.814 -8.489 26.923 1.00 17.26 C
+ANISOU 423 CA TYR A 54 2190 2277 2090 -151 -706 380 C
+ATOM 424 C TYR A 54 21.500 -9.801 27.153 1.00 17.52 C
+ANISOU 424 C TYR A 54 2126 2325 2207 -161 -708 446 C
+ATOM 425 O TYR A 54 20.800 -10.791 27.331 1.00 17.53 O
+ANISOU 425 O TYR A 54 2098 2340 2224 -125 -664 439 O
+ATOM 426 CB TYR A 54 20.781 -8.147 25.448 1.00 15.88 C
+ANISOU 426 CB TYR A 54 1991 2092 1952 -128 -659 343 C
+ATOM 427 CG TYR A 54 19.666 -7.180 25.141 1.00 15.71 C
+ANISOU 427 CG TYR A 54 2051 2062 1857 -98 -634 275 C
+ATOM 428 CD1 TYR A 54 18.353 -7.614 25.039 1.00 16.04 C
+ANISOU 428 CD1 TYR A 54 2100 2115 1881 -46 -576 238 C
+ATOM 429 CD2 TYR A 54 19.916 -5.823 25.004 1.00 15.93 C
+ANISOU 429 CD2 TYR A 54 2146 2070 1837 -123 -670 256 C
+ATOM 430 CE1 TYR A 54 17.320 -6.725 24.759 1.00 16.34 C
+ANISOU 430 CE1 TYR A 54 2203 2145 1861 -17 -549 189 C
+ATOM 431 CE2 TYR A 54 18.897 -4.929 24.714 1.00 16.57 C
+ANISOU 431 CE2 TYR A 54 2297 2141 1858 -93 -641 200 C
+ATOM 432 CZ TYR A 54 17.596 -5.382 24.598 1.00 17.28 C
+ANISOU 432 CZ TYR A 54 2388 2243 1935 -39 -578 169 C
+ATOM 433 OH TYR A 54 16.582 -4.489 24.330 1.00 18.46 O
+ANISOU 433 OH TYR A 54 2600 2383 2033 -7 -547 126 O
+ATOM 434 N GLU A 55 22.849 -9.837 27.217 1.00 18.17 N
+ANISOU 434 N GLU A 55 2157 2401 2346 -210 -755 513 N
+ATOM 435 CA GLU A 55 23.536 -11.110 27.478 1.00 18.88 C
+ANISOU 435 CA GLU A 55 2147 2503 2523 -216 -749 585 C
+ATOM 436 C GLU A 55 23.132 -11.677 28.833 1.00 19.05 C
+ANISOU 436 C GLU A 55 2191 2544 2503 -224 -778 605 C
+ATOM 437 O GLU A 55 22.911 -12.883 28.953 1.00 19.30 O
+ANISOU 437 O GLU A 55 2158 2588 2585 -196 -739 625 O
+ATOM 438 CB GLU A 55 25.069 -10.991 27.409 1.00 22.09 C
+ANISOU 438 CB GLU A 55 2489 2902 3003 -271 -801 674 C
+ATOM 439 CG GLU A 55 25.638 -10.894 26.003 1.00 27.99 C
+ANISOU 439 CG GLU A 55 3177 3632 3827 -252 -751 679 C
+ATOM 440 CD GLU A 55 25.669 -12.141 25.133 1.00 34.81 C
+ANISOU 440 CD GLU A 55 3953 4491 4783 -201 -658 687 C
+ATOM 441 OE1 GLU A 55 25.127 -13.194 25.538 1.00 33.74 O
+ANISOU 441 OE1 GLU A 55 3796 4366 4658 -173 -623 681 O
+ATOM 442 OE2 GLU A 55 26.209 -12.043 24.007 1.00 39.00 O
+ANISOU 442 OE2 GLU A 55 4443 5004 5372 -188 -615 697 O
+ATOM 443 N ASP A 56 22.991 -10.802 29.841 1.00 18.58 N
+ANISOU 443 N ASP A 56 2230 2482 2347 -260 -845 597 N
+ATOM 444 CA ASP A 56 22.594 -11.263 31.171 1.00 18.89 C
+ANISOU 444 CA ASP A 56 2304 2538 2334 -269 -872 616 C
+ATOM 445 C ASP A 56 21.151 -11.742 31.203 1.00 19.04 C
+ANISOU 445 C ASP A 56 2346 2569 2318 -198 -798 556 C
+ATOM 446 O ASP A 56 20.872 -12.782 31.794 1.00 20.06 O
+ANISOU 446 O ASP A 56 2434 2719 2470 -182 -783 583 O
+ATOM 447 CB ASP A 56 22.838 -10.181 32.232 1.00 20.13 C
+ANISOU 447 CB ASP A 56 2578 2683 2388 -329 -960 623 C
+ATOM 448 CG ASP A 56 24.304 -9.937 32.525 1.00 23.92 C
+ANISOU 448 CG ASP A 56 3026 3156 2907 -413 -1053 708 C
+ATOM 449 OD1 ASP A 56 25.133 -10.830 32.216 1.00 23.66 O
+ANISOU 449 OD1 ASP A 56 2869 3134 2985 -422 -1049 781 O
+ATOM 450 OD2 ASP A 56 24.630 -8.853 33.067 1.00 25.46 O
+ANISOU 450 OD2 ASP A 56 3320 3330 3023 -470 -1130 709 O
+ATOM 451 N LEU A 57 20.235 -11.002 30.566 1.00 18.53 N
+ANISOU 451 N LEU A 57 2342 2493 2205 -158 -754 482 N
+ATOM 452 CA LEU A 57 18.835 -11.405 30.531 1.00 18.71 C
+ANISOU 452 CA LEU A 57 2381 2527 2202 -93 -686 437 C
+ATOM 453 C LEU A 57 18.663 -12.733 29.781 1.00 18.63 C
+ANISOU 453 C LEU A 57 2260 2529 2289 -57 -628 448 C
+ATOM 454 O LEU A 57 17.847 -13.565 30.166 1.00 18.76 O
+ANISOU 454 O LEU A 57 2258 2561 2308 -21 -595 449 O
+ATOM 455 CB LEU A 57 17.989 -10.323 29.851 1.00 19.11 C
+ANISOU 455 CB LEU A 57 2503 2561 2198 -60 -651 369 C
+ATOM 456 CG LEU A 57 17.861 -9.013 30.615 1.00 21.19 C
+ANISOU 456 CG LEU A 57 2895 2804 2353 -81 -690 346 C
+ATOM 457 CD1 LEU A 57 17.170 -7.968 29.770 1.00 22.03 C
+ANISOU 457 CD1 LEU A 57 3054 2892 2426 -49 -650 287 C
+ATOM 458 CD2 LEU A 57 17.084 -9.216 31.913 1.00 22.04 C
+ANISOU 458 CD2 LEU A 57 3070 2920 2385 -60 -683 350 C
+ATOM 459 N LEU A 58 19.446 -12.932 28.724 1.00 17.87 N
+ANISOU 459 N LEU A 58 2097 2422 2272 -68 -616 459 N
+ATOM 460 CA LEU A 58 19.353 -14.126 27.908 1.00 18.31 C
+ANISOU 460 CA LEU A 58 2064 2478 2414 -36 -557 464 C
+ATOM 461 C LEU A 58 19.824 -15.379 28.634 1.00 18.99 C
+ANISOU 461 C LEU A 58 2077 2577 2561 -45 -564 529 C
+ATOM 462 O LEU A 58 19.291 -16.458 28.361 1.00 19.97 O
+ANISOU 462 O LEU A 58 2154 2705 2731 -10 -514 525 O
+ATOM 463 CB LEU A 58 20.098 -13.912 26.579 1.00 18.33 C
+ANISOU 463 CB LEU A 58 2030 2459 2476 -42 -534 458 C
+ATOM 464 CG LEU A 58 19.768 -14.878 25.447 1.00 19.20 C
+ANISOU 464 CG LEU A 58 2085 2557 2651 -5 -460 438 C
+ATOM 465 CD1 LEU A 58 18.284 -14.903 25.133 1.00 18.38 C
+ANISOU 465 CD1 LEU A 58 2022 2459 2502 35 -423 379 C
+ATOM 466 CD2 LEU A 58 20.620 -14.581 24.225 1.00 20.01 C
+ANISOU 466 CD2 LEU A 58 2163 2637 2805 -13 -438 438 C
+ATOM 467 N ILE A 59 20.748 -15.251 29.613 1.00 18.93 N
+ANISOU 467 N ILE A 59 2065 2578 2550 -94 -630 590 N
+ATOM 468 CA ILE A 59 21.213 -16.402 30.410 1.00 20.28 C
+ANISOU 468 CA ILE A 59 2165 2764 2778 -106 -643 661 C
+ATOM 469 C ILE A 59 20.039 -17.065 31.138 1.00 20.86 C
+ANISOU 469 C ILE A 59 2255 2857 2813 -69 -619 643 C
+ATOM 470 O ILE A 59 20.042 -18.276 31.340 1.00 21.11 O
+ANISOU 470 O ILE A 59 2214 2898 2908 -55 -597 681 O
+ATOM 471 CB ILE A 59 22.308 -15.997 31.439 1.00 22.03 C
+ANISOU 471 CB ILE A 59 2392 2992 2986 -174 -732 734 C
+ATOM 472 CG1 ILE A 59 23.587 -15.552 30.751 1.00 24.25 C
+ANISOU 472 CG1 ILE A 59 2630 3255 3329 -213 -757 777 C
+ATOM 473 CG2 ILE A 59 22.606 -17.132 32.438 1.00 23.10 C
+ANISOU 473 CG2 ILE A 59 2463 3149 3164 -188 -750 808 C
+ATOM 474 CD1 ILE A 59 24.600 -14.933 31.734 1.00 26.45 C
+ANISOU 474 CD1 ILE A 59 2926 3538 3584 -292 -861 852 C
+ATOM 475 N ARG A 60 19.043 -16.267 31.544 1.00 21.21 N
+ANISOU 475 N ARG A 60 2395 2907 2757 -51 -622 591 N
+ATOM 476 CA ARG A 60 17.885 -16.790 32.250 1.00 22.07 C
+ANISOU 476 CA ARG A 60 2522 3034 2828 -12 -596 581 C
+ATOM 477 C ARG A 60 16.844 -17.440 31.336 1.00 21.30 C
+ANISOU 477 C ARG A 60 2388 2934 2769 44 -524 543 C
+ATOM 478 O ARG A 60 15.812 -17.882 31.826 1.00 22.28 O
+ANISOU 478 O ARG A 60 2522 3074 2870 80 -500 539 O
+ATOM 479 CB ARG A 60 17.247 -15.694 33.120 1.00 24.65 C
+ANISOU 479 CB ARG A 60 2970 3364 3034 -11 -620 552 C
+ATOM 480 CG ARG A 60 18.246 -14.947 33.999 1.00 29.44 C
+ANISOU 480 CG ARG A 60 3633 3965 3587 -77 -701 585 C
+ATOM 481 CD ARG A 60 18.917 -15.852 35.008 1.00 33.62 C
+ANISOU 481 CD ARG A 60 4112 4515 4147 -112 -745 661 C
+ATOM 482 NE ARG A 60 20.227 -15.335 35.399 1.00 37.98 N
+ANISOU 482 NE ARG A 60 4675 5059 4695 -189 -830 711 N
+ATOM 483 CZ ARG A 60 21.142 -16.030 36.067 1.00 40.16 C
+ANISOU 483 CZ ARG A 60 4890 5351 5020 -237 -881 793 C
+ATOM 484 NH1 ARG A 60 22.307 -15.479 36.372 1.00 39.79 N
+ANISOU 484 NH1 ARG A 60 4853 5294 4970 -313 -964 846 N
+ATOM 485 NH2 ARG A 60 20.898 -17.284 36.432 1.00 40.17 N
+ANISOU 485 NH2 ARG A 60 4813 5375 5075 -212 -853 830 N
+ATOM 486 N LYS A 61 17.089 -17.491 30.014 1.00 19.36 N
+ANISOU 486 N LYS A 61 2107 2668 2580 50 -491 517 N
+ATOM 487 CA LYS A 61 16.134 -18.067 29.078 1.00 18.81 C
+ANISOU 487 CA LYS A 61 2015 2591 2540 92 -432 481 C
+ATOM 488 C LYS A 61 16.645 -19.373 28.501 1.00 19.17 C
+ANISOU 488 C LYS A 61 1973 2624 2687 94 -401 509 C
+ATOM 489 O LYS A 61 17.832 -19.513 28.216 1.00 20.35 O
+ANISOU 489 O LYS A 61 2081 2760 2892 68 -408 540 O
+ATOM 490 CB LYS A 61 15.853 -17.072 27.936 1.00 19.82 C
+ANISOU 490 CB LYS A 61 2188 2701 2642 98 -414 424 C
+ATOM 491 CG LYS A 61 15.324 -15.717 28.401 1.00 22.51 C
+ANISOU 491 CG LYS A 61 2620 3046 2885 101 -435 394 C
+ATOM 492 CD LYS A 61 14.023 -15.821 29.196 1.00 26.00 C
+ANISOU 492 CD LYS A 61 3096 3507 3275 139 -418 394 C
+ATOM 493 CE LYS A 61 13.493 -14.456 29.568 1.00 29.36 C
+ANISOU 493 CE LYS A 61 3620 3928 3608 150 -423 363 C
+ATOM 494 NZ LYS A 61 12.260 -14.538 30.405 1.00 32.04 N
+ANISOU 494 NZ LYS A 61 3994 4282 3897 193 -397 373 N
+ATOM 495 N SER A 62 15.745 -20.338 28.359 1.00 17.84 N
+ANISOU 495 N SER A 62 1776 2457 2545 125 -365 504 N
+ATOM 496 CA SER A 62 16.030 -21.625 27.751 1.00 17.70 C
+ANISOU 496 CA SER A 62 1690 2418 2617 132 -327 521 C
+ATOM 497 C SER A 62 15.168 -21.747 26.476 1.00 16.11 C
+ANISOU 497 C SER A 62 1510 2194 2419 152 -285 468 C
+ATOM 498 O SER A 62 14.219 -20.985 26.286 1.00 15.44 O
+ANISOU 498 O SER A 62 1477 2118 2273 164 -288 431 O
+ATOM 499 CB SER A 62 15.673 -22.756 28.709 1.00 20.52 C
+ANISOU 499 CB SER A 62 2000 2793 3004 144 -328 566 C
+ATOM 500 OG SER A 62 16.454 -22.685 29.891 1.00 23.82 O
+ANISOU 500 OG SER A 62 2401 3234 3417 120 -372 620 O
+ATOM 501 N ASN A 63 15.466 -22.730 25.611 1.00 15.74 N
+ANISOU 501 N ASN A 63 1426 2113 2442 155 -244 467 N
+ATOM 502 CA ASN A 63 14.663 -22.963 24.399 1.00 15.24 C
+ANISOU 502 CA ASN A 63 1389 2022 2378 164 -210 420 C
+ATOM 503 C ASN A 63 13.166 -23.023 24.663 1.00 15.14 C
+ANISOU 503 C ASN A 63 1396 2029 2325 181 -221 410 C
+ATOM 504 O ASN A 63 12.399 -22.427 23.914 1.00 15.00 O
+ANISOU 504 O ASN A 63 1422 2008 2270 182 -218 372 O
+ATOM 505 CB ASN A 63 15.077 -24.261 23.732 1.00 15.61 C
+ANISOU 505 CB ASN A 63 1400 2028 2503 167 -165 429 C
+ATOM 506 CG ASN A 63 16.449 -24.203 23.162 1.00 17.36 C
+ANISOU 506 CG ASN A 63 1606 2220 2770 158 -136 440 C
+ATOM 507 OD1 ASN A 63 16.926 -23.144 22.757 1.00 17.17 O
+ANISOU 507 OD1 ASN A 63 1610 2198 2717 147 -145 422 O
+ATOM 508 ND2 ASN A 63 17.110 -25.341 23.087 1.00 17.34 N
+ANISOU 508 ND2 ASN A 63 1556 2186 2845 164 -96 474 N
+ATOM 509 N HIS A 64 12.750 -23.729 25.736 1.00 15.18 N
+ANISOU 509 N HIS A 64 1366 2058 2344 194 -233 450 N
+ATOM 510 CA HIS A 64 11.332 -23.876 26.064 1.00 15.34 C
+ANISOU 510 CA HIS A 64 1395 2098 2337 214 -239 456 C
+ATOM 511 C HIS A 64 10.643 -22.586 26.518 1.00 15.59 C
+ANISOU 511 C HIS A 64 1476 2159 2288 228 -257 445 C
+ATOM 512 O HIS A 64 9.414 -22.564 26.635 1.00 16.33 O
+ANISOU 512 O HIS A 64 1578 2267 2361 249 -255 453 O
+ATOM 513 CB HIS A 64 11.090 -25.001 27.087 1.00 16.13 C
+ANISOU 513 CB HIS A 64 1440 2214 2474 228 -243 507 C
+ATOM 514 CG HIS A 64 11.550 -24.698 28.481 1.00 17.26 C
+ANISOU 514 CG HIS A 64 1574 2393 2592 231 -269 545 C
+ATOM 515 ND1 HIS A 64 12.805 -25.063 28.912 1.00 18.51 N
+ANISOU 515 ND1 HIS A 64 1694 2548 2790 213 -277 575 N
+ATOM 516 CD2 HIS A 64 10.890 -24.109 29.506 1.00 18.35 C
+ANISOU 516 CD2 HIS A 64 1738 2566 2667 250 -286 562 C
+ATOM 517 CE1 HIS A 64 12.887 -24.663 30.171 1.00 18.91 C
+ANISOU 517 CE1 HIS A 64 1754 2634 2797 213 -308 606 C
+ATOM 518 NE2 HIS A 64 11.768 -24.069 30.566 1.00 19.00 N
+ANISOU 518 NE2 HIS A 64 1810 2667 2742 237 -311 595 N
+ATOM 519 N ASN A 65 11.413 -21.525 26.808 1.00 14.89 N
+ANISOU 519 N ASN A 65 1421 2078 2157 217 -274 433 N
+ATOM 520 CA ASN A 65 10.825 -20.244 27.197 1.00 15.45 C
+ANISOU 520 CA ASN A 65 1553 2168 2150 231 -285 418 C
+ATOM 521 C ASN A 65 10.364 -19.437 25.979 1.00 15.62 C
+ANISOU 521 C ASN A 65 1613 2173 2150 229 -272 373 C
+ATOM 522 O ASN A 65 9.615 -18.487 26.144 1.00 16.44 O
+ANISOU 522 O ASN A 65 1761 2288 2198 247 -271 365 O
+ATOM 523 CB ASN A 65 11.814 -19.399 27.993 1.00 16.32 C
+ANISOU 523 CB ASN A 65 1695 2287 2218 213 -315 422 C
+ATOM 524 CG ASN A 65 12.130 -19.936 29.354 1.00 20.06 C
+ANISOU 524 CG ASN A 65 2148 2782 2691 212 -336 470 C
+ATOM 525 OD1 ASN A 65 13.288 -19.972 29.757 1.00 21.53 O
+ANISOU 525 OD1 ASN A 65 2319 2968 2893 182 -363 491 O
+ATOM 526 ND2 ASN A 65 11.113 -20.354 30.094 1.00 20.32 N
+ANISOU 526 ND2 ASN A 65 2177 2836 2708 243 -325 495 N
+ATOM 527 N PHE A 66 10.834 -19.782 24.766 1.00 14.81 N
+ANISOU 527 N PHE A 66 1497 2042 2089 208 -259 348 N
+ATOM 528 CA PHE A 66 10.445 -19.072 23.556 1.00 14.55 C
+ANISOU 528 CA PHE A 66 1500 1993 2036 201 -250 308 C
+ATOM 529 C PHE A 66 9.285 -19.790 22.901 1.00 15.70 C
+ANISOU 529 C PHE A 66 1633 2130 2202 205 -239 311 C
+ATOM 530 O PHE A 66 9.473 -20.833 22.284 1.00 17.06 O
+ANISOU 530 O PHE A 66 1783 2277 2423 190 -227 309 O
+ATOM 531 CB PHE A 66 11.624 -18.973 22.581 1.00 13.81 C
+ANISOU 531 CB PHE A 66 1409 1871 1969 175 -240 280 C
+ATOM 532 CG PHE A 66 12.755 -18.158 23.140 1.00 14.30 C
+ANISOU 532 CG PHE A 66 1481 1940 2013 164 -260 284 C
+ATOM 533 CD1 PHE A 66 12.739 -16.779 23.058 1.00 15.07 C
+ANISOU 533 CD1 PHE A 66 1628 2043 2053 161 -275 261 C
+ATOM 534 CD2 PHE A 66 13.840 -18.771 23.734 1.00 14.97 C
+ANISOU 534 CD2 PHE A 66 1524 2022 2140 153 -266 318 C
+ATOM 535 CE1 PHE A 66 13.791 -16.027 23.574 1.00 15.66 C
+ANISOU 535 CE1 PHE A 66 1717 2122 2112 143 -302 269 C
+ATOM 536 CE2 PHE A 66 14.884 -18.017 24.257 1.00 15.64 C
+ANISOU 536 CE2 PHE A 66 1617 2114 2212 134 -295 333 C
+ATOM 537 CZ PHE A 66 14.840 -16.648 24.190 1.00 15.18 C
+ANISOU 537 CZ PHE A 66 1615 2061 2093 127 -316 307 C
+ATOM 538 N LEU A 67 8.095 -19.249 23.059 1.00 14.73 N
+ANISOU 538 N LEU A 67 1528 2026 2045 223 -242 323 N
+ATOM 539 CA LEU A 67 6.890 -19.851 22.496 1.00 15.02 C
+ANISOU 539 CA LEU A 67 1549 2058 2102 223 -241 341 C
+ATOM 540 C LEU A 67 6.660 -19.315 21.087 1.00 14.82 C
+ANISOU 540 C LEU A 67 1556 2011 2063 197 -242 307 C
+ATOM 541 O LEU A 67 6.407 -18.125 20.903 1.00 14.57 O
+ANISOU 541 O LEU A 67 1556 1989 1989 204 -242 295 O
+ATOM 542 CB LEU A 67 5.687 -19.563 23.389 1.00 16.22 C
+ANISOU 542 CB LEU A 67 1694 2240 2231 259 -240 387 C
+ATOM 543 CG LEU A 67 5.825 -20.012 24.845 1.00 19.15 C
+ANISOU 543 CG LEU A 67 2040 2634 2603 286 -238 424 C
+ATOM 544 CD1 LEU A 67 4.603 -19.600 25.664 1.00 20.19 C
+ANISOU 544 CD1 LEU A 67 2174 2792 2706 330 -225 471 C
+ATOM 545 CD2 LEU A 67 6.082 -21.512 24.947 1.00 20.70 C
+ANISOU 545 CD2 LEU A 67 2184 2820 2861 273 -243 444 C
+ATOM 546 N VAL A 68 6.797 -20.185 20.094 1.00 13.69 N
+ANISOU 546 N VAL A 68 1411 1836 1954 166 -241 291 N
+ATOM 547 CA VAL A 68 6.672 -19.779 18.702 1.00 13.84 C
+ANISOU 547 CA VAL A 68 1470 1832 1958 135 -243 257 C
+ATOM 548 C VAL A 68 5.478 -20.455 18.106 1.00 14.57 C
+ANISOU 548 C VAL A 68 1559 1913 2065 113 -262 282 C
+ATOM 549 O VAL A 68 5.380 -21.671 18.188 1.00 14.93 O
+ANISOU 549 O VAL A 68 1585 1941 2148 103 -265 298 O
+ATOM 550 CB VAL A 68 7.958 -20.136 17.936 1.00 14.82 C
+ANISOU 550 CB VAL A 68 1612 1918 2099 114 -221 215 C
+ATOM 551 CG1 VAL A 68 7.847 -19.711 16.467 1.00 14.89 C
+ANISOU 551 CG1 VAL A 68 1670 1902 2084 82 -220 178 C
+ATOM 552 CG2 VAL A 68 9.173 -19.485 18.597 1.00 15.58 C
+ANISOU 552 CG2 VAL A 68 1702 2028 2190 132 -210 205 C
+ATOM 553 N GLN A 69 4.540 -19.672 17.571 1.00 14.79 N
+ANISOU 553 N GLN A 69 1602 1952 2065 104 -278 294 N
+ATOM 554 CA GLN A 69 3.320 -20.238 17.038 1.00 16.19 C
+ANISOU 554 CA GLN A 69 1772 2122 2259 77 -307 333 C
+ATOM 555 C GLN A 69 3.083 -19.685 15.636 1.00 17.21 C
+ANISOU 555 C GLN A 69 1946 2232 2361 33 -323 309 C
+ATOM 556 O GLN A 69 3.122 -18.475 15.425 1.00 16.72 O
+ANISOU 556 O GLN A 69 1901 2187 2267 43 -316 296 O
+ATOM 557 CB GLN A 69 2.170 -19.888 17.999 1.00 18.04 C
+ANISOU 557 CB GLN A 69 1963 2396 2497 114 -313 402 C
+ATOM 558 CG GLN A 69 0.888 -20.656 17.771 1.00 21.51 C
+ANISOU 558 CG GLN A 69 2373 2833 2968 91 -347 466 C
+ATOM 559 CD GLN A 69 -0.161 -20.174 18.731 1.00 25.03 C
+ANISOU 559 CD GLN A 69 2773 3317 3418 139 -339 540 C
+ATOM 560 OE1 GLN A 69 0.106 -19.927 19.909 1.00 25.84 O
+ANISOU 560 OE1 GLN A 69 2862 3444 3514 190 -309 547 O
+ATOM 561 NE2 GLN A 69 -1.385 -20.021 18.241 1.00 26.21 N
+ANISOU 561 NE2 GLN A 69 2905 3473 3582 121 -365 602 N
+ATOM 562 N ALA A 70 2.875 -20.594 14.677 1.00 19.00 N
+ANISOU 562 N ALA A 70 2201 2421 2599 -17 -344 301 N
+ATOM 563 CA ALA A 70 2.620 -20.293 13.267 1.00 20.96 C
+ANISOU 563 CA ALA A 70 2502 2644 2818 -71 -366 280 C
+ATOM 564 C ALA A 70 1.139 -20.600 13.043 1.00 23.17 C
+ANISOU 564 C ALA A 70 2762 2930 3110 -104 -418 350 C
+ATOM 565 O ALA A 70 0.751 -21.762 13.002 1.00 23.52 O
+ANISOU 565 O ALA A 70 2803 2952 3183 -131 -442 374 O
+ATOM 566 CB ALA A 70 3.471 -21.204 12.398 1.00 20.97 C
+ANISOU 566 CB ALA A 70 2561 2590 2818 -106 -351 226 C
+ATOM 567 N GLY A 71 0.297 -19.573 13.046 1.00 24.68 N
+ANISOU 567 N GLY A 71 2932 3155 3291 -97 -433 393 N
+ATOM 568 CA GLY A 71 -1.148 -19.764 12.969 1.00 25.82 C
+ANISOU 568 CA GLY A 71 3039 3312 3459 -122 -480 480 C
+ATOM 569 C GLY A 71 -1.586 -20.403 14.272 1.00 26.30 C
+ANISOU 569 C GLY A 71 3035 3394 3562 -76 -472 536 C
+ATOM 570 O GLY A 71 -1.283 -19.875 15.340 1.00 27.29 O
+ANISOU 570 O GLY A 71 3133 3550 3687 -11 -430 534 O
+ATOM 571 N AASN A 72 -2.203 -21.577 14.195 0.50 25.88 N
+ANISOU 571 N AASN A 72 2967 3324 3544 -112 -512 581 N
+ATOM 572 N BASN A 72 -2.232 -21.574 14.208 0.50 26.13 N
+ANISOU 572 N BASN A 72 2996 3356 3576 -112 -512 583 N
+ATOM 573 CA AASN A 72 -2.607 -22.309 15.390 0.50 25.81 C
+ANISOU 573 CA AASN A 72 2894 3333 3579 -72 -506 637 C
+ATOM 574 CA BASN A 72 -2.637 -22.282 15.426 0.50 26.29 C
+ANISOU 574 CA BASN A 72 2953 3396 3641 -70 -505 639 C
+ATOM 575 C AASN A 72 -1.585 -23.402 15.775 0.50 25.30 C
+ANISOU 575 C AASN A 72 2844 3241 3527 -65 -484 581 C
+ATOM 576 C BASN A 72 -1.713 -23.458 15.794 0.50 25.45 C
+ANISOU 576 C BASN A 72 2858 3261 3550 -67 -489 590 C
+ATOM 577 O AASN A 72 -1.765 -24.044 16.810 0.50 25.73 O
+ANISOU 577 O AASN A 72 2848 3311 3618 -30 -476 620 O
+ATOM 578 O BASN A 72 -2.036 -24.222 16.705 0.50 25.81 O
+ANISOU 578 O BASN A 72 2853 3318 3635 -41 -489 637 O
+ATOM 579 CB AASN A 72 -3.990 -22.935 15.174 0.50 27.13 C
+ANISOU 579 CB AASN A 72 3023 3498 3786 -113 -566 734 C
+ATOM 580 CB BASN A 72 -4.102 -22.729 15.351 0.50 28.37 C
+ANISOU 580 CB BASN A 72 3169 3666 3945 -100 -560 746 C
+ATOM 581 CG AASN A 72 -4.706 -23.325 16.447 0.50 29.97 C
+ANISOU 581 CG AASN A 72 3301 3891 4194 -61 -557 819 C
+ATOM 582 CG BASN A 72 -4.444 -23.658 14.208 0.50 32.49 C
+ANISOU 582 CG BASN A 72 3733 4141 4471 -192 -627 749 C
+ATOM 583 OD1AASN A 72 -4.849 -22.526 17.378 0.50 30.90 O
+ANISOU 583 OD1AASN A 72 3382 4048 4309 10 -511 846 O
+ATOM 584 OD1BASN A 72 -3.749 -24.647 13.927 0.50 34.05 O
+ANISOU 584 OD1BASN A 72 3977 4295 4666 -221 -629 691 O
+ATOM 585 ND2AASN A 72 -5.171 -24.566 16.514 0.50 30.55 N
+ANISOU 585 ND2AASN A 72 3352 3945 4310 -93 -598 863 N
+ATOM 586 ND2BASN A 72 -5.547 -23.372 13.532 0.50 33.10 N
+ANISOU 586 ND2BASN A 72 3798 4222 4556 -241 -683 824 N
+ATOM 587 N AVAL A 73 -0.530 -23.633 14.956 0.75 24.08 N
+ANISOU 587 N AVAL A 73 2756 3045 3347 -96 -471 497 N
+ATOM 588 N BVAL A 73 -0.584 -23.618 15.080 0.25 23.95 N
+ANISOU 588 N BVAL A 73 2733 3034 3335 -91 -471 504 N
+ATOM 589 CA AVAL A 73 0.414 -24.705 15.245 0.75 23.44 C
+ANISOU 589 CA AVAL A 73 2687 2933 3288 -90 -446 455 C
+ATOM 590 CA BVAL A 73 0.344 -24.718 15.304 0.25 22.97 C
+ANISOU 590 CA BVAL A 73 2623 2875 3231 -89 -448 461 C
+ATOM 591 C AVAL A 73 1.668 -24.214 15.976 0.75 21.47 C
+ANISOU 591 C AVAL A 73 2429 2701 3030 -34 -389 407 C
+ATOM 592 C BVAL A 73 1.640 -24.244 15.966 0.25 21.72 C
+ANISOU 592 C BVAL A 73 2460 2730 3061 -36 -390 408 C
+ATOM 593 O AVAL A 73 2.283 -23.222 15.597 0.75 20.54 O
+ANISOU 593 O AVAL A 73 2341 2588 2876 -27 -367 363 O
+ATOM 594 O BVAL A 73 2.279 -23.304 15.502 0.25 21.51 O
+ANISOU 594 O BVAL A 73 2468 2705 2999 -32 -369 361 O
+ATOM 595 CB AVAL A 73 0.763 -25.565 14.001 0.75 24.81 C
+ANISOU 595 CB AVAL A 73 2938 3038 3449 -155 -460 407 C
+ATOM 596 CB BVAL A 73 0.577 -25.518 13.997 0.25 23.51 C
+ANISOU 596 CB BVAL A 73 2769 2878 3287 -159 -468 418 C
+ATOM 597 CG1AVAL A 73 1.636 -24.807 13.009 0.75 25.84 C
+ANISOU 597 CG1AVAL A 73 3138 3149 3532 -169 -432 334 C
+ATOM 598 CG1BVAL A 73 1.798 -26.431 14.097 0.25 24.00 C
+ANISOU 598 CG1BVAL A 73 2857 2897 3364 -147 -422 361 C
+ATOM 599 CG2AVAL A 73 1.436 -26.868 14.414 0.75 25.38 C
+ANISOU 599 CG2AVAL A 73 3009 3074 3558 -147 -435 388 C
+ATOM 600 CG2BVAL A 73 -0.667 -26.320 13.638 0.25 23.85 C
+ANISOU 600 CG2BVAL A 73 2809 2903 3351 -215 -535 482 C
+ATOM 601 N GLN A 74 2.014 -24.909 17.059 1.00 20.75 N
+ANISOU 601 N GLN A 74 2292 2618 2972 2 -370 423 N
+ATOM 602 CA GLN A 74 3.186 -24.589 17.836 1.00 19.17 C
+ANISOU 602 CA GLN A 74 2079 2433 2770 46 -327 391 C
+ATOM 603 C GLN A 74 4.454 -25.134 17.203 1.00 18.22 C
+ANISOU 603 C GLN A 74 2000 2265 2658 28 -296 331 C
+ATOM 604 O GLN A 74 4.478 -26.264 16.693 1.00 18.47 O
+ANISOU 604 O GLN A 74 2053 2250 2715 -2 -298 324 O
+ATOM 605 CB GLN A 74 3.034 -25.162 19.243 1.00 19.18 C
+ANISOU 605 CB GLN A 74 2017 2464 2807 86 -322 440 C
+ATOM 606 CG GLN A 74 3.779 -24.366 20.307 1.00 19.39 C
+ANISOU 606 CG GLN A 74 2025 2529 2815 135 -293 433 C
+ATOM 607 CD GLN A 74 3.183 -23.013 20.563 1.00 21.32 C
+ANISOU 607 CD GLN A 74 2277 2810 3015 159 -294 447 C
+ATOM 608 OE1 GLN A 74 2.013 -22.747 20.265 1.00 21.97 O
+ANISOU 608 OE1 GLN A 74 2352 2901 3093 154 -314 487 O
+ATOM 609 NE2 GLN A 74 3.972 -22.133 21.159 1.00 21.51 N
+ANISOU 609 NE2 GLN A 74 2313 2853 3008 187 -273 422 N
+ATOM 610 N LEU A 75 5.519 -24.334 17.242 1.00 17.05 N
+ANISOU 610 N LEU A 75 1864 2124 2489 49 -264 291 N
+ATOM 611 CA LEU A 75 6.809 -24.770 16.729 1.00 17.04 C
+ANISOU 611 CA LEU A 75 1892 2081 2503 42 -224 246 C
+ATOM 612 C LEU A 75 7.735 -25.145 17.865 1.00 16.56 C
+ANISOU 612 C LEU A 75 1778 2034 2479 79 -199 263 C
+ATOM 613 O LEU A 75 7.725 -24.505 18.912 1.00 17.40 O
+ANISOU 613 O LEU A 75 1848 2187 2575 108 -208 287 O
+ATOM 614 CB LEU A 75 7.454 -23.702 15.837 1.00 17.69 C
+ANISOU 614 CB LEU A 75 2020 2155 2545 34 -207 199 C
+ATOM 615 CG LEU A 75 6.621 -23.233 14.636 1.00 19.89 C
+ANISOU 615 CG LEU A 75 2354 2421 2782 -7 -233 183 C
+ATOM 616 CD1 LEU A 75 7.402 -22.256 13.792 1.00 20.45 C
+ANISOU 616 CD1 LEU A 75 2468 2484 2818 -12 -210 136 C
+ATOM 617 CD2 LEU A 75 6.150 -24.405 13.778 1.00 21.66 C
+ANISOU 617 CD2 LEU A 75 2622 2593 3016 -52 -245 178 C
+ATOM 618 N ARG A 76 8.516 -26.197 17.669 1.00 14.98 N
+ANISOU 618 N ARG A 76 1580 1790 2321 75 -166 253 N
+ATOM 619 CA ARG A 76 9.440 -26.670 18.686 1.00 14.65 C
+ANISOU 619 CA ARG A 76 1483 1758 2325 104 -142 278 C
+ATOM 620 C ARG A 76 10.784 -25.974 18.535 1.00 15.18 C
+ANISOU 620 C ARG A 76 1556 1822 2391 115 -110 257 C
+ATOM 621 O ARG A 76 11.405 -26.099 17.487 1.00 16.02 O
+ANISOU 621 O ARG A 76 1705 1882 2501 103 -73 224 O
+ATOM 622 CB ARG A 76 9.611 -28.184 18.570 1.00 15.16 C
+ANISOU 622 CB ARG A 76 1542 1774 2447 98 -118 289 C
+ATOM 623 CG ARG A 76 10.429 -28.788 19.702 1.00 15.73 C
+ANISOU 623 CG ARG A 76 1544 1859 2574 127 -99 329 C
+ATOM 624 CD ARG A 76 10.493 -30.311 19.588 1.00 16.39 C
+ANISOU 624 CD ARG A 76 1620 1890 2716 122 -73 342 C
+ATOM 625 NE ARG A 76 9.152 -30.898 19.628 1.00 17.45 N
+ANISOU 625 NE ARG A 76 1758 2025 2848 104 -115 359 N
+ATOM 626 CZ ARG A 76 8.486 -31.179 20.744 1.00 18.47 C
+ANISOU 626 CZ ARG A 76 1826 2198 2994 120 -148 409 C
+ATOM 627 NH1 ARG A 76 9.049 -30.980 21.932 1.00 17.24 N
+ANISOU 627 NH1 ARG A 76 1608 2087 2855 151 -144 443 N
+ATOM 628 NH2 ARG A 76 7.256 -31.675 20.681 1.00 18.11 N
+ANISOU 628 NH2 ARG A 76 1781 2151 2948 101 -186 432 N
+ATOM 629 N VAL A 77 11.234 -25.254 19.574 1.00 14.60 N
+ANISOU 629 N VAL A 77 1442 1795 2310 136 -124 281 N
+ATOM 630 CA VAL A 77 12.504 -24.530 19.581 1.00 14.79 C
+ANISOU 630 CA VAL A 77 1462 1822 2336 142 -106 274 C
+ATOM 631 C VAL A 77 13.634 -25.433 20.060 1.00 15.27 C
+ANISOU 631 C VAL A 77 1473 1863 2465 153 -74 309 C
+ATOM 632 O VAL A 77 13.610 -25.910 21.200 1.00 15.58 O
+ANISOU 632 O VAL A 77 1462 1929 2530 164 -91 352 O
+ATOM 633 CB VAL A 77 12.396 -23.241 20.417 1.00 14.63 C
+ANISOU 633 CB VAL A 77 1438 1855 2267 150 -144 283 C
+ATOM 634 CG1 VAL A 77 13.738 -22.496 20.457 1.00 15.23 C
+ANISOU 634 CG1 VAL A 77 1508 1931 2347 148 -136 284 C
+ATOM 635 CG2 VAL A 77 11.286 -22.353 19.859 1.00 15.19 C
+ANISOU 635 CG2 VAL A 77 1555 1939 2278 143 -166 254 C
+ATOM 636 N ILE A 78 14.606 -25.704 19.183 1.00 14.95 N
+ANISOU 636 N ILE A 78 1447 1776 2457 151 -24 296 N
+ATOM 637 CA ILE A 78 15.726 -26.579 19.519 1.00 15.44 C
+ANISOU 637 CA ILE A 78 1458 1813 2595 165 18 339 C
+ATOM 638 C ILE A 78 17.072 -25.865 19.681 1.00 15.44 C
+ANISOU 638 C ILE A 78 1428 1822 2617 169 29 366 C
+ATOM 639 O ILE A 78 18.089 -26.513 19.933 1.00 16.12 O
+ANISOU 639 O ILE A 78 1463 1887 2773 181 65 414 O
+ATOM 640 CB ILE A 78 15.821 -27.724 18.493 1.00 16.42 C
+ANISOU 640 CB ILE A 78 1617 1865 2757 167 81 319 C
+ATOM 641 CG1 ILE A 78 16.122 -27.179 17.085 1.00 17.67 C
+ANISOU 641 CG1 ILE A 78 1846 1983 2883 159 119 270 C
+ATOM 642 CG2 ILE A 78 14.532 -28.525 18.490 1.00 16.90 C
+ANISOU 642 CG2 ILE A 78 1700 1918 2805 156 57 305 C
+ATOM 643 CD1 ILE A 78 16.430 -28.295 16.044 1.00 18.94 C
+ANISOU 643 CD1 ILE A 78 2057 2061 3078 164 196 251 C
+ATOM 644 N GLY A 79 17.071 -24.547 19.607 1.00 15.03 N
+ANISOU 644 N GLY A 79 1401 1801 2510 159 -6 346 N
+ATOM 645 CA GLY A 79 18.273 -23.758 19.811 1.00 15.04 C
+ANISOU 645 CA GLY A 79 1374 1814 2527 155 -10 377 C
+ATOM 646 C GLY A 79 17.946 -22.286 19.759 1.00 15.10 C
+ANISOU 646 C GLY A 79 1422 1855 2460 141 -57 345 C
+ATOM 647 O GLY A 79 16.938 -21.896 19.168 1.00 14.94 O
+ANISOU 647 O GLY A 79 1454 1836 2384 138 -65 295 O
+ATOM 648 N HIS A 80 18.773 -21.465 20.388 1.00 14.85 N
+ANISOU 648 N HIS A 80 1366 1849 2427 130 -91 379 N
+ATOM 649 CA HIS A 80 18.582 -20.020 20.321 1.00 14.66 C
+ANISOU 649 CA HIS A 80 1385 1849 2335 116 -132 350 C
+ATOM 650 C HIS A 80 19.904 -19.333 20.423 1.00 15.30 C
+ANISOU 650 C HIS A 80 1440 1931 2443 101 -145 390 C
+ATOM 651 O HIS A 80 20.814 -19.802 21.123 1.00 15.86 O
+ANISOU 651 O HIS A 80 1452 2003 2570 95 -151 455 O
+ATOM 652 CB HIS A 80 17.588 -19.490 21.366 1.00 14.91 C
+ANISOU 652 CB HIS A 80 1439 1924 2301 114 -188 341 C
+ATOM 653 CG HIS A 80 18.070 -19.617 22.771 1.00 16.66 C
+ANISOU 653 CG HIS A 80 1623 2172 2534 105 -229 397 C
+ATOM 654 ND1 HIS A 80 17.910 -20.787 23.482 1.00 17.48 N
+ANISOU 654 ND1 HIS A 80 1682 2281 2678 115 -222 432 N
+ATOM 655 CD2 HIS A 80 18.705 -18.716 23.556 1.00 17.84 C
+ANISOU 655 CD2 HIS A 80 1778 2344 2659 82 -280 424 C
+ATOM 656 CE1 HIS A 80 18.440 -20.563 24.674 1.00 18.30 C
+ANISOU 656 CE1 HIS A 80 1764 2412 2779 98 -268 480 C
+ATOM 657 NE2 HIS A 80 18.929 -19.326 24.760 1.00 18.47 N
+ANISOU 657 NE2 HIS A 80 1818 2442 2758 76 -306 477 N
+ATOM 658 N SER A 81 20.031 -18.237 19.705 1.00 14.84 N
+ANISOU 658 N SER A 81 1420 1870 2347 92 -151 359 N
+ATOM 659 CA SER A 81 21.265 -17.465 19.755 1.00 14.86 C
+ANISOU 659 CA SER A 81 1398 1873 2373 74 -171 401 C
+ATOM 660 C SER A 81 20.972 -16.018 19.462 1.00 14.66 C
+ANISOU 660 C SER A 81 1430 1863 2279 59 -208 359 C
+ATOM 661 O SER A 81 19.970 -15.697 18.822 1.00 15.19 O
+ANISOU 661 O SER A 81 1548 1929 2294 69 -196 299 O
+ATOM 662 CB SER A 81 22.291 -18.011 18.768 1.00 16.73 C
+ANISOU 662 CB SER A 81 1600 2070 2686 87 -103 429 C
+ATOM 663 OG SER A 81 21.809 -17.919 17.441 1.00 20.31 O
+ANISOU 663 OG SER A 81 2105 2497 3114 102 -53 368 O
+ATOM 664 N AMET A 82 21.828 -15.125 19.951 0.50 14.30 N
+ANISOU 664 N AMET A 82 1375 1829 2230 32 -258 397 N
+ATOM 665 N BMET A 82 21.839 -15.141 19.938 0.50 14.04 N
+ANISOU 665 N BMET A 82 1341 1796 2199 33 -256 397 N
+ATOM 666 CA AMET A 82 21.664 -13.700 19.723 0.50 14.74 C
+ANISOU 666 CA AMET A 82 1484 1893 2223 16 -295 362 C
+ATOM 667 CA BMET A 82 21.699 -13.721 19.712 0.50 14.21 C
+ANISOU 667 CA BMET A 82 1415 1826 2160 16 -294 364 C
+ATOM 668 C AMET A 82 22.712 -13.224 18.723 0.50 15.23 C
+ANISOU 668 C AMET A 82 1526 1934 2328 10 -272 382 C
+ATOM 669 C BMET A 82 22.718 -13.294 18.664 0.50 14.88 C
+ANISOU 669 C BMET A 82 1480 1888 2288 12 -266 382 C
+ATOM 670 O AMET A 82 23.905 -13.470 18.919 0.50 16.17 O
+ANISOU 670 O AMET A 82 1586 2045 2514 -2 -274 453 O
+ATOM 671 O BMET A 82 23.890 -13.665 18.753 0.50 15.61 O
+ANISOU 671 O BMET A 82 1511 1969 2453 5 -257 451 O
+ATOM 672 CB AMET A 82 21.801 -12.929 21.041 0.50 15.23 C
+ANISOU 672 CB AMET A 82 1567 1980 2242 -15 -375 388 C
+ATOM 673 CB BMET A 82 21.937 -12.966 21.026 0.50 14.18 C
+ANISOU 673 CB BMET A 82 1426 1844 2116 -17 -375 395 C
+ATOM 674 CG AMET A 82 21.614 -11.442 20.874 0.50 17.47 C
+ANISOU 674 CG AMET A 82 1915 2267 2458 -31 -413 351 C
+ATOM 675 CG BMET A 82 21.759 -11.474 20.898 0.50 15.64 C
+ANISOU 675 CG BMET A 82 1675 2033 2234 -34 -415 359 C
+ATOM 676 SD AMET A 82 21.828 -10.548 22.424 0.50 20.86 S
+ANISOU 676 SD AMET A 82 2388 2711 2825 -73 -506 379 S
+ATOM 677 SD BMET A 82 21.374 -10.707 22.484 0.50 15.97 S
+ANISOU 677 SD BMET A 82 1780 2095 2192 -61 -495 362 S
+ATOM 678 CE AMET A 82 20.402 -11.108 23.302 0.50 20.46 C
+ANISOU 678 CE AMET A 82 2376 2679 2717 -43 -496 344 C
+ATOM 679 CE BMET A 82 22.877 -11.090 23.413 0.50 12.42 C
+ANISOU 679 CE BMET A 82 1267 1648 1803 -108 -552 463 C
+ATOM 680 N GLN A 83 22.270 -12.561 17.647 1.00 15.01 N
+ANISOU 680 N GLN A 83 1542 1897 2265 19 -248 327 N
+ATOM 681 CA GLN A 83 23.164 -12.017 16.627 1.00 15.04 C
+ANISOU 681 CA GLN A 83 1533 1881 2299 16 -223 341 C
+ATOM 682 C GLN A 83 22.849 -10.536 16.608 1.00 13.84 C
+ANISOU 682 C GLN A 83 1433 1744 2080 -4 -275 308 C
+ATOM 683 O GLN A 83 21.761 -10.157 16.187 1.00 14.15 O
+ANISOU 683 O GLN A 83 1526 1789 2062 6 -269 245 O
+ATOM 684 CB GLN A 83 22.915 -12.619 15.247 1.00 17.78 C
+ANISOU 684 CB GLN A 83 1894 2200 2662 45 -140 304 C
+ATOM 685 CG GLN A 83 23.871 -12.027 14.206 1.00 22.38 C
+ANISOU 685 CG GLN A 83 2466 2763 3275 46 -109 324 C
+ATOM 686 CD GLN A 83 23.630 -12.527 12.802 1.00 27.19 C
+ANISOU 686 CD GLN A 83 3106 3341 3886 72 -26 284 C
+ATOM 687 OE1 GLN A 83 22.667 -13.246 12.515 1.00 27.58 O
+ANISOU 687 OE1 GLN A 83 3192 3381 3906 83 1 235 O
+ATOM 688 NE2 GLN A 83 24.504 -12.142 11.883 1.00 28.65 N
+ANISOU 688 NE2 GLN A 83 3279 3504 4102 79 15 307 N
+ATOM 689 N ASN A 84 23.741 -9.705 17.152 1.00 13.13 N
+ANISOU 689 N ASN A 84 1329 1659 1999 -36 -333 354 N
+ATOM 690 CA ASN A 84 23.516 -8.266 17.264 1.00 12.86 C
+ANISOU 690 CA ASN A 84 1351 1634 1902 -59 -388 327 C
+ATOM 691 C ASN A 84 22.187 -8.003 18.043 1.00 12.30 C
+ANISOU 691 C ASN A 84 1344 1580 1748 -53 -415 273 C
+ATOM 692 O ASN A 84 22.073 -8.505 19.170 1.00 13.18 O
+ANISOU 692 O ASN A 84 1453 1703 1853 -60 -442 295 O
+ATOM 693 CB ASN A 84 23.643 -7.595 15.893 1.00 13.60 C
+ANISOU 693 CB ASN A 84 1455 1714 1997 -50 -352 300 C
+ATOM 694 CG ASN A 84 24.979 -7.902 15.287 1.00 16.97 C
+ANISOU 694 CG ASN A 84 1817 2124 2509 -50 -321 365 C
+ATOM 695 OD1 ASN A 84 26.030 -7.659 15.897 1.00 18.65 O
+ANISOU 695 OD1 ASN A 84 1987 2336 2761 -80 -368 437 O
+ATOM 696 ND2 ASN A 84 24.965 -8.478 14.103 1.00 17.35 N
+ANISOU 696 ND2 ASN A 84 1855 2154 2584 -19 -241 348 N
+ATOM 697 N CYS A 85 21.183 -7.327 17.448 1.00 11.65 N
+ANISOU 697 N CYS A 85 1317 1500 1611 -38 -400 211 N
+ATOM 698 CA CYS A 85 19.935 -7.077 18.150 1.00 11.74 C
+ANISOU 698 CA CYS A 85 1382 1524 1553 -26 -414 172 C
+ATOM 699 C CYS A 85 18.805 -8.021 17.785 1.00 11.93 C
+ANISOU 699 C CYS A 85 1403 1555 1577 7 -364 141 C
+ATOM 700 O CYS A 85 17.658 -7.743 18.135 1.00 12.25 O
+ANISOU 700 O CYS A 85 1484 1605 1564 22 -366 113 O
+ATOM 701 CB CYS A 85 19.518 -5.626 17.998 1.00 12.25 C
+ANISOU 701 CB CYS A 85 1510 1586 1558 -33 -439 138 C
+ATOM 702 SG CYS A 85 20.771 -4.475 18.599 1.00 14.49 S
+ANISOU 702 SG CYS A 85 1812 1858 1834 -81 -513 176 S
+ATOM 703 N VAL A 86 19.106 -9.142 17.124 1.00 11.92 N
+ANISOU 703 N VAL A 86 1354 1543 1631 17 -318 152 N
+ATOM 704 CA AVAL A 86 18.063 -10.123 16.816 0.80 12.69 C
+ANISOU 704 CA AVAL A 86 1452 1642 1728 40 -279 128 C
+ATOM 705 CA BVAL A 86 18.084 -10.108 16.770 0.20 12.62 C
+ANISOU 705 CA BVAL A 86 1442 1632 1719 40 -279 127 C
+ATOM 706 C VAL A 86 18.368 -11.466 17.447 1.00 13.31 C
+ANISOU 706 C VAL A 86 1483 1718 1854 47 -267 163 C
+ATOM 707 O VAL A 86 19.522 -11.792 17.744 1.00 13.89 O
+ANISOU 707 O VAL A 86 1515 1785 1978 36 -272 209 O
+ATOM 708 CB AVAL A 86 17.715 -10.290 15.315 0.80 13.96 C
+ANISOU 708 CB AVAL A 86 1624 1787 1895 47 -232 93 C
+ATOM 709 CB BVAL A 86 17.964 -10.163 15.216 0.20 13.40 C
+ANISOU 709 CB BVAL A 86 1550 1713 1828 44 -232 96 C
+ATOM 710 CG1AVAL A 86 17.232 -8.980 14.704 0.80 14.98 C
+ANISOU 710 CG1AVAL A 86 1797 1922 1975 41 -245 60 C
+ATOM 711 CG1BVAL A 86 17.427 -11.492 14.704 0.20 13.91 C
+ANISOU 711 CG1BVAL A 86 1607 1764 1916 57 -188 85 C
+ATOM 712 CG2AVAL A 86 18.874 -10.884 14.538 0.80 14.71 C
+ANISOU 712 CG2AVAL A 86 1683 1855 2049 46 -191 115 C
+ATOM 713 CG2BVAL A 86 17.115 -9.007 14.699 0.20 14.01 C
+ANISOU 713 CG2BVAL A 86 1676 1800 1849 42 -245 58 C
+ATOM 714 N LEU A 87 17.311 -12.214 17.743 1.00 12.95 N
+ANISOU 714 N LEU A 87 1444 1682 1797 63 -256 150 N
+ATOM 715 CA LEU A 87 17.437 -13.555 18.248 1.00 13.45 C
+ANISOU 715 CA LEU A 87 1464 1742 1906 72 -239 179 C
+ATOM 716 C LEU A 87 17.087 -14.460 17.060 1.00 12.81 C
+ANISOU 716 C LEU A 87 1383 1635 1851 82 -185 155 C
+ATOM 717 O LEU A 87 16.214 -14.148 16.232 1.00 12.84 O
+ANISOU 717 O LEU A 87 1425 1635 1819 82 -176 116 O
+ATOM 718 CB LEU A 87 16.456 -13.848 19.385 1.00 14.73 C
+ANISOU 718 CB LEU A 87 1632 1927 2037 84 -262 185 C
+ATOM 719 CG LEU A 87 16.676 -13.104 20.677 1.00 17.21 C
+ANISOU 719 CG LEU A 87 1963 2262 2314 75 -312 207 C
+ATOM 720 CD1 LEU A 87 15.555 -13.409 21.659 1.00 17.72 C
+ANISOU 720 CD1 LEU A 87 2043 2347 2342 95 -320 209 C
+ATOM 721 CD2 LEU A 87 18.026 -13.431 21.279 1.00 19.12 C
+ANISOU 721 CD2 LEU A 87 2162 2502 2602 53 -333 259 C
+ATOM 722 N LYS A 88 17.808 -15.569 16.962 1.00 12.70 N
+ANISOU 722 N LYS A 88 1328 1598 1898 87 -150 182 N
+ATOM 723 CA LYS A 88 17.600 -16.588 15.957 1.00 12.67 C
+ANISOU 723 CA LYS A 88 1334 1560 1921 95 -95 163 C
+ATOM 724 C LYS A 88 17.188 -17.806 16.736 1.00 12.90 C
+ANISOU 724 C LYS A 88 1333 1590 1978 105 -93 185 C
+ATOM 725 O LYS A 88 17.975 -18.321 17.525 1.00 13.84 O
+ANISOU 725 O LYS A 88 1402 1711 2146 109 -93 232 O
+ATOM 726 CB LYS A 88 18.899 -16.875 15.190 1.00 13.93 C
+ANISOU 726 CB LYS A 88 1473 1683 2136 100 -42 184 C
+ATOM 727 CG LYS A 88 19.258 -15.755 14.219 1.00 17.96 C
+ANISOU 727 CG LYS A 88 2015 2189 2621 92 -36 161 C
+ATOM 728 CD LYS A 88 20.490 -16.070 13.376 1.00 22.34 C
+ANISOU 728 CD LYS A 88 2553 2703 3230 103 28 185 C
+ATOM 729 CE LYS A 88 21.738 -16.137 14.208 1.00 26.94 C
+ANISOU 729 CE LYS A 88 3066 3292 3880 106 21 258 C
+ATOM 730 NZ LYS A 88 22.952 -15.999 13.363 1.00 28.94 N
+ANISOU 730 NZ LYS A 88 3299 3515 4180 116 74 291 N
+ATOM 731 N LEU A 89 15.950 -18.220 16.574 1.00 12.44 N
+ANISOU 731 N LEU A 89 1301 1534 1893 106 -97 159 N
+ATOM 732 CA LEU A 89 15.403 -19.373 17.256 1.00 12.59 C
+ANISOU 732 CA LEU A 89 1294 1554 1937 114 -98 179 C
+ATOM 733 C LEU A 89 15.367 -20.511 16.264 1.00 12.94 C
+ANISOU 733 C LEU A 89 1356 1549 2012 113 -48 163 C
+ATOM 734 O LEU A 89 14.620 -20.459 15.287 1.00 13.54 O
+ANISOU 734 O LEU A 89 1483 1607 2054 100 -42 125 O
+ATOM 735 CB LEU A 89 13.982 -19.063 17.753 1.00 12.75 C
+ANISOU 735 CB LEU A 89 1331 1607 1908 116 -137 171 C
+ATOM 736 CG LEU A 89 13.831 -17.772 18.569 1.00 13.26 C
+ANISOU 736 CG LEU A 89 1403 1710 1923 120 -178 176 C
+ATOM 737 CD1 LEU A 89 12.360 -17.539 18.932 1.00 14.00 C
+ANISOU 737 CD1 LEU A 89 1515 1830 1976 129 -200 174 C
+ATOM 738 CD2 LEU A 89 14.701 -17.814 19.810 1.00 14.04 C
+ANISOU 738 CD2 LEU A 89 1466 1827 2044 123 -197 217 C
+ATOM 739 N LYS A 90 16.203 -21.522 16.472 1.00 12.58 N
+ANISOU 739 N LYS A 90 1274 1477 2030 124 -10 194 N
+ATOM 740 CA LYS A 90 16.232 -22.674 15.595 1.00 13.10 C
+ANISOU 740 CA LYS A 90 1365 1485 2125 126 46 179 C
+ATOM 741 C LYS A 90 15.051 -23.539 15.962 1.00 13.08 C
+ANISOU 741 C LYS A 90 1366 1485 2118 120 22 178 C
+ATOM 742 O LYS A 90 14.830 -23.805 17.137 1.00 13.52 O
+ANISOU 742 O LYS A 90 1371 1575 2191 129 -8 213 O
+ATOM 743 CB LYS A 90 17.536 -23.458 15.769 1.00 15.25 C
+ANISOU 743 CB LYS A 90 1591 1726 2476 146 101 223 C
+ATOM 744 CG LYS A 90 17.687 -24.519 14.697 1.00 19.98 C
+ANISOU 744 CG LYS A 90 2237 2255 3100 152 174 202 C
+ATOM 745 CD LYS A 90 18.937 -25.357 14.862 1.00 26.70 C
+ANISOU 745 CD LYS A 90 3041 3069 4037 179 242 252 C
+ATOM 746 CE LYS A 90 18.950 -26.460 13.827 1.00 31.95 C
+ANISOU 746 CE LYS A 90 3769 3655 4717 188 320 225 C
+ATOM 747 NZ LYS A 90 20.250 -27.184 13.784 1.00 34.61 N
+ANISOU 747 NZ LYS A 90 4068 3943 5138 222 407 276 N
+ATOM 748 N VAL A 91 14.239 -23.892 14.982 1.00 13.01 N
+ANISOU 748 N VAL A 91 1419 1445 2081 102 29 140 N
+ATOM 749 CA VAL A 91 13.080 -24.738 15.204 1.00 13.59 C
+ANISOU 749 CA VAL A 91 1498 1516 2152 89 1 144 C
+ATOM 750 C VAL A 91 13.290 -26.080 14.510 1.00 13.94 C
+ANISOU 750 C VAL A 91 1577 1489 2230 84 52 133 C
+ATOM 751 O VAL A 91 14.153 -26.193 13.635 1.00 14.24 O
+ANISOU 751 O VAL A 91 1654 1478 2276 88 111 113 O
+ATOM 752 CB VAL A 91 11.760 -24.046 14.810 1.00 13.54 C
+ANISOU 752 CB VAL A 91 1528 1533 2083 64 -51 124 C
+ATOM 753 CG1 VAL A 91 11.470 -22.870 15.748 1.00 13.86 C
+ANISOU 753 CG1 VAL A 91 1531 1640 2097 79 -93 143 C
+ATOM 754 CG2 VAL A 91 11.792 -23.576 13.358 1.00 13.61 C
+ANISOU 754 CG2 VAL A 91 1613 1508 2049 39 -33 78 C
+ATOM 755 N ASP A 92 12.510 -27.098 14.887 1.00 14.52 N
+ANISOU 755 N ASP A 92 1643 1553 2322 75 33 149 N
+ATOM 756 CA ASP A 92 12.713 -28.432 14.308 1.00 15.39 C
+ANISOU 756 CA ASP A 92 1792 1588 2466 69 81 140 C
+ATOM 757 C ASP A 92 12.040 -28.640 12.940 1.00 16.15 C
+ANISOU 757 C ASP A 92 1994 1631 2511 28 81 92 C
+ATOM 758 O ASP A 92 12.151 -29.724 12.366 1.00 17.58 O
+ANISOU 758 O ASP A 92 2231 1741 2708 18 121 77 O
+ATOM 759 CB ASP A 92 12.298 -29.535 15.300 1.00 16.92 C
+ANISOU 759 CB ASP A 92 1931 1787 2710 77 64 181 C
+ATOM 760 CG ASP A 92 10.803 -29.782 15.434 1.00 21.75 C
+ANISOU 760 CG ASP A 92 2553 2417 3296 47 -3 188 C
+ATOM 761 OD1 ASP A 92 10.011 -28.950 14.931 1.00 21.92 O
+ANISOU 761 OD1 ASP A 92 2611 2460 3260 22 -45 169 O
+ATOM 762 OD2 ASP A 92 10.423 -30.804 16.052 1.00 24.89 O
+ANISOU 762 OD2 ASP A 92 2915 2806 3734 49 -14 220 O
+ATOM 763 N THR A 93 11.319 -27.629 12.442 1.00 15.46 N
+ANISOU 763 N THR A 93 1939 1574 2361 1 33 71 N
+ATOM 764 CA THR A 93 10.601 -27.740 11.184 1.00 15.98 C
+ANISOU 764 CA THR A 93 2104 1596 2373 -47 18 33 C
+ATOM 765 C THR A 93 10.936 -26.576 10.273 1.00 15.60 C
+ANISOU 765 C THR A 93 2101 1555 2272 -55 29 -2 C
+ATOM 766 O THR A 93 10.857 -25.414 10.682 1.00 15.87 O
+ANISOU 766 O THR A 93 2088 1651 2291 -43 -1 9 O
+ATOM 767 CB THR A 93 9.091 -27.772 11.474 1.00 18.02 C
+ANISOU 767 CB THR A 93 2348 1888 2611 -82 -67 59 C
+ATOM 768 OG1 THR A 93 8.807 -28.909 12.282 1.00 19.65 O
+ANISOU 768 OG1 THR A 93 2512 2085 2869 -75 -75 93 O
+ATOM 769 CG2 THR A 93 8.231 -27.818 10.214 1.00 18.56 C
+ANISOU 769 CG2 THR A 93 2512 1918 2621 -145 -103 33 C
+ATOM 770 N ALA A 94 11.321 -26.885 9.036 1.00 15.11 N
+ANISOU 770 N ALA A 94 2136 1424 2181 -75 76 -44 N
+ATOM 771 CA ALA A 94 11.580 -25.846 8.051 1.00 15.27 C
+ANISOU 771 CA ALA A 94 2209 1446 2147 -87 87 -77 C
+ATOM 772 C ALA A 94 10.227 -25.287 7.629 1.00 14.37 C
+ANISOU 772 C ALA A 94 2124 1362 1976 -140 3 -79 C
+ATOM 773 O ALA A 94 9.266 -26.049 7.472 1.00 14.40 O
+ANISOU 773 O ALA A 94 2162 1342 1968 -183 -41 -72 O
+ATOM 774 CB ALA A 94 12.280 -26.436 6.838 1.00 15.99 C
+ANISOU 774 CB ALA A 94 2408 1451 2218 -95 164 -119 C
+ATOM 775 N ASN A 95 10.133 -23.953 7.445 1.00 13.14 N
+ANISOU 775 N ASN A 95 1950 1255 1786 -141 -22 -83 N
+ATOM 776 CA ASN A 95 8.883 -23.366 6.989 1.00 12.83 C
+ANISOU 776 CA ASN A 95 1934 1243 1698 -190 -96 -76 C
+ATOM 777 C ASN A 95 8.594 -23.845 5.583 1.00 14.44 C
+ANISOU 777 C ASN A 95 2259 1381 1848 -249 -97 -111 C
+ATOM 778 O ASN A 95 9.373 -23.554 4.678 1.00 15.01 O
+ANISOU 778 O ASN A 95 2395 1421 1889 -248 -45 -150 O
+ATOM 779 CB ASN A 95 8.974 -21.836 7.015 1.00 11.70 C
+ANISOU 779 CB ASN A 95 1754 1158 1533 -175 -111 -75 C
+ATOM 780 CG ASN A 95 7.671 -21.166 6.662 1.00 12.68 C
+ANISOU 780 CG ASN A 95 1885 1314 1617 -219 -184 -54 C
+ATOM 781 OD1 ASN A 95 6.665 -21.818 6.312 1.00 12.65 O
+ANISOU 781 OD1 ASN A 95 1915 1291 1601 -268 -232 -37 O
+ATOM 782 ND2 ASN A 95 7.654 -19.854 6.755 1.00 13.33 N
+ANISOU 782 ND2 ASN A 95 1933 1446 1685 -204 -197 -48 N
+ATOM 783 N PRO A 96 7.498 -24.592 5.381 1.00 15.09 N
+ANISOU 783 N PRO A 96 2378 1442 1916 -304 -156 -95 N
+ATOM 784 CA PRO A 96 7.194 -25.071 4.022 1.00 15.91 C
+ANISOU 784 CA PRO A 96 2611 1476 1956 -371 -165 -128 C
+ATOM 785 C PRO A 96 6.869 -23.969 3.029 1.00 16.81 C
+ANISOU 785 C PRO A 96 2771 1609 2007 -411 -196 -140 C
+ATOM 786 O PRO A 96 6.955 -24.177 1.819 1.00 18.67 O
+ANISOU 786 O PRO A 96 3125 1787 2182 -458 -185 -178 O
+ATOM 787 CB PRO A 96 6.007 -26.020 4.234 1.00 16.85 C
+ANISOU 787 CB PRO A 96 2739 1579 2084 -424 -239 -91 C
+ATOM 788 CG PRO A 96 5.365 -25.537 5.452 1.00 17.21 C
+ANISOU 788 CG PRO A 96 2656 1705 2179 -394 -285 -32 C
+ATOM 789 CD PRO A 96 6.454 -24.999 6.343 1.00 15.27 C
+ANISOU 789 CD PRO A 96 2328 1500 1975 -311 -220 -40 C
+ATOM 790 N ALYS A 97 6.497 -22.792 3.536 0.50 16.18 N
+ANISOU 790 N ALYS A 97 2603 1608 1938 -391 -232 -109 N
+ATOM 791 N BLYS A 97 6.498 -22.794 3.526 0.50 15.87 N
+ANISOU 791 N BLYS A 97 2564 1568 1898 -392 -232 -109 N
+ATOM 792 CA ALYS A 97 6.197 -21.633 2.715 0.50 16.25 C
+ANISOU 792 CA ALYS A 97 2636 1643 1896 -422 -261 -113 C
+ATOM 793 CA BLYS A 97 6.186 -21.657 2.678 0.50 15.62 C
+ANISOU 793 CA BLYS A 97 2560 1561 1815 -424 -262 -113 C
+ATOM 794 C ALYS A 97 7.398 -20.685 2.599 0.50 16.20 C
+ANISOU 794 C ALYS A 97 2614 1653 1889 -368 -193 -146 C
+ATOM 795 C BLYS A 97 7.397 -20.733 2.479 0.50 15.87 C
+ANISOU 795 C BLYS A 97 2585 1605 1841 -374 -192 -149 C
+ATOM 796 O ALYS A 97 7.196 -19.507 2.312 0.50 16.30 O
+ANISOU 796 O ALYS A 97 2606 1709 1879 -373 -216 -138 O
+ATOM 797 O BLYS A 97 7.210 -19.616 1.997 0.50 15.98 O
+ANISOU 797 O BLYS A 97 2598 1652 1823 -387 -213 -148 O
+ATOM 798 CB ALYS A 97 4.997 -20.876 3.290 0.50 17.71 C
+ANISOU 798 CB ALYS A 97 2736 1897 2095 -434 -339 -50 C
+ATOM 799 CB BLYS A 97 5.028 -20.859 3.292 0.50 16.13 C
+ANISOU 799 CB BLYS A 97 2533 1698 1896 -431 -337 -51 C
+ATOM 800 CG ALYS A 97 3.707 -21.681 3.258 0.50 21.36 C
+ANISOU 800 CG ALYS A 97 3212 2347 2559 -497 -418 -3 C
+ATOM 801 CG BLYS A 97 3.787 -21.702 3.563 0.50 18.13 C
+ANISOU 801 CG BLYS A 97 2776 1946 2165 -478 -409 2 C
+ATOM 802 CD ALYS A 97 2.514 -20.817 3.626 0.50 25.21 C
+ANISOU 802 CD ALYS A 97 3618 2900 3060 -508 -487 69 C
+ATOM 803 CD BLYS A 97 2.659 -20.874 4.168 0.50 20.47 C
+ANISOU 803 CD BLYS A 97 2981 2314 2485 -476 -472 74 C
+ATOM 804 CE ALYS A 97 1.247 -21.628 3.735 0.50 28.84 C
+ANISOU 804 CE ALYS A 97 4069 3352 3536 -564 -565 134 C
+ATOM 805 CE BLYS A 97 1.497 -21.748 4.586 0.50 23.28 C
+ANISOU 805 CE BLYS A 97 3308 2666 2870 -513 -538 139 C
+ATOM 806 NZ ALYS A 97 1.311 -22.583 4.872 0.50 31.00 N
+ANISOU 806 NZ ALYS A 97 4286 3624 3867 -522 -549 151 N
+ATOM 807 NZ BLYS A 97 0.450 -20.970 5.306 0.50 24.86 N
+ANISOU 807 NZ BLYS A 97 3407 2934 3103 -497 -582 220 N
+ATOM 808 N THR A 98 8.635 -21.173 2.838 1.00 15.64 N
+ANISOU 808 N THR A 98 2547 1549 1848 -317 -110 -174 N
+ATOM 809 CA THR A 98 9.819 -20.315 2.707 1.00 15.75 C
+ANISOU 809 CA THR A 98 2542 1576 1867 -270 -48 -195 C
+ATOM 810 C THR A 98 10.036 -19.955 1.256 1.00 17.30 C
+ANISOU 810 C THR A 98 2842 1736 1997 -305 -26 -232 C
+ATOM 811 O THR A 98 10.207 -20.836 0.419 1.00 18.89 O
+ANISOU 811 O THR A 98 3148 1866 2165 -332 9 -263 O
+ATOM 812 CB THR A 98 11.098 -20.973 3.223 1.00 15.79 C
+ANISOU 812 CB THR A 98 2523 1549 1925 -210 37 -202 C
+ATOM 813 OG1 THR A 98 10.913 -21.371 4.576 1.00 14.95 O
+ANISOU 813 OG1 THR A 98 2326 1476 1878 -181 15 -166 O
+ATOM 814 CG2 THR A 98 12.291 -20.020 3.161 1.00 16.33 C
+ANISOU 814 CG2 THR A 98 2558 1638 2009 -164 90 -207 C
+ATOM 815 N PRO A 99 9.971 -18.662 0.943 1.00 17.35 N
+ANISOU 815 N PRO A 99 2825 1788 1980 -308 -48 -229 N
+ATOM 816 CA PRO A 99 10.220 -18.251 -0.440 1.00 17.36 C
+ANISOU 816 CA PRO A 99 2921 1759 1916 -340 -26 -262 C
+ATOM 817 C PRO A 99 11.719 -18.183 -0.682 1.00 17.89 C
+ANISOU 817 C PRO A 99 3000 1796 2001 -284 75 -286 C
+ATOM 818 O PRO A 99 12.539 -18.301 0.246 1.00 18.10 O
+ANISOU 818 O PRO A 99 2949 1834 2093 -225 117 -271 O
+ATOM 819 CB PRO A 99 9.616 -16.844 -0.472 1.00 17.74 C
+ANISOU 819 CB PRO A 99 2916 1876 1950 -354 -86 -239 C
+ATOM 820 CG PRO A 99 9.944 -16.303 0.908 1.00 18.63 C
+ANISOU 820 CG PRO A 99 2906 2044 2130 -291 -83 -211 C
+ATOM 821 CD PRO A 99 9.806 -17.493 1.835 1.00 16.90 C
+ANISOU 821 CD PRO A 99 2660 1807 1953 -276 -83 -197 C
+ATOM 822 N LYS A 100 12.124 -17.929 -1.950 1.00 18.01 N
+ANISOU 822 N LYS A 100 3110 1775 1960 -303 116 -318 N
+ATOM 823 CA LYS A 100 13.535 -17.625 -2.236 1.00 17.86 C
+ANISOU 823 CA LYS A 100 3088 1736 1961 -246 211 -328 C
+ATOM 824 C LYS A 100 13.794 -16.281 -1.557 1.00 16.86 C
+ANISOU 824 C LYS A 100 2847 1688 1873 -214 182 -300 C
+ATOM 825 O LYS A 100 12.915 -15.410 -1.609 1.00 17.12 O
+ANISOU 825 O LYS A 100 2856 1769 1878 -249 106 -290 O
+ATOM 826 CB LYS A 100 13.781 -17.459 -3.727 1.00 20.30 C
+ANISOU 826 CB LYS A 100 3518 2000 2196 -274 254 -363 C
+ATOM 827 CG LYS A 100 13.806 -18.781 -4.460 1.00 25.36 C
+ANISOU 827 CG LYS A 100 4294 2549 2793 -297 305 -396 C
+ATOM 828 CD LYS A 100 13.957 -18.552 -5.942 1.00 30.62 C
+ANISOU 828 CD LYS A 100 5093 3170 3371 -332 340 -431 C
+ATOM 829 CE LYS A 100 13.870 -19.846 -6.690 1.00 34.80 C
+ANISOU 829 CE LYS A 100 5777 3601 3843 -365 383 -468 C
+ATOM 830 NZ LYS A 100 13.923 -19.616 -8.154 1.00 37.87 N
+ANISOU 830 NZ LYS A 100 6311 3946 4134 -404 413 -503 N
+ATOM 831 N TYR A 101 14.880 -16.181 -0.805 1.00 16.48 N
+ANISOU 831 N TYR A 101 2722 1649 1891 -152 233 -279 N
+ATOM 832 CA TYR A 101 15.128 -14.952 -0.066 1.00 16.55 C
+ANISOU 832 CA TYR A 101 2629 1725 1935 -127 198 -252 C
+ATOM 833 C TYR A 101 16.581 -14.602 0.070 1.00 17.45 C
+ANISOU 833 C TYR A 101 2697 1834 2099 -73 267 -232 C
+ATOM 834 O TYR A 101 17.465 -15.432 -0.117 1.00 18.21 O
+ANISOU 834 O TYR A 101 2816 1879 2224 -42 348 -229 O
+ATOM 835 CB TYR A 101 14.446 -14.990 1.329 1.00 15.77 C
+ANISOU 835 CB TYR A 101 2444 1674 1873 -121 131 -225 C
+ATOM 836 CG TYR A 101 15.146 -15.902 2.316 1.00 15.73 C
+ANISOU 836 CG TYR A 101 2390 1652 1934 -80 170 -204 C
+ATOM 837 CD1 TYR A 101 14.886 -17.261 2.336 1.00 15.94 C
+ANISOU 837 CD1 TYR A 101 2457 1632 1967 -88 191 -212 C
+ATOM 838 CD2 TYR A 101 16.069 -15.402 3.228 1.00 16.30 C
+ANISOU 838 CD2 TYR A 101 2376 1754 2064 -37 181 -172 C
+ATOM 839 CE1 TYR A 101 15.528 -18.107 3.223 1.00 17.03 C
+ANISOU 839 CE1 TYR A 101 2546 1755 2170 -49 228 -188 C
+ATOM 840 CE2 TYR A 101 16.721 -16.242 4.126 1.00 16.87 C
+ANISOU 840 CE2 TYR A 101 2398 1813 2199 -3 212 -144 C
+ATOM 841 CZ TYR A 101 16.426 -17.592 4.137 1.00 18.00 C
+ANISOU 841 CZ TYR A 101 2577 1913 2351 -8 236 -152 C
+ATOM 842 OH TYR A 101 17.050 -18.451 5.005 1.00 19.69 O
+ANISOU 842 OH TYR A 101 2740 2112 2629 25 269 -122 O
+ATOM 843 N LYS A 102 16.813 -13.342 0.419 1.00 17.07 N
+ANISOU 843 N LYS A 102 2583 1839 2065 -62 232 -213 N
+ATOM 844 CA LYS A 102 18.117 -12.782 0.702 1.00 17.29 C
+ANISOU 844 CA LYS A 102 2549 1875 2147 -18 273 -181 C
+ATOM 845 C LYS A 102 17.931 -11.785 1.830 1.00 17.01 C
+ANISOU 845 C LYS A 102 2427 1902 2135 -15 200 -157 C
+ATOM 846 O LYS A 102 16.841 -11.228 2.005 1.00 17.36 O
+ANISOU 846 O LYS A 102 2472 1982 2143 -44 132 -169 O
+ATOM 847 CB LYS A 102 18.666 -12.018 -0.521 1.00 19.57 C
+ANISOU 847 CB LYS A 102 2879 2152 2405 -19 314 -190 C
+ATOM 848 CG LYS A 102 19.172 -12.891 -1.652 1.00 25.57 C
+ANISOU 848 CG LYS A 102 3730 2843 3144 -9 408 -209 C
+ATOM 849 CD LYS A 102 19.560 -12.019 -2.838 1.00 30.51 C
+ANISOU 849 CD LYS A 102 4398 3464 3730 -13 439 -217 C
+ATOM 850 CE LYS A 102 19.942 -12.850 -4.039 1.00 34.71 C
+ANISOU 850 CE LYS A 102 5043 3923 4223 -8 534 -241 C
+ATOM 851 NZ LYS A 102 20.222 -11.998 -5.223 1.00 37.67 N
+ANISOU 851 NZ LYS A 102 5466 4297 4550 -15 561 -250 N
+ATOM 852 N PHE A 103 18.997 -11.533 2.573 1.00 16.41 N
+ANISOU 852 N PHE A 103 2279 1836 2119 18 214 -118 N
+ATOM 853 CA PHE A 103 18.994 -10.484 3.584 1.00 16.22 C
+ANISOU 853 CA PHE A 103 2188 1863 2111 19 147 -95 C
+ATOM 854 C PHE A 103 19.847 -9.382 3.004 1.00 16.98 C
+ANISOU 854 C PHE A 103 2271 1966 2214 25 161 -80 C
+ATOM 855 O PHE A 103 20.994 -9.634 2.601 1.00 18.29 O
+ANISOU 855 O PHE A 103 2426 2103 2420 50 225 -52 O
+ATOM 856 CB PHE A 103 19.613 -10.957 4.902 1.00 15.69 C
+ANISOU 856 CB PHE A 103 2052 1803 2106 41 140 -53 C
+ATOM 857 CG PHE A 103 18.795 -11.943 5.708 1.00 15.24 C
+ANISOU 857 CG PHE A 103 1993 1748 2051 38 119 -60 C
+ATOM 858 CD1 PHE A 103 17.445 -12.132 5.446 1.00 15.08 C
+ANISOU 858 CD1 PHE A 103 2018 1733 1978 12 87 -95 C
+ATOM 859 CD2 PHE A 103 19.352 -12.609 6.784 1.00 15.50 C
+ANISOU 859 CD2 PHE A 103 1970 1780 2139 57 123 -22 C
+ATOM 860 CE1 PHE A 103 16.690 -13.014 6.217 1.00 15.35 C
+ANISOU 860 CE1 PHE A 103 2043 1770 2018 10 65 -93 C
+ATOM 861 CE2 PHE A 103 18.597 -13.493 7.545 1.00 15.76 C
+ANISOU 861 CE2 PHE A 103 1998 1817 2174 55 102 -25 C
+ATOM 862 CZ PHE A 103 17.267 -13.671 7.274 1.00 15.43 C
+ANISOU 862 CZ PHE A 103 2000 1780 2082 33 73 -60 C
+ATOM 863 N VAL A 104 19.279 -8.182 2.889 1.00 16.37 N
+ANISOU 863 N VAL A 104 2197 1924 2100 5 107 -93 N
+ATOM 864 CA VAL A 104 20.033 -7.044 2.376 1.00 17.50 C
+ANISOU 864 CA VAL A 104 2324 2076 2249 8 110 -77 C
+ATOM 865 C VAL A 104 19.980 -5.887 3.348 1.00 17.45 C
+ANISOU 865 C VAL A 104 2271 2109 2250 2 39 -60 C
+ATOM 866 O VAL A 104 18.977 -5.694 4.025 1.00 18.38 O
+ANISOU 866 O VAL A 104 2392 2249 2341 -10 -12 -76 O
+ATOM 867 CB VAL A 104 19.568 -6.605 0.972 1.00 19.51 C
+ANISOU 867 CB VAL A 104 2641 2325 2449 -12 127 -110 C
+ATOM 868 CG1 VAL A 104 19.602 -7.772 -0.011 1.00 20.51 C
+ANISOU 868 CG1 VAL A 104 2834 2403 2554 -11 197 -131 C
+ATOM 869 CG2 VAL A 104 18.188 -5.980 1.030 1.00 21.03 C
+ANISOU 869 CG2 VAL A 104 2852 2550 2590 -44 60 -136 C
+ATOM 870 N ARG A 105 21.056 -5.114 3.423 1.00 15.80 N
+ANISOU 870 N ARG A 105 2023 1904 2078 10 37 -24 N
+ATOM 871 CA ARG A 105 21.085 -3.918 4.245 1.00 15.43 C
+ANISOU 871 CA ARG A 105 1946 1886 2031 -1 -31 -9 C
+ATOM 872 C ARG A 105 20.948 -2.766 3.265 1.00 16.07 C
+ANISOU 872 C ARG A 105 2048 1975 2081 -13 -37 -24 C
+ATOM 873 O ARG A 105 21.814 -2.585 2.403 1.00 16.45 O
+ANISOU 873 O ARG A 105 2089 2009 2150 -6 4 -4 O
+ATOM 874 CB ARG A 105 22.391 -3.812 5.050 1.00 15.61 C
+ANISOU 874 CB ARG A 105 1910 1905 2118 7 -42 50 C
+ATOM 875 CG ARG A 105 22.422 -2.551 5.896 1.00 16.10 C
+ANISOU 875 CG ARG A 105 1958 1989 2171 -12 -119 62 C
+ATOM 876 CD ARG A 105 23.630 -2.518 6.815 1.00 16.65 C
+ANISOU 876 CD ARG A 105 1972 2054 2298 -16 -147 126 C
+ATOM 877 NE ARG A 105 23.615 -1.344 7.690 1.00 16.81 N
+ANISOU 877 NE ARG A 105 1998 2089 2299 -42 -226 133 N
+ATOM 878 CZ ARG A 105 22.963 -1.276 8.847 1.00 17.76 C
+ANISOU 878 CZ ARG A 105 2140 2221 2387 -51 -276 117 C
+ATOM 879 NH1 ARG A 105 22.257 -2.313 9.283 1.00 15.50 N
+ANISOU 879 NH1 ARG A 105 1863 1938 2090 -38 -257 96 N
+ATOM 880 NH2 ARG A 105 23.019 -0.174 9.580 1.00 16.68 N
+ANISOU 880 NH2 ARG A 105 2021 2088 2227 -74 -342 122 N
+ATOM 881 N ILE A 106 19.843 -2.020 3.359 1.00 16.34 N
+ANISOU 881 N ILE A 106 2107 2033 2069 -30 -83 -53 N
+ATOM 882 CA ILE A 106 19.591 -0.952 2.403 1.00 17.54 C
+ANISOU 882 CA ILE A 106 2279 2195 2192 -43 -89 -66 C
+ATOM 883 C ILE A 106 20.273 0.351 2.775 1.00 18.38 C
+ANISOU 883 C ILE A 106 2356 2311 2318 -47 -128 -40 C
+ATOM 884 O ILE A 106 20.686 0.548 3.914 1.00 18.30 O
+ANISOU 884 O ILE A 106 2320 2302 2331 -46 -166 -18 O
+ATOM 885 CB ILE A 106 18.079 -0.754 2.154 1.00 18.39 C
+ANISOU 885 CB ILE A 106 2423 2319 2246 -60 -113 -99 C
+ATOM 886 CG1 ILE A 106 17.349 -0.412 3.456 1.00 18.46 C
+ANISOU 886 CG1 ILE A 106 2423 2345 2247 -57 -162 -99 C
+ATOM 887 CG2 ILE A 106 17.482 -1.941 1.420 1.00 19.36 C
+ANISOU 887 CG2 ILE A 106 2585 2427 2345 -68 -76 -122 C
+ATOM 888 CD1 ILE A 106 15.965 0.091 3.254 1.00 19.73 C
+ANISOU 888 CD1 ILE A 106 2607 2523 2368 -69 -185 -114 C
+ATOM 889 N GLN A 107 20.428 1.226 1.782 1.00 19.23 N
+ANISOU 889 N GLN A 107 2470 2421 2414 -55 -122 -41 N
+ATOM 890 CA GLN A 107 20.997 2.545 1.964 1.00 19.73 C
+ANISOU 890 CA GLN A 107 2511 2492 2493 -62 -161 -18 C
+ATOM 891 C GLN A 107 19.865 3.537 2.207 1.00 18.47 C
+ANISOU 891 C GLN A 107 2377 2349 2291 -75 -206 -44 C
+ATOM 892 O GLN A 107 18.742 3.340 1.721 1.00 17.38 O
+ANISOU 892 O GLN A 107 2268 2221 2116 -80 -196 -72 O
+ATOM 893 CB GLN A 107 21.745 2.950 0.676 1.00 23.23 C
+ANISOU 893 CB GLN A 107 2947 2930 2949 -61 -123 -1 C
+ATOM 894 CG GLN A 107 22.876 1.997 0.305 1.00 29.27 C
+ANISOU 894 CG GLN A 107 3689 3673 3760 -41 -61 33 C
+ATOM 895 CD GLN A 107 24.026 2.049 1.285 1.00 36.32 C
+ANISOU 895 CD GLN A 107 4527 4559 4716 -36 -86 88 C
+ATOM 896 OE1 GLN A 107 24.225 3.026 2.019 1.00 38.70 O
+ANISOU 896 OE1 GLN A 107 4809 4869 5026 -53 -152 106 O
+ATOM 897 NE2 GLN A 107 24.829 0.996 1.300 1.00 37.97 N
+ANISOU 897 NE2 GLN A 107 4710 4747 4969 -14 -34 122 N
+ATOM 898 N PRO A 108 20.146 4.681 2.862 1.00 18.14 N
+ANISOU 898 N PRO A 108 2328 2308 2256 -82 -254 -30 N
+ATOM 899 CA PRO A 108 19.108 5.716 2.987 1.00 17.93 C
+ANISOU 899 CA PRO A 108 2328 2291 2193 -88 -285 -51 C
+ATOM 900 C PRO A 108 18.660 6.165 1.590 1.00 17.22 C
+ANISOU 900 C PRO A 108 2246 2212 2084 -96 -261 -61 C
+ATOM 901 O PRO A 108 19.462 6.189 0.647 1.00 17.68 O
+ANISOU 901 O PRO A 108 2289 2269 2161 -99 -235 -46 O
+ATOM 902 CB PRO A 108 19.811 6.845 3.755 1.00 19.73 C
+ANISOU 902 CB PRO A 108 2553 2507 2435 -98 -334 -30 C
+ATOM 903 CG PRO A 108 21.269 6.568 3.594 1.00 21.30 C
+ANISOU 903 CG PRO A 108 2711 2697 2685 -102 -330 10 C
+ATOM 904 CD PRO A 108 21.423 5.100 3.467 1.00 19.01 C
+ANISOU 904 CD PRO A 108 2406 2406 2409 -88 -284 11 C
+ATOM 905 N GLY A 109 17.382 6.434 1.449 1.00 15.99 N
+ANISOU 905 N GLY A 109 2113 2069 1895 -99 -266 -79 N
+ATOM 906 CA GLY A 109 16.807 6.791 0.158 1.00 16.21 C
+ANISOU 906 CA GLY A 109 2149 2110 1901 -113 -251 -83 C
+ATOM 907 C GLY A 109 16.074 5.638 -0.506 1.00 16.96 C
+ANISOU 907 C GLY A 109 2262 2210 1971 -123 -223 -97 C
+ATOM 908 O GLY A 109 15.191 5.862 -1.338 1.00 18.41 O
+ANISOU 908 O GLY A 109 2460 2407 2128 -141 -223 -99 O
+ATOM 909 N AGLN A 110 16.422 4.397 -0.138 0.75 16.76 N
+ANISOU 909 N AGLN A 110 2239 2173 1955 -114 -202 -104 N
+ATOM 910 N BGLN A 110 16.445 4.390 -0.161 0.25 16.16 N
+ANISOU 910 N BGLN A 110 2164 2097 1880 -114 -201 -104 N
+ATOM 911 CA AGLN A 110 15.768 3.237 -0.714 0.75 16.95 C
+ANISOU 911 CA AGLN A 110 2291 2196 1955 -126 -179 -118 C
+ATOM 912 CA BGLN A 110 15.829 3.187 -0.717 0.25 15.84 C
+ANISOU 912 CA BGLN A 110 2150 2054 1816 -125 -177 -118 C
+ATOM 913 C AGLN A 110 14.440 2.952 -0.068 0.75 16.11 C
+ANISOU 913 C AGLN A 110 2190 2100 1832 -129 -203 -120 C
+ATOM 914 C BGLN A 110 14.470 2.926 -0.075 0.25 15.71 C
+ANISOU 914 C BGLN A 110 2140 2049 1782 -129 -202 -120 C
+ATOM 915 O AGLN A 110 14.240 3.191 1.125 0.75 16.11 O
+ANISOU 915 O AGLN A 110 2176 2103 1844 -110 -224 -114 O
+ATOM 916 O BGLN A 110 14.293 3.143 1.123 0.25 15.80 O
+ANISOU 916 O BGLN A 110 2136 2063 1806 -110 -223 -114 O
+ATOM 917 CB AGLN A 110 16.693 2.020 -0.709 0.75 19.14 C
+ANISOU 917 CB AGLN A 110 2570 2450 2251 -114 -138 -121 C
+ATOM 918 CB BGLN A 110 16.764 1.974 -0.537 0.25 16.49 C
+ANISOU 918 CB BGLN A 110 2230 2113 1920 -111 -139 -120 C
+ATOM 919 CG AGLN A 110 17.940 2.248 -1.555 0.75 23.45 C
+ANISOU 919 CG AGLN A 110 3110 2983 2815 -108 -101 -110 C
+ATOM 920 CG BGLN A 110 16.218 0.644 -1.057 0.25 17.81 C
+ANISOU 920 CG BGLN A 110 2436 2268 2063 -123 -112 -138 C
+ATOM 921 CD AGLN A 110 17.625 2.582 -2.992 0.75 30.28 C
+ANISOU 921 CD AGLN A 110 4009 3852 3643 -131 -84 -118 C
+ATOM 922 CD BGLN A 110 15.922 0.672 -2.535 0.25 19.23 C
+ANISOU 922 CD BGLN A 110 2659 2445 2201 -152 -94 -149 C
+ATOM 923 OE1AGLN A 110 17.015 1.792 -3.727 0.75 33.04 O
+ANISOU 923 OE1AGLN A 110 4405 4194 3954 -150 -65 -137 O
+ATOM 924 OE1BGLN A 110 16.709 1.161 -3.348 0.25 20.49 O
+ANISOU 924 OE1BGLN A 110 2822 2600 2362 -150 -68 -144 O
+ATOM 925 NE2AGLN A 110 18.015 3.774 -3.418 0.75 30.91 N
+ANISOU 925 NE2AGLN A 110 4069 3944 3730 -133 -95 -103 N
+ATOM 926 NE2BGLN A 110 14.760 0.153 -2.910 0.25 17.17 N
+ANISOU 926 NE2BGLN A 110 2433 2187 1903 -181 -110 -158 N
+ATOM 927 N THR A 111 13.508 2.467 -0.876 1.00 15.42 N
+ANISOU 927 N THR A 111 2128 2018 1715 -155 -202 -122 N
+ATOM 928 CA THR A 111 12.177 2.177 -0.420 1.00 15.01 C
+ANISOU 928 CA THR A 111 2075 1977 1651 -162 -225 -111 C
+ATOM 929 C THR A 111 12.007 0.676 -0.190 1.00 14.44 C
+ANISOU 929 C THR A 111 2020 1891 1577 -166 -214 -120 C
+ATOM 930 O THR A 111 12.800 -0.137 -0.654 1.00 15.56 O
+ANISOU 930 O THR A 111 2183 2012 1718 -169 -183 -138 O
+ATOM 931 CB THR A 111 11.189 2.708 -1.461 1.00 15.57 C
+ANISOU 931 CB THR A 111 2156 2063 1695 -197 -243 -94 C
+ATOM 932 OG1 THR A 111 11.488 2.051 -2.697 1.00 16.40 O
+ANISOU 932 OG1 THR A 111 2302 2157 1773 -229 -226 -109 O
+ATOM 933 CG2 THR A 111 11.297 4.211 -1.623 1.00 15.53 C
+ANISOU 933 CG2 THR A 111 2132 2071 1698 -190 -254 -81 C
+ATOM 934 N PHE A 112 10.950 0.319 0.518 1.00 13.51 N
+ANISOU 934 N PHE A 112 1891 1782 1460 -163 -234 -104 N
+ATOM 935 CA PHE A 112 10.598 -1.063 0.784 1.00 13.06 C
+ANISOU 935 CA PHE A 112 1846 1713 1403 -170 -231 -107 C
+ATOM 936 C PHE A 112 9.173 -1.129 1.275 1.00 12.87 C
+ANISOU 936 C PHE A 112 1805 1706 1378 -175 -261 -74 C
+ATOM 937 O PHE A 112 8.617 -0.121 1.728 1.00 12.86 O
+ANISOU 937 O PHE A 112 1779 1722 1383 -158 -274 -50 O
+ATOM 938 CB PHE A 112 11.550 -1.690 1.813 1.00 13.30 C
+ANISOU 938 CB PHE A 112 1862 1730 1462 -136 -210 -121 C
+ATOM 939 CG PHE A 112 11.648 -0.996 3.149 1.00 13.25 C
+ANISOU 939 CG PHE A 112 1824 1736 1476 -101 -224 -109 C
+ATOM 940 CD1 PHE A 112 12.527 0.058 3.340 1.00 14.26 C
+ANISOU 940 CD1 PHE A 112 1942 1864 1613 -87 -225 -112 C
+ATOM 941 CD2 PHE A 112 10.881 -1.409 4.218 1.00 13.58 C
+ANISOU 941 CD2 PHE A 112 1852 1784 1524 -84 -236 -94 C
+ATOM 942 CE1 PHE A 112 12.649 0.667 4.581 1.00 14.94 C
+ANISOU 942 CE1 PHE A 112 2015 1953 1709 -61 -241 -105 C
+ATOM 943 CE2 PHE A 112 11.024 -0.820 5.466 1.00 14.05 C
+ANISOU 943 CE2 PHE A 112 1897 1848 1592 -52 -244 -86 C
+ATOM 944 CZ PHE A 112 11.895 0.226 5.637 1.00 14.59 C
+ANISOU 944 CZ PHE A 112 1967 1914 1664 -43 -248 -94 C
+ATOM 945 N SER A 113 8.584 -2.325 1.254 1.00 12.27 N
+ANISOU 945 N SER A 113 1742 1622 1298 -194 -268 -68 N
+ATOM 946 CA SER A 113 7.231 -2.520 1.754 1.00 12.47 C
+ANISOU 946 CA SER A 113 1744 1662 1331 -198 -296 -25 C
+ATOM 947 C SER A 113 7.324 -3.072 3.152 1.00 12.94 C
+ANISOU 947 C SER A 113 1779 1720 1416 -156 -286 -23 C
+ATOM 948 O SER A 113 8.199 -3.891 3.424 1.00 13.55 O
+ANISOU 948 O SER A 113 1868 1781 1502 -147 -266 -53 O
+ATOM 949 CB SER A 113 6.494 -3.535 0.894 1.00 13.09 C
+ANISOU 949 CB SER A 113 1853 1730 1390 -252 -320 -12 C
+ATOM 950 OG SER A 113 6.426 -3.026 -0.426 1.00 14.30 O
+ANISOU 950 OG SER A 113 2038 1885 1513 -296 -333 -13 O
+ATOM 951 N VAL A 114 6.388 -2.710 4.000 1.00 12.29 N
+ANISOU 951 N VAL A 114 1666 1656 1348 -132 -296 16 N
+ATOM 952 CA VAL A 114 6.309 -3.243 5.354 1.00 12.81 C
+ANISOU 952 CA VAL A 114 1711 1722 1433 -93 -287 25 C
+ATOM 953 C VAL A 114 5.016 -4.014 5.481 1.00 13.03 C
+ANISOU 953 C VAL A 114 1720 1758 1472 -107 -308 73 C
+ATOM 954 O VAL A 114 3.956 -3.520 5.093 1.00 13.21 O
+ANISOU 954 O VAL A 114 1727 1794 1497 -122 -325 121 O
+ATOM 955 CB VAL A 114 6.321 -2.096 6.393 1.00 12.98 C
+ANISOU 955 CB VAL A 114 1719 1753 1458 -46 -275 34 C
+ATOM 956 CG1 VAL A 114 5.995 -2.605 7.800 1.00 13.23 C
+ANISOU 956 CG1 VAL A 114 1736 1787 1503 -6 -266 52 C
+ATOM 957 CG2 VAL A 114 7.642 -1.359 6.377 1.00 13.58 C
+ANISOU 957 CG2 VAL A 114 1813 1819 1527 -37 -264 -7 C
+ATOM 958 N LEU A 115 5.084 -5.218 6.060 1.00 12.47 N
+ANISOU 958 N LEU A 115 1646 1679 1415 -102 -306 70 N
+ATOM 959 CA LEU A 115 3.894 -5.974 6.346 1.00 12.54 C
+ANISOU 959 CA LEU A 115 1630 1694 1439 -111 -327 122 C
+ATOM 960 C LEU A 115 3.703 -5.818 7.851 1.00 12.81 C
+ANISOU 960 C LEU A 115 1635 1741 1492 -51 -306 143 C
+ATOM 961 O LEU A 115 4.403 -6.474 8.629 1.00 13.18 O
+ANISOU 961 O LEU A 115 1683 1779 1546 -29 -292 116 O
+ATOM 962 CB LEU A 115 4.037 -7.458 5.964 1.00 12.90 C
+ANISOU 962 CB LEU A 115 1697 1718 1487 -147 -340 106 C
+ATOM 963 CG LEU A 115 2.822 -8.307 6.284 1.00 14.50 C
+ANISOU 963 CG LEU A 115 1872 1925 1710 -160 -368 165 C
+ATOM 964 CD1 LEU A 115 1.620 -7.870 5.469 1.00 15.37 C
+ANISOU 964 CD1 LEU A 115 1973 2049 1819 -202 -406 224 C
+ATOM 965 CD2 LEU A 115 3.100 -9.764 6.033 1.00 14.68 C
+ANISOU 965 CD2 LEU A 115 1923 1921 1735 -192 -377 142 C
+ATOM 966 N AALA A 116 2.831 -4.892 8.282 0.50 12.53 N
+ANISOU 966 N AALA A 116 1576 1721 1462 -22 -299 190 N
+ATOM 967 N BALA A 116 2.781 -4.931 8.250 0.50 12.98 N
+ANISOU 967 N BALA A 116 1632 1778 1520 -24 -300 193 N
+ATOM 968 CA AALA A 116 2.624 -4.675 9.718 0.50 13.17 C
+ANISOU 968 CA AALA A 116 1643 1809 1552 39 -271 210 C
+ATOM 969 CA BALA A 116 2.439 -4.683 9.648 0.50 14.18 C
+ANISOU 969 CA BALA A 116 1766 1938 1682 36 -274 220 C
+ATOM 970 C AALA A 116 1.810 -5.835 10.275 0.50 13.37 C
+ANISOU 970 C AALA A 116 1638 1840 1603 43 -280 257 C
+ATOM 971 C BALA A 116 1.816 -5.963 10.194 0.50 14.72 C
+ANISOU 971 C BALA A 116 1808 2010 1775 37 -283 256 C
+ATOM 972 O AALA A 116 0.739 -6.137 9.755 0.50 13.60 O
+ANISOU 972 O AALA A 116 1640 1877 1651 17 -302 314 O
+ATOM 973 O BALA A 116 0.984 -6.577 9.520 0.50 15.10 O
+ANISOU 973 O BALA A 116 1837 2061 1839 -2 -313 298 O
+ATOM 974 CB AALA A 116 1.907 -3.354 9.963 0.50 13.83 C
+ANISOU 974 CB AALA A 116 1721 1901 1635 74 -249 250 C
+ATOM 975 CB BALA A 116 1.442 -3.535 9.736 0.50 14.78 C
+ANISOU 975 CB BALA A 116 1826 2025 1765 62 -258 276 C
+ATOM 976 N ACYS A 117 2.327 -6.495 11.304 0.75 13.30 N
+ANISOU 976 N ACYS A 117 1629 1828 1597 71 -266 237 N
+ATOM 977 N BCYS A 117 2.247 -6.387 11.372 0.25 14.79 N
+ANISOU 977 N BCYS A 117 1817 2018 1786 76 -264 241 N
+ATOM 978 CA ACYS A 117 1.697 -7.643 11.954 0.75 13.87 C
+ANISOU 978 CA ACYS A 117 1670 1905 1694 80 -272 278 C
+ATOM 979 CA BCYS A 117 1.815 -7.651 11.942 0.25 15.40 C
+ANISOU 979 CA BCYS A 117 1867 2097 1886 78 -272 270 C
+ATOM 980 C ACYS A 117 1.506 -7.426 13.414 0.75 14.56 C
+ANISOU 980 C ACYS A 117 1750 2001 1782 142 -240 300 C
+ATOM 981 C BCYS A 117 1.597 -7.519 13.450 0.25 15.40 C
+ANISOU 981 C BCYS A 117 1857 2107 1888 141 -240 295 C
+ATOM 982 O ACYS A 117 2.265 -6.683 14.028 0.75 14.38 O
+ANISOU 982 O ACYS A 117 1758 1973 1732 170 -218 262 O
+ATOM 983 O BCYS A 117 2.357 -6.821 14.110 0.25 15.48 O
+ANISOU 983 O BCYS A 117 1897 2112 1872 170 -219 258 O
+ATOM 984 CB ACYS A 117 2.543 -8.892 11.752 0.75 14.43 C
+ANISOU 984 CB ACYS A 117 1751 1960 1771 49 -287 233 C
+ATOM 985 CB BCYS A 117 2.882 -8.701 11.636 0.25 16.62 C
+ANISOU 985 CB BCYS A 117 2039 2234 2040 47 -284 214 C
+ATOM 986 SG ACYS A 117 2.803 -9.323 10.034 0.75 14.59 S
+ANISOU 986 SG ACYS A 117 1800 1960 1782 -24 -317 203 S
+ATOM 987 SG BCYS A 117 2.292 -10.412 11.656 0.25 20.52 S
+ANISOU 987 SG BCYS A 117 2509 2722 2567 20 -309 245 S
+ATOM 988 N TYR A 118 0.570 -8.188 13.997 1.00 15.18 N
+ANISOU 988 N TYR A 118 1791 2090 1887 158 -239 360 N
+ATOM 989 CA TYR A 118 0.296 -8.220 15.447 1.00 16.61 C
+ANISOU 989 CA TYR A 118 1964 2278 2067 219 -205 388 C
+ATOM 990 C TYR A 118 -0.002 -9.668 15.797 1.00 18.17 C
+ANISOU 990 C TYR A 118 2126 2481 2297 210 -223 416 C
+ATOM 991 O TYR A 118 -0.763 -10.310 15.085 1.00 18.33 O
+ANISOU 991 O TYR A 118 2115 2504 2348 173 -253 459 O
+ATOM 992 CB TYR A 118 -0.905 -7.330 15.835 1.00 17.19 C
+ANISOU 992 CB TYR A 118 2023 2361 2148 267 -169 462 C
+ATOM 993 CG TYR A 118 -0.613 -5.889 15.531 1.00 17.88 C
+ANISOU 993 CG TYR A 118 2149 2438 2205 279 -148 434 C
+ATOM 994 CD1 TYR A 118 0.120 -5.113 16.416 1.00 18.60 C
+ANISOU 994 CD1 TYR A 118 2294 2518 2255 318 -117 390 C
+ATOM 995 CD2 TYR A 118 -0.904 -5.351 14.286 1.00 18.85 C
+ANISOU 995 CD2 TYR A 118 2263 2562 2337 240 -169 444 C
+ATOM 996 CE1 TYR A 118 0.471 -3.810 16.108 1.00 19.34 C
+ANISOU 996 CE1 TYR A 118 2428 2598 2321 323 -102 360 C
+ATOM 997 CE2 TYR A 118 -0.509 -4.069 13.946 1.00 19.60 C
+ANISOU 997 CE2 TYR A 118 2393 2647 2406 246 -153 412 C
+ATOM 998 CZ TYR A 118 0.167 -3.297 14.865 1.00 20.22 C
+ANISOU 998 CZ TYR A 118 2523 2712 2448 289 -119 371 C
+ATOM 999 OH TYR A 118 0.539 -2.027 14.526 1.00 21.79 O
+ANISOU 999 OH TYR A 118 2759 2898 2623 292 -107 342 O
+ATOM 1000 N ASN A 119 0.643 -10.210 16.842 1.00 18.87 N
+ANISOU 1000 N ASN A 119 2222 2571 2379 235 -211 393 N
+ATOM 1001 CA ASN A 119 0.439 -11.600 17.254 1.00 20.10 C
+ANISOU 1001 CA ASN A 119 2341 2729 2567 229 -226 418 C
+ATOM 1002 C ASN A 119 0.702 -12.594 16.117 1.00 19.55 C
+ANISOU 1002 C ASN A 119 2266 2644 2519 164 -266 395 C
+ATOM 1003 O ASN A 119 -0.008 -13.593 15.977 1.00 20.20 O
+ANISOU 1003 O ASN A 119 2314 2726 2635 144 -290 439 O
+ATOM 1004 CB ASN A 119 -0.981 -11.790 17.805 1.00 22.64 C
+ANISOU 1004 CB ASN A 119 2617 3068 2918 263 -213 512 C
+ATOM 1005 CG ASN A 119 -1.294 -10.896 18.970 1.00 27.97 C
+ANISOU 1005 CG ASN A 119 3308 3751 3568 333 -160 538 C
+ATOM 1006 OD1 ASN A 119 -2.158 -10.021 18.891 1.00 30.85 O
+ANISOU 1006 OD1 ASN A 119 3668 4120 3934 362 -133 588 O
+ATOM 1007 ND2 ASN A 119 -0.591 -11.091 20.070 1.00 29.18 N
+ANISOU 1007 ND2 ASN A 119 3485 3905 3698 362 -143 508 N
+ATOM 1008 N GLY A 120 1.679 -12.285 15.272 1.00 18.20 N
+ANISOU 1008 N GLY A 120 2131 2457 2328 131 -274 329 N
+ATOM 1009 CA GLY A 120 2.021 -13.141 14.143 1.00 17.98 C
+ANISOU 1009 CA GLY A 120 2116 2406 2310 73 -301 300 C
+ATOM 1010 C GLY A 120 1.039 -13.089 12.987 1.00 18.05 C
+ANISOU 1010 C GLY A 120 2124 2411 2323 27 -334 335 C
+ATOM 1011 O GLY A 120 1.168 -13.860 12.037 1.00 18.15 O
+ANISOU 1011 O GLY A 120 2158 2400 2337 -27 -360 316 O
+ATOM 1012 N SER A 121 0.031 -12.200 13.059 1.00 17.88 N
+ANISOU 1012 N SER A 121 2081 2410 2303 45 -332 393 N
+ATOM 1013 CA SER A 121 -0.988 -12.098 12.025 1.00 19.05 C
+ANISOU 1013 CA SER A 121 2219 2559 2461 -2 -369 444 C
+ATOM 1014 C SER A 121 -0.884 -10.784 11.263 1.00 19.31 C
+ANISOU 1014 C SER A 121 2273 2595 2467 -10 -363 428 C
+ATOM 1015 O SER A 121 -0.858 -9.709 11.855 1.00 18.83 O
+ANISOU 1015 O SER A 121 2210 2548 2397 40 -327 432 O
+ATOM 1016 CB SER A 121 -2.379 -12.227 12.637 1.00 21.46 C
+ANISOU 1016 CB SER A 121 2465 2885 2805 22 -374 548 C
+ATOM 1017 OG SER A 121 -2.553 -13.527 13.175 1.00 25.54 O
+ANISOU 1017 OG SER A 121 2958 3397 3349 18 -389 568 O
+ATOM 1018 N PRO A 122 -0.842 -10.855 9.929 1.00 20.18 N
+ANISOU 1018 N PRO A 122 2413 2691 2563 -75 -399 411 N
+ATOM 1019 CA PRO A 122 -0.716 -9.623 9.136 1.00 20.36 C
+ANISOU 1019 CA PRO A 122 2456 2719 2562 -87 -395 397 C
+ATOM 1020 C PRO A 122 -1.952 -8.725 9.210 1.00 20.01 C
+ANISOU 1020 C PRO A 122 2367 2697 2538 -69 -395 485 C
+ATOM 1021 O PRO A 122 -3.095 -9.193 9.177 1.00 20.24 O
+ANISOU 1021 O PRO A 122 2354 2734 2600 -88 -424 570 O
+ATOM 1022 CB PRO A 122 -0.453 -10.148 7.715 1.00 22.14 C
+ANISOU 1022 CB PRO A 122 2727 2920 2764 -165 -436 364 C
+ATOM 1023 CG PRO A 122 0.095 -11.574 7.925 1.00 22.93 C
+ANISOU 1023 CG PRO A 122 2849 2995 2868 -178 -438 324 C
+ATOM 1024 CD PRO A 122 -0.761 -12.055 9.076 1.00 20.91 C
+ANISOU 1024 CD PRO A 122 2534 2757 2652 -142 -439 393 C
+ATOM 1025 N SER A 123 -1.723 -7.421 9.339 1.00 19.28 N
+ANISOU 1025 N SER A 123 2282 2613 2432 -32 -360 472 N
+ATOM 1026 CA SER A 123 -2.812 -6.455 9.398 1.00 19.98 C
+ANISOU 1026 CA SER A 123 2331 2718 2542 -8 -348 555 C
+ATOM 1027 C SER A 123 -2.866 -5.587 8.166 1.00 19.22 C
+ANISOU 1027 C SER A 123 2247 2623 2433 -52 -369 555 C
+ATOM 1028 O SER A 123 -3.958 -5.209 7.743 1.00 19.82 O
+ANISOU 1028 O SER A 123 2283 2711 2537 -68 -386 643 O
+ATOM 1029 CB SER A 123 -2.716 -5.583 10.640 1.00 23.07 C
+ANISOU 1029 CB SER A 123 2721 3113 2931 77 -283 556 C
+ATOM 1030 OG SER A 123 -1.507 -4.852 10.632 1.00 27.68 O
+ANISOU 1030 OG SER A 123 3356 3686 3475 89 -263 467 O
+ATOM 1031 N GLY A 124 -1.705 -5.226 7.622 1.00 17.37 N
+ANISOU 1031 N GLY A 124 2063 2377 2159 -69 -366 466 N
+ATOM 1032 CA GLY A 124 -1.677 -4.368 6.453 1.00 16.81 C
+ANISOU 1032 CA GLY A 124 2006 2308 2073 -109 -383 464 C
+ATOM 1033 C GLY A 124 -0.319 -4.237 5.824 1.00 15.64 C
+ANISOU 1033 C GLY A 124 1914 2145 1884 -130 -381 366 C
+ATOM 1034 O GLY A 124 0.683 -4.635 6.408 1.00 14.83 O
+ANISOU 1034 O GLY A 124 1835 2030 1769 -105 -358 302 O
+ATOM 1035 N VAL A 125 -0.281 -3.697 4.620 1.00 15.52 N
+ANISOU 1035 N VAL A 125 1915 2130 1850 -177 -403 362 N
+ATOM 1036 CA VAL A 125 0.955 -3.526 3.900 1.00 16.15 C
+ANISOU 1036 CA VAL A 125 2046 2196 1894 -198 -398 280 C
+ATOM 1037 C VAL A 125 1.037 -2.116 3.362 1.00 16.23 C
+ANISOU 1037 C VAL A 125 2054 2216 1896 -194 -388 283 C
+ATOM 1038 O VAL A 125 0.028 -1.552 2.933 1.00 16.69 O
+ANISOU 1038 O VAL A 125 2082 2289 1970 -211 -406 352 O
+ATOM 1039 CB VAL A 125 1.136 -4.627 2.825 1.00 18.52 C
+ANISOU 1039 CB VAL A 125 2389 2477 2169 -270 -434 256 C
+ATOM 1040 CG1 VAL A 125 0.022 -4.589 1.791 1.00 20.02 C
+ANISOU 1040 CG1 VAL A 125 2575 2676 2356 -337 -487 322 C
+ATOM 1041 CG2 VAL A 125 2.511 -4.563 2.175 1.00 19.01 C
+ANISOU 1041 CG2 VAL A 125 2505 2520 2196 -278 -413 171 C
+ATOM 1042 N TYR A 126 2.205 -1.514 3.481 1.00 16.20 N
+ANISOU 1042 N TYR A 126 2076 2204 1874 -167 -359 217 N
+ATOM 1043 CA TYR A 126 2.408 -0.148 3.015 1.00 16.17 C
+ANISOU 1043 CA TYR A 126 2073 2207 1864 -161 -349 215 C
+ATOM 1044 C TYR A 126 3.842 0.066 2.588 1.00 15.60 C
+ANISOU 1044 C TYR A 126 2039 2122 1767 -165 -336 139 C
+ATOM 1045 O TYR A 126 4.736 -0.688 2.960 1.00 15.94 O
+ANISOU 1045 O TYR A 126 2102 2149 1804 -156 -324 92 O
+ATOM 1046 CB TYR A 126 1.958 0.884 4.064 1.00 16.49 C
+ANISOU 1046 CB TYR A 126 2086 2252 1926 -98 -316 249 C
+ATOM 1047 CG TYR A 126 2.669 0.757 5.389 1.00 17.12 C
+ANISOU 1047 CG TYR A 126 2180 2320 2004 -43 -285 209 C
+ATOM 1048 CD1 TYR A 126 3.901 1.356 5.601 1.00 17.77 C
+ANISOU 1048 CD1 TYR A 126 2293 2390 2069 -27 -271 147 C
+ATOM 1049 CD2 TYR A 126 2.115 0.027 6.430 1.00 18.46 C
+ANISOU 1049 CD2 TYR A 126 2334 2491 2190 -13 -275 237 C
+ATOM 1050 CE1 TYR A 126 4.560 1.241 6.817 1.00 18.59 C
+ANISOU 1050 CE1 TYR A 126 2413 2482 2168 14 -252 117 C
+ATOM 1051 CE2 TYR A 126 2.758 -0.085 7.654 1.00 19.26 C
+ANISOU 1051 CE2 TYR A 126 2452 2581 2283 33 -250 202 C
+ATOM 1052 CZ TYR A 126 3.979 0.529 7.845 1.00 19.71 C
+ANISOU 1052 CZ TYR A 126 2542 2625 2320 43 -241 143 C
+ATOM 1053 OH TYR A 126 4.608 0.427 9.064 1.00 22.38 O
+ANISOU 1053 OH TYR A 126 2901 2953 2649 80 -226 116 O
+ATOM 1054 N AGLN A 127 4.050 1.061 1.748 0.50 15.62 N
+ANISOU 1054 N AGLN A 127 2048 2129 1759 -181 -338 136 N
+ATOM 1055 N BGLN A 127 4.090 1.164 1.886 0.50 15.49 N
+ANISOU 1055 N BGLN A 127 2029 2111 1743 -174 -334 134 N
+ATOM 1056 CA AGLN A 127 5.336 1.360 1.175 0.50 15.80 C
+ANISOU 1056 CA AGLN A 127 2100 2140 1761 -189 -326 78 C
+ATOM 1057 CA BGLN A 127 5.413 1.506 1.423 0.50 15.72 C
+ANISOU 1057 CA BGLN A 127 2088 2131 1755 -177 -321 75 C
+ATOM 1058 C AGLN A 127 5.965 2.540 1.890 0.50 16.49 C
+ANISOU 1058 C AGLN A 127 2180 2225 1858 -142 -304 61 C
+ATOM 1059 C BGLN A 127 6.095 2.480 2.372 0.50 16.20 C
+ANISOU 1059 C BGLN A 127 2144 2186 1826 -125 -297 55 C
+ATOM 1060 O AGLN A 127 5.306 3.560 2.092 0.50 16.63 O
+ANISOU 1060 O AGLN A 127 2180 2252 1888 -123 -300 97 O
+ATOM 1061 O BGLN A 127 5.462 3.402 2.878 0.50 16.36 O
+ANISOU 1061 O BGLN A 127 2147 2211 1858 -97 -289 88 O
+ATOM 1062 CB AGLN A 127 5.117 1.674 -0.313 0.50 16.38 C
+ANISOU 1062 CB AGLN A 127 2189 2223 1814 -245 -349 91 C
+ATOM 1063 CB BGLN A 127 5.315 2.096 0.015 0.50 17.00 C
+ANISOU 1063 CB BGLN A 127 2260 2301 1899 -223 -338 85 C
+ATOM 1064 CG AGLN A 127 6.368 1.792 -1.131 0.50 18.09 C
+ANISOU 1064 CG AGLN A 127 2441 2428 2006 -261 -336 39 C
+ATOM 1065 CG BGLN A 127 6.631 2.112 -0.715 0.50 19.17 C
+ANISOU 1065 CG BGLN A 127 2569 2563 2152 -236 -324 30 C
+ATOM 1066 CD AGLN A 127 7.089 0.490 -1.349 0.50 18.85 C
+ANISOU 1066 CD AGLN A 127 2576 2501 2085 -274 -323 -4 C
+ATOM 1067 CD BGLN A 127 7.033 0.761 -1.249 0.50 19.69 C
+ANISOU 1067 CD BGLN A 127 2674 2610 2195 -268 -323 0 C
+ATOM 1068 OE1AGLN A 127 6.666 -0.598 -0.912 0.50 18.45 O
+ANISOU 1068 OE1AGLN A 127 2529 2441 2039 -277 -329 1 O
+ATOM 1069 OE1BGLN A 127 6.501 -0.300 -0.868 0.50 20.09 O
+ANISOU 1069 OE1BGLN A 127 2729 2655 2250 -275 -333 10 O
+ATOM 1070 NE2AGLN A 127 8.210 0.583 -2.023 0.50 19.51 N
+ANISOU 1070 NE2AGLN A 127 2689 2572 2154 -278 -299 -43 N
+ATOM 1071 NE2BGLN A 127 8.008 0.774 -2.125 0.50 19.03 N
+ANISOU 1071 NE2BGLN A 127 2625 2514 2090 -283 -305 -36 N
+ATOM 1072 N ACYS A 128 7.225 2.400 2.294 0.50 16.47 N
+ANISOU 1072 N ACYS A 128 2195 2209 1853 -124 -288 13 N
+ATOM 1073 N BCYS A 128 7.382 2.261 2.606 0.50 16.43 N
+ANISOU 1073 N BCYS A 128 2191 2201 1851 -114 -285 6 N
+ATOM 1074 CA ACYS A 128 7.942 3.478 2.975 0.50 16.78 C
+ANISOU 1074 CA ACYS A 128 2236 2241 1898 -89 -277 -4 C
+ATOM 1075 CA BCYS A 128 8.255 3.071 3.448 0.50 17.09 C
+ANISOU 1075 CA BCYS A 128 2279 2275 1941 -78 -273 -16 C
+ATOM 1076 C ACYS A 128 9.416 3.592 2.486 0.50 16.85 C
+ANISOU 1076 C ACYS A 128 2259 2239 1904 -99 -272 -44 C
+ATOM 1077 C BCYS A 128 9.557 3.356 2.718 0.50 17.04 C
+ANISOU 1077 C BCYS A 128 2284 2260 1930 -94 -270 -49 C
+ATOM 1078 O ACYS A 128 9.746 3.008 1.463 0.50 16.70 O
+ANISOU 1078 O ACYS A 128 2252 2219 1876 -130 -269 -57 O
+ATOM 1079 O BCYS A 128 9.936 2.632 1.810 0.50 16.87 O
+ANISOU 1079 O BCYS A 128 2274 2236 1902 -123 -266 -63 O
+ATOM 1080 CB ACYS A 128 7.831 3.331 4.489 0.50 17.30 C
+ANISOU 1080 CB ACYS A 128 2301 2299 1972 -46 -267 -1 C
+ATOM 1081 CB BCYS A 128 8.549 2.332 4.751 0.50 18.43 C
+ANISOU 1081 CB BCYS A 128 2450 2435 2118 -49 -266 -27 C
+ATOM 1082 SG ACYS A 128 8.691 1.883 5.141 0.50 19.72 S
+ANISOU 1082 SG ACYS A 128 2613 2596 2283 -42 -265 -31 S
+ATOM 1083 SG BCYS A 128 7.272 2.509 6.011 0.50 23.03 S
+ANISOU 1083 SG BCYS A 128 3024 3023 2705 -8 -258 13 S
+ATOM 1084 N ALA A 129 10.286 4.364 3.171 1.00 17.09 N
+ANISOU 1084 N ALA A 129 2293 2258 1942 -75 -270 -59 N
+ATOM 1085 CA ALA A 129 11.650 4.578 2.712 1.00 17.20 C
+ANISOU 1085 CA ALA A 129 2310 2263 1962 -84 -268 -82 C
+ATOM 1086 C ALA A 129 12.538 4.679 3.922 1.00 16.36 C
+ANISOU 1086 C ALA A 129 2206 2142 1869 -61 -274 -91 C
+ATOM 1087 O ALA A 129 12.115 5.142 4.987 1.00 17.23 O
+ANISOU 1087 O ALA A 129 2327 2246 1972 -39 -283 -85 O
+ATOM 1088 CB ALA A 129 11.767 5.848 1.894 1.00 17.51 C
+ANISOU 1088 CB ALA A 129 2348 2306 1999 -96 -273 -76 C
+ATOM 1089 N MET A 130 13.787 4.272 3.753 1.00 14.85 N
+ANISOU 1089 N MET A 130 2008 1942 1694 -68 -270 -101 N
+ATOM 1090 CA MET A 130 14.793 4.474 4.787 1.00 14.43 C
+ANISOU 1090 CA MET A 130 1952 1873 1656 -57 -286 -99 C
+ATOM 1091 C MET A 130 15.149 5.964 4.667 1.00 14.95 C
+ANISOU 1091 C MET A 130 2025 1933 1720 -61 -307 -95 C
+ATOM 1092 O MET A 130 15.626 6.382 3.618 1.00 15.32 O
+ANISOU 1092 O MET A 130 2061 1984 1776 -75 -301 -92 O
+ATOM 1093 CB MET A 130 16.023 3.600 4.511 1.00 14.88 C
+ANISOU 1093 CB MET A 130 1989 1922 1742 -63 -271 -96 C
+ATOM 1094 CG MET A 130 17.144 3.773 5.526 1.00 16.66 C
+ANISOU 1094 CG MET A 130 2203 2135 1991 -60 -295 -81 C
+ATOM 1095 SD MET A 130 16.663 3.502 7.255 1.00 17.10 S
+ANISOU 1095 SD MET A 130 2278 2187 2031 -45 -322 -81 S
+ATOM 1096 CE MET A 130 15.931 1.868 7.146 1.00 15.89 C
+ANISOU 1096 CE MET A 130 2113 2043 1880 -35 -287 -88 C
+ATOM 1097 N ARG A 131 14.805 6.763 5.672 1.00 14.67 N
+ANISOU 1097 N ARG A 131 2015 1887 1670 -48 -327 -94 N
+ATOM 1098 CA ARG A 131 15.075 8.199 5.615 1.00 14.63 C
+ANISOU 1098 CA ARG A 131 2027 1870 1662 -53 -347 -91 C
+ATOM 1099 C ARG A 131 16.579 8.470 5.700 1.00 15.11 C
+ANISOU 1099 C ARG A 131 2077 1917 1747 -72 -374 -82 C
+ATOM 1100 O ARG A 131 17.321 7.663 6.261 1.00 15.31 O
+ANISOU 1100 O ARG A 131 2090 1938 1788 -75 -383 -74 O
+ATOM 1101 CB ARG A 131 14.359 8.906 6.784 1.00 14.75 C
+ANISOU 1101 CB ARG A 131 2088 1867 1650 -32 -355 -94 C
+ATOM 1102 CG ARG A 131 12.853 8.693 6.868 1.00 15.21 C
+ANISOU 1102 CG ARG A 131 2152 1936 1693 -8 -325 -88 C
+ATOM 1103 CD ARG A 131 12.112 9.087 5.600 1.00 15.22 C
+ANISOU 1103 CD ARG A 131 2128 1956 1700 -15 -307 -75 C
+ATOM 1104 NE ARG A 131 12.512 10.422 5.144 1.00 14.93 N
+ANISOU 1104 NE ARG A 131 2100 1907 1667 -24 -319 -75 N
+ATOM 1105 CZ ARG A 131 12.205 10.925 3.951 1.00 14.97 C
+ANISOU 1105 CZ ARG A 131 2081 1926 1680 -38 -312 -63 C
+ATOM 1106 NH1 ARG A 131 11.460 10.230 3.101 1.00 14.04 N
+ANISOU 1106 NH1 ARG A 131 1936 1834 1563 -48 -297 -50 N
+ATOM 1107 NH2 ARG A 131 12.629 12.136 3.606 1.00 14.38 N
+ANISOU 1107 NH2 ARG A 131 2013 1839 1611 -45 -325 -61 N
+ATOM 1108 N PRO A 132 17.057 9.636 5.226 1.00 15.38 N
+ANISOU 1108 N PRO A 132 2112 1942 1788 -85 -393 -75 N
+ATOM 1109 CA PRO A 132 18.491 9.948 5.366 1.00 15.82 C
+ANISOU 1109 CA PRO A 132 2154 1985 1874 -105 -426 -54 C
+ATOM 1110 C PRO A 132 18.982 9.985 6.832 1.00 16.21 C
+ANISOU 1110 C PRO A 132 2233 2010 1915 -113 -469 -47 C
+ATOM 1111 O PRO A 132 20.180 9.803 7.070 1.00 17.50 O
+ANISOU 1111 O PRO A 132 2373 2166 2109 -134 -498 -19 O
+ATOM 1112 CB PRO A 132 18.614 11.299 4.676 1.00 16.65 C
+ANISOU 1112 CB PRO A 132 2262 2083 1981 -116 -440 -48 C
+ATOM 1113 CG PRO A 132 17.506 11.284 3.656 1.00 16.44 C
+ANISOU 1113 CG PRO A 132 2227 2079 1941 -105 -399 -61 C
+ATOM 1114 CD PRO A 132 16.361 10.665 4.424 1.00 15.17 C
+ANISOU 1114 CD PRO A 132 2092 1921 1752 -84 -383 -77 C
+ATOM 1115 N ASN A 133 18.087 10.206 7.816 1.00 14.91 N
+ANISOU 1115 N ASN A 133 2123 1833 1710 -98 -473 -67 N
+ATOM 1116 CA ASN A 133 18.488 10.161 9.234 1.00 14.67 C
+ANISOU 1116 CA ASN A 133 2134 1779 1661 -109 -513 -62 C
+ATOM 1117 C ASN A 133 18.338 8.731 9.835 1.00 14.76 C
+ANISOU 1117 C ASN A 133 2127 1806 1674 -96 -496 -62 C
+ATOM 1118 O ASN A 133 18.393 8.562 11.050 1.00 14.97 O
+ANISOU 1118 O ASN A 133 2193 1818 1678 -99 -521 -61 O
+ATOM 1119 CB ASN A 133 17.697 11.176 10.071 1.00 15.33 C
+ANISOU 1119 CB ASN A 133 2299 1833 1694 -97 -521 -83 C
+ATOM 1120 CG ASN A 133 16.214 10.909 10.098 1.00 15.79 C
+ANISOU 1120 CG ASN A 133 2370 1903 1728 -56 -467 -100 C
+ATOM 1121 OD1 ASN A 133 15.728 9.883 9.605 1.00 15.06 O
+ANISOU 1121 OD1 ASN A 133 2231 1841 1651 -41 -433 -99 O
+ATOM 1122 ND2 ASN A 133 15.454 11.831 10.669 1.00 16.61 N
+ANISOU 1122 ND2 ASN A 133 2540 1978 1793 -36 -456 -112 N
+ATOM 1123 N PHE A 134 18.104 7.718 8.982 1.00 14.43 N
+ANISOU 1123 N PHE A 134 2034 1791 1657 -83 -454 -63 N
+ATOM 1124 CA PHE A 134 18.012 6.312 9.351 1.00 15.16 C
+ANISOU 1124 CA PHE A 134 2103 1897 1760 -72 -434 -60 C
+ATOM 1125 C PHE A 134 16.803 5.931 10.198 1.00 15.02 C
+ANISOU 1125 C PHE A 134 2120 1882 1706 -47 -419 -77 C
+ATOM 1126 O PHE A 134 16.792 4.877 10.839 1.00 15.26 O
+ANISOU 1126 O PHE A 134 2138 1918 1740 -40 -414 -72 O
+ATOM 1127 CB PHE A 134 19.291 5.830 10.006 1.00 15.66 C
+ANISOU 1127 CB PHE A 134 2145 1952 1854 -93 -468 -29 C
+ATOM 1128 CG PHE A 134 20.480 5.964 9.086 1.00 17.62 C
+ANISOU 1128 CG PHE A 134 2344 2200 2151 -112 -470 0 C
+ATOM 1129 CD1 PHE A 134 20.732 5.016 8.114 1.00 19.31 C
+ANISOU 1129 CD1 PHE A 134 2511 2428 2400 -101 -422 8 C
+ATOM 1130 CD2 PHE A 134 21.369 7.012 9.226 1.00 19.06 C
+ANISOU 1130 CD2 PHE A 134 2532 2365 2344 -140 -520 26 C
+ATOM 1131 CE1 PHE A 134 21.843 5.131 7.281 1.00 20.53 C
+ANISOU 1131 CE1 PHE A 134 2621 2578 2600 -110 -413 42 C
+ATOM 1132 CE2 PHE A 134 22.476 7.120 8.396 1.00 20.32 C
+ANISOU 1132 CE2 PHE A 134 2640 2525 2556 -153 -519 64 C
+ATOM 1133 CZ PHE A 134 22.710 6.176 7.437 1.00 20.35 C
+ANISOU 1133 CZ PHE A 134 2594 2543 2595 -135 -462 73 C
+ATOM 1134 N THR A 135 15.760 6.743 10.140 1.00 14.48 N
+ANISOU 1134 N THR A 135 2087 1810 1607 -29 -404 -91 N
+ATOM 1135 CA THR A 135 14.475 6.389 10.724 1.00 14.62 C
+ANISOU 1135 CA THR A 135 2126 1833 1598 2 -376 -96 C
+ATOM 1136 C THR A 135 13.558 5.992 9.541 1.00 14.74 C
+ANISOU 1136 C THR A 135 2102 1872 1627 10 -340 -95 C
+ATOM 1137 O THR A 135 13.902 6.189 8.367 1.00 14.52 O
+ANISOU 1137 O THR A 135 2047 1852 1617 -8 -337 -95 O
+ATOM 1138 CB THR A 135 13.860 7.611 11.436 1.00 15.36 C
+ANISOU 1138 CB THR A 135 2285 1900 1652 20 -376 -102 C
+ATOM 1139 OG1 THR A 135 13.529 8.620 10.477 1.00 16.63 O
+ANISOU 1139 OG1 THR A 135 2442 2059 1817 19 -365 -103 O
+ATOM 1140 CG2 THR A 135 14.745 8.161 12.529 1.00 15.23 C
+ANISOU 1140 CG2 THR A 135 2325 1852 1610 2 -420 -105 C
+ATOM 1141 N ILE A 136 12.395 5.430 9.852 1.00 14.48 N
+ANISOU 1141 N ILE A 136 2069 1849 1584 34 -314 -87 N
+ATOM 1142 CA ILE A 136 11.362 5.231 8.863 1.00 15.24 C
+ANISOU 1142 CA ILE A 136 2138 1964 1688 36 -290 -76 C
+ATOM 1143 C ILE A 136 10.103 5.840 9.436 1.00 15.66 C
+ANISOU 1143 C ILE A 136 2215 2012 1722 69 -267 -57 C
+ATOM 1144 O ILE A 136 9.949 5.927 10.654 1.00 15.42 O
+ANISOU 1144 O ILE A 136 2221 1966 1672 95 -262 -57 O
+ATOM 1145 CB ILE A 136 11.154 3.773 8.380 1.00 16.56 C
+ANISOU 1145 CB ILE A 136 2269 2151 1873 25 -280 -73 C
+ATOM 1146 CG1 ILE A 136 10.532 2.890 9.459 1.00 17.44 C
+ANISOU 1146 CG1 ILE A 136 2382 2265 1980 48 -272 -61 C
+ATOM 1147 CG2 ILE A 136 12.448 3.165 7.826 1.00 17.63 C
+ANISOU 1147 CG2 ILE A 136 2386 2284 2029 0 -288 -88 C
+ATOM 1148 CD1 ILE A 136 9.987 1.590 8.900 1.00 18.35 C
+ANISOU 1148 CD1 ILE A 136 2465 2396 2111 37 -262 -52 C
+ATOM 1149 N ALYS A 137 9.196 6.293 8.569 0.50 16.39 N
+ANISOU 1149 N ALYS A 137 2290 2116 1822 70 -251 -36 N
+ATOM 1150 N BLYS A 137 9.209 6.274 8.558 0.50 16.47 N
+ANISOU 1150 N BLYS A 137 2299 2126 1832 69 -252 -37 N
+ATOM 1151 CA ALYS A 137 7.929 6.844 9.037 0.50 17.56 C
+ANISOU 1151 CA ALYS A 137 2450 2258 1963 107 -221 -4 C
+ATOM 1152 CA BLYS A 137 7.936 6.833 8.974 0.50 17.72 C
+ANISOU 1152 CA BLYS A 137 2468 2279 1985 105 -222 -4 C
+ATOM 1153 C ALYS A 137 6.887 5.782 8.750 0.50 17.91 C
+ANISOU 1153 C ALYS A 137 2452 2327 2025 107 -210 30 C
+ATOM 1154 C BLYS A 137 6.920 5.736 8.717 0.50 17.94 C
+ANISOU 1154 C BLYS A 137 2455 2332 2030 105 -211 29 C
+ATOM 1155 O ALYS A 137 6.343 5.738 7.658 0.50 18.13 O
+ANISOU 1155 O ALYS A 137 2446 2372 2069 83 -214 52 O
+ATOM 1156 O BLYS A 137 6.413 5.631 7.608 0.50 18.10 O
+ANISOU 1156 O BLYS A 137 2441 2371 2066 80 -216 50 O
+ATOM 1157 CB ALYS A 137 7.610 8.173 8.334 0.50 20.10 C
+ANISOU 1157 CB ALYS A 137 2776 2572 2288 108 -211 9 C
+ATOM 1158 CB BLYS A 137 7.601 8.067 8.115 0.50 20.49 C
+ANISOU 1158 CB BLYS A 137 2817 2627 2342 101 -214 10 C
+ATOM 1159 CG ALYS A 137 8.672 9.240 8.580 0.50 24.65 C
+ANISOU 1159 CG ALYS A 137 3396 3121 2850 101 -229 -23 C
+ATOM 1160 CG BLYS A 137 8.547 9.239 8.322 0.50 25.54 C
+ANISOU 1160 CG BLYS A 137 3499 3238 2966 98 -227 -18 C
+ATOM 1161 CD ALYS A 137 8.340 10.542 7.865 0.50 28.93 C
+ANISOU 1161 CD ALYS A 137 3939 3654 3399 102 -218 -8 C
+ATOM 1162 CD BLYS A 137 8.454 10.239 7.173 0.50 29.94 C
+ANISOU 1162 CD BLYS A 137 4039 3799 3538 82 -228 -7 C
+ATOM 1163 CE ALYS A 137 7.600 11.508 8.754 0.50 32.40 C
+ANISOU 1163 CE ALYS A 137 4429 4061 3822 148 -181 8 C
+ATOM 1164 CE BLYS A 137 8.724 11.649 7.635 0.50 33.45 C
+ANISOU 1164 CE BLYS A 137 4534 4206 3967 98 -225 -17 C
+ATOM 1165 NZ ALYS A 137 8.483 12.051 9.819 0.50 34.48 N
+ANISOU 1165 NZ ALYS A 137 4766 4283 4051 152 -197 -28 N
+ATOM 1166 NZ BLYS A 137 9.352 12.475 6.565 0.50 34.98 N
+ANISOU 1166 NZ BLYS A 137 4711 4404 4176 67 -246 -24 N
+ATOM 1167 N GLY A 138 6.673 4.891 9.709 1.00 17.84 N
+ANISOU 1167 N GLY A 138 2446 2319 2013 127 -202 35 N
+ATOM 1168 CA GLY A 138 5.745 3.780 9.550 1.00 18.27 C
+ANISOU 1168 CA GLY A 138 2460 2394 2086 125 -198 70 C
+ATOM 1169 C GLY A 138 4.449 3.921 10.307 1.00 17.75 C
+ANISOU 1169 C GLY A 138 2391 2328 2027 170 -163 123 C
+ATOM 1170 O GLY A 138 4.066 5.022 10.697 1.00 18.35 O
+ANISOU 1170 O GLY A 138 2492 2386 2092 205 -133 139 O
+ATOM 1171 N SER A 139 3.747 2.813 10.483 1.00 16.95 N
+ANISOU 1171 N SER A 139 2255 2242 1942 172 -163 156 N
+ATOM 1172 CA SER A 139 2.511 2.779 11.237 1.00 17.34 C
+ANISOU 1172 CA SER A 139 2291 2292 2003 218 -127 217 C
+ATOM 1173 C SER A 139 2.627 1.538 12.081 1.00 18.01 C
+ANISOU 1173 C SER A 139 2372 2384 2089 226 -132 213 C
+ATOM 1174 O SER A 139 2.438 0.427 11.594 1.00 18.46 O
+ANISOU 1174 O SER A 139 2391 2458 2167 194 -158 224 O
+ATOM 1175 CB SER A 139 1.310 2.717 10.300 1.00 18.70 C
+ANISOU 1175 CB SER A 139 2409 2483 2211 202 -129 287 C
+ATOM 1176 OG SER A 139 0.131 2.477 11.049 1.00 23.01 O
+ANISOU 1176 OG SER A 139 2930 3033 2779 245 -96 358 O
+ATOM 1177 N PHE A 140 3.090 1.719 13.311 1.00 17.22 N
+ANISOU 1177 N PHE A 140 2317 2266 1959 262 -113 188 N
+ATOM 1178 CA PHE A 140 3.374 0.600 14.192 1.00 17.88 C
+ANISOU 1178 CA PHE A 140 2400 2355 2040 268 -120 179 C
+ATOM 1179 C PHE A 140 2.824 0.838 15.576 1.00 20.15 C
+ANISOU 1179 C PHE A 140 2721 2629 2306 328 -76 206 C
+ATOM 1180 O PHE A 140 3.184 1.818 16.205 1.00 21.50 O
+ANISOU 1180 O PHE A 140 2955 2774 2439 353 -56 183 O
+ATOM 1181 CB PHE A 140 4.896 0.431 14.317 1.00 16.98 C
+ANISOU 1181 CB PHE A 140 2313 2232 1906 238 -153 113 C
+ATOM 1182 CG PHE A 140 5.648 0.038 13.067 1.00 16.74 C
+ANISOU 1182 CG PHE A 140 2256 2211 1894 184 -188 83 C
+ATOM 1183 CD1 PHE A 140 5.592 -1.254 12.584 1.00 17.75 C
+ANISOU 1183 CD1 PHE A 140 2344 2352 2047 157 -205 88 C
+ATOM 1184 CD2 PHE A 140 6.484 0.939 12.430 1.00 16.89 C
+ANISOU 1184 CD2 PHE A 140 2295 2219 1902 162 -202 49 C
+ATOM 1185 CE1 PHE A 140 6.315 -1.619 11.454 1.00 17.58 C
+ANISOU 1185 CE1 PHE A 140 2311 2331 2036 112 -227 59 C
+ATOM 1186 CE2 PHE A 140 7.224 0.564 11.320 1.00 17.58 C
+ANISOU 1186 CE2 PHE A 140 2363 2312 2005 118 -225 24 C
+ATOM 1187 CZ PHE A 140 7.144 -0.713 10.843 1.00 17.08 C
+ANISOU 1187 CZ PHE A 140 2268 2259 1962 95 -234 27 C
+ATOM 1188 N LEU A 141 2.006 -0.071 16.069 1.00 20.53 N
+ANISOU 1188 N LEU A 141 2734 2692 2374 351 -61 253 N
+ATOM 1189 CA LEU A 141 1.467 0.022 17.427 1.00 22.25 C
+ANISOU 1189 CA LEU A 141 2985 2898 2571 412 -13 283 C
+ATOM 1190 C LEU A 141 2.194 -0.996 18.303 1.00 22.71 C
+ANISOU 1190 C LEU A 141 3053 2961 2613 405 -35 254 C
+ATOM 1191 O LEU A 141 3.009 -1.765 17.799 1.00 22.61 O
+ANISOU 1191 O LEU A 141 3014 2961 2616 356 -82 219 O
+ATOM 1192 CB LEU A 141 -0.022 -0.321 17.412 1.00 23.61 C
+ANISOU 1192 CB LEU A 141 3101 3085 2785 446 22 372 C
+ATOM 1193 CG LEU A 141 -0.880 0.558 16.561 1.00 26.86 C
+ANISOU 1193 CG LEU A 141 3488 3495 3224 453 44 422 C
+ATOM 1194 CD1 LEU A 141 -2.217 -0.070 16.370 1.00 28.11 C
+ANISOU 1194 CD1 LEU A 141 3570 3675 3437 466 57 518 C
+ATOM 1195 CD2 LEU A 141 -1.000 1.953 17.161 1.00 27.94 C
+ANISOU 1195 CD2 LEU A 141 3693 3596 3325 508 105 421 C
+ATOM 1196 N ASN A 142 1.876 -1.054 19.615 1.00 23.13 N
+ANISOU 1196 N ASN A 142 3145 3005 2638 455 3 273 N
+ATOM 1197 CA ASN A 142 2.473 -2.056 20.495 1.00 23.46 C
+ANISOU 1197 CA ASN A 142 3191 3055 2668 448 -19 255 C
+ATOM 1198 C ASN A 142 2.080 -3.453 20.002 1.00 21.95 C
+ANISOU 1198 C ASN A 142 2914 2895 2533 425 -43 287 C
+ATOM 1199 O ASN A 142 0.950 -3.667 19.566 1.00 22.17 O
+ANISOU 1199 O ASN A 142 2891 2935 2599 439 -25 346 O
+ATOM 1200 CB ASN A 142 2.077 -1.814 21.953 1.00 26.50 C
+ANISOU 1200 CB ASN A 142 3638 3423 3007 507 31 276 C
+ATOM 1201 CG ASN A 142 2.744 -0.586 22.522 1.00 33.37 C
+ANISOU 1201 CG ASN A 142 4614 4256 3811 514 40 230 C
+ATOM 1202 OD1 ASN A 142 3.924 -0.317 22.266 1.00 35.67 O
+ANISOU 1202 OD1 ASN A 142 4930 4539 4085 465 -11 174 O
+ATOM 1203 ND2 ASN A 142 2.005 0.198 23.302 1.00 35.11 N
+ANISOU 1203 ND2 ASN A 142 4901 4448 3992 576 107 256 N
+ATOM 1204 N GLY A 143 3.065 -4.323 19.913 1.00 20.23 N
+ANISOU 1204 N GLY A 143 2679 2684 2323 383 -87 248 N
+ATOM 1205 CA GLY A 143 2.872 -5.658 19.374 1.00 18.71 C
+ANISOU 1205 CA GLY A 143 2418 2512 2180 354 -114 266 C
+ATOM 1206 C GLY A 143 3.365 -5.788 17.939 1.00 16.65 C
+ANISOU 1206 C GLY A 143 2132 2251 1943 298 -149 234 C
+ATOM 1207 O GLY A 143 3.442 -6.903 17.428 1.00 16.13 O
+ANISOU 1207 O GLY A 143 2026 2193 1911 266 -173 235 O
+ATOM 1208 N SER A 144 3.691 -4.663 17.268 1.00 15.41 N
+ANISOU 1208 N SER A 144 2005 2082 1767 286 -150 207 N
+ATOM 1209 CA SER A 144 4.151 -4.716 15.875 1.00 14.02 C
+ANISOU 1209 CA SER A 144 1811 1906 1609 235 -179 178 C
+ATOM 1210 C SER A 144 5.623 -5.030 15.716 1.00 13.25 C
+ANISOU 1210 C SER A 144 1726 1799 1508 202 -204 123 C
+ATOM 1211 O SER A 144 6.059 -5.283 14.594 1.00 12.34 O
+ANISOU 1211 O SER A 144 1598 1682 1408 163 -220 101 O
+ATOM 1212 CB SER A 144 3.856 -3.411 15.150 1.00 14.75 C
+ANISOU 1212 CB SER A 144 1922 1992 1689 234 -170 179 C
+ATOM 1213 OG SER A 144 4.555 -2.361 15.795 1.00 16.91 O
+ANISOU 1213 OG SER A 144 2250 2249 1925 253 -159 147 O
+ATOM 1214 N CYS A 145 6.413 -5.035 16.803 1.00 13.27 N
+ANISOU 1214 N CYS A 145 1754 1797 1493 216 -206 107 N
+ATOM 1215 CA CYS A 145 7.837 -5.364 16.678 1.00 13.16 C
+ANISOU 1215 CA CYS A 145 1740 1774 1484 185 -230 69 C
+ATOM 1216 C CYS A 145 8.043 -6.722 16.046 1.00 12.44 C
+ANISOU 1216 C CYS A 145 1604 1686 1434 158 -237 69 C
+ATOM 1217 O CYS A 145 7.218 -7.618 16.221 1.00 12.76 O
+ANISOU 1217 O CYS A 145 1619 1736 1494 167 -232 96 O
+ATOM 1218 CB CYS A 145 8.549 -5.254 18.016 1.00 14.52 C
+ANISOU 1218 CB CYS A 145 1941 1942 1633 197 -239 66 C
+ATOM 1219 SG CYS A 145 8.542 -3.580 18.699 1.00 19.18 S
+ANISOU 1219 SG CYS A 145 2609 2515 2164 219 -233 55 S
+ATOM 1220 N GLY A 146 9.054 -6.812 15.211 1.00 11.62 N
+ANISOU 1220 N GLY A 146 1498 1572 1345 128 -246 39 N
+ATOM 1221 CA GLY A 146 9.297 -8.040 14.474 1.00 11.65 C
+ANISOU 1221 CA GLY A 146 1474 1568 1383 104 -244 34 C
+ATOM 1222 C GLY A 146 8.639 -8.028 13.111 1.00 11.50 C
+ANISOU 1222 C GLY A 146 1458 1546 1365 80 -242 30 C
+ATOM 1223 O GLY A 146 8.938 -8.880 12.282 1.00 12.48 O
+ANISOU 1223 O GLY A 146 1578 1655 1507 55 -237 17 O
+ATOM 1224 N SER A 147 7.753 -7.040 12.831 1.00 11.19 N
+ANISOU 1224 N SER A 147 1431 1517 1305 86 -243 43 N
+ATOM 1225 CA SER A 147 7.204 -6.880 11.475 1.00 11.25 C
+ANISOU 1225 CA SER A 147 1443 1522 1310 55 -249 43 C
+ATOM 1226 C SER A 147 8.385 -6.510 10.565 1.00 11.68 C
+ANISOU 1226 C SER A 147 1516 1561 1359 31 -246 2 C
+ATOM 1227 O SER A 147 9.322 -5.827 11.010 1.00 11.33 O
+ANISOU 1227 O SER A 147 1480 1514 1310 44 -243 -15 O
+ATOM 1228 CB SER A 147 6.210 -5.723 11.428 1.00 12.25 C
+ANISOU 1228 CB SER A 147 1573 1662 1420 69 -249 71 C
+ATOM 1229 OG SER A 147 5.054 -6.012 12.198 1.00 13.30 O
+ANISOU 1229 OG SER A 147 1685 1807 1562 96 -244 120 O
+ATOM 1230 N VAL A 148 8.354 -6.970 9.308 1.00 11.17 N
+ANISOU 1230 N VAL A 148 1463 1485 1295 -4 -246 -10 N
+ATOM 1231 CA VAL A 148 9.493 -6.779 8.444 1.00 11.78 C
+ANISOU 1231 CA VAL A 148 1560 1546 1370 -22 -233 -44 C
+ATOM 1232 C VAL A 148 9.223 -5.923 7.220 1.00 12.04 C
+ANISOU 1232 C VAL A 148 1614 1581 1381 -47 -239 -51 C
+ATOM 1233 O VAL A 148 8.088 -5.781 6.767 1.00 11.94 O
+ANISOU 1233 O VAL A 148 1603 1578 1356 -65 -256 -28 O
+ATOM 1234 CB VAL A 148 10.129 -8.138 8.036 1.00 12.63 C
+ANISOU 1234 CB VAL A 148 1675 1627 1497 -36 -213 -60 C
+ATOM 1235 CG1 VAL A 148 10.607 -8.914 9.260 1.00 12.66 C
+ANISOU 1235 CG1 VAL A 148 1651 1630 1529 -10 -206 -50 C
+ATOM 1236 CG2 VAL A 148 9.180 -8.973 7.195 1.00 13.55 C
+ANISOU 1236 CG2 VAL A 148 1812 1732 1603 -71 -223 -55 C
+ATOM 1237 N GLY A 149 10.312 -5.371 6.699 1.00 12.16 N
+ANISOU 1237 N GLY A 149 1641 1587 1394 -51 -225 -76 N
+ATOM 1238 CA GLY A 149 10.362 -4.619 5.460 1.00 12.30 C
+ANISOU 1238 CA GLY A 149 1680 1602 1390 -76 -224 -87 C
+ATOM 1239 C GLY A 149 11.095 -5.441 4.419 1.00 12.43 C
+ANISOU 1239 C GLY A 149 1725 1592 1405 -98 -198 -111 C
+ATOM 1240 O GLY A 149 12.033 -6.187 4.731 1.00 12.20 O
+ANISOU 1240 O GLY A 149 1692 1545 1400 -84 -172 -121 O
+ATOM 1241 N PHE A 150 10.650 -5.327 3.175 1.00 12.00 N
+ANISOU 1241 N PHE A 150 1703 1533 1322 -134 -202 -117 N
+ATOM 1242 CA PHE A 150 11.198 -6.146 2.114 1.00 13.19 C
+ANISOU 1242 CA PHE A 150 1901 1652 1460 -157 -172 -141 C
+ATOM 1243 C PHE A 150 10.981 -5.537 0.748 1.00 14.59 C
+ANISOU 1243 C PHE A 150 2117 1828 1599 -193 -176 -148 C
+ATOM 1244 O PHE A 150 10.124 -4.675 0.576 1.00 14.07 O
+ANISOU 1244 O PHE A 150 2039 1788 1519 -209 -211 -128 O
+ATOM 1245 CB PHE A 150 10.498 -7.529 2.164 1.00 13.42 C
+ANISOU 1245 CB PHE A 150 1951 1662 1486 -177 -178 -138 C
+ATOM 1246 CG PHE A 150 8.997 -7.465 1.967 1.00 14.35 C
+ANISOU 1246 CG PHE A 150 2071 1797 1583 -212 -228 -110 C
+ATOM 1247 CD1 PHE A 150 8.154 -7.170 3.021 1.00 15.42 C
+ANISOU 1247 CD1 PHE A 150 2157 1963 1740 -192 -256 -74 C
+ATOM 1248 CD2 PHE A 150 8.432 -7.691 0.721 1.00 15.45 C
+ANISOU 1248 CD2 PHE A 150 2264 1922 1683 -267 -246 -111 C
+ATOM 1249 CE1 PHE A 150 6.783 -7.040 2.825 1.00 16.35 C
+ANISOU 1249 CE1 PHE A 150 2266 2097 1848 -220 -297 -33 C
+ATOM 1250 CE2 PHE A 150 7.052 -7.611 0.541 1.00 16.30 C
+ANISOU 1250 CE2 PHE A 150 2366 2048 1780 -305 -299 -70 C
+ATOM 1251 CZ PHE A 150 6.239 -7.292 1.593 1.00 15.96 C
+ANISOU 1251 CZ PHE A 150 2261 2036 1767 -279 -322 -28 C
+ATOM 1252 N ASN A 151 11.734 -6.041 -0.222 1.00 15.13 N
+ANISOU 1252 N ASN A 151 2234 1864 1650 -206 -137 -174 N
+ATOM 1253 CA ASN A 151 11.561 -5.768 -1.644 1.00 16.70 C
+ANISOU 1253 CA ASN A 151 2490 2054 1802 -247 -136 -185 C
+ATOM 1254 C ASN A 151 11.469 -7.132 -2.334 1.00 18.24 C
+ANISOU 1254 C ASN A 151 2759 2203 1967 -277 -115 -205 C
+ATOM 1255 O ASN A 151 11.926 -8.137 -1.785 1.00 17.68 O
+ANISOU 1255 O ASN A 151 2690 2107 1922 -254 -83 -215 O
+ATOM 1256 CB ASN A 151 12.736 -4.982 -2.203 1.00 17.55 C
+ANISOU 1256 CB ASN A 151 2598 2158 1913 -227 -96 -196 C
+ATOM 1257 CG ASN A 151 12.678 -3.526 -1.848 1.00 21.16 C
+ANISOU 1257 CG ASN A 151 3002 2653 2385 -214 -125 -177 C
+ATOM 1258 OD1 ASN A 151 12.018 -2.729 -2.525 1.00 23.71 O
+ANISOU 1258 OD1 ASN A 151 3333 2995 2679 -243 -154 -168 O
+ATOM 1259 ND2 ASN A 151 13.342 -3.149 -0.770 1.00 19.82 N
+ANISOU 1259 ND2 ASN A 151 2779 2494 2257 -172 -122 -169 N
+ATOM 1260 N ILE A 152 10.860 -7.188 -3.527 1.00 19.82 N
+ANISOU 1260 N ILE A 152 3027 2392 2112 -333 -133 -211 N
+ATOM 1261 CA ILE A 152 10.779 -8.458 -4.255 1.00 22.59 C
+ANISOU 1261 CA ILE A 152 3469 2691 2424 -368 -114 -235 C
+ATOM 1262 C ILE A 152 11.333 -8.271 -5.655 1.00 25.21 C
+ANISOU 1262 C ILE A 152 3883 2993 2701 -391 -75 -260 C
+ATOM 1263 O ILE A 152 11.049 -7.265 -6.296 1.00 25.64 O
+ANISOU 1263 O ILE A 152 3936 3075 2730 -415 -102 -249 O
+ATOM 1264 CB ILE A 152 9.350 -9.069 -4.286 1.00 23.47 C
+ANISOU 1264 CB ILE A 152 3603 2802 2511 -428 -184 -213 C
+ATOM 1265 CG1 ILE A 152 8.720 -9.144 -2.884 1.00 24.58 C
+ANISOU 1265 CG1 ILE A 152 3656 2977 2707 -401 -221 -178 C
+ATOM 1266 CG2 ILE A 152 9.360 -10.453 -4.972 1.00 24.13 C
+ANISOU 1266 CG2 ILE A 152 3794 2822 2552 -466 -163 -242 C
+ATOM 1267 CD1 ILE A 152 7.304 -9.608 -2.866 1.00 25.76 C
+ANISOU 1267 CD1 ILE A 152 3812 3132 2845 -455 -290 -141 C
+ATOM 1268 N ASP A 153 12.157 -9.211 -6.114 1.00 26.83 N
+ANISOU 1268 N ASP A 153 4161 3142 2891 -379 -5 -292 N
+ATOM 1269 CA ASP A 153 12.655 -9.198 -7.484 1.00 28.74 C
+ANISOU 1269 CA ASP A 153 4501 3347 3071 -400 42 -317 C
+ATOM 1270 C ASP A 153 12.170 -10.512 -8.056 1.00 29.83 C
+ANISOU 1270 C ASP A 153 4755 3426 3155 -448 44 -342 C
+ATOM 1271 O ASP A 153 12.773 -11.548 -7.779 1.00 30.55 O
+ANISOU 1271 O ASP A 153 4875 3468 3264 -416 105 -360 O
+ATOM 1272 CB ASP A 153 14.184 -9.123 -7.546 1.00 31.89 C
+ANISOU 1272 CB ASP A 153 4891 3723 3503 -332 141 -327 C
+ATOM 1273 CG ASP A 153 14.688 -8.981 -8.971 1.00 40.02 C
+ANISOU 1273 CG ASP A 153 6021 4717 4468 -348 196 -349 C
+ATOM 1274 OD1 ASP A 153 13.977 -8.356 -9.795 1.00 41.47 O
+ANISOU 1274 OD1 ASP A 153 6244 4920 4593 -404 145 -348 O
+ATOM 1275 OD2 ASP A 153 15.789 -9.501 -9.268 1.00 43.80 O
+ANISOU 1275 OD2 ASP A 153 6541 5147 4955 -303 293 -361 O
+ATOM 1276 N TYR A 154 11.037 -10.469 -8.789 1.00 29.57 N
+ANISOU 1276 N TYR A 154 4783 3395 3057 -529 -29 -336 N
+ATOM 1277 CA TYR A 154 10.327 -11.603 -9.381 1.00 30.13 C
+ANISOU 1277 CA TYR A 154 4970 3411 3065 -599 -57 -351 C
+ATOM 1278 C TYR A 154 9.896 -12.627 -8.298 1.00 29.86 C
+ANISOU 1278 C TYR A 154 4899 3367 3080 -589 -80 -341 C
+ATOM 1279 O TYR A 154 8.809 -12.476 -7.736 1.00 30.57 O
+ANISOU 1279 O TYR A 154 4925 3498 3191 -620 -165 -302 O
+ATOM 1280 CB TYR A 154 11.081 -12.243 -10.574 0.50 30.31 C
+ANISOU 1280 CB TYR A 154 5145 3358 3015 -610 24 -398 C
+ATOM 1281 CG TYR A 154 10.357 -13.446 -11.143 0.50 31.41 C
+ANISOU 1281 CG TYR A 154 5418 3431 3083 -686 -9 -418 C
+ATOM 1282 CD1 TYR A 154 9.054 -13.341 -11.609 0.50 32.51 C
+ANISOU 1282 CD1 TYR A 154 5593 3587 3171 -784 -120 -392 C
+ATOM 1283 CD2 TYR A 154 10.964 -14.693 -11.188 0.50 32.38 C
+ANISOU 1283 CD2 TYR A 154 5632 3475 3196 -663 70 -455 C
+ATOM 1284 CE1 TYR A 154 8.372 -14.447 -12.100 0.50 33.48 C
+ANISOU 1284 CE1 TYR A 154 5842 3648 3230 -863 -162 -403 C
+ATOM 1285 CE2 TYR A 154 10.290 -15.808 -11.669 0.50 33.42 C
+ANISOU 1285 CE2 TYR A 154 5893 3541 3262 -736 36 -474 C
+ATOM 1286 CZ TYR A 154 8.994 -15.680 -12.131 0.50 34.48 C
+ANISOU 1286 CZ TYR A 154 6066 3693 3342 -840 -84 -449 C
+ATOM 1287 OH TYR A 154 8.328 -16.774 -12.627 0.50 36.31 O
+ANISOU 1287 OH TYR A 154 6433 3857 3507 -922 -128 -463 O
+ATOM 1288 N ASP A 155 10.732 -13.629 -7.970 1.00 28.99 N
+ANISOU 1288 N ASP A 155 4819 3204 2992 -543 -1 -370 N
+ATOM 1289 CA ASP A 155 10.368 -14.624 -6.961 1.00 28.27 C
+ANISOU 1289 CA ASP A 155 4692 3101 2947 -533 -20 -360 C
+ATOM 1290 C ASP A 155 11.249 -14.600 -5.720 1.00 26.66 C
+ANISOU 1290 C ASP A 155 4375 2920 2834 -445 33 -350 C
+ATOM 1291 O ASP A 155 11.085 -15.455 -4.854 1.00 27.06 O
+ANISOU 1291 O ASP A 155 4396 2961 2927 -429 28 -342 O
+ATOM 1292 CB ASP A 155 10.346 -16.038 -7.566 1.00 30.93 C
+ANISOU 1292 CB ASP A 155 5167 3350 3233 -570 10 -394 C
+ATOM 1293 CG ASP A 155 11.673 -16.511 -8.140 1.00 36.67 C
+ANISOU 1293 CG ASP A 155 5979 4010 3946 -521 136 -436 C
+ATOM 1294 OD1 ASP A 155 12.607 -15.683 -8.250 1.00 37.43 O
+ANISOU 1294 OD1 ASP A 155 6029 4128 4064 -465 196 -435 O
+ATOM 1295 OD2 ASP A 155 11.772 -17.708 -8.495 1.00 39.58 O
+ANISOU 1295 OD2 ASP A 155 6460 4298 4281 -537 176 -465 O
+ATOM 1296 N CYS A 156 12.175 -13.637 -5.622 1.00 24.66 N
+ANISOU 1296 N CYS A 156 4061 2698 2611 -390 78 -346 N
+ATOM 1297 CA CYS A 156 13.076 -13.566 -4.484 1.00 23.25 C
+ANISOU 1297 CA CYS A 156 3780 2540 2516 -314 122 -330 C
+ATOM 1298 C CYS A 156 12.758 -12.398 -3.587 1.00 20.76 C
+ANISOU 1298 C CYS A 156 3346 2300 2241 -297 62 -297 C
+ATOM 1299 O CYS A 156 12.827 -11.248 -4.023 1.00 20.48 O
+ANISOU 1299 O CYS A 156 3294 2298 2191 -301 50 -292 O
+ATOM 1300 CB CYS A 156 14.525 -13.518 -4.955 1.00 24.48 C
+ANISOU 1300 CB CYS A 156 3957 2659 2683 -262 226 -343 C
+ATOM 1301 SG CYS A 156 15.738 -13.478 -3.610 1.00 27.04 S
+ANISOU 1301 SG CYS A 156 4155 3003 3114 -177 276 -310 S
+ATOM 1302 N VAL A 157 12.484 -12.680 -2.310 1.00 18.60 N
+ANISOU 1302 N VAL A 157 2993 2052 2021 -273 34 -275 N
+ATOM 1303 CA VAL A 157 12.218 -11.620 -1.344 1.00 17.05 C
+ANISOU 1303 CA VAL A 157 2695 1921 1862 -250 -13 -245 C
+ATOM 1304 C VAL A 157 13.514 -11.180 -0.700 1.00 15.71 C
+ANISOU 1304 C VAL A 157 2462 1761 1745 -190 35 -237 C
+ATOM 1305 O VAL A 157 14.196 -11.995 -0.084 1.00 15.50 O
+ANISOU 1305 O VAL A 157 2416 1712 1762 -156 77 -233 O
+ATOM 1306 CB VAL A 157 11.247 -12.102 -0.243 1.00 17.28 C
+ANISOU 1306 CB VAL A 157 2674 1973 1918 -254 -67 -219 C
+ATOM 1307 CG1 VAL A 157 10.950 -10.990 0.757 1.00 17.60 C
+ANISOU 1307 CG1 VAL A 157 2624 2074 1989 -227 -108 -189 C
+ATOM 1308 CG2 VAL A 157 9.958 -12.653 -0.847 1.00 18.06 C
+ANISOU 1308 CG2 VAL A 157 2831 2058 1974 -319 -121 -214 C
+ATOM 1309 N SER A 158 13.840 -9.894 -0.794 1.00 15.06 N
+ANISOU 1309 N SER A 158 2344 1714 1665 -178 25 -229 N
+ATOM 1310 CA SER A 158 15.008 -9.358 -0.111 1.00 14.90 C
+ANISOU 1310 CA SER A 158 2258 1707 1698 -129 54 -212 C
+ATOM 1311 C SER A 158 14.517 -8.654 1.138 1.00 14.32 C
+ANISOU 1311 C SER A 158 2111 1683 1649 -118 -5 -189 C
+ATOM 1312 O SER A 158 13.944 -7.567 1.050 1.00 14.24 O
+ANISOU 1312 O SER A 158 2087 1705 1618 -132 -47 -183 O
+ATOM 1313 CB SER A 158 15.755 -8.366 -0.997 1.00 17.17 C
+ANISOU 1313 CB SER A 158 2555 1997 1973 -125 81 -214 C
+ATOM 1314 OG SER A 158 16.436 -9.063 -2.024 1.00 20.62 O
+ANISOU 1314 OG SER A 158 3059 2382 2392 -122 154 -230 O
+ATOM 1315 N PHE A 159 14.725 -9.276 2.299 1.00 13.50 N
+ANISOU 1315 N PHE A 159 1963 1580 1587 -92 -6 -174 N
+ATOM 1316 CA PHE A 159 14.327 -8.676 3.565 1.00 13.12 C
+ANISOU 1316 CA PHE A 159 1856 1572 1557 -78 -55 -152 C
+ATOM 1317 C PHE A 159 15.366 -7.649 3.959 1.00 12.99 C
+ANISOU 1317 C PHE A 159 1799 1570 1566 -54 -52 -138 C
+ATOM 1318 O PHE A 159 16.559 -7.954 3.983 1.00 13.40 O
+ANISOU 1318 O PHE A 159 1835 1603 1655 -34 -12 -127 O
+ATOM 1319 CB PHE A 159 14.245 -9.749 4.654 1.00 12.61 C
+ANISOU 1319 CB PHE A 159 1763 1503 1525 -61 -55 -139 C
+ATOM 1320 CG PHE A 159 13.131 -10.726 4.411 1.00 11.64 C
+ANISOU 1320 CG PHE A 159 1674 1367 1381 -86 -69 -146 C
+ATOM 1321 CD1 PHE A 159 11.819 -10.392 4.702 1.00 12.23 C
+ANISOU 1321 CD1 PHE A 159 1742 1471 1436 -104 -121 -133 C
+ATOM 1322 CD2 PHE A 159 13.391 -11.978 3.887 1.00 11.94 C
+ANISOU 1322 CD2 PHE A 159 1754 1360 1424 -94 -28 -160 C
+ATOM 1323 CE1 PHE A 159 10.793 -11.300 4.508 1.00 12.59 C
+ANISOU 1323 CE1 PHE A 159 1811 1504 1468 -132 -142 -128 C
+ATOM 1324 CE2 PHE A 159 12.357 -12.881 3.669 1.00 12.59 C
+ANISOU 1324 CE2 PHE A 159 1872 1425 1485 -125 -50 -164 C
+ATOM 1325 CZ PHE A 159 11.064 -12.538 3.991 1.00 12.27 C
+ANISOU 1325 CZ PHE A 159 1816 1420 1428 -146 -111 -145 C
+ATOM 1326 N CYS A 160 14.918 -6.444 4.317 1.00 12.93 N
+ANISOU 1326 N CYS A 160 1774 1596 1544 -56 -96 -132 N
+ATOM 1327 CA CYS A 160 15.839 -5.365 4.668 1.00 13.50 C
+ANISOU 1327 CA CYS A 160 1816 1679 1634 -42 -104 -118 C
+ATOM 1328 C CYS A 160 15.596 -4.739 6.011 1.00 13.22 C
+ANISOU 1328 C CYS A 160 1752 1668 1604 -30 -148 -103 C
+ATOM 1329 O CYS A 160 16.451 -3.984 6.456 1.00 13.85 O
+ANISOU 1329 O CYS A 160 1811 1751 1700 -23 -161 -89 O
+ATOM 1330 CB CYS A 160 15.838 -4.296 3.580 1.00 14.93 C
+ANISOU 1330 CB CYS A 160 2017 1866 1789 -58 -105 -128 C
+ATOM 1331 SG CYS A 160 14.213 -3.572 3.272 1.00 15.19 S
+ANISOU 1331 SG CYS A 160 2072 1925 1776 -81 -147 -136 S
+ATOM 1332 N TYR A 161 14.433 -4.952 6.614 1.00 12.04 N
+ANISOU 1332 N TYR A 161 1606 1533 1436 -29 -171 -103 N
+ATOM 1333 CA TYR A 161 14.112 -4.270 7.849 1.00 11.92 C
+ANISOU 1333 CA TYR A 161 1578 1535 1414 -14 -205 -90 C
+ATOM 1334 C TYR A 161 13.335 -5.134 8.797 1.00 11.21 C
+ANISOU 1334 C TYR A 161 1479 1452 1326 -1 -212 -80 C
+ATOM 1335 O TYR A 161 12.520 -5.929 8.377 1.00 11.05 O
+ANISOU 1335 O TYR A 161 1466 1431 1302 -10 -204 -81 O
+ATOM 1336 CB TYR A 161 13.272 -3.020 7.497 1.00 11.04 C
+ANISOU 1336 CB TYR A 161 1484 1439 1270 -19 -224 -94 C
+ATOM 1337 CG TYR A 161 12.873 -2.174 8.686 1.00 11.13 C
+ANISOU 1337 CG TYR A 161 1499 1462 1268 1 -248 -83 C
+ATOM 1338 CD1 TYR A 161 13.734 -1.221 9.206 1.00 12.22 C
+ANISOU 1338 CD1 TYR A 161 1642 1594 1405 4 -266 -82 C
+ATOM 1339 CD2 TYR A 161 11.614 -2.292 9.256 1.00 11.72 C
+ANISOU 1339 CD2 TYR A 161 1577 1549 1328 15 -253 -70 C
+ATOM 1340 CE1 TYR A 161 13.370 -0.445 10.303 1.00 12.77 C
+ANISOU 1340 CE1 TYR A 161 1733 1666 1453 20 -286 -76 C
+ATOM 1341 CE2 TYR A 161 11.245 -1.535 10.356 1.00 12.42 C
+ANISOU 1341 CE2 TYR A 161 1680 1641 1399 39 -263 -60 C
+ATOM 1342 CZ TYR A 161 12.120 -0.604 10.873 1.00 12.57 C
+ANISOU 1342 CZ TYR A 161 1717 1649 1409 41 -279 -67 C
+ATOM 1343 OH TYR A 161 11.751 0.138 11.977 1.00 12.95 O
+ANISOU 1343 OH TYR A 161 1797 1693 1430 63 -287 -61 O
+ATOM 1344 N MET A 162 13.585 -4.974 10.085 1.00 10.28 N
+ANISOU 1344 N MET A 162 1349 1341 1214 16 -230 -66 N
+ATOM 1345 CA MET A 162 12.783 -5.594 11.126 1.00 10.68 C
+ANISOU 1345 CA MET A 162 1393 1402 1261 32 -238 -51 C
+ATOM 1346 C MET A 162 12.509 -4.476 12.131 1.00 10.72 C
+ANISOU 1346 C MET A 162 1416 1418 1238 49 -260 -44 C
+ATOM 1347 O MET A 162 13.429 -3.757 12.531 1.00 10.71 O
+ANISOU 1347 O MET A 162 1424 1411 1235 45 -277 -45 O
+ATOM 1348 CB MET A 162 13.469 -6.782 11.785 1.00 11.91 C
+ANISOU 1348 CB MET A 162 1523 1551 1451 37 -230 -39 C
+ATOM 1349 CG MET A 162 12.631 -7.332 12.936 1.00 12.92 C
+ANISOU 1349 CG MET A 162 1644 1693 1574 56 -240 -21 C
+ATOM 1350 SD MET A 162 13.162 -8.961 13.503 1.00 15.17 S
+ANISOU 1350 SD MET A 162 1893 1969 1903 60 -227 -4 S
+ATOM 1351 CE MET A 162 12.432 -9.997 12.218 1.00 16.30 C
+ANISOU 1351 CE MET A 162 2042 2095 2055 44 -201 -18 C
+ATOM 1352 N HIS A 163 11.245 -4.306 12.496 1.00 10.85 N
+ANISOU 1352 N HIS A 163 1442 1446 1233 66 -259 -33 N
+ATOM 1353 CA HIS A 163 10.862 -3.230 13.394 1.00 10.78 C
+ANISOU 1353 CA HIS A 163 1463 1439 1192 88 -267 -27 C
+ATOM 1354 C HIS A 163 11.218 -3.501 14.829 1.00 10.88 C
+ANISOU 1354 C HIS A 163 1486 1451 1197 103 -278 -17 C
+ATOM 1355 O HIS A 163 10.858 -4.554 15.333 1.00 11.36 O
+ANISOU 1355 O HIS A 163 1525 1519 1271 113 -271 -1 O
+ATOM 1356 CB HIS A 163 9.363 -2.967 13.299 1.00 11.80 C
+ANISOU 1356 CB HIS A 163 1596 1579 1309 107 -252 -6 C
+ATOM 1357 CG HIS A 163 8.995 -1.754 14.072 1.00 12.60 C
+ANISOU 1357 CG HIS A 163 1737 1674 1376 134 -246 -1 C
+ATOM 1358 ND1 HIS A 163 9.637 -0.545 13.857 1.00 13.89 N
+ANISOU 1358 ND1 HIS A 163 1932 1824 1522 125 -257 -21 N
+ATOM 1359 CD2 HIS A 163 8.139 -1.619 15.105 1.00 13.61 C
+ANISOU 1359 CD2 HIS A 163 1884 1803 1484 172 -229 23 C
+ATOM 1360 CE1 HIS A 163 9.124 0.289 14.740 1.00 14.58 C
+ANISOU 1360 CE1 HIS A 163 2062 1900 1576 155 -245 -12 C
+ATOM 1361 NE2 HIS A 163 8.222 -0.307 15.514 1.00 14.16 N
+ANISOU 1361 NE2 HIS A 163 2005 1855 1519 186 -224 14 N
+ATOM 1362 N HIS A 164 11.850 -2.524 15.504 1.00 10.72 N
+ANISOU 1362 N HIS A 164 1504 1420 1151 102 -297 -23 N
+ATOM 1363 CA HIS A 164 12.191 -2.691 16.911 1.00 12.02 C
+ANISOU 1363 CA HIS A 164 1691 1581 1297 109 -315 -12 C
+ATOM 1364 C HIS A 164 11.654 -1.626 17.827 1.00 13.54 C
+ANISOU 1364 C HIS A 164 1951 1761 1434 131 -314 -13 C
+ATOM 1365 O HIS A 164 11.296 -1.961 18.960 1.00 14.57 O
+ANISOU 1365 O HIS A 164 2104 1892 1541 150 -310 -1 O
+ATOM 1366 CB HIS A 164 13.720 -2.699 17.140 1.00 12.32 C
+ANISOU 1366 CB HIS A 164 1722 1610 1352 75 -351 -10 C
+ATOM 1367 CG HIS A 164 14.408 -3.927 16.654 1.00 11.31 C
+ANISOU 1367 CG HIS A 164 1532 1487 1278 62 -345 1 C
+ATOM 1368 ND1 HIS A 164 15.090 -4.762 17.524 1.00 11.61 N
+ANISOU 1368 ND1 HIS A 164 1547 1526 1337 53 -361 25 N
+ATOM 1369 CD2 HIS A 164 14.549 -4.392 15.393 1.00 11.50 C
+ANISOU 1369 CD2 HIS A 164 1520 1510 1338 54 -321 -6 C
+ATOM 1370 CE1 HIS A 164 15.623 -5.706 16.765 1.00 11.94 C
+ANISOU 1370 CE1 HIS A 164 1538 1568 1431 46 -342 33 C
+ATOM 1371 NE2 HIS A 164 15.308 -5.537 15.478 1.00 12.33 N
+ANISOU 1371 NE2 HIS A 164 1584 1614 1487 47 -316 11 N
+ATOM 1372 N AMET A 165 11.586 -0.360 17.376 0.50 14.49 N
+ANISOU 1372 N AMET A 165 2107 1865 1532 126 -317 -29 N
+ATOM 1373 N BMET A 165 11.783 -0.326 17.439 0.50 13.59 N
+ANISOU 1373 N BMET A 165 1993 1751 1418 126 -317 -29 N
+ATOM 1374 CA AMET A 165 11.139 0.666 18.305 0.50 16.09 C
+ANISOU 1374 CA AMET A 165 2385 2048 1679 154 -305 -30 C
+ATOM 1375 CA BMET A 165 11.504 0.797 18.336 0.50 14.00 C
+ANISOU 1375 CA BMET A 165 2125 1782 1414 148 -313 -32 C
+ATOM 1376 C AMET A 165 10.595 1.912 17.722 0.50 15.90 C
+ANISOU 1376 C AMET A 165 2389 2011 1640 169 -281 -37 C
+ATOM 1377 C BMET A 165 10.702 1.944 17.739 0.50 14.88 C
+ANISOU 1377 C BMET A 165 2261 1882 1511 168 -283 -38 C
+ATOM 1378 O AMET A 165 10.776 2.215 16.550 0.50 15.72 O
+ANISOU 1378 O AMET A 165 2340 1991 1642 146 -292 -48 O
+ATOM 1379 O BMET A 165 10.842 2.241 16.560 0.50 14.65 O
+ANISOU 1379 O BMET A 165 2205 1856 1506 147 -292 -48 O
+ATOM 1380 CB AMET A 165 12.260 1.033 19.260 0.50 18.07 C
+ANISOU 1380 CB AMET A 165 2700 2275 1892 129 -348 -39 C
+ATOM 1381 CB BMET A 165 12.844 1.448 18.767 0.50 13.85 C
+ANISOU 1381 CB BMET A 165 2153 1739 1371 111 -364 -44 C
+ATOM 1382 CG AMET A 165 13.510 1.441 18.567 0.50 21.85 C
+ANISOU 1382 CG AMET A 165 3156 2749 2397 85 -389 -47 C
+ATOM 1383 CG BMET A 165 13.883 0.481 19.312 0.50 14.29 C
+ANISOU 1383 CG BMET A 165 2179 1802 1450 75 -407 -30 C
+ATOM 1384 SD AMET A 165 14.871 1.411 19.737 0.50 29.90 S
+ANISOU 1384 SD AMET A 165 4189 3763 3410 48 -446 -30 S
+ATOM 1385 SD BMET A 165 13.470 -0.155 20.945 0.50 15.29 S
+ANISOU 1385 SD BMET A 165 2343 1928 1536 91 -411 -13 S
+ATOM 1386 CE AMET A 165 14.286 0.130 20.907 0.50 30.34 C
+ANISOU 1386 CE AMET A 165 4248 3833 3446 84 -417 -14 C
+ATOM 1387 CE BMET A 165 13.829 1.249 21.920 0.50 19.00 C
+ANISOU 1387 CE BMET A 165 2937 2357 1926 73 -447 -26 C
+ATOM 1388 N GLU A 166 9.962 2.669 18.591 1.00 16.13 N
+ANISOU 1388 N GLU A 166 2493 2015 1619 199 -262 -36 N
+ATOM 1389 CA GLU A 166 9.355 3.908 18.240 1.00 17.53 C
+ANISOU 1389 CA GLU A 166 2711 2172 1777 221 -233 -39 C
+ATOM 1390 C GLU A 166 10.049 4.945 19.115 1.00 19.53 C
+ANISOU 1390 C GLU A 166 3063 2383 1974 209 -257 -62 C
+ATOM 1391 O GLU A 166 10.099 4.793 20.337 1.00 20.14 O
+ANISOU 1391 O GLU A 166 3201 2445 2007 219 -259 -61 O
+ATOM 1392 CB GLU A 166 7.885 3.883 18.595 1.00 19.56 C
+ANISOU 1392 CB GLU A 166 2977 2430 2027 279 -169 -7 C
+ATOM 1393 CG GLU A 166 7.200 5.177 18.243 1.00 23.51 C
+ANISOU 1393 CG GLU A 166 3512 2905 2515 306 -131 -1 C
+ATOM 1394 CD GLU A 166 5.719 4.914 18.267 1.00 27.84 C
+ANISOU 1394 CD GLU A 166 4030 3466 3083 360 -68 49 C
+ATOM 1395 OE1 GLU A 166 5.148 4.841 19.378 1.00 29.33 O
+ANISOU 1395 OE1 GLU A 166 4265 3640 3240 405 -28 68 O
+ATOM 1396 OE2 GLU A 166 5.144 4.697 17.176 1.00 27.18 O
+ANISOU 1396 OE2 GLU A 166 3872 3407 3047 354 -62 75 O
+ATOM 1397 N LEU A 167 10.596 5.973 18.494 1.00 20.80 N
+ANISOU 1397 N LEU A 167 3244 2526 2134 184 -279 -79 N
+ATOM 1398 CA LEU A 167 11.246 7.053 19.220 1.00 23.30 C
+ANISOU 1398 CA LEU A 167 3661 2796 2395 166 -309 -100 C
+ATOM 1399 C LEU A 167 10.170 7.948 19.834 1.00 25.62 C
+ANISOU 1399 C LEU A 167 4043 3052 2639 220 -247 -99 C
+ATOM 1400 O LEU A 167 9.054 8.016 19.312 1.00 25.54 O
+ANISOU 1400 O LEU A 167 3997 3053 2653 264 -187 -78 O
+ATOM 1401 CB LEU A 167 12.109 7.853 18.227 1.00 24.19 C
+ANISOU 1401 CB LEU A 167 3754 2902 2534 124 -348 -113 C
+ATOM 1402 CG LEU A 167 13.150 7.045 17.422 1.00 26.98 C
+ANISOU 1402 CG LEU A 167 4016 3291 2946 79 -394 -107 C
+ATOM 1403 CD1 LEU A 167 14.029 7.967 16.621 1.00 28.28 C
+ANISOU 1403 CD1 LEU A 167 4176 3442 3127 40 -432 -114 C
+ATOM 1404 CD2 LEU A 167 14.022 6.155 18.327 1.00 27.79 C
+ANISOU 1404 CD2 LEU A 167 4117 3399 3045 50 -439 -97 C
+ATOM 1405 N PRO A 168 10.502 8.716 20.885 1.00 27.44 N
+ANISOU 1405 N PRO A 168 4393 3232 2800 214 -261 -117 N
+ATOM 1406 CA PRO A 168 9.495 9.604 21.486 1.00 28.84 C
+ANISOU 1406 CA PRO A 168 4669 3364 2926 271 -190 -117 C
+ATOM 1407 C PRO A 168 8.854 10.601 20.525 1.00 30.15 C
+ANISOU 1407 C PRO A 168 4820 3517 3119 298 -144 -111 C
+ATOM 1408 O PRO A 168 7.806 11.147 20.853 1.00 31.65 O
+ANISOU 1408 O PRO A 168 5059 3678 3287 360 -67 -95 O
+ATOM 1409 CB PRO A 168 10.264 10.307 22.605 1.00 29.60 C
+ANISOU 1409 CB PRO A 168 4906 3403 2940 240 -231 -145 C
+ATOM 1410 CG PRO A 168 11.376 9.380 22.945 1.00 29.87 C
+ANISOU 1410 CG PRO A 168 4903 3464 2981 179 -313 -145 C
+ATOM 1411 CD PRO A 168 11.767 8.736 21.646 1.00 27.74 C
+ANISOU 1411 CD PRO A 168 4489 3251 2801 155 -339 -133 C
+ATOM 1412 N THR A 169 9.448 10.838 19.342 1.00 29.64 N
+ANISOU 1412 N THR A 169 4686 3473 3103 257 -187 -118 N
+ATOM 1413 CA THR A 169 8.869 11.743 18.351 1.00 29.70 C
+ANISOU 1413 CA THR A 169 4668 3475 3142 278 -149 -108 C
+ATOM 1414 C THR A 169 7.931 11.078 17.330 1.00 29.13 C
+ANISOU 1414 C THR A 169 4478 3455 3136 302 -111 -70 C
+ATOM 1415 O THR A 169 7.497 11.738 16.388 1.00 29.33 O
+ANISOU 1415 O THR A 169 4469 3484 3194 311 -89 -55 O
+ATOM 1416 CB THR A 169 9.946 12.533 17.623 1.00 31.65 C
+ANISOU 1416 CB THR A 169 4914 3711 3402 222 -211 -131 C
+ATOM 1417 OG1 THR A 169 10.933 11.626 17.118 1.00 32.87 O
+ANISOU 1417 OG1 THR A 169 4986 3909 3595 169 -276 -134 O
+ATOM 1418 CG2 THR A 169 10.574 13.602 18.502 1.00 32.20 C
+ANISOU 1418 CG2 THR A 169 5117 3714 3405 203 -239 -159 C
+ATOM 1419 N GLY A 170 7.618 9.799 17.517 1.00 28.09 N
+ANISOU 1419 N GLY A 170 4288 3363 3024 310 -107 -52 N
+ATOM 1420 CA GLY A 170 6.690 9.104 16.634 1.00 27.29 C
+ANISOU 1420 CA GLY A 170 4084 3306 2979 327 -78 -12 C
+ATOM 1421 C GLY A 170 7.276 8.478 15.392 1.00 25.98 C
+ANISOU 1421 C GLY A 170 3825 3184 2863 276 -126 -18 C
+ATOM 1422 O GLY A 170 6.531 7.969 14.548 1.00 26.76 O
+ANISOU 1422 O GLY A 170 3849 3314 3003 280 -110 14 O
+ATOM 1423 N VAL A 171 8.602 8.553 15.235 1.00 23.64 N
+ANISOU 1423 N VAL A 171 3537 2884 2562 226 -185 -54 N
+ATOM 1424 CA VAL A 171 9.262 7.930 14.096 1.00 21.19 C
+ANISOU 1424 CA VAL A 171 3148 2609 2295 182 -223 -60 C
+ATOM 1425 C VAL A 171 9.803 6.561 14.543 1.00 17.38 C
+ANISOU 1425 C VAL A 171 2636 2147 1821 166 -248 -64 C
+ATOM 1426 O VAL A 171 9.847 6.266 15.735 1.00 17.18 O
+ANISOU 1426 O VAL A 171 2655 2109 1765 180 -248 -66 O
+ATOM 1427 CB VAL A 171 10.323 8.817 13.418 1.00 22.74 C
+ANISOU 1427 CB VAL A 171 3351 2792 2497 143 -262 -82 C
+ATOM 1428 CG1 VAL A 171 9.690 10.084 12.853 1.00 23.85 C
+ANISOU 1428 CG1 VAL A 171 3511 2915 2636 161 -234 -74 C
+ATOM 1429 CG2 VAL A 171 11.443 9.141 14.386 1.00 23.08 C
+ANISOU 1429 CG2 VAL A 171 3457 2805 2507 118 -307 -104 C
+ATOM 1430 N HIS A 172 10.166 5.722 13.586 1.00 15.44 N
+ANISOU 1430 N HIS A 172 2320 1932 1615 137 -265 -64 N
+ATOM 1431 CA HIS A 172 10.508 4.343 13.854 1.00 13.98 C
+ANISOU 1431 CA HIS A 172 2098 1766 1447 127 -277 -62 C
+ATOM 1432 C HIS A 172 11.940 3.965 13.543 1.00 13.47 C
+ANISOU 1432 C HIS A 172 2010 1704 1405 86 -317 -76 C
+ATOM 1433 O HIS A 172 12.551 4.481 12.612 1.00 13.64 O
+ANISOU 1433 O HIS A 172 2016 1725 1443 62 -330 -84 O
+ATOM 1434 CB HIS A 172 9.512 3.472 13.081 1.00 13.55 C
+ANISOU 1434 CB HIS A 172 1986 1740 1423 134 -251 -41 C
+ATOM 1435 CG HIS A 172 8.096 3.784 13.471 1.00 13.40 C
+ANISOU 1435 CG HIS A 172 1979 1719 1392 177 -211 -10 C
+ATOM 1436 ND1 HIS A 172 7.228 4.426 12.601 1.00 14.72 N
+ANISOU 1436 ND1 HIS A 172 2129 1892 1572 184 -190 13 N
+ATOM 1437 CD2 HIS A 172 7.501 3.693 14.686 1.00 14.40 C
+ANISOU 1437 CD2 HIS A 172 2140 1836 1495 216 -186 6 C
+ATOM 1438 CE1 HIS A 172 6.107 4.609 13.283 1.00 15.27 C
+ANISOU 1438 CE1 HIS A 172 2212 1955 1633 229 -150 48 C
+ATOM 1439 NE2 HIS A 172 6.228 4.194 14.544 1.00 15.66 N
+ANISOU 1439 NE2 HIS A 172 2297 1995 1659 252 -143 44 N
+ATOM 1440 N ALA A 173 12.452 3.012 14.322 1.00 12.95 N
+ANISOU 1440 N ALA A 173 1934 1642 1343 80 -331 -72 N
+ATOM 1441 CA ALA A 173 13.821 2.530 14.168 1.00 12.79 C
+ANISOU 1441 CA ALA A 173 1885 1623 1353 46 -364 -72 C
+ATOM 1442 C ALA A 173 13.843 1.028 14.231 1.00 12.27 C
+ANISOU 1442 C ALA A 173 1771 1575 1317 48 -352 -61 C
+ATOM 1443 O ALA A 173 13.033 0.406 14.916 1.00 12.33 O
+ANISOU 1443 O ALA A 173 1781 1590 1312 72 -336 -53 O
+ATOM 1444 CB ALA A 173 14.713 3.092 15.263 1.00 13.06 C
+ANISOU 1444 CB ALA A 173 1967 1635 1362 27 -408 -69 C
+ATOM 1445 N GLY A 174 14.761 0.447 13.481 1.00 11.78 N
+ANISOU 1445 N GLY A 174 1663 1516 1295 26 -356 -57 N
+ATOM 1446 CA GLY A 174 14.888 -0.994 13.445 1.00 11.54 C
+ANISOU 1446 CA GLY A 174 1590 1496 1298 28 -340 -47 C
+ATOM 1447 C GLY A 174 16.188 -1.435 12.847 1.00 11.18 C
+ANISOU 1447 C GLY A 174 1505 1445 1298 6 -341 -36 C
+ATOM 1448 O GLY A 174 17.097 -0.636 12.618 1.00 11.32 O
+ANISOU 1448 O GLY A 174 1524 1453 1323 -12 -363 -29 O
+ATOM 1449 N THR A 175 16.261 -2.716 12.564 1.00 10.81 N
+ANISOU 1449 N THR A 175 1423 1401 1283 10 -314 -30 N
+ATOM 1450 CA THR A 175 17.491 -3.329 12.129 1.00 10.66 C
+ANISOU 1450 CA THR A 175 1365 1372 1314 -1 -302 -10 C
+ATOM 1451 C THR A 175 17.367 -3.974 10.774 1.00 10.85 C
+ANISOU 1451 C THR A 175 1378 1390 1355 1 -256 -25 C
+ATOM 1452 O THR A 175 16.261 -4.147 10.274 1.00 11.09 O
+ANISOU 1452 O THR A 175 1427 1426 1360 6 -241 -47 O
+ATOM 1453 CB THR A 175 17.861 -4.455 13.166 1.00 11.46 C
+ANISOU 1453 CB THR A 175 1438 1473 1442 3 -307 17 C
+ATOM 1454 OG1 THR A 175 16.924 -5.534 13.087 1.00 11.86 O
+ANISOU 1454 OG1 THR A 175 1485 1530 1492 19 -277 4 O
+ATOM 1455 CG2 THR A 175 17.958 -3.963 14.586 1.00 10.45 C
+ANISOU 1455 CG2 THR A 175 1331 1350 1289 -4 -355 32 C
+ATOM 1456 N ASP A 176 18.499 -4.410 10.211 1.00 10.92 N
+ANISOU 1456 N ASP A 176 1357 1384 1409 -3 -231 -6 N
+ATOM 1457 CA ASP A 176 18.444 -5.296 9.071 1.00 11.27 C
+ANISOU 1457 CA ASP A 176 1402 1414 1467 2 -177 -19 C
+ATOM 1458 C ASP A 176 18.223 -6.736 9.677 1.00 12.10 C
+ANISOU 1458 C ASP A 176 1491 1512 1593 14 -159 -11 C
+ATOM 1459 O ASP A 176 18.096 -6.893 10.907 1.00 12.09 O
+ANISOU 1459 O ASP A 176 1476 1524 1594 17 -190 5 O
+ATOM 1460 CB ASP A 176 19.709 -5.176 8.218 1.00 12.43 C
+ANISOU 1460 CB ASP A 176 1529 1542 1652 2 -144 2 C
+ATOM 1461 CG ASP A 176 20.997 -5.503 8.928 1.00 14.28 C
+ANISOU 1461 CG ASP A 176 1714 1768 1944 5 -146 55 C
+ATOM 1462 OD1 ASP A 176 20.945 -6.153 10.000 1.00 12.59 O
+ANISOU 1462 OD1 ASP A 176 1481 1558 1743 8 -165 72 O
+ATOM 1463 OD2 ASP A 176 22.059 -5.109 8.421 1.00 16.57 O
+ANISOU 1463 OD2 ASP A 176 1979 2047 2269 4 -132 86 O
+ATOM 1464 N LEU A 177 18.214 -7.776 8.839 1.00 12.56 N
+ANISOU 1464 N LEU A 177 1557 1549 1667 18 -108 -21 N
+ATOM 1465 CA LEU A 177 17.977 -9.134 9.340 1.00 13.37 C
+ANISOU 1465 CA LEU A 177 1647 1641 1791 28 -91 -14 C
+ATOM 1466 C LEU A 177 19.229 -9.788 9.950 1.00 14.68 C
+ANISOU 1466 C LEU A 177 1765 1794 2020 40 -71 31 C
+ATOM 1467 O LEU A 177 19.141 -10.901 10.466 1.00 15.23 O
+ANISOU 1467 O LEU A 177 1817 1855 2115 49 -57 43 O
+ATOM 1468 CB LEU A 177 17.292 -10.027 8.318 1.00 13.37 C
+ANISOU 1468 CB LEU A 177 1687 1618 1774 23 -52 -44 C
+ATOM 1469 CG LEU A 177 15.764 -9.973 8.325 1.00 14.51 C
+ANISOU 1469 CG LEU A 177 1860 1781 1872 9 -85 -67 C
+ATOM 1470 CD1 LEU A 177 15.215 -10.582 9.597 1.00 15.35 C
+ANISOU 1470 CD1 LEU A 177 1940 1903 1990 20 -110 -50 C
+ATOM 1471 CD2 LEU A 177 15.227 -8.547 8.101 1.00 15.65 C
+ANISOU 1471 CD2 LEU A 177 2019 1950 1976 -1 -120 -78 C
+ATOM 1472 N GLU A 178 20.370 -9.083 9.938 1.00 14.29 N
+ANISOU 1472 N GLU A 178 1687 1743 1999 38 -76 64 N
+ATOM 1473 CA GLU A 178 21.541 -9.484 10.702 1.00 13.76 C
+ANISOU 1473 CA GLU A 178 1564 1671 1995 43 -76 123 C
+ATOM 1474 C GLU A 178 21.486 -8.861 12.125 1.00 13.43 C
+ANISOU 1474 C GLU A 178 1508 1657 1938 26 -152 143 C
+ATOM 1475 O GLU A 178 22.376 -9.100 12.928 1.00 13.86 O
+ANISOU 1475 O GLU A 178 1516 1712 2037 20 -171 198 O
+ATOM 1476 CB GLU A 178 22.832 -9.097 9.978 1.00 15.67 C
+ANISOU 1476 CB GLU A 178 1777 1894 2282 47 -44 162 C
+ATOM 1477 CG GLU A 178 22.961 -9.834 8.661 1.00 20.95 C
+ANISOU 1477 CG GLU A 178 2469 2527 2963 68 43 145 C
+ATOM 1478 CD GLU A 178 24.223 -9.546 7.877 1.00 29.38 C
+ANISOU 1478 CD GLU A 178 3511 3573 4079 81 92 189 C
+ATOM 1479 OE1 GLU A 178 24.984 -8.632 8.273 1.00 29.50 O
+ANISOU 1479 OE1 GLU A 178 3485 3603 4119 68 49 235 O
+ATOM 1480 OE2 GLU A 178 24.452 -10.242 6.861 1.00 33.24 O
+ANISOU 1480 OE2 GLU A 178 4024 4025 4580 103 175 182 O
+ATOM 1481 N GLY A 179 20.467 -8.044 12.419 1.00 13.13 N
+ANISOU 1481 N GLY A 179 1512 1640 1836 18 -194 105 N
+ATOM 1482 CA GLY A 179 20.307 -7.465 13.737 1.00 12.66 C
+ANISOU 1482 CA GLY A 179 1460 1601 1751 6 -257 117 C
+ATOM 1483 C GLY A 179 21.024 -6.160 13.973 1.00 12.23 C
+ANISOU 1483 C GLY A 179 1411 1548 1686 -18 -306 136 C
+ATOM 1484 O GLY A 179 21.067 -5.710 15.109 1.00 12.53 O
+ANISOU 1484 O GLY A 179 1464 1596 1702 -34 -361 151 O
+ATOM 1485 N ASN A 180 21.583 -5.550 12.928 1.00 11.78 N
+ANISOU 1485 N ASN A 180 1351 1482 1645 -22 -289 137 N
+ATOM 1486 CA ASN A 180 22.268 -4.273 13.077 1.00 12.01 C
+ANISOU 1486 CA ASN A 180 1386 1510 1668 -47 -339 158 C
+ATOM 1487 C ASN A 180 21.296 -3.149 12.821 1.00 11.40 C
+ANISOU 1487 C ASN A 180 1367 1440 1525 -48 -357 106 C
+ATOM 1488 O ASN A 180 20.701 -3.072 11.748 1.00 10.73 O
+ANISOU 1488 O ASN A 180 1297 1355 1425 -35 -318 71 O
+ATOM 1489 CB ASN A 180 23.447 -4.180 12.113 1.00 13.42 C
+ANISOU 1489 CB ASN A 180 1521 1674 1905 -49 -310 197 C
+ATOM 1490 CG ASN A 180 24.560 -5.117 12.483 1.00 16.66 C
+ANISOU 1490 CG ASN A 180 1866 2074 2390 -49 -296 267 C
+ATOM 1491 OD1 ASN A 180 25.033 -5.908 11.663 1.00 18.84 O
+ANISOU 1491 OD1 ASN A 180 2108 2333 2715 -25 -227 285 O
+ATOM 1492 ND2 ASN A 180 24.992 -5.054 13.726 1.00 16.09 N
+ANISOU 1492 ND2 ASN A 180 1778 2009 2326 -74 -358 310 N
+ATOM 1493 N PHE A 181 21.136 -2.246 13.795 1.00 11.37 N
+ANISOU 1493 N PHE A 181 1401 1438 1479 -66 -415 105 N
+ATOM 1494 CA PHE A 181 20.248 -1.104 13.610 1.00 11.91 C
+ANISOU 1494 CA PHE A 181 1528 1509 1490 -63 -427 62 C
+ATOM 1495 C PHE A 181 20.686 -0.235 12.452 1.00 12.38 C
+ANISOU 1495 C PHE A 181 1580 1562 1561 -71 -419 60 C
+ATOM 1496 O PHE A 181 21.881 -0.094 12.176 1.00 12.34 O
+ANISOU 1496 O PHE A 181 1538 1548 1602 -89 -430 100 O
+ATOM 1497 CB PHE A 181 20.201 -0.235 14.871 1.00 12.24 C
+ANISOU 1497 CB PHE A 181 1623 1544 1484 -81 -487 65 C
+ATOM 1498 CG PHE A 181 19.085 -0.590 15.813 1.00 12.39 C
+ANISOU 1498 CG PHE A 181 1681 1570 1456 -60 -481 43 C
+ATOM 1499 CD1 PHE A 181 19.280 -1.514 16.825 1.00 12.74 C
+ANISOU 1499 CD1 PHE A 181 1711 1620 1510 -62 -494 68 C
+ATOM 1500 CD2 PHE A 181 17.854 0.039 15.721 1.00 12.69 C
+ANISOU 1500 CD2 PHE A 181 1768 1609 1444 -36 -461 5 C
+ATOM 1501 CE1 PHE A 181 18.258 -1.822 17.714 1.00 12.99 C
+ANISOU 1501 CE1 PHE A 181 1778 1658 1498 -40 -486 52 C
+ATOM 1502 CE2 PHE A 181 16.828 -0.277 16.600 1.00 13.19 C
+ANISOU 1502 CE2 PHE A 181 1865 1678 1470 -11 -449 -5 C
+ATOM 1503 CZ PHE A 181 17.031 -1.207 17.593 1.00 13.05 C
+ANISOU 1503 CZ PHE A 181 1834 1666 1458 -12 -461 17 C
+ATOM 1504 N TYR A 182 19.702 0.341 11.784 1.00 11.78 N
+ANISOU 1504 N TYR A 182 1537 1491 1449 -58 -398 19 N
+ATOM 1505 CA TYR A 182 19.973 1.380 10.817 1.00 12.63 C
+ANISOU 1505 CA TYR A 182 1648 1594 1557 -67 -400 14 C
+ATOM 1506 C TYR A 182 20.218 2.634 11.653 1.00 13.60 C
+ANISOU 1506 C TYR A 182 1812 1704 1651 -89 -460 20 C
+ATOM 1507 O TYR A 182 19.486 2.909 12.615 1.00 14.08 O
+ANISOU 1507 O TYR A 182 1923 1761 1665 -83 -478 2 O
+ATOM 1508 CB TYR A 182 18.765 1.574 9.929 1.00 12.36 C
+ANISOU 1508 CB TYR A 182 1636 1569 1491 -50 -364 -26 C
+ATOM 1509 CG TYR A 182 18.689 0.495 8.878 1.00 12.38 C
+ANISOU 1509 CG TYR A 182 1610 1576 1518 -41 -312 -31 C
+ATOM 1510 CD1 TYR A 182 19.511 0.528 7.766 1.00 12.83 C
+ANISOU 1510 CD1 TYR A 182 1643 1626 1605 -46 -286 -20 C
+ATOM 1511 CD2 TYR A 182 17.862 -0.604 9.045 1.00 12.57 C
+ANISOU 1511 CD2 TYR A 182 1635 1606 1534 -27 -287 -44 C
+ATOM 1512 CE1 TYR A 182 19.456 -0.465 6.802 1.00 12.90 C
+ANISOU 1512 CE1 TYR A 182 1644 1631 1626 -38 -232 -28 C
+ATOM 1513 CE2 TYR A 182 17.792 -1.601 8.089 1.00 12.93 C
+ANISOU 1513 CE2 TYR A 182 1670 1648 1595 -23 -242 -52 C
+ATOM 1514 CZ TYR A 182 18.601 -1.534 6.970 1.00 13.28 C
+ANISOU 1514 CZ TYR A 182 1702 1681 1661 -29 -212 -46 C
+ATOM 1515 OH TYR A 182 18.538 -2.508 5.998 1.00 13.15 O
+ANISOU 1515 OH TYR A 182 1692 1653 1651 -25 -162 -57 O
+ATOM 1516 N GLY A 183 21.282 3.338 11.320 1.00 13.88 N
+ANISOU 1516 N GLY A 183 1830 1729 1714 -113 -488 49 N
+ATOM 1517 CA GLY A 183 21.632 4.549 12.030 1.00 15.00 C
+ANISOU 1517 CA GLY A 183 2017 1853 1830 -142 -551 58 C
+ATOM 1518 C GLY A 183 22.167 4.279 13.408 1.00 15.58 C
+ANISOU 1518 C GLY A 183 2106 1916 1898 -167 -605 87 C
+ATOM 1519 O GLY A 183 22.626 3.178 13.716 1.00 15.49 O
+ANISOU 1519 O GLY A 183 2050 1914 1923 -166 -597 118 O
+ATOM 1520 N PRO A 184 22.081 5.295 14.261 1.00 15.71 N
+ANISOU 1520 N PRO A 184 2194 1910 1864 -190 -659 79 N
+ATOM 1521 CA PRO A 184 22.700 5.199 15.592 1.00 15.80 C
+ANISOU 1521 CA PRO A 184 2234 1908 1861 -227 -724 112 C
+ATOM 1522 C PRO A 184 21.818 4.666 16.712 1.00 15.71 C
+ANISOU 1522 C PRO A 184 2274 1897 1796 -209 -716 86 C
+ATOM 1523 O PRO A 184 22.202 4.708 17.880 1.00 16.85 O
+ANISOU 1523 O PRO A 184 2463 2028 1912 -241 -773 107 O
+ATOM 1524 CB PRO A 184 23.004 6.662 15.886 1.00 16.92 C
+ANISOU 1524 CB PRO A 184 2447 2017 1965 -264 -787 110 C
+ATOM 1525 CG PRO A 184 21.820 7.366 15.282 1.00 17.42 C
+ANISOU 1525 CG PRO A 184 2552 2077 1988 -224 -734 51 C
+ATOM 1526 CD PRO A 184 21.576 6.658 13.991 1.00 15.87 C
+ANISOU 1526 CD PRO A 184 2274 1912 1842 -190 -667 46 C
+ATOM 1527 N PHE A 185 20.626 4.205 16.356 1.00 15.02 N
+ANISOU 1527 N PHE A 185 2187 1827 1693 -159 -649 45 N
+ATOM 1528 CA PHE A 185 19.631 3.816 17.322 1.00 15.08 C
+ANISOU 1528 CA PHE A 185 2245 1836 1649 -134 -632 22 C
+ATOM 1529 C PHE A 185 19.972 2.543 18.048 1.00 15.67 C
+ANISOU 1529 C PHE A 185 2280 1925 1746 -138 -639 52 C
+ATOM 1530 O PHE A 185 20.717 1.701 17.548 1.00 15.41 O
+ANISOU 1530 O PHE A 185 2167 1908 1780 -146 -631 84 O
+ATOM 1531 CB PHE A 185 18.245 3.763 16.665 1.00 14.67 C
+ANISOU 1531 CB PHE A 185 2196 1798 1582 -83 -562 -17 C
+ATOM 1532 CG PHE A 185 17.918 5.097 16.038 1.00 14.96 C
+ANISOU 1532 CG PHE A 185 2271 1816 1595 -80 -557 -41 C
+ATOM 1533 CD1 PHE A 185 17.777 6.231 16.819 1.00 15.71 C
+ANISOU 1533 CD1 PHE A 185 2458 1877 1632 -89 -586 -54 C
+ATOM 1534 CD2 PHE A 185 17.856 5.235 14.665 1.00 15.58 C
+ANISOU 1534 CD2 PHE A 185 2299 1909 1710 -72 -527 -47 C
+ATOM 1535 CE1 PHE A 185 17.550 7.473 16.232 1.00 15.86 C
+ANISOU 1535 CE1 PHE A 185 2512 1878 1637 -87 -581 -71 C
+ATOM 1536 CE2 PHE A 185 17.627 6.471 14.088 1.00 15.63 C
+ANISOU 1536 CE2 PHE A 185 2336 1901 1701 -73 -526 -62 C
+ATOM 1537 CZ PHE A 185 17.450 7.580 14.874 1.00 15.37 C
+ANISOU 1537 CZ PHE A 185 2389 1835 1617 -78 -552 -74 C
+ATOM 1538 N VAL A 186 19.484 2.448 19.269 1.00 16.07 N
+ANISOU 1538 N VAL A 186 2393 1970 1744 -134 -652 45 N
+ATOM 1539 CA VAL A 186 19.714 1.295 20.124 1.00 16.52 C
+ANISOU 1539 CA VAL A 186 2422 2041 1814 -139 -663 74 C
+ATOM 1540 C VAL A 186 18.408 0.767 20.679 1.00 16.78 C
+ANISOU 1540 C VAL A 186 2486 2085 1806 -92 -614 47 C
+ATOM 1541 O VAL A 186 17.436 1.513 20.778 1.00 17.71 O
+ANISOU 1541 O VAL A 186 2669 2189 1870 -63 -588 13 O
+ATOM 1542 CB VAL A 186 20.699 1.623 21.273 1.00 17.66 C
+ANISOU 1542 CB VAL A 186 2610 2167 1934 -196 -747 112 C
+ATOM 1543 CG1 VAL A 186 22.088 1.924 20.725 1.00 18.92 C
+ANISOU 1543 CG1 VAL A 186 2715 2320 2153 -245 -797 160 C
+ATOM 1544 CG2 VAL A 186 20.188 2.782 22.130 1.00 18.38 C
+ANISOU 1544 CG2 VAL A 186 2830 2224 1930 -204 -773 80 C
+ATOM 1545 N ASP A 187 18.386 -0.515 21.077 1.00 15.60 N
+ANISOU 1545 N ASP A 187 2285 1956 1684 -81 -601 69 N
+ATOM 1546 CA ASP A 187 17.180 -1.106 21.642 1.00 15.58 C
+ANISOU 1546 CA ASP A 187 2303 1966 1651 -37 -557 53 C
+ATOM 1547 C ASP A 187 17.101 -0.911 23.133 1.00 16.90 C
+ANISOU 1547 C ASP A 187 2549 2120 1752 -47 -590 61 C
+ATOM 1548 O ASP A 187 17.132 -1.857 23.916 1.00 16.91 O
+ANISOU 1548 O ASP A 187 2531 2136 1759 -47 -597 85 O
+ATOM 1549 CB ASP A 187 16.973 -2.565 21.246 1.00 15.08 C
+ANISOU 1549 CB ASP A 187 2152 1930 1649 -16 -519 67 C
+ATOM 1550 CG ASP A 187 18.169 -3.478 21.361 1.00 15.13 C
+ANISOU 1550 CG ASP A 187 2089 1944 1717 -48 -548 111 C
+ATOM 1551 OD1 ASP A 187 19.244 -3.005 21.797 1.00 15.07 O
+ANISOU 1551 OD1 ASP A 187 2092 1923 1709 -92 -606 141 O
+ATOM 1552 OD2 ASP A 187 18.030 -4.666 21.026 1.00 14.64 O
+ANISOU 1552 OD2 ASP A 187 1961 1897 1704 -29 -512 121 O
+ATOM 1553 N ARG A 188 16.993 0.352 23.513 1.00 18.27 N
+ANISOU 1553 N ARG A 188 2821 2263 1859 -57 -611 40 N
+ATOM 1554 CA ARG A 188 16.915 0.803 24.882 1.00 20.54 C
+ANISOU 1554 CA ARG A 188 3215 2525 2064 -70 -642 40 C
+ATOM 1555 C ARG A 188 15.979 2.000 24.892 1.00 22.19 C
+ANISOU 1555 C ARG A 188 3521 2702 2206 -35 -603 0 C
+ATOM 1556 O ARG A 188 16.006 2.826 23.979 1.00 21.85 O
+ANISOU 1556 O ARG A 188 3475 2648 2178 -36 -596 -19 O
+ATOM 1557 CB ARG A 188 18.315 1.222 25.371 1.00 23.06 C
+ANISOU 1557 CB ARG A 188 3562 2825 2376 -146 -735 70 C
+ATOM 1558 CG ARG A 188 18.378 1.486 26.858 1.00 28.82 C
+ANISOU 1558 CG ARG A 188 4405 3529 3017 -173 -780 76 C
+ATOM 1559 CD ARG A 188 19.755 1.913 27.332 1.00 34.58 C
+ANISOU 1559 CD ARG A 188 5164 4237 3738 -260 -885 114 C
+ATOM 1560 NE ARG A 188 19.637 2.726 28.541 1.00 39.48 N
+ANISOU 1560 NE ARG A 188 5940 4813 4246 -288 -924 99 N
+ATOM 1561 CZ ARG A 188 20.650 3.073 29.325 1.00 42.92 C
+ANISOU 1561 CZ ARG A 188 6437 5225 4646 -369 -1024 134 C
+ATOM 1562 NH1 ARG A 188 21.884 2.678 29.040 1.00 43.29 N
+ANISOU 1562 NH1 ARG A 188 6388 5290 4771 -431 -1096 195 N
+ATOM 1563 NH2 ARG A 188 20.434 3.803 30.412 1.00 43.34 N
+ANISOU 1563 NH2 ARG A 188 6649 5232 4584 -392 -1053 113 N
+ATOM 1564 N GLN A 189 15.143 2.089 25.912 1.00 24.10 N
+ANISOU 1564 N GLN A 189 3850 2930 2379 -2 -573 -9 N
+ATOM 1565 CA GLN A 189 14.193 3.177 26.044 1.00 26.30 C
+ANISOU 1565 CA GLN A 189 4227 3172 2593 41 -522 -40 C
+ATOM 1566 C GLN A 189 14.930 4.350 26.661 1.00 28.13 C
+ANISOU 1566 C GLN A 189 4583 3352 2753 -10 -582 -54 C
+ATOM 1567 O GLN A 189 14.955 4.501 27.883 1.00 28.84 O
+ANISOU 1567 O GLN A 189 4780 3414 2765 -22 -601 -54 O
+ATOM 1568 CB GLN A 189 13.013 2.731 26.905 1.00 28.62 C
+ANISOU 1568 CB GLN A 189 4560 3469 2846 103 -454 -36 C
+ATOM 1569 CG GLN A 189 11.848 3.700 26.891 1.00 33.55 C
+ANISOU 1569 CG GLN A 189 5266 4059 3421 164 -378 -56 C
+ATOM 1570 CD GLN A 189 10.793 3.236 27.855 1.00 39.90 C
+ANISOU 1570 CD GLN A 189 6110 4864 4185 225 -312 -40 C
+ATOM 1571 OE1 GLN A 189 10.375 2.071 27.855 1.00 41.94 O
+ANISOU 1571 OE1 GLN A 189 6280 5166 4490 248 -292 -13 O
+ATOM 1572 NE2 GLN A 189 10.354 4.137 28.711 1.00 40.98 N
+ANISOU 1572 NE2 GLN A 189 6387 4950 4234 254 -275 -54 N
+ATOM 1573 N THR A 190 15.597 5.137 25.811 1.00 29.21 N
+ANISOU 1573 N THR A 190 4705 3476 2918 -45 -618 -63 N
+ATOM 1574 CA THR A 190 16.412 6.287 26.208 1.00 30.97 C
+ANISOU 1574 CA THR A 190 5034 3648 3086 -104 -687 -71 C
+ATOM 1575 C THR A 190 16.145 7.506 25.303 1.00 31.77 C
+ANISOU 1575 C THR A 190 5160 3722 3190 -89 -662 -100 C
+ATOM 1576 O THR A 190 15.420 7.392 24.308 1.00 32.40 O
+ANISOU 1576 O THR A 190 5161 3828 3322 -39 -597 -107 O
+ATOM 1577 CB THR A 190 17.915 5.902 26.162 1.00 33.71 C
+ANISOU 1577 CB THR A 190 5318 4010 3480 -186 -788 -31 C
+ATOM 1578 OG1 THR A 190 18.225 5.263 24.922 1.00 35.59 O
+ANISOU 1578 OG1 THR A 190 5408 4293 3822 -179 -774 -14 O
+ATOM 1579 CG2 THR A 190 18.348 5.087 27.338 1.00 34.74 C
+ANISOU 1579 CG2 THR A 190 5465 4150 3586 -220 -835 1 C
+ATOM 1580 N ALA A 191 16.753 8.667 25.625 1.00 31.73 N
+ANISOU 1580 N ALA A 191 5262 3663 3131 -138 -719 -112 N
+ATOM 1581 CA ALA A 191 16.636 9.844 24.794 1.00 32.04 C
+ANISOU 1581 CA ALA A 191 5322 3675 3178 -132 -705 -134 C
+ATOM 1582 C ALA A 191 17.438 9.584 23.530 1.00 32.03 C
+ANISOU 1582 C ALA A 191 5178 3715 3276 -162 -740 -110 C
+ATOM 1583 O ALA A 191 18.667 9.639 23.539 1.00 33.57 O
+ANISOU 1583 O ALA A 191 5351 3910 3496 -232 -828 -80 O
+ATOM 1584 CB ALA A 191 17.189 11.058 25.515 1.00 32.37 C
+ANISOU 1584 CB ALA A 191 5515 3644 3138 -185 -768 -149 C
+ATOM 1585 N GLN A 192 16.744 9.214 22.473 1.00 30.11 N
+ANISOU 1585 N GLN A 192 4838 3510 3093 -110 -671 -115 N
+ATOM 1586 CA GLN A 192 17.362 8.979 21.185 1.00 28.86 C
+ANISOU 1586 CA GLN A 192 4556 3388 3022 -128 -686 -98 C
+ATOM 1587 C GLN A 192 16.641 9.910 20.261 1.00 28.78 C
+ANISOU 1587 C GLN A 192 4553 3366 3017 -92 -634 -122 C
+ATOM 1588 O GLN A 192 15.459 9.689 19.992 1.00 30.27 O
+ANISOU 1588 O GLN A 192 4729 3568 3204 -31 -556 -134 O
+ATOM 1589 CB GLN A 192 17.121 7.544 20.715 1.00 28.03 C
+ANISOU 1589 CB GLN A 192 4330 3339 2979 -100 -647 -81 C
+ATOM 1590 CG GLN A 192 17.466 6.488 21.725 1.00 27.39 C
+ANISOU 1590 CG GLN A 192 4245 3272 2891 -117 -676 -57 C
+ATOM 1591 CD GLN A 192 17.504 5.185 21.001 1.00 24.21 C
+ANISOU 1591 CD GLN A 192 3715 2920 2566 -101 -647 -38 C
+ATOM 1592 OE1 GLN A 192 18.318 5.000 20.097 1.00 22.45 O
+ANISOU 1592 OE1 GLN A 192 3411 2712 2406 -125 -666 -19 O
+ATOM 1593 NE2 GLN A 192 16.608 4.276 21.359 1.00 23.00 N
+ANISOU 1593 NE2 GLN A 192 3545 2788 2407 -57 -597 -41 N
+ATOM 1594 N ALA A 193 17.306 10.977 19.816 1.00 27.11 N
+ANISOU 1594 N ALA A 193 4362 3127 2810 -129 -677 -124 N
+ATOM 1595 CA ALA A 193 16.657 11.916 18.912 1.00 26.29 C
+ANISOU 1595 CA ALA A 193 4262 3013 2715 -96 -629 -143 C
+ATOM 1596 C ALA A 193 17.154 11.718 17.499 1.00 25.22 C
+ANISOU 1596 C ALA A 193 4005 2918 2661 -109 -634 -126 C
+ATOM 1597 O ALA A 193 18.320 11.376 17.282 1.00 25.57 O
+ANISOU 1597 O ALA A 193 3993 2976 2745 -157 -693 -99 O
+ATOM 1598 CB ALA A 193 16.894 13.340 19.361 1.00 26.29 C
+ANISOU 1598 CB ALA A 193 4384 2947 2658 -122 -662 -160 C
+ATOM 1599 N ALA A 194 16.261 11.895 16.535 1.00 23.81 N
+ANISOU 1599 N ALA A 194 3784 2757 2506 -66 -571 -136 N
+ATOM 1600 CA ALA A 194 16.617 11.758 15.133 1.00 22.55 C
+ANISOU 1600 CA ALA A 194 3522 2633 2414 -76 -568 -123 C
+ATOM 1601 C ALA A 194 17.257 13.041 14.614 1.00 20.69 C
+ANISOU 1601 C ALA A 194 3308 2368 2184 -108 -606 -122 C
+ATOM 1602 O ALA A 194 16.939 14.141 15.065 1.00 20.78 O
+ANISOU 1602 O ALA A 194 3411 2333 2150 -104 -607 -139 O
+ATOM 1603 CB ALA A 194 15.384 11.422 14.309 1.00 22.80 C
+ANISOU 1603 CB ALA A 194 3502 2696 2465 -25 -493 -129 C
+ATOM 1604 N GLY A 195 18.140 12.891 13.641 1.00 18.81 N
+ANISOU 1604 N GLY A 195 2987 2156 2004 -136 -632 -100 N
+ATOM 1605 CA GLY A 195 18.752 14.027 12.981 1.00 18.20 C
+ANISOU 1605 CA GLY A 195 2911 2060 1945 -164 -665 -92 C
+ATOM 1606 C GLY A 195 17.782 14.641 11.989 1.00 17.45 C
+ANISOU 1606 C GLY A 195 2800 1973 1857 -127 -606 -108 C
+ATOM 1607 O GLY A 195 16.600 14.274 11.937 1.00 17.25 O
+ANISOU 1607 O GLY A 195 2772 1964 1819 -82 -544 -122 O
+ATOM 1608 N THR A 196 18.293 15.530 11.144 1.00 16.59 N
+ANISOU 1608 N THR A 196 2668 1859 1776 -148 -627 -97 N
+ATOM 1609 CA THR A 196 17.483 16.239 10.165 1.00 16.96 C
+ANISOU 1609 CA THR A 196 2699 1913 1834 -121 -581 -105 C
+ATOM 1610 C THR A 196 16.846 15.288 9.210 1.00 17.50 C
+ANISOU 1610 C THR A 196 2685 2034 1931 -95 -527 -101 C
+ATOM 1611 O THR A 196 17.541 14.425 8.663 1.00 17.04 O
+ANISOU 1611 O THR A 196 2559 2007 1909 -111 -536 -87 O
+ATOM 1612 CB THR A 196 18.339 17.238 9.386 1.00 18.41 C
+ANISOU 1612 CB THR A 196 2861 2086 2049 -155 -621 -88 C
+ATOM 1613 OG1 THR A 196 19.041 18.066 10.303 1.00 19.49 O
+ANISOU 1613 OG1 THR A 196 3079 2169 2157 -191 -684 -87 O
+ATOM 1614 CG2 THR A 196 17.516 18.113 8.465 1.00 19.24 C
+ANISOU 1614 CG2 THR A 196 2955 2193 2161 -131 -578 -92 C
+ATOM 1615 N ASP A 197 15.517 15.412 9.024 1.00 17.89 N
+ANISOU 1615 N ASP A 197 2743 2089 1966 -54 -470 -110 N
+ATOM 1616 CA ASP A 197 14.850 14.565 8.047 1.00 18.28 C
+ANISOU 1616 CA ASP A 197 2719 2186 2041 -38 -428 -102 C
+ATOM 1617 C ASP A 197 14.922 15.240 6.692 1.00 17.83 C
+ANISOU 1617 C ASP A 197 2617 2144 2013 -50 -423 -90 C
+ATOM 1618 O ASP A 197 13.995 15.929 6.257 1.00 20.27 O
+ANISOU 1618 O ASP A 197 2930 2452 2321 -30 -392 -83 O
+ATOM 1619 CB ASP A 197 13.431 14.139 8.441 1.00 20.37 C
+ANISOU 1619 CB ASP A 197 2997 2457 2285 4 -377 -102 C
+ATOM 1620 CG ASP A 197 12.899 12.932 7.682 1.00 23.82 C
+ANISOU 1620 CG ASP A 197 3365 2940 2744 8 -350 -91 C
+ATOM 1621 OD1 ASP A 197 13.654 12.353 6.864 1.00 20.44 O
+ANISOU 1621 OD1 ASP A 197 2888 2537 2342 -18 -366 -90 O
+ATOM 1622 OD2 ASP A 197 11.747 12.542 7.934 1.00 28.73 O
+ANISOU 1622 OD2 ASP A 197 3987 3570 3357 38 -313 -81 O
+ATOM 1623 N ATHR A 198 16.073 15.084 6.036 0.50 16.35 N
+ANISOU 1623 N ATHR A 198 2387 1970 1855 -81 -454 -81 N
+ATOM 1624 N BTHR A 198 16.027 14.973 6.021 0.50 16.18 N
+ANISOU 1624 N BTHR A 198 2362 1952 1834 -80 -451 -81 N
+ATOM 1625 CA ATHR A 198 16.273 15.688 4.726 0.50 15.97 C
+ANISOU 1625 CA ATHR A 198 2296 1938 1834 -94 -450 -68 C
+ATOM 1626 CA BTHR A 198 16.431 15.485 4.722 0.50 15.73 C
+ANISOU 1626 CA BTHR A 198 2258 1911 1806 -97 -452 -67 C
+ATOM 1627 C ATHR A 198 15.435 14.991 3.669 0.50 15.27 C
+ANISOU 1627 C ATHR A 198 2161 1890 1751 -84 -407 -63 C
+ATOM 1628 C BTHR A 198 15.577 14.886 3.597 0.50 15.16 C
+ANISOU 1628 C BTHR A 198 2140 1880 1741 -88 -409 -63 C
+ATOM 1629 O ATHR A 198 14.972 13.861 3.855 0.50 15.28 O
+ANISOU 1629 O ATHR A 198 2153 1908 1743 -73 -386 -69 O
+ATOM 1630 O BTHR A 198 15.248 13.702 3.663 0.50 15.19 O
+ANISOU 1630 O BTHR A 198 2128 1903 1740 -81 -390 -68 O
+ATOM 1631 CB ATHR A 198 17.753 15.778 4.371 0.50 17.51 C
+ANISOU 1631 CB ATHR A 198 2460 2133 2061 -126 -489 -51 C
+ATOM 1632 CB BTHR A 198 17.918 15.133 4.570 0.50 16.74 C
+ANISOU 1632 CB BTHR A 198 2355 2043 1965 -126 -488 -51 C
+ATOM 1633 OG1ATHR A 198 18.310 14.471 4.399 0.50 18.42 O
+ANISOU 1633 OG1ATHR A 198 2540 2270 2191 -130 -483 -46 O
+ATOM 1634 OG1BTHR A 198 18.659 15.683 5.672 0.50 17.41 O
+ANISOU 1634 OG1BTHR A 198 2486 2088 2041 -145 -540 -48 O
+ATOM 1635 CG2ATHR A 198 18.524 16.703 5.296 0.50 17.78 C
+ANISOU 1635 CG2ATHR A 198 2543 2123 2089 -148 -545 -46 C
+ATOM 1636 CG2BTHR A 198 18.499 15.622 3.285 0.50 17.17 C
+ANISOU 1636 CG2BTHR A 198 2360 2113 2051 -142 -487 -32 C
+ATOM 1637 N THR A 199 15.201 15.692 2.578 1.00 14.19 N
+ANISOU 1637 N THR A 199 1998 1767 1627 -91 -398 -51 N
+ATOM 1638 CA THR A 199 14.404 15.175 1.472 1.00 13.47 C
+ANISOU 1638 CA THR A 199 1870 1712 1538 -93 -367 -41 C
+ATOM 1639 C THR A 199 15.302 14.448 0.475 1.00 12.86 C
+ANISOU 1639 C THR A 199 1754 1658 1475 -115 -366 -39 C
+ATOM 1640 O THR A 199 16.404 14.913 0.194 1.00 13.34 O
+ANISOU 1640 O THR A 199 1801 1711 1555 -128 -384 -31 O
+ATOM 1641 CB THR A 199 13.546 16.279 0.859 1.00 14.60 C
+ANISOU 1641 CB THR A 199 2008 1857 1684 -89 -355 -22 C
+ATOM 1642 OG1 THR A 199 12.711 16.839 1.874 1.00 15.22 O
+ANISOU 1642 OG1 THR A 199 2126 1907 1749 -59 -342 -21 O
+ATOM 1643 CG2 THR A 199 12.667 15.765 -0.281 1.00 15.03 C
+ANISOU 1643 CG2 THR A 199 2025 1949 1736 -100 -333 -4 C
+ATOM 1644 N ILE A 200 14.861 13.264 -0.011 1.00 12.06 N
+ANISOU 1644 N ILE A 200 1639 1580 1363 -118 -342 -43 N
+ATOM 1645 CA ILE A 200 15.633 12.442 -0.950 1.00 12.31 C
+ANISOU 1645 CA ILE A 200 1650 1627 1402 -134 -327 -44 C
+ATOM 1646 C ILE A 200 15.432 12.991 -2.363 1.00 11.85 C
+ANISOU 1646 C ILE A 200 1575 1587 1338 -153 -318 -30 C
+ATOM 1647 O ILE A 200 14.510 12.616 -3.089 1.00 11.58 O
+ANISOU 1647 O ILE A 200 1543 1573 1284 -166 -304 -27 O
+ATOM 1648 CB ILE A 200 15.218 10.951 -0.852 1.00 12.52 C
+ANISOU 1648 CB ILE A 200 1682 1662 1412 -132 -306 -57 C
+ATOM 1649 CG1 ILE A 200 15.204 10.474 0.626 1.00 12.89 C
+ANISOU 1649 CG1 ILE A 200 1744 1693 1460 -112 -317 -67 C
+ATOM 1650 CG2 ILE A 200 16.162 10.099 -1.689 1.00 12.93 C
+ANISOU 1650 CG2 ILE A 200 1724 1717 1471 -142 -282 -59 C
+ATOM 1651 CD1 ILE A 200 14.183 9.365 0.910 1.00 14.24 C
+ANISOU 1651 CD1 ILE A 200 1923 1873 1614 -105 -302 -73 C
+ATOM 1652 N THR A 201 16.317 13.911 -2.732 1.00 11.75 N
+ANISOU 1652 N THR A 201 1548 1570 1348 -158 -329 -18 N
+ATOM 1653 CA THR A 201 16.264 14.631 -3.995 1.00 12.03 C
+ANISOU 1653 CA THR A 201 1566 1622 1383 -175 -324 -1 C
+ATOM 1654 C THR A 201 16.083 13.743 -5.217 1.00 12.46 C
+ANISOU 1654 C THR A 201 1622 1698 1412 -193 -294 -2 C
+ATOM 1655 O THR A 201 15.218 14.024 -6.052 1.00 13.25 O
+ANISOU 1655 O THR A 201 1723 1817 1493 -212 -293 8 O
+ATOM 1656 CB THR A 201 17.526 15.476 -4.150 1.00 13.15 C
+ANISOU 1656 CB THR A 201 1688 1753 1557 -177 -339 16 C
+ATOM 1657 OG1 THR A 201 17.749 16.207 -2.951 1.00 13.77 O
+ANISOU 1657 OG1 THR A 201 1778 1802 1650 -168 -373 15 O
+ATOM 1658 CG2 THR A 201 17.479 16.386 -5.360 1.00 14.00 C
+ANISOU 1658 CG2 THR A 201 1775 1876 1668 -192 -336 37 C
+ATOM 1659 N VAL A 202 16.888 12.675 -5.341 1.00 11.54 N
+ANISOU 1659 N VAL A 202 1512 1577 1297 -189 -270 -12 N
+ATOM 1660 CA VAL A 202 16.798 11.804 -6.519 1.00 12.15 C
+ANISOU 1660 CA VAL A 202 1608 1665 1342 -206 -235 -18 C
+ATOM 1661 C VAL A 202 15.402 11.170 -6.634 1.00 12.21 C
+ANISOU 1661 C VAL A 202 1642 1685 1313 -225 -241 -28 C
+ATOM 1662 O VAL A 202 14.899 10.999 -7.736 1.00 12.15 O
+ANISOU 1662 O VAL A 202 1653 1690 1273 -253 -233 -23 O
+ATOM 1663 CB VAL A 202 17.929 10.751 -6.579 1.00 13.19 C
+ANISOU 1663 CB VAL A 202 1747 1781 1485 -192 -197 -24 C
+ATOM 1664 CG1 VAL A 202 17.770 9.698 -5.480 1.00 14.16 C
+ANISOU 1664 CG1 VAL A 202 1879 1889 1611 -177 -196 -42 C
+ATOM 1665 CG2 VAL A 202 18.012 10.102 -7.959 1.00 14.05 C
+ANISOU 1665 CG2 VAL A 202 1887 1892 1558 -207 -153 -28 C
+ATOM 1666 N ASN A 203 14.756 10.889 -5.487 1.00 12.28 N
+ANISOU 1666 N ASN A 203 1651 1688 1328 -211 -257 -35 N
+ATOM 1667 CA ASN A 203 13.419 10.315 -5.495 1.00 12.14 C
+ANISOU 1667 CA ASN A 203 1648 1681 1284 -228 -266 -32 C
+ATOM 1668 C ASN A 203 12.385 11.343 -5.906 1.00 12.09 C
+ANISOU 1668 C ASN A 203 1626 1693 1276 -244 -287 -2 C
+ATOM 1669 O ASN A 203 11.470 11.014 -6.664 1.00 12.27 O
+ANISOU 1669 O ASN A 203 1657 1731 1272 -277 -295 15 O
+ATOM 1670 CB ASN A 203 13.086 9.747 -4.116 1.00 12.23 C
+ANISOU 1670 CB ASN A 203 1660 1681 1308 -203 -272 -42 C
+ATOM 1671 CG ASN A 203 13.839 8.482 -3.781 1.00 12.94 C
+ANISOU 1671 CG ASN A 203 1764 1755 1397 -193 -251 -65 C
+ATOM 1672 OD1 ASN A 203 14.704 8.031 -4.528 1.00 12.49 O
+ANISOU 1672 OD1 ASN A 203 1717 1691 1335 -200 -225 -74 O
+ATOM 1673 ND2 ASN A 203 13.543 7.903 -2.603 1.00 12.93 N
+ANISOU 1673 ND2 ASN A 203 1763 1746 1404 -173 -256 -72 N
+ATOM 1674 N VAL A 204 12.549 12.612 -5.486 1.00 11.53 N
+ANISOU 1674 N VAL A 204 1532 1617 1232 -225 -298 10 N
+ATOM 1675 CA VAL A 204 11.614 13.665 -5.908 1.00 11.74 C
+ANISOU 1675 CA VAL A 204 1539 1657 1264 -236 -311 45 C
+ATOM 1676 C VAL A 204 11.696 13.853 -7.408 1.00 12.06 C
+ANISOU 1676 C VAL A 204 1578 1719 1285 -274 -312 60 C
+ATOM 1677 O VAL A 204 10.667 13.959 -8.069 1.00 12.65 O
+ANISOU 1677 O VAL A 204 1647 1814 1347 -304 -325 92 O
+ATOM 1678 CB VAL A 204 11.899 14.998 -5.193 1.00 12.37 C
+ANISOU 1678 CB VAL A 204 1605 1719 1374 -207 -318 51 C
+ATOM 1679 CG1 VAL A 204 10.971 16.096 -5.711 1.00 12.86 C
+ANISOU 1679 CG1 VAL A 204 1644 1793 1447 -216 -324 92 C
+ATOM 1680 CG2 VAL A 204 11.731 14.836 -3.687 1.00 11.91 C
+ANISOU 1680 CG2 VAL A 204 1563 1636 1325 -172 -317 37 C
+ATOM 1681 N LEU A 205 12.920 13.831 -7.961 1.00 11.62 N
+ANISOU 1681 N LEU A 205 1529 1659 1227 -275 -297 42 N
+ATOM 1682 CA LEU A 205 13.080 13.980 -9.409 1.00 11.61 C
+ANISOU 1682 CA LEU A 205 1534 1676 1201 -309 -291 55 C
+ATOM 1683 C LEU A 205 12.439 12.817 -10.129 1.00 12.03 C
+ANISOU 1683 C LEU A 205 1627 1739 1206 -346 -288 51 C
+ATOM 1684 O LEU A 205 11.742 13.024 -11.120 1.00 11.50 O
+ANISOU 1684 O LEU A 205 1567 1691 1112 -388 -304 76 O
+ATOM 1685 CB LEU A 205 14.560 14.080 -9.785 1.00 11.82 C
+ANISOU 1685 CB LEU A 205 1561 1693 1238 -295 -266 43 C
+ATOM 1686 CG LEU A 205 15.223 15.375 -9.349 1.00 12.51 C
+ANISOU 1686 CG LEU A 205 1609 1772 1370 -272 -280 57 C
+ATOM 1687 CD1 LEU A 205 16.733 15.246 -9.360 1.00 13.36 C
+ANISOU 1687 CD1 LEU A 205 1710 1866 1501 -253 -259 52 C
+ATOM 1688 CD2 LEU A 205 14.733 16.542 -10.186 1.00 13.75 C
+ANISOU 1688 CD2 LEU A 205 1744 1949 1530 -293 -295 89 C
+ATOM 1689 N ALA A 206 12.630 11.587 -9.620 1.00 12.01 N
+ANISOU 1689 N ALA A 206 1654 1719 1192 -337 -273 21 N
+ATOM 1690 CA ALA A 206 12.019 10.411 -10.254 1.00 12.58 C
+ANISOU 1690 CA ALA A 206 1774 1791 1214 -376 -273 15 C
+ATOM 1691 C ALA A 206 10.483 10.546 -10.260 1.00 13.06 C
+ANISOU 1691 C ALA A 206 1821 1871 1269 -409 -315 53 C
+ATOM 1692 O ALA A 206 9.841 10.284 -11.270 1.00 12.97 O
+ANISOU 1692 O ALA A 206 1838 1872 1217 -462 -334 73 O
+ATOM 1693 CB ALA A 206 12.426 9.154 -9.509 1.00 13.02 C
+ANISOU 1693 CB ALA A 206 1854 1822 1269 -354 -251 -19 C
+ATOM 1694 N TRP A 207 9.924 11.046 -9.151 1.00 12.31 N
+ANISOU 1694 N TRP A 207 1684 1778 1215 -378 -327 70 N
+ATOM 1695 CA TRP A 207 8.484 11.237 -9.044 1.00 12.72 C
+ANISOU 1695 CA TRP A 207 1712 1846 1275 -399 -358 120 C
+ATOM 1696 C TRP A 207 7.993 12.353 -9.993 1.00 12.88 C
+ANISOU 1696 C TRP A 207 1705 1890 1298 -430 -378 168 C
+ATOM 1697 O TRP A 207 6.919 12.226 -10.565 1.00 13.64 O
+ANISOU 1697 O TRP A 207 1798 2004 1382 -476 -409 215 O
+ATOM 1698 CB TRP A 207 8.134 11.468 -7.574 1.00 13.10 C
+ANISOU 1698 CB TRP A 207 1730 1883 1366 -347 -352 125 C
+ATOM 1699 CG TRP A 207 6.764 11.990 -7.302 1.00 13.61 C
+ANISOU 1699 CG TRP A 207 1756 1960 1455 -349 -368 187 C
+ATOM 1700 CD1 TRP A 207 5.613 11.271 -7.141 1.00 14.89 C
+ANISOU 1700 CD1 TRP A 207 1911 2131 1617 -369 -387 226 C
+ATOM 1701 CD2 TRP A 207 6.432 13.349 -7.037 1.00 13.53 C
+ANISOU 1701 CD2 TRP A 207 1708 1951 1482 -323 -362 222 C
+ATOM 1702 NE1 TRP A 207 4.581 12.114 -6.796 1.00 15.38 N
+ANISOU 1702 NE1 TRP A 207 1926 2200 1718 -353 -388 290 N
+ATOM 1703 CE2 TRP A 207 5.061 13.396 -6.721 1.00 14.69 C
+ANISOU 1703 CE2 TRP A 207 1823 2106 1652 -322 -369 286 C
+ATOM 1704 CE3 TRP A 207 7.177 14.530 -6.990 1.00 14.59 C
+ANISOU 1704 CE3 TRP A 207 1833 2076 1635 -297 -349 208 C
+ATOM 1705 CZ2 TRP A 207 4.421 14.585 -6.382 1.00 15.53 C
+ANISOU 1705 CZ2 TRP A 207 1891 2210 1800 -292 -355 335 C
+ATOM 1706 CZ3 TRP A 207 6.536 15.709 -6.670 1.00 15.61 C
+ANISOU 1706 CZ3 TRP A 207 1929 2200 1800 -272 -341 251 C
+ATOM 1707 CH2 TRP A 207 5.175 15.729 -6.384 1.00 15.54 C
+ANISOU 1707 CH2 TRP A 207 1892 2198 1814 -268 -340 314 C
+ATOM 1708 N LEU A 208 8.814 13.381 -10.235 1.00 12.37 N
+ANISOU 1708 N LEU A 208 1624 1825 1250 -411 -364 160 N
+ATOM 1709 CA LEU A 208 8.452 14.412 -11.218 1.00 12.13 C
+ANISOU 1709 CA LEU A 208 1569 1818 1222 -441 -381 204 C
+ATOM 1710 C LEU A 208 8.433 13.799 -12.619 1.00 12.89 C
+ANISOU 1710 C LEU A 208 1709 1928 1260 -504 -394 206 C
+ATOM 1711 O LEU A 208 7.538 14.110 -13.409 1.00 13.49 O
+ANISOU 1711 O LEU A 208 1774 2027 1324 -554 -427 258 O
+ATOM 1712 CB LEU A 208 9.446 15.566 -11.142 1.00 11.68 C
+ANISOU 1712 CB LEU A 208 1490 1754 1195 -407 -363 191 C
+ATOM 1713 CG LEU A 208 9.330 16.445 -9.891 1.00 13.13 C
+ANISOU 1713 CG LEU A 208 1641 1919 1430 -354 -357 196 C
+ATOM 1714 CD1 LEU A 208 10.419 17.506 -9.884 1.00 13.35 C
+ANISOU 1714 CD1 LEU A 208 1654 1935 1482 -330 -348 182 C
+ATOM 1715 CD2 LEU A 208 7.956 17.130 -9.824 1.00 13.49 C
+ANISOU 1715 CD2 LEU A 208 1647 1975 1502 -360 -369 260 C
+ATOM 1716 N TYR A 209 9.367 12.870 -12.916 1.00 12.85 N
+ANISOU 1716 N TYR A 209 1759 1907 1216 -505 -369 155 N
+ATOM 1717 CA TYR A 209 9.341 12.143 -14.193 1.00 13.30 C
+ANISOU 1717 CA TYR A 209 1880 1968 1206 -564 -375 150 C
+ATOM 1718 C TYR A 209 8.069 11.310 -14.283 1.00 14.51 C
+ANISOU 1718 C TYR A 209 2056 2126 1332 -617 -417 179 C
+ATOM 1719 O TYR A 209 7.423 11.315 -15.316 1.00 15.06 O
+ANISOU 1719 O TYR A 209 2150 2212 1362 -682 -452 215 O
+ATOM 1720 CB TYR A 209 10.556 11.234 -14.364 1.00 12.99 C
+ANISOU 1720 CB TYR A 209 1901 1901 1135 -545 -327 93 C
+ATOM 1721 CG TYR A 209 11.758 11.992 -14.871 1.00 13.05 C
+ANISOU 1721 CG TYR A 209 1898 1909 1153 -518 -291 83 C
+ATOM 1722 CD1 TYR A 209 11.814 12.446 -16.178 1.00 13.88 C
+ANISOU 1722 CD1 TYR A 209 2026 2029 1217 -557 -292 102 C
+ATOM 1723 CD2 TYR A 209 12.843 12.240 -14.048 1.00 13.62 C
+ANISOU 1723 CD2 TYR A 209 1937 1964 1272 -457 -258 60 C
+ATOM 1724 CE1 TYR A 209 12.907 13.155 -16.649 1.00 14.59 C
+ANISOU 1724 CE1 TYR A 209 2103 2121 1321 -531 -257 100 C
+ATOM 1725 CE2 TYR A 209 13.943 12.953 -14.506 1.00 14.55 C
+ANISOU 1725 CE2 TYR A 209 2039 2083 1406 -434 -229 63 C
+ATOM 1726 CZ TYR A 209 13.975 13.397 -15.814 1.00 14.96 C
+ANISOU 1726 CZ TYR A 209 2111 2151 1421 -469 -226 82 C
+ATOM 1727 OH TYR A 209 15.049 14.115 -16.279 1.00 16.11 O
+ANISOU 1727 OH TYR A 209 2235 2299 1587 -445 -196 92 O
+ATOM 1728 N ALA A 210 7.680 10.629 -13.183 1.00 14.89 N
+ANISOU 1728 N ALA A 210 2094 2161 1404 -591 -418 170 N
+ATOM 1729 CA ALA A 210 6.429 9.851 -13.171 1.00 15.35 C
+ANISOU 1729 CA ALA A 210 2163 2224 1447 -640 -463 208 C
+ATOM 1730 C ALA A 210 5.231 10.755 -13.445 1.00 16.18 C
+ANISOU 1730 C ALA A 210 2209 2359 1579 -673 -507 291 C
+ATOM 1731 O ALA A 210 4.309 10.368 -14.163 1.00 16.64 O
+ANISOU 1731 O ALA A 210 2286 2430 1608 -745 -557 340 O
+ATOM 1732 CB ALA A 210 6.246 9.164 -11.820 1.00 15.41 C
+ANISOU 1732 CB ALA A 210 2153 2215 1488 -595 -452 192 C
+ATOM 1733 N ALA A 211 5.247 11.971 -12.900 1.00 15.83 N
+ANISOU 1733 N ALA A 211 2098 2324 1593 -624 -491 314 N
+ATOM 1734 CA ALA A 211 4.178 12.927 -13.105 1.00 15.93 C
+ANISOU 1734 CA ALA A 211 2048 2362 1643 -643 -520 398 C
+ATOM 1735 C ALA A 211 4.077 13.306 -14.578 1.00 16.27 C
+ANISOU 1735 C ALA A 211 2108 2428 1647 -714 -553 430 C
+ATOM 1736 O ALA A 211 2.978 13.279 -15.138 1.00 17.39 O
+ANISOU 1736 O ALA A 211 2234 2590 1784 -777 -603 504 O
+ATOM 1737 CB ALA A 211 4.407 14.152 -12.240 1.00 16.23 C
+ANISOU 1737 CB ALA A 211 2027 2395 1745 -571 -485 402 C
+ATOM 1738 N VAL A 212 5.210 13.588 -15.237 1.00 15.64 N
+ANISOU 1738 N VAL A 212 2063 2345 1535 -709 -527 380 N
+ATOM 1739 CA VAL A 212 5.187 13.927 -16.663 1.00 16.48 C
+ANISOU 1739 CA VAL A 212 2194 2472 1595 -775 -554 407 C
+ATOM 1740 C VAL A 212 4.654 12.777 -17.487 1.00 18.29 C
+ANISOU 1740 C VAL A 212 2499 2699 1751 -858 -596 415 C
+ATOM 1741 O VAL A 212 3.796 12.996 -18.351 1.00 19.31 O
+ANISOU 1741 O VAL A 212 2625 2852 1860 -933 -650 483 O
+ATOM 1742 CB VAL A 212 6.574 14.389 -17.150 1.00 16.59 C
+ANISOU 1742 CB VAL A 212 2233 2480 1591 -745 -509 353 C
+ATOM 1743 CG1 VAL A 212 6.583 14.581 -18.668 1.00 16.85 C
+ANISOU 1743 CG1 VAL A 212 2307 2533 1563 -815 -532 376 C
+ATOM 1744 CG2 VAL A 212 6.969 15.674 -16.451 1.00 17.06 C
+ANISOU 1744 CG2 VAL A 212 2217 2542 1723 -679 -483 360 C
+ATOM 1745 N ILE A 213 5.112 11.552 -17.202 1.00 19.03 N
+ANISOU 1745 N ILE A 213 2661 2762 1805 -851 -576 352 N
+ATOM 1746 CA ILE A 213 4.654 10.357 -17.930 1.00 20.91 C
+ANISOU 1746 CA ILE A 213 2989 2988 1967 -932 -615 351 C
+ATOM 1747 C ILE A 213 3.142 10.195 -17.791 1.00 23.56 C
+ANISOU 1747 C ILE A 213 3284 3341 2324 -989 -688 438 C
+ATOM 1748 O ILE A 213 2.457 9.941 -18.777 1.00 24.76 O
+ANISOU 1748 O ILE A 213 3478 3505 2427 -1081 -749 486 O
+ATOM 1749 CB ILE A 213 5.416 9.109 -17.418 1.00 21.25 C
+ANISOU 1749 CB ILE A 213 3102 2991 1982 -898 -572 270 C
+ATOM 1750 CG1 ILE A 213 6.904 9.189 -17.803 1.00 21.73 C
+ANISOU 1750 CG1 ILE A 213 3208 3032 2015 -853 -501 200 C
+ATOM 1751 CG2 ILE A 213 4.783 7.803 -17.918 1.00 21.99 C
+ANISOU 1751 CG2 ILE A 213 3287 3063 2006 -978 -616 272 C
+ATOM 1752 CD1 ILE A 213 7.788 8.246 -17.083 1.00 22.87 C
+ANISOU 1752 CD1 ILE A 213 3387 3140 2162 -797 -445 132 C
+ATOM 1753 N ASN A 214 2.620 10.439 -16.588 1.00 24.22 N
+ANISOU 1753 N ASN A 214 3286 3431 2488 -934 -681 468 N
+ATOM 1754 CA ASN A 214 1.204 10.282 -16.300 1.00 26.05 C
+ANISOU 1754 CA ASN A 214 3465 3677 2756 -973 -738 560 C
+ATOM 1755 C ASN A 214 0.343 11.544 -16.522 1.00 27.69 C
+ANISOU 1755 C ASN A 214 3578 3920 3022 -985 -764 662 C
+ATOM 1756 O ASN A 214 -0.799 11.581 -16.055 1.00 29.91 O
+ANISOU 1756 O ASN A 214 3792 4213 3358 -992 -794 750 O
+ATOM 1757 CB ASN A 214 1.016 9.716 -14.899 1.00 27.31 C
+ANISOU 1757 CB ASN A 214 3592 3819 2964 -909 -712 545 C
+ATOM 1758 CG ASN A 214 1.479 8.279 -14.822 1.00 30.24 C
+ANISOU 1758 CG ASN A 214 4054 4159 3279 -923 -708 474 C
+ATOM 1759 OD1 ASN A 214 0.744 7.346 -15.163 1.00 32.47 O
+ANISOU 1759 OD1 ASN A 214 4375 4434 3529 -994 -763 505 O
+ATOM 1760 ND2 ASN A 214 2.714 8.047 -14.430 1.00 29.78 N
+ANISOU 1760 ND2 ASN A 214 4032 4076 3206 -863 -645 381 N
+ATOM 1761 N GLY A 215 0.848 12.529 -17.260 1.00 26.51 N
+ANISOU 1761 N GLY A 215 3423 3787 2864 -988 -753 660 N
+ATOM 1762 CA GLY A 215 0.065 13.709 -17.623 1.00 26.05 C
+ANISOU 1762 CA GLY A 215 3281 3761 2856 -1007 -778 759 C
+ATOM 1763 C GLY A 215 0.186 15.021 -16.870 1.00 24.55 C
+ANISOU 1763 C GLY A 215 3001 3575 2753 -920 -726 778 C
+ATOM 1764 O GLY A 215 -0.239 16.059 -17.380 1.00 25.20 O
+ANISOU 1764 O GLY A 215 3024 3681 2871 -937 -741 852 O
+ATOM 1765 N AASP A 216 0.744 14.999 -15.654 0.50 23.04 N
+ANISOU 1765 N AASP A 216 2803 3359 2594 -829 -667 714 N
+ATOM 1766 N BASP A 216 0.748 14.992 -15.660 0.50 23.39 N
+ANISOU 1766 N BASP A 216 2847 3402 2637 -830 -668 714 N
+ATOM 1767 CA AASP A 216 0.891 16.222 -14.868 0.50 22.25 C
+ANISOU 1767 CA AASP A 216 2635 3253 2567 -747 -618 725 C
+ATOM 1768 CA BASP A 216 0.909 16.203 -14.862 0.50 22.94 C
+ANISOU 1768 CA BASP A 216 2724 3339 2653 -747 -617 722 C
+ATOM 1769 C AASP A 216 2.182 16.909 -15.280 0.50 22.70 C
+ANISOU 1769 C AASP A 216 2716 3305 2605 -722 -585 655 C
+ATOM 1770 C BASP A 216 2.192 16.893 -15.307 0.50 23.02 C
+ANISOU 1770 C BASP A 216 2758 3346 2642 -724 -587 654 C
+ATOM 1771 O AASP A 216 3.265 16.409 -14.988 0.50 23.46 O
+ANISOU 1771 O AASP A 216 2864 3380 2669 -689 -555 565 O
+ATOM 1772 O BASP A 216 3.280 16.379 -15.060 0.50 23.77 O
+ANISOU 1772 O BASP A 216 2909 3421 2703 -696 -558 564 O
+ATOM 1773 CB AASP A 216 0.863 15.910 -13.369 0.50 22.37 C
+ANISOU 1773 CB AASP A 216 2639 3240 2621 -669 -575 695 C
+ATOM 1774 CB BASP A 216 0.959 15.849 -13.368 0.50 24.09 C
+ANISOU 1774 CB BASP A 216 2863 3457 2833 -669 -574 686 C
+ATOM 1775 CG AASP A 216 -0.442 15.298 -12.907 0.50 24.19 C
+ANISOU 1775 CG AASP A 216 2835 3475 2882 -685 -600 774 C
+ATOM 1776 CG BASP A 216 -0.170 16.456 -12.563 0.50 27.89 C
+ANISOU 1776 CG BASP A 216 3267 3938 3393 -629 -559 775 C
+ATOM 1777 OD1AASP A 216 -1.477 15.540 -13.561 0.50 24.19 O
+ANISOU 1777 OD1AASP A 216 2790 3500 2902 -743 -644 877 O
+ATOM 1778 OD1BASP A 216 -0.595 17.580 -12.895 0.50 28.66 O
+ANISOU 1778 OD1BASP A 216 3309 4047 3535 -626 -554 842 O
+ATOM 1779 OD2AASP A 216 -0.430 14.579 -11.889 0.50 25.07 O
+ANISOU 1779 OD2AASP A 216 2960 3567 3001 -642 -577 741 O
+ATOM 1780 OD2BASP A 216 -0.618 15.812 -11.589 0.50 29.52 O
+ANISOU 1780 OD2BASP A 216 3469 4129 3618 -597 -546 781 O
+ATOM 1781 N ARG A 217 2.073 18.016 -16.019 1.00 21.99 N
+ANISOU 1781 N ARG A 217 2585 3236 2534 -740 -594 705 N
+ATOM 1782 CA ARG A 217 3.233 18.713 -16.564 1.00 20.81 C
+ANISOU 1782 CA ARG A 217 2453 3087 2367 -726 -572 655 C
+ATOM 1783 C ARG A 217 3.263 20.218 -16.299 1.00 19.92 C
+ANISOU 1783 C ARG A 217 2271 2973 2323 -678 -545 689 C
+ATOM 1784 O ARG A 217 4.105 20.898 -16.881 1.00 19.51 O
+ANISOU 1784 O ARG A 217 2224 2927 2263 -675 -535 665 O
+ATOM 1785 CB ARG A 217 3.252 18.535 -18.107 0.50 21.37 C
+ANISOU 1785 CB ARG A 217 2559 3186 2373 -814 -615 677 C
+ATOM 1786 CG ARG A 217 2.978 17.127 -18.645 0.50 23.57 C
+ANISOU 1786 CG ARG A 217 2916 3465 2575 -885 -654 663 C
+ATOM 1787 CD ARG A 217 2.523 17.152 -20.100 0.50 25.14 C
+ANISOU 1787 CD ARG A 217 3143 3693 2718 -984 -710 717 C
+ATOM 1788 NE ARG A 217 3.525 17.746 -20.981 0.50 25.70 N
+ANISOU 1788 NE ARG A 217 3240 3770 2753 -983 -686 679 N
+ATOM 1789 CZ ARG A 217 4.427 17.041 -21.650 0.50 25.29 C
+ANISOU 1789 CZ ARG A 217 3284 3705 2620 -1002 -669 609 C
+ATOM 1790 NH1 ARG A 217 5.318 17.652 -22.418 0.50 24.48 N
+ANISOU 1790 NH1 ARG A 217 3197 3610 2493 -996 -642 587 N
+ATOM 1791 NH2 ARG A 217 4.448 15.719 -21.555 0.50 23.66 N
+ANISOU 1791 NH2 ARG A 217 3159 3476 2355 -1029 -676 567 N
+ATOM 1792 N TRP A 218 2.347 20.759 -15.483 1.00 19.50 N
+ANISOU 1792 N TRP A 218 2159 2912 2339 -640 -532 750 N
+ATOM 1793 CA TRP A 218 2.290 22.214 -15.276 1.00 19.27 C
+ANISOU 1793 CA TRP A 218 2071 2875 2374 -597 -503 788 C
+ATOM 1794 C TRP A 218 3.589 22.829 -14.740 1.00 19.18 C
+ANISOU 1794 C TRP A 218 2084 2834 2369 -535 -463 704 C
+ATOM 1795 O TRP A 218 3.833 24.006 -14.958 1.00 19.69 O
+ANISOU 1795 O TRP A 218 2116 2896 2469 -518 -450 724 O
+ATOM 1796 CB TRP A 218 1.102 22.617 -14.384 1.00 19.08 C
+ANISOU 1796 CB TRP A 218 1990 2837 2422 -556 -480 866 C
+ATOM 1797 CG TRP A 218 1.172 22.070 -12.987 1.00 18.92 C
+ANISOU 1797 CG TRP A 218 1998 2781 2409 -491 -442 816 C
+ATOM 1798 CD1 TRP A 218 0.547 20.956 -12.513 1.00 19.63 C
+ANISOU 1798 CD1 TRP A 218 2098 2871 2488 -499 -453 828 C
+ATOM 1799 CD2 TRP A 218 1.858 22.655 -11.864 1.00 19.21 C
+ANISOU 1799 CD2 TRP A 218 2055 2774 2468 -410 -390 754 C
+ATOM 1800 NE1 TRP A 218 0.866 20.766 -11.187 1.00 19.83 N
+ANISOU 1800 NE1 TRP A 218 2152 2860 2523 -426 -408 770 N
+ATOM 1801 CE2 TRP A 218 1.651 21.805 -10.761 1.00 19.68 C
+ANISOU 1801 CE2 TRP A 218 2142 2813 2523 -373 -370 726 C
+ATOM 1802 CE3 TRP A 218 2.647 23.803 -11.692 1.00 19.71 C
+ANISOU 1802 CE3 TRP A 218 2123 2814 2553 -370 -363 720 C
+ATOM 1803 CZ2 TRP A 218 2.230 22.048 -9.514 1.00 19.83 C
+ANISOU 1803 CZ2 TRP A 218 2196 2788 2549 -302 -327 663 C
+ATOM 1804 CZ3 TRP A 218 3.229 24.034 -10.460 1.00 20.19 C
+ANISOU 1804 CZ3 TRP A 218 2220 2828 2621 -302 -323 658 C
+ATOM 1805 CH2 TRP A 218 3.000 23.174 -9.383 1.00 20.04 C
+ANISOU 1805 CH2 TRP A 218 2233 2790 2592 -270 -306 631 C
+ATOM 1806 N PHE A 219 4.383 22.040 -14.003 1.00 18.30 N
+ANISOU 1806 N PHE A 219 2026 2700 2228 -503 -446 619 N
+ATOM 1807 CA PHE A 219 5.624 22.483 -13.356 1.00 17.79 C
+ANISOU 1807 CA PHE A 219 1985 2603 2170 -448 -415 545 C
+ATOM 1808 C PHE A 219 6.842 22.530 -14.276 1.00 18.51 C
+ANISOU 1808 C PHE A 219 2102 2707 2225 -472 -423 502 C
+ATOM 1809 O PHE A 219 7.911 22.994 -13.861 1.00 18.69 O
+ANISOU 1809 O PHE A 219 2134 2706 2260 -434 -405 455 O
+ATOM 1810 CB PHE A 219 5.920 21.590 -12.136 1.00 16.65 C
+ANISOU 1810 CB PHE A 219 1881 2429 2014 -407 -396 485 C
+ATOM 1811 CG PHE A 219 5.997 20.133 -12.506 1.00 15.65 C
+ANISOU 1811 CG PHE A 219 1796 2318 1831 -447 -415 455 C
+ATOM 1812 CD1 PHE A 219 7.163 19.591 -13.018 1.00 15.83 C
+ANISOU 1812 CD1 PHE A 219 1862 2342 1810 -461 -414 395 C
+ATOM 1813 CD2 PHE A 219 4.885 19.316 -12.400 1.00 15.39 C
+ANISOU 1813 CD2 PHE A 219 1759 2296 1791 -472 -432 495 C
+ATOM 1814 CE1 PHE A 219 7.210 18.266 -13.417 1.00 15.82 C
+ANISOU 1814 CE1 PHE A 219 1908 2348 1755 -497 -425 369 C
+ATOM 1815 CE2 PHE A 219 4.956 17.985 -12.749 1.00 15.80 C
+ANISOU 1815 CE2 PHE A 219 1857 2356 1790 -512 -452 467 C
+ATOM 1816 CZ PHE A 219 6.103 17.475 -13.293 1.00 15.51 C
+ANISOU 1816 CZ PHE A 219 1871 2316 1705 -526 -447 402 C
+ATOM 1817 N LEU A 220 6.703 22.044 -15.520 1.00 18.09 N
+ANISOU 1817 N LEU A 220 2060 2687 2125 -536 -450 522 N
+ATOM 1818 CA LEU A 220 7.800 22.117 -16.472 1.00 19.03 C
+ANISOU 1818 CA LEU A 220 2204 2817 2208 -556 -448 490 C
+ATOM 1819 C LEU A 220 7.971 23.571 -16.859 1.00 20.12 C
+ANISOU 1819 C LEU A 220 2291 2963 2392 -547 -447 528 C
+ATOM 1820 O LEU A 220 6.988 24.309 -16.991 1.00 20.85 O
+ANISOU 1820 O LEU A 220 2333 3066 2522 -558 -460 597 O
+ATOM 1821 CB LEU A 220 7.525 21.266 -17.709 1.00 19.05 C
+ANISOU 1821 CB LEU A 220 2247 2850 2142 -629 -475 503 C
+ATOM 1822 CG LEU A 220 7.424 19.768 -17.467 1.00 19.56 C
+ANISOU 1822 CG LEU A 220 2373 2904 2156 -645 -477 463 C
+ATOM 1823 CD1 LEU A 220 7.122 19.044 -18.764 1.00 19.47 C
+ANISOU 1823 CD1 LEU A 220 2414 2915 2069 -725 -507 479 C
+ATOM 1824 CD2 LEU A 220 8.694 19.212 -16.777 1.00 20.00 C
+ANISOU 1824 CD2 LEU A 220 2467 2928 2205 -591 -436 381 C
+ATOM 1825 N ASN A 221 9.214 23.996 -16.965 1.00 20.10 N
+ANISOU 1825 N ASN A 221 2295 2950 2392 -523 -430 490 N
+ATOM 1826 CA ASN A 221 9.510 25.383 -17.252 1.00 20.10 C
+ANISOU 1826 CA ASN A 221 2248 2950 2438 -510 -429 521 C
+ATOM 1827 C ASN A 221 10.545 25.542 -18.362 1.00 19.74 C
+ANISOU 1827 C ASN A 221 2211 2925 2365 -531 -427 511 C
+ATOM 1828 O ASN A 221 11.001 24.563 -18.944 1.00 20.14 O
+ANISOU 1828 O ASN A 221 2310 2986 2357 -554 -421 482 O
+ATOM 1829 CB ASN A 221 9.905 26.097 -15.960 1.00 20.92 C
+ANISOU 1829 CB ASN A 221 2341 3011 2598 -448 -412 496 C
+ATOM 1830 CG ASN A 221 11.146 25.546 -15.329 1.00 23.14 C
+ANISOU 1830 CG ASN A 221 2661 3267 2866 -417 -398 428 C
+ATOM 1831 OD1 ASN A 221 12.101 25.106 -15.998 1.00 22.57 O
+ANISOU 1831 OD1 ASN A 221 2607 3206 2763 -430 -393 405 O
+ATOM 1832 ND2 ASN A 221 11.167 25.582 -14.017 1.00 23.81 N
+ANISOU 1832 ND2 ASN A 221 2758 3312 2975 -375 -390 400 N
+ATOM 1833 N ARG A 222 10.877 26.784 -18.683 1.00 18.88 N
+ANISOU 1833 N ARG A 222 2057 2819 2299 -522 -429 542 N
+ATOM 1834 CA ARG A 222 11.832 27.102 -19.726 1.00 18.93 C
+ANISOU 1834 CA ARG A 222 2060 2843 2288 -537 -424 545 C
+ATOM 1835 C ARG A 222 13.271 27.127 -19.238 1.00 18.41 C
+ANISOU 1835 C ARG A 222 2006 2750 2238 -493 -403 498 C
+ATOM 1836 O ARG A 222 14.134 27.579 -19.982 1.00 18.72 O
+ANISOU 1836 O ARG A 222 2032 2802 2280 -496 -395 510 O
+ATOM 1837 CB ARG A 222 11.491 28.498 -20.253 1.00 20.02 C
+ANISOU 1837 CB ARG A 222 2137 2997 2475 -546 -439 607 C
+ATOM 1838 CG ARG A 222 10.094 28.584 -20.823 1.00 23.44 C
+ANISOU 1838 CG ARG A 222 2546 3462 2899 -595 -463 672 C
+ATOM 1839 CD ARG A 222 9.746 29.989 -21.277 1.00 26.45 C
+ANISOU 1839 CD ARG A 222 2858 3854 3336 -601 -474 740 C
+ATOM 1840 NE ARG A 222 8.499 29.999 -22.037 1.00 28.59 N
+ANISOU 1840 NE ARG A 222 3103 4163 3597 -658 -502 815 N
+ATOM 1841 CZ ARG A 222 8.402 29.730 -23.335 1.00 31.63 C
+ANISOU 1841 CZ ARG A 222 3500 4591 3926 -722 -526 845 C
+ATOM 1842 NH1 ARG A 222 9.488 29.449 -24.047 1.00 31.12 N
+ANISOU 1842 NH1 ARG A 222 3476 4538 3813 -730 -515 807 N
+ATOM 1843 NH2 ARG A 222 7.218 29.741 -23.933 1.00 31.84 N
+ANISOU 1843 NH2 ARG A 222 3501 4649 3946 -780 -560 921 N
+ATOM 1844 N PHE A 223 13.552 26.663 -18.016 1.00 17.24 N
+ANISOU 1844 N PHE A 223 1880 2567 2104 -456 -395 453 N
+ATOM 1845 CA PHE A 223 14.877 26.810 -17.437 1.00 17.43 C
+ANISOU 1845 CA PHE A 223 1905 2561 2156 -418 -384 423 C
+ATOM 1846 C PHE A 223 15.704 25.551 -17.362 1.00 15.35 C
+ANISOU 1846 C PHE A 223 1685 2292 1855 -409 -360 381 C
+ATOM 1847 O PHE A 223 15.192 24.438 -17.466 1.00 15.55 O
+ANISOU 1847 O PHE A 223 1751 2326 1831 -425 -350 360 O
+ATOM 1848 CB PHE A 223 14.761 27.413 -16.009 1.00 18.71 C
+ANISOU 1848 CB PHE A 223 2060 2680 2368 -381 -397 409 C
+ATOM 1849 CG PHE A 223 13.758 28.531 -15.821 1.00 20.74 C
+ANISOU 1849 CG PHE A 223 2286 2930 2664 -380 -409 447 C
+ATOM 1850 CD1 PHE A 223 13.624 29.530 -16.768 1.00 22.13 C
+ANISOU 1850 CD1 PHE A 223 2419 3129 2861 -400 -417 496 C
+ATOM 1851 CD2 PHE A 223 12.977 28.595 -14.684 1.00 22.23 C
+ANISOU 1851 CD2 PHE A 223 2490 3088 2870 -355 -406 437 C
+ATOM 1852 CE1 PHE A 223 12.696 30.547 -16.598 1.00 23.38 C
+ANISOU 1852 CE1 PHE A 223 2545 3277 3060 -396 -421 538 C
+ATOM 1853 CE2 PHE A 223 12.071 29.627 -14.501 1.00 23.56 C
+ANISOU 1853 CE2 PHE A 223 2631 3243 3077 -346 -405 478 C
+ATOM 1854 CZ PHE A 223 11.935 30.596 -15.459 1.00 23.59 C
+ANISOU 1854 CZ PHE A 223 2589 3269 3106 -367 -412 529 C
+ATOM 1855 N THR A 224 17.002 25.743 -17.157 1.00 14.22 N
+ANISOU 1855 N THR A 224 1530 2131 1741 -383 -350 374 N
+ATOM 1856 CA THR A 224 17.923 24.681 -16.819 1.00 13.87 C
+ANISOU 1856 CA THR A 224 1516 2071 1683 -362 -324 342 C
+ATOM 1857 C THR A 224 18.777 25.156 -15.619 1.00 14.09 C
+ANISOU 1857 C THR A 224 1523 2060 1769 -330 -344 335 C
+ATOM 1858 O THR A 224 18.645 26.293 -15.133 1.00 14.76 O
+ANISOU 1858 O THR A 224 1582 2130 1898 -326 -376 351 O
+ATOM 1859 CB THR A 224 18.695 24.154 -18.032 1.00 14.52 C
+ANISOU 1859 CB THR A 224 1613 2174 1731 -369 -284 352 C
+ATOM 1860 OG1 THR A 224 19.214 22.865 -17.666 1.00 14.05 O
+ANISOU 1860 OG1 THR A 224 1594 2096 1648 -351 -251 318 O
+ATOM 1861 CG2 THR A 224 19.849 25.052 -18.412 1.00 14.98 C
+ANISOU 1861 CG2 THR A 224 1625 2231 1837 -353 -280 390 C
+ATOM 1862 N THR A 225 19.601 24.275 -15.099 1.00 13.19 N
+ANISOU 1862 N THR A 225 1427 1930 1656 -310 -327 314 N
+ATOM 1863 CA THR A 225 20.500 24.563 -14.003 1.00 13.50 C
+ANISOU 1863 CA THR A 225 1450 1933 1745 -289 -350 314 C
+ATOM 1864 C THR A 225 21.729 23.647 -14.160 1.00 13.55 C
+ANISOU 1864 C THR A 225 1455 1935 1756 -272 -316 321 C
+ATOM 1865 O THR A 225 21.844 22.918 -15.145 1.00 13.01 O
+ANISOU 1865 O THR A 225 1403 1888 1651 -273 -269 323 O
+ATOM 1866 CB THR A 225 19.759 24.407 -12.648 1.00 15.53 C
+ANISOU 1866 CB THR A 225 1737 2164 2000 -281 -375 279 C
+ATOM 1867 OG1 THR A 225 20.659 24.812 -11.628 1.00 17.08 O
+ANISOU 1867 OG1 THR A 225 1926 2324 2239 -269 -407 283 O
+ATOM 1868 CG2 THR A 225 19.333 22.975 -12.374 1.00 16.36 C
+ANISOU 1868 CG2 THR A 225 1881 2273 2060 -277 -349 242 C
+ATOM 1869 N THR A 226 22.671 23.746 -13.226 1.00 13.79 N
+ANISOU 1869 N THR A 226 1469 1936 1834 -257 -339 332 N
+ATOM 1870 CA THR A 226 23.834 22.885 -13.142 1.00 13.97 C
+ANISOU 1870 CA THR A 226 1483 1950 1876 -238 -308 348 C
+ATOM 1871 C THR A 226 23.718 22.116 -11.827 1.00 14.17 C
+ANISOU 1871 C THR A 226 1535 1950 1898 -231 -325 314 C
+ATOM 1872 O THR A 226 22.936 22.501 -10.957 1.00 13.64 O
+ANISOU 1872 O THR A 226 1489 1869 1823 -239 -365 286 O
+ATOM 1873 CB THR A 226 25.130 23.738 -13.146 1.00 16.08 C
+ANISOU 1873 CB THR A 226 1692 2204 2212 -234 -332 409 C
+ATOM 1874 OG1 THR A 226 25.192 24.499 -11.938 1.00 16.64 O
+ANISOU 1874 OG1 THR A 226 1760 2243 2318 -246 -401 409 O
+ATOM 1875 CG2 THR A 226 25.245 24.618 -14.361 1.00 17.33 C
+ANISOU 1875 CG2 THR A 226 1819 2387 2379 -240 -320 448 C
+ATOM 1876 N ALEU A 227 24.519 21.061 -11.653 0.50 14.30 N
+ANISOU 1876 N ALEU A 227 1551 1958 1924 -213 -291 321 N
+ATOM 1877 N BLEU A 227 24.524 21.056 -11.640 0.50 14.01 N
+ANISOU 1877 N BLEU A 227 1515 1922 1888 -213 -291 321 N
+ATOM 1878 CA ALEU A 227 24.520 20.302 -10.408 0.50 15.27 C
+ANISOU 1878 CA ALEU A 227 1694 2059 2049 -206 -308 296 C
+ATOM 1879 CA BLEU A 227 24.508 20.322 -10.373 0.50 14.69 C
+ANISOU 1879 CA BLEU A 227 1621 1985 1977 -207 -310 295 C
+ATOM 1880 C ALEU A 227 24.897 21.190 -9.216 0.50 15.82 C
+ANISOU 1880 C ALEU A 227 1749 2099 2162 -218 -380 311 C
+ATOM 1881 C BLEU A 227 24.873 21.224 -9.206 0.50 15.51 C
+ANISOU 1881 C BLEU A 227 1711 2060 2123 -219 -382 311 C
+ATOM 1882 O ALEU A 227 24.223 21.149 -8.192 0.50 16.27 O
+ANISOU 1882 O ALEU A 227 1842 2140 2200 -224 -412 274 O
+ATOM 1883 O BLEU A 227 24.172 21.226 -8.197 0.50 15.90 O
+ANISOU 1883 O BLEU A 227 1795 2093 2152 -225 -414 273 O
+ATOM 1884 CB ALEU A 227 25.476 19.108 -10.535 0.50 15.64 C
+ANISOU 1884 CB ALEU A 227 1732 2100 2112 -183 -254 317 C
+ATOM 1885 CB BLEU A 227 25.440 19.112 -10.410 0.50 14.62 C
+ANISOU 1885 CB BLEU A 227 1603 1969 1982 -184 -260 314 C
+ATOM 1886 CG ALEU A 227 25.138 17.847 -9.735 0.50 17.11 C
+ANISOU 1886 CG ALEU A 227 1952 2274 2273 -174 -240 278 C
+ATOM 1887 CG BLEU A 227 24.906 17.875 -11.109 0.50 15.35 C
+ANISOU 1887 CG BLEU A 227 1740 2074 2019 -174 -192 279 C
+ATOM 1888 CD1ALEU A 227 23.676 17.439 -9.907 0.50 17.60 C
+ANISOU 1888 CD1ALEU A 227 2069 2351 2268 -185 -232 217 C
+ATOM 1889 CD1BLEU A 227 25.881 16.725 -10.955 0.50 15.25 C
+ANISOU 1889 CD1BLEU A 227 1720 2045 2030 -146 -141 300 C
+ATOM 1890 CD2ALEU A 227 26.019 16.702 -10.161 0.50 17.33 C
+ANISOU 1890 CD2ALEU A 227 1975 2297 2314 -147 -170 301 C
+ATOM 1891 CD2BLEU A 227 23.531 17.463 -10.562 0.50 15.94 C
+ANISOU 1891 CD2BLEU A 227 1864 2153 2040 -187 -211 218 C
+ATOM 1892 N ASN A 228 25.916 22.051 -9.374 1.00 15.51 N
+ANISOU 1892 N ASN A 228 1664 2052 2179 -225 -408 368 N
+ATOM 1893 CA ASN A 228 26.326 22.950 -8.300 1.00 15.00 C
+ANISOU 1893 CA ASN A 228 1596 1953 2151 -245 -486 386 C
+ATOM 1894 C ASN A 228 25.286 24.033 -7.986 1.00 14.90 C
+ANISOU 1894 C ASN A 228 1620 1930 2114 -260 -525 350 C
+ATOM 1895 O ASN A 228 25.056 24.317 -6.813 1.00 15.98 O
+ANISOU 1895 O ASN A 228 1794 2032 2243 -271 -572 328 O
+ATOM 1896 CB ASN A 228 27.700 23.551 -8.581 1.00 15.85 C
+ANISOU 1896 CB ASN A 228 1641 2053 2327 -253 -510 464 C
+ATOM 1897 CG ASN A 228 28.840 22.550 -8.522 1.00 19.59 C
+ANISOU 1897 CG ASN A 228 2077 2526 2841 -237 -480 514 C
+ATOM 1898 OD1 ASN A 228 29.929 22.794 -9.060 1.00 21.73 O
+ANISOU 1898 OD1 ASN A 228 2288 2799 3169 -233 -473 588 O
+ATOM 1899 ND2 ASN A 228 28.635 21.411 -7.881 1.00 20.10 N
+ANISOU 1899 ND2 ASN A 228 2169 2585 2882 -226 -459 482 N
+ATOM 1900 N ASP A 229 24.638 24.604 -9.002 1.00 14.47 N
+ANISOU 1900 N ASP A 229 1556 1898 2042 -260 -501 347 N
+ATOM 1901 CA ASP A 229 23.626 25.638 -8.756 1.00 14.83 C
+ANISOU 1901 CA ASP A 229 1631 1932 2073 -269 -529 323 C
+ATOM 1902 C ASP A 229 22.417 25.008 -8.087 1.00 15.00 C
+ANISOU 1902 C ASP A 229 1704 1950 2044 -259 -513 267 C
+ATOM 1903 O ASP A 229 21.915 25.535 -7.090 1.00 15.74 O
+ANISOU 1903 O ASP A 229 1840 2011 2132 -261 -544 245 O
+ATOM 1904 CB ASP A 229 23.213 26.348 -10.049 1.00 17.00 C
+ANISOU 1904 CB ASP A 229 1876 2237 2347 -273 -507 342 C
+ATOM 1905 CG ASP A 229 22.101 27.337 -9.811 1.00 23.28 C
+ANISOU 1905 CG ASP A 229 2696 3018 3131 -278 -525 323 C
+ATOM 1906 OD1 ASP A 229 22.347 28.337 -9.109 1.00 25.03 O
+ANISOU 1906 OD1 ASP A 229 2930 3199 3380 -287 -572 331 O
+ATOM 1907 OD2 ASP A 229 20.957 27.068 -10.265 1.00 24.97 O
+ANISOU 1907 OD2 ASP A 229 2923 3257 3308 -273 -492 302 O
+ATOM 1908 N PHE A 230 21.979 23.838 -8.584 1.00 14.41 N
+ANISOU 1908 N PHE A 230 1635 1907 1935 -249 -463 247 N
+ATOM 1909 CA PHE A 230 20.850 23.142 -7.980 1.00 14.40 C
+ANISOU 1909 CA PHE A 230 1676 1905 1891 -240 -449 203 C
+ATOM 1910 C PHE A 230 21.151 22.818 -6.516 1.00 15.23 C
+ANISOU 1910 C PHE A 230 1813 1975 2000 -235 -479 184 C
+ATOM 1911 O PHE A 230 20.308 23.067 -5.661 1.00 16.01 O
+ANISOU 1911 O PHE A 230 1952 2052 2080 -229 -491 157 O
+ATOM 1912 CB PHE A 230 20.527 21.845 -8.745 1.00 13.67 C
+ANISOU 1912 CB PHE A 230 1586 1845 1762 -236 -398 189 C
+ATOM 1913 CG PHE A 230 19.422 21.092 -8.049 1.00 14.69 C
+ANISOU 1913 CG PHE A 230 1754 1973 1855 -229 -389 150 C
+ATOM 1914 CD1 PHE A 230 18.100 21.467 -8.213 1.00 15.26 C
+ANISOU 1914 CD1 PHE A 230 1837 2056 1905 -233 -387 144 C
+ATOM 1915 CD2 PHE A 230 19.715 20.119 -7.106 1.00 15.80 C
+ANISOU 1915 CD2 PHE A 230 1914 2097 1991 -218 -389 129 C
+ATOM 1916 CE1 PHE A 230 17.088 20.834 -7.504 1.00 16.46 C
+ANISOU 1916 CE1 PHE A 230 2018 2204 2030 -225 -380 119 C
+ATOM 1917 CE2 PHE A 230 18.704 19.520 -6.370 1.00 16.25 C
+ANISOU 1917 CE2 PHE A 230 2005 2151 2019 -210 -385 99 C
+ATOM 1918 CZ PHE A 230 17.399 19.868 -6.589 1.00 16.71 C
+ANISOU 1918 CZ PHE A 230 2073 2221 2056 -212 -379 95 C
+ATOM 1919 N ASN A 231 22.374 22.361 -6.232 1.00 15.00 N
+ANISOU 1919 N ASN A 231 1764 1935 1998 -237 -491 205 N
+ATOM 1920 CA ASN A 231 22.758 22.003 -4.873 1.00 15.46 C
+ANISOU 1920 CA ASN A 231 1851 1963 2061 -239 -525 195 C
+ATOM 1921 C ASN A 231 22.802 23.158 -3.914 1.00 16.96 C
+ANISOU 1921 C ASN A 231 2076 2110 2259 -255 -585 195 C
+ATOM 1922 O ASN A 231 22.591 22.932 -2.725 1.00 17.72 O
+ANISOU 1922 O ASN A 231 2219 2178 2334 -255 -607 170 O
+ATOM 1923 CB ASN A 231 24.050 21.215 -4.849 1.00 16.36 C
+ANISOU 1923 CB ASN A 231 1929 2078 2210 -240 -523 231 C
+ATOM 1924 CG ASN A 231 23.829 19.796 -5.314 1.00 18.15 C
+ANISOU 1924 CG ASN A 231 2152 2331 2414 -220 -461 213 C
+ATOM 1925 OD1 ASN A 231 22.721 19.254 -5.242 1.00 18.68 O
+ANISOU 1925 OD1 ASN A 231 2253 2409 2436 -211 -436 169 O
+ATOM 1926 ND2 ASN A 231 24.868 19.145 -5.804 1.00 19.47 N
+ANISOU 1926 ND2 ASN A 231 2279 2506 2612 -211 -431 250 N
+ATOM 1927 N LEU A 232 22.976 24.394 -4.396 1.00 17.68 N
+ANISOU 1927 N LEU A 232 2152 2191 2374 -267 -609 220 N
+ATOM 1928 CA LEU A 232 22.885 25.567 -3.519 1.00 19.22 C
+ANISOU 1928 CA LEU A 232 2396 2337 2569 -283 -662 214 C
+ATOM 1929 C LEU A 232 21.437 25.670 -3.002 1.00 19.67 C
+ANISOU 1929 C LEU A 232 2511 2382 2580 -261 -634 166 C
+ATOM 1930 O LEU A 232 21.223 25.880 -1.806 1.00 20.80 O
+ANISOU 1930 O LEU A 232 2721 2482 2700 -262 -658 142 O
+ATOM 1931 CB LEU A 232 23.257 26.842 -4.289 1.00 20.79 C
+ANISOU 1931 CB LEU A 232 2564 2531 2805 -298 -684 250 C
+ATOM 1932 CG LEU A 232 24.717 26.974 -4.677 1.00 23.66 C
+ANISOU 1932 CG LEU A 232 2869 2897 3222 -320 -719 310 C
+ATOM 1933 CD1 LEU A 232 24.933 28.250 -5.452 1.00 24.78 C
+ANISOU 1933 CD1 LEU A 232 2982 3035 3398 -333 -739 345 C
+ATOM 1934 CD2 LEU A 232 25.615 26.984 -3.447 1.00 24.66 C
+ANISOU 1934 CD2 LEU A 232 3027 2980 3364 -349 -789 327 C
+ATOM 1935 N VAL A 233 20.459 25.417 -3.886 1.00 18.99 N
+ANISOU 1935 N VAL A 233 2402 2334 2479 -243 -580 157 N
+ATOM 1936 CA VAL A 233 19.045 25.406 -3.533 1.00 18.83 C
+ANISOU 1936 CA VAL A 233 2420 2309 2424 -220 -547 128 C
+ATOM 1937 C VAL A 233 18.700 24.193 -2.684 1.00 18.78 C
+ANISOU 1937 C VAL A 233 2444 2304 2386 -206 -531 97 C
+ATOM 1938 O VAL A 233 18.008 24.331 -1.675 1.00 19.12 O
+ANISOU 1938 O VAL A 233 2544 2316 2405 -190 -528 74 O
+ATOM 1939 CB VAL A 233 18.177 25.464 -4.804 1.00 20.10 C
+ANISOU 1939 CB VAL A 233 2538 2514 2584 -214 -505 142 C
+ATOM 1940 CG1 VAL A 233 16.694 25.454 -4.446 1.00 20.95 C
+ANISOU 1940 CG1 VAL A 233 2676 2618 2668 -191 -471 128 C
+ATOM 1941 CG2 VAL A 233 18.525 26.699 -5.624 1.00 20.92 C
+ANISOU 1941 CG2 VAL A 233 2610 2616 2722 -228 -521 175 C
+ATOM 1942 N ALA A 234 19.239 23.018 -3.016 1.00 18.51 N
+ANISOU 1942 N ALA A 234 2379 2302 2354 -209 -520 99 N
+ATOM 1943 CA ALA A 234 18.996 21.802 -2.227 1.00 19.45 C
+ANISOU 1943 CA ALA A 234 2521 2423 2446 -197 -506 73 C
+ATOM 1944 C ALA A 234 19.449 22.000 -0.771 1.00 20.44 C
+ANISOU 1944 C ALA A 234 2700 2501 2564 -201 -549 61 C
+ATOM 1945 O ALA A 234 18.700 21.699 0.153 1.00 20.35 O
+ANISOU 1945 O ALA A 234 2737 2472 2521 -185 -538 34 O
+ATOM 1946 CB ALA A 234 19.732 20.621 -2.849 1.00 19.88 C
+ANISOU 1946 CB ALA A 234 2534 2510 2511 -201 -488 82 C
+ATOM 1947 N MET A 235 20.620 22.616 -0.569 1.00 20.53 N
+ANISOU 1947 N MET A 235 2708 2489 2605 -227 -599 85 N
+ATOM 1948 CA MET A 235 21.139 22.894 0.770 1.00 21.06 C
+ANISOU 1948 CA MET A 235 2833 2506 2661 -244 -653 80 C
+ATOM 1949 C MET A 235 20.163 23.771 1.556 1.00 19.75 C
+ANISOU 1949 C MET A 235 2748 2297 2458 -231 -651 50 C
+ATOM 1950 O MET A 235 19.813 23.447 2.691 1.00 19.72 O
+ANISOU 1950 O MET A 235 2808 2267 2418 -223 -654 24 O
+ATOM 1951 CB MET A 235 22.522 23.574 0.668 1.00 23.60 C
+ANISOU 1951 CB MET A 235 3132 2810 3027 -282 -716 124 C
+ATOM 1952 CG MET A 235 23.037 24.121 1.984 1.00 29.30 C
+ANISOU 1952 CG MET A 235 3926 3474 3734 -313 -786 124 C
+ATOM 1953 SD MET A 235 24.257 23.025 2.705 1.00 42.88 S
+ANISOU 1953 SD MET A 235 5622 5196 5473 -340 -831 157 S
+ATOM 1954 CE MET A 235 25.589 23.247 1.552 1.00 39.42 C
+ANISOU 1954 CE MET A 235 5082 4783 5112 -362 -851 231 C
+ATOM 1955 N LYS A 236 19.700 24.853 0.927 1.00 18.47 N
+ANISOU 1955 N LYS A 236 2583 2127 2306 -226 -639 57 N
+ATOM 1956 CA LYS A 236 18.792 25.785 1.563 1.00 17.97 C
+ANISOU 1956 CA LYS A 236 2595 2016 2215 -208 -625 36 C
+ATOM 1957 C LYS A 236 17.493 25.121 2.014 1.00 17.43 C
+ANISOU 1957 C LYS A 236 2555 1957 2112 -167 -566 10 C
+ATOM 1958 O LYS A 236 16.951 25.470 3.058 1.00 18.51 O
+ANISOU 1958 O LYS A 236 2773 2045 2214 -149 -556 -12 O
+ATOM 1959 CB LYS A 236 18.530 26.978 0.623 1.00 20.89 C
+ANISOU 1959 CB LYS A 236 2939 2384 2613 -207 -616 56 C
+ATOM 1960 CG LYS A 236 17.528 27.986 1.164 1.00 26.53 C
+ANISOU 1960 CG LYS A 236 3727 3048 3307 -180 -586 42 C
+ATOM 1961 CD LYS A 236 17.172 29.030 0.127 1.00 33.01 C
+ANISOU 1961 CD LYS A 236 4508 3874 4161 -177 -569 68 C
+ATOM 1962 CE LYS A 236 15.990 29.854 0.572 1.00 37.50 C
+ANISOU 1962 CE LYS A 236 5137 4397 4715 -139 -519 61 C
+ATOM 1963 NZ LYS A 236 16.358 30.835 1.631 1.00 40.05 N
+ANISOU 1963 NZ LYS A 236 5567 4634 5015 -148 -550 42 N
+ATOM 1964 N TYR A 237 17.020 24.124 1.260 1.00 15.66 N
+ANISOU 1964 N TYR A 237 2267 1790 1895 -153 -527 15 N
+ATOM 1965 CA TYR A 237 15.746 23.472 1.564 1.00 14.78 C
+ANISOU 1965 CA TYR A 237 2168 1692 1758 -118 -474 2 C
+ATOM 1966 C TYR A 237 15.852 22.109 2.238 1.00 14.96 C
+ANISOU 1966 C TYR A 237 2196 1729 1759 -114 -473 -16 C
+ATOM 1967 O TYR A 237 14.861 21.366 2.262 1.00 15.72 O
+ANISOU 1967 O TYR A 237 2282 1848 1841 -89 -431 -19 O
+ATOM 1968 CB TYR A 237 14.899 23.373 0.286 1.00 14.56 C
+ANISOU 1968 CB TYR A 237 2073 1712 1748 -110 -433 26 C
+ATOM 1969 CG TYR A 237 14.367 24.728 -0.118 1.00 15.63 C
+ANISOU 1969 CG TYR A 237 2211 1826 1900 -101 -420 47 C
+ATOM 1970 CD1 TYR A 237 13.223 25.245 0.467 1.00 16.68 C
+ANISOU 1970 CD1 TYR A 237 2387 1928 2023 -65 -377 51 C
+ATOM 1971 CD2 TYR A 237 15.067 25.534 -1.005 1.00 16.39 C
+ANISOU 1971 CD2 TYR A 237 2272 1928 2027 -126 -446 66 C
+ATOM 1972 CE1 TYR A 237 12.778 26.527 0.169 1.00 17.54 C
+ANISOU 1972 CE1 TYR A 237 2503 2010 2152 -53 -360 73 C
+ATOM 1973 CE2 TYR A 237 14.617 26.808 -1.333 1.00 16.88 C
+ANISOU 1973 CE2 TYR A 237 2339 1968 2108 -118 -434 86 C
+ATOM 1974 CZ TYR A 237 13.486 27.312 -0.721 1.00 18.39 C
+ANISOU 1974 CZ TYR A 237 2574 2123 2289 -82 -391 89 C
+ATOM 1975 OH TYR A 237 13.013 28.560 -1.046 1.00 19.90 O
+ANISOU 1975 OH TYR A 237 2769 2289 2504 -70 -372 114 O
+ATOM 1976 N AASN A 238 17.029 21.783 2.777 0.50 14.71 N
+ANISOU 1976 N AASN A 238 2175 1685 1729 -140 -520 -21 N
+ATOM 1977 N BASN A 238 17.031 21.780 2.788 0.50 14.49 N
+ANISOU 1977 N BASN A 238 2148 1657 1700 -140 -520 -21 N
+ATOM 1978 CA AASN A 238 17.254 20.514 3.458 0.50 15.20 C
+ANISOU 1978 CA AASN A 238 2240 1759 1775 -138 -523 -33 C
+ATOM 1979 CA BASN A 238 17.284 20.504 3.467 0.50 14.74 C
+ANISOU 1979 CA BASN A 238 2182 1701 1718 -139 -524 -33 C
+ATOM 1980 C AASN A 238 16.986 19.323 2.549 0.50 14.96 C
+ANISOU 1980 C AASN A 238 2143 1785 1758 -131 -487 -28 C
+ATOM 1981 C BASN A 238 17.054 19.295 2.568 0.50 14.80 C
+ANISOU 1981 C BASN A 238 2122 1765 1739 -133 -489 -28 C
+ATOM 1982 O AASN A 238 16.317 18.373 2.941 0.50 15.04 O
+ANISOU 1982 O AASN A 238 2159 1809 1749 -112 -459 -41 O
+ATOM 1983 O BASN A 238 16.509 18.281 3.000 0.50 14.95 O
+ANISOU 1983 O BASN A 238 2144 1796 1739 -117 -466 -41 O
+ATOM 1984 CB AASN A 238 16.460 20.437 4.761 0.50 17.13 C
+ANISOU 1984 CB AASN A 238 2562 1969 1976 -112 -506 -57 C
+ATOM 1985 CB BASN A 238 16.506 20.379 4.782 0.50 15.99 C
+ANISOU 1985 CB BASN A 238 2416 1827 1832 -114 -508 -57 C
+ATOM 1986 CG AASN A 238 16.882 21.508 5.733 0.50 21.05 C
+ANISOU 1986 CG AASN A 238 3145 2403 2451 -126 -546 -66 C
+ATOM 1987 CG BASN A 238 17.068 21.220 5.903 0.50 18.49 C
+ANISOU 1987 CG BASN A 238 2820 2082 2124 -131 -554 -67 C
+ATOM 1988 OD1AASN A 238 16.104 22.393 6.115 0.50 22.39 O
+ANISOU 1988 OD1AASN A 238 3377 2533 2598 -103 -521 -75 O
+ATOM 1989 OD1BASN A 238 18.118 21.861 5.772 0.50 18.96 O
+ANISOU 1989 OD1BASN A 238 2879 2122 2202 -168 -609 -53 O
+ATOM 1990 ND2AASN A 238 18.142 21.469 6.126 0.50 21.55 N
+ANISOU 1990 ND2AASN A 238 3215 2452 2521 -167 -611 -58 N
+ATOM 1991 ND2BASN A 238 16.368 21.244 7.026 0.50 19.10 N
+ANISOU 1991 ND2BASN A 238 2978 2124 2157 -105 -534 -89 N
+ATOM 1992 N TYR A 239 17.462 19.417 1.309 1.00 14.63 N
+ANISOU 1992 N TYR A 239 2042 1771 1744 -147 -485 -8 N
+ATOM 1993 CA TYR A 239 17.378 18.342 0.336 1.00 14.81 C
+ANISOU 1993 CA TYR A 239 2014 1840 1775 -147 -454 -4 C
+ATOM 1994 C TYR A 239 18.779 17.746 0.260 1.00 15.52 C
+ANISOU 1994 C TYR A 239 2074 1933 1890 -165 -474 10 C
+ATOM 1995 O TYR A 239 19.769 18.452 0.460 1.00 16.11 O
+ANISOU 1995 O TYR A 239 2147 1986 1987 -183 -514 29 O
+ATOM 1996 CB TYR A 239 17.039 18.905 -1.050 1.00 14.64 C
+ANISOU 1996 CB TYR A 239 1953 1844 1764 -154 -435 14 C
+ATOM 1997 CG TYR A 239 15.569 18.840 -1.373 1.00 14.52 C
+ANISOU 1997 CG TYR A 239 1940 1846 1730 -140 -401 13 C
+ATOM 1998 CD1 TYR A 239 14.637 19.491 -0.584 1.00 14.91 C
+ANISOU 1998 CD1 TYR A 239 2026 1870 1769 -118 -394 12 C
+ATOM 1999 CD2 TYR A 239 15.115 18.175 -2.502 1.00 14.55 C
+ANISOU 1999 CD2 TYR A 239 1911 1889 1728 -151 -376 22 C
+ATOM 2000 CE1 TYR A 239 13.281 19.426 -0.871 1.00 15.52 C
+ANISOU 2000 CE1 TYR A 239 2095 1964 1839 -104 -361 26 C
+ATOM 2001 CE2 TYR A 239 13.766 18.114 -2.809 1.00 15.01 C
+ANISOU 2001 CE2 TYR A 239 1965 1964 1773 -146 -355 34 C
+ATOM 2002 CZ TYR A 239 12.850 18.743 -1.992 1.00 15.84 C
+ANISOU 2002 CZ TYR A 239 2094 2047 1877 -121 -347 41 C
+ATOM 2003 OH TYR A 239 11.509 18.631 -2.269 1.00 16.32 O
+ANISOU 2003 OH TYR A 239 2142 2126 1936 -115 -324 67 O
+ATOM 2004 N AGLU A 240 18.870 16.448 -0.030 0.50 15.37 N
+ANISOU 2004 N AGLU A 240 2031 1938 1870 -160 -446 6 N
+ATOM 2005 N BGLU A 240 18.868 16.461 -0.067 0.50 15.60 N
+ANISOU 2005 N BGLU A 240 2060 1969 1900 -160 -446 6 N
+ATOM 2006 CA AGLU A 240 20.154 15.777 -0.186 0.50 16.23 C
+ANISOU 2006 CA AGLU A 240 2106 2050 2009 -169 -451 28 C
+ATOM 2007 CA BGLU A 240 20.151 15.796 -0.223 0.50 16.61 C
+ANISOU 2007 CA BGLU A 240 2154 2099 2058 -169 -450 28 C
+ATOM 2008 C AGLU A 240 20.879 16.322 -1.420 0.50 16.43 C
+ANISOU 2008 C AGLU A 240 2090 2088 2064 -180 -444 58 C
+ATOM 2009 C BGLU A 240 20.878 16.350 -1.428 0.50 16.61 C
+ANISOU 2009 C BGLU A 240 2113 2111 2087 -180 -444 58 C
+ATOM 2010 O AGLU A 240 20.244 16.585 -2.438 0.50 15.69 O
+ANISOU 2010 O AGLU A 240 1989 2015 1956 -179 -417 53 O
+ATOM 2011 O BGLU A 240 20.249 16.611 -2.453 0.50 15.86 O
+ANISOU 2011 O BGLU A 240 2011 2037 1979 -179 -417 53 O
+ATOM 2012 CB AGLU A 240 19.925 14.265 -0.355 0.50 18.78 C
+ANISOU 2012 CB AGLU A 240 2421 2394 2322 -157 -409 14 C
+ATOM 2013 CB BGLU A 240 19.929 14.302 -0.446 0.50 19.82 C
+ANISOU 2013 CB BGLU A 240 2550 2526 2454 -157 -408 15 C
+ATOM 2014 CG AGLU A 240 19.511 13.580 0.931 0.50 23.01 C
+ANISOU 2014 CG AGLU A 240 2988 2918 2839 -147 -418 -6 C
+ATOM 2015 CG BGLU A 240 19.757 13.549 0.847 0.50 25.74 C
+ANISOU 2015 CG BGLU A 240 3326 3262 3190 -149 -418 -1 C
+ATOM 2016 CD AGLU A 240 20.607 13.558 1.976 0.50 27.97 C
+ANISOU 2016 CD AGLU A 240 3616 3521 3489 -158 -460 13 C
+ATOM 2017 CD BGLU A 240 19.839 12.057 0.654 0.50 32.83 C
+ANISOU 2017 CD BGLU A 240 4209 4175 4091 -139 -381 -6 C
+ATOM 2018 OE1AGLU A 240 21.558 12.757 1.825 0.50 28.30 O
+ANISOU 2018 OE1AGLU A 240 3622 3567 3563 -160 -451 38 O
+ATOM 2019 OE1BGLU A 240 19.029 11.520 -0.134 0.50 34.72 O
+ANISOU 2019 OE1BGLU A 240 4450 4433 4308 -135 -343 -22 O
+ATOM 2020 OE2AGLU A 240 20.521 14.346 2.943 0.50 29.56 O
+ANISOU 2020 OE2AGLU A 240 3858 3697 3677 -165 -502 8 O
+ATOM 2021 OE2BGLU A 240 20.715 11.421 1.281 0.50 35.82 O
+ANISOU 2021 OE2BGLU A 240 4574 4543 4493 -140 -390 10 O
+ATOM 2022 N PRO A 241 22.205 16.501 -1.358 1.00 17.14 N
+ANISOU 2022 N PRO A 241 2153 2168 2193 -191 -466 92 N
+ATOM 2023 CA PRO A 241 22.942 16.989 -2.541 1.00 18.08 C
+ANISOU 2023 CA PRO A 241 2227 2298 2344 -196 -454 129 C
+ATOM 2024 C PRO A 241 22.812 15.998 -3.698 1.00 17.98 C
+ANISOU 2024 C PRO A 241 2198 2315 2320 -182 -387 124 C
+ATOM 2025 O PRO A 241 22.874 14.796 -3.468 1.00 18.99 O
+ANISOU 2025 O PRO A 241 2329 2443 2441 -171 -359 115 O
+ATOM 2026 CB PRO A 241 24.400 17.037 -2.063 1.00 19.59 C
+ANISOU 2026 CB PRO A 241 2383 2473 2589 -208 -485 182 C
+ATOM 2027 CG PRO A 241 24.323 17.034 -0.568 1.00 19.93 C
+ANISOU 2027 CG PRO A 241 2465 2487 2620 -222 -542 169 C
+ATOM 2028 CD PRO A 241 23.111 16.247 -0.217 1.00 17.24 C
+ANISOU 2028 CD PRO A 241 2168 2155 2229 -203 -511 114 C
+ATOM 2029 N LEU A 242 22.540 16.485 -4.895 1.00 17.16 N
+ANISOU 2029 N LEU A 242 2081 2229 2211 -185 -365 132 N
+ATOM 2030 CA LEU A 242 22.418 15.624 -6.060 1.00 17.79 C
+ANISOU 2030 CA LEU A 242 2160 2329 2268 -176 -302 127 C
+ATOM 2031 C LEU A 242 23.822 15.392 -6.612 1.00 17.81 C
+ANISOU 2031 C LEU A 242 2124 2329 2316 -165 -271 175 C
+ATOM 2032 O LEU A 242 24.618 16.325 -6.735 1.00 17.96 O
+ANISOU 2032 O LEU A 242 2108 2343 2374 -171 -297 215 O
+ATOM 2033 CB LEU A 242 21.514 16.262 -7.115 1.00 18.10 C
+ANISOU 2033 CB LEU A 242 2211 2391 2274 -188 -292 115 C
+ATOM 2034 CG LEU A 242 20.945 15.279 -8.128 1.00 19.57 C
+ANISOU 2034 CG LEU A 242 2425 2597 2415 -191 -240 96 C
+ATOM 2035 CD1 LEU A 242 19.885 14.396 -7.492 1.00 20.27 C
+ANISOU 2035 CD1 LEU A 242 2550 2685 2468 -192 -238 58 C
+ATOM 2036 CD2 LEU A 242 20.350 16.000 -9.280 1.00 19.83 C
+ANISOU 2036 CD2 LEU A 242 2458 2652 2423 -210 -238 103 C
+ATOM 2037 N THR A 243 24.131 14.138 -6.881 1.00 18.16 N
+ANISOU 2037 N THR A 243 2176 2371 2353 -148 -216 171 N
+ATOM 2038 CA THR A 243 25.435 13.756 -7.399 1.00 18.67 C
+ANISOU 2038 CA THR A 243 2205 2427 2461 -129 -169 223 C
+ATOM 2039 C THR A 243 25.333 13.318 -8.861 1.00 19.12 C
+ANISOU 2039 C THR A 243 2288 2496 2482 -118 -94 215 C
+ATOM 2040 O THR A 243 24.223 13.074 -9.370 1.00 18.82 O
+ANISOU 2040 O THR A 243 2298 2470 2382 -132 -85 168 O
+ATOM 2041 CB THR A 243 26.018 12.618 -6.543 1.00 19.51 C
+ANISOU 2041 CB THR A 243 2302 2515 2595 -111 -150 234 C
+ATOM 2042 OG1 THR A 243 25.257 11.425 -6.756 1.00 19.15 O
+ANISOU 2042 OG1 THR A 243 2306 2470 2500 -103 -103 186 O
+ATOM 2043 CG2 THR A 243 26.099 12.973 -5.073 1.00 20.65 C
+ANISOU 2043 CG2 THR A 243 2434 2647 2764 -127 -225 239 C
+ATOM 2044 N GLN A 244 26.491 13.150 -9.526 1.00 19.36 N
+ANISOU 2044 N GLN A 244 2287 2517 2550 -95 -42 267 N
+ATOM 2045 CA GLN A 244 26.496 12.626 -10.886 1.00 19.60 C
+ANISOU 2045 CA GLN A 244 2356 2551 2540 -81 41 261 C
+ATOM 2046 C GLN A 244 25.936 11.192 -10.896 1.00 19.31 C
+ANISOU 2046 C GLN A 244 2382 2500 2454 -73 89 213 C
+ATOM 2047 O GLN A 244 25.228 10.841 -11.832 1.00 19.52 O
+ANISOU 2047 O GLN A 244 2468 2530 2417 -83 125 179 O
+ATOM 2048 CB GLN A 244 27.908 12.662 -11.481 1.00 21.32 C
+ANISOU 2048 CB GLN A 244 2529 2757 2816 -48 101 335 C
+ATOM 2049 CG GLN A 244 27.948 12.291 -12.963 1.00 24.67 C
+ANISOU 2049 CG GLN A 244 3001 3180 3193 -31 191 332 C
+ATOM 2050 CD GLN A 244 27.099 13.215 -13.796 1.00 27.50 C
+ANISOU 2050 CD GLN A 244 3381 3566 3501 -62 161 309 C
+ATOM 2051 OE1 GLN A 244 27.194 14.445 -13.689 1.00 28.95 O
+ANISOU 2051 OE1 GLN A 244 3514 3767 3719 -76 105 337 O
+ATOM 2052 NE2 GLN A 244 26.239 12.644 -14.629 1.00 26.25 N
+ANISOU 2052 NE2 GLN A 244 3302 3412 3261 -76 196 259 N
+ATOM 2053 N ASP A 245 26.150 10.409 -9.818 1.00 18.53 N
+ANISOU 2053 N ASP A 245 2271 2384 2386 -60 86 214 N
+ATOM 2054 CA ASP A 245 25.574 9.066 -9.707 1.00 18.09 C
+ANISOU 2054 CA ASP A 245 2274 2313 2287 -56 124 166 C
+ATOM 2055 C ASP A 245 24.045 9.134 -9.768 1.00 16.92 C
+ANISOU 2055 C ASP A 245 2178 2185 2068 -93 79 104 C
+ATOM 2056 O ASP A 245 23.437 8.335 -10.466 1.00 17.01 O
+ANISOU 2056 O ASP A 245 2251 2189 2021 -101 116 70 O
+ATOM 2057 CB ASP A 245 26.001 8.387 -8.399 1.00 20.87 C
+ANISOU 2057 CB ASP A 245 2592 2649 2687 -42 107 180 C
+ATOM 2058 CG ASP A 245 27.274 7.574 -8.483 1.00 27.71 C
+ANISOU 2058 CG ASP A 245 3428 3489 3613 -2 180 237 C
+ATOM 2059 OD1 ASP A 245 28.003 7.709 -9.493 1.00 28.66 O
+ANISOU 2059 OD1 ASP A 245 3544 3601 3744 20 244 273 O
+ATOM 2060 OD2 ASP A 245 27.551 6.809 -7.530 1.00 30.69 O
+ANISOU 2060 OD2 ASP A 245 3785 3852 4024 8 174 248 O
+ATOM 2061 N HIS A 246 23.429 10.114 -9.083 1.00 15.98 N
+ANISOU 2061 N HIS A 246 2032 2084 1955 -114 0 96 N
+ATOM 2062 CA HIS A 246 21.969 10.269 -9.127 1.00 15.49 C
+ANISOU 2062 CA HIS A 246 2009 2041 1837 -146 -39 52 C
+ATOM 2063 C HIS A 246 21.504 10.639 -10.533 1.00 15.40 C
+ANISOU 2063 C HIS A 246 2030 2044 1775 -167 -19 47 C
+ATOM 2064 O HIS A 246 20.479 10.138 -10.994 1.00 15.05 O
+ANISOU 2064 O HIS A 246 2037 2007 1676 -192 -20 17 O
+ATOM 2065 CB HIS A 246 21.508 11.368 -8.176 1.00 15.78 C
+ANISOU 2065 CB HIS A 246 2012 2089 1896 -157 -114 55 C
+ATOM 2066 CG HIS A 246 21.770 11.078 -6.743 1.00 17.82 C
+ANISOU 2066 CG HIS A 246 2251 2332 2186 -144 -143 54 C
+ATOM 2067 ND1 HIS A 246 22.203 12.070 -5.882 1.00 19.11 N
+ANISOU 2067 ND1 HIS A 246 2381 2491 2389 -146 -197 75 N
+ATOM 2068 CD2 HIS A 246 21.645 9.920 -6.061 1.00 19.14 C
+ANISOU 2068 CD2 HIS A 246 2434 2488 2352 -134 -129 37 C
+ATOM 2069 CE1 HIS A 246 22.337 11.483 -4.706 1.00 19.83 C
+ANISOU 2069 CE1 HIS A 246 2470 2568 2495 -138 -215 70 C
+ATOM 2070 NE2 HIS A 246 21.998 10.194 -4.760 1.00 20.16 N
+ANISOU 2070 NE2 HIS A 246 2537 2608 2516 -129 -174 48 N
+ATOM 2071 N VAL A 247 22.246 11.522 -11.204 1.00 15.42 N
+ANISOU 2071 N VAL A 247 2002 2054 1801 -161 -10 83 N
+ATOM 2072 CA VAL A 247 21.930 11.926 -12.569 1.00 15.51 C
+ANISOU 2072 CA VAL A 247 2044 2082 1767 -182 10 85 C
+ATOM 2073 C VAL A 247 21.958 10.715 -13.495 1.00 16.08 C
+ANISOU 2073 C VAL A 247 2190 2136 1784 -181 82 65 C
+ATOM 2074 O VAL A 247 21.051 10.539 -14.308 1.00 16.35 O
+ANISOU 2074 O VAL A 247 2279 2181 1753 -215 78 42 O
+ATOM 2075 CB VAL A 247 22.896 13.023 -13.073 1.00 16.23 C
+ANISOU 2075 CB VAL A 247 2085 2181 1902 -168 18 134 C
+ATOM 2076 CG1 VAL A 247 22.681 13.298 -14.560 1.00 17.00 C
+ANISOU 2076 CG1 VAL A 247 2220 2293 1947 -186 50 137 C
+ATOM 2077 CG2 VAL A 247 22.733 14.297 -12.255 1.00 17.00 C
+ANISOU 2077 CG2 VAL A 247 2124 2290 2044 -177 -57 150 C
+ATOM 2078 N ASP A 248 22.964 9.855 -13.327 1.00 16.47 N
+ANISOU 2078 N ASP A 248 2240 2157 1861 -143 144 78 N
+ATOM 2079 CA ASP A 248 23.084 8.653 -14.146 1.00 17.07 C
+ANISOU 2079 CA ASP A 248 2398 2205 1885 -134 226 58 C
+ATOM 2080 C ASP A 248 21.953 7.675 -13.877 1.00 17.14 C
+ANISOU 2080 C ASP A 248 2470 2205 1838 -164 205 6 C
+ATOM 2081 O ASP A 248 21.438 7.067 -14.812 1.00 17.79 O
+ANISOU 2081 O ASP A 248 2636 2275 1848 -189 234 -21 O
+ATOM 2082 CB ASP A 248 24.433 7.972 -13.911 1.00 18.42 C
+ANISOU 2082 CB ASP A 248 2546 2342 2111 -81 302 92 C
+ATOM 2083 CG ASP A 248 25.621 8.798 -14.361 1.00 21.95 C
+ANISOU 2083 CG ASP A 248 2938 2793 2610 -51 336 155 C
+ATOM 2084 OD1 ASP A 248 25.426 9.733 -15.170 1.00 22.47 O
+ANISOU 2084 OD1 ASP A 248 3003 2881 2652 -70 318 162 O
+ATOM 2085 OD2 ASP A 248 26.742 8.511 -13.904 1.00 24.76 O
+ANISOU 2085 OD2 ASP A 248 3247 3128 3031 -10 376 200 O
+ATOM 2086 N ILE A 249 21.549 7.528 -12.614 1.00 16.87 N
+ANISOU 2086 N ILE A 249 2398 2176 1835 -165 152 -6 N
+ATOM 2087 CA ILE A 249 20.432 6.648 -12.257 1.00 17.46 C
+ANISOU 2087 CA ILE A 249 2522 2245 1865 -193 126 -48 C
+ATOM 2088 C ILE A 249 19.119 7.132 -12.904 1.00 16.76 C
+ANISOU 2088 C ILE A 249 2467 2183 1717 -247 74 -62 C
+ATOM 2089 O ILE A 249 18.263 6.320 -13.253 1.00 17.06 O
+ANISOU 2089 O ILE A 249 2569 2212 1701 -279 69 -89 O
+ATOM 2090 CB ILE A 249 20.323 6.530 -10.715 1.00 19.59 C
+ANISOU 2090 CB ILE A 249 2738 2517 2187 -177 83 -49 C
+ATOM 2091 CG1 ILE A 249 21.526 5.765 -10.147 1.00 20.92 C
+ANISOU 2091 CG1 ILE A 249 2886 2655 2407 -132 136 -33 C
+ATOM 2092 CG2 ILE A 249 19.034 5.855 -10.297 1.00 21.07 C
+ANISOU 2092 CG2 ILE A 249 2960 2709 2335 -209 42 -82 C
+ATOM 2093 CD1 ILE A 249 21.709 5.942 -8.653 1.00 22.51 C
+ANISOU 2093 CD1 ILE A 249 3018 2864 2672 -115 89 -17 C
+ATOM 2094 N LEU A 250 18.972 8.455 -13.087 1.00 15.50 N
+ANISOU 2094 N LEU A 250 2261 2054 1573 -259 32 -39 N
+ATOM 2095 CA LEU A 250 17.794 9.034 -13.730 1.00 15.60 C
+ANISOU 2095 CA LEU A 250 2291 2096 1540 -310 -18 -37 C
+ATOM 2096 C LEU A 250 17.834 8.995 -15.268 1.00 16.87 C
+ANISOU 2096 C LEU A 250 2518 2255 1636 -339 17 -36 C
+ATOM 2097 O LEU A 250 16.844 9.354 -15.898 1.00 17.10 O
+ANISOU 2097 O LEU A 250 2569 2306 1623 -388 -24 -30 O
+ATOM 2098 CB LEU A 250 17.591 10.474 -13.267 1.00 14.27 C
+ANISOU 2098 CB LEU A 250 2045 1956 1420 -306 -71 -10 C
+ATOM 2099 CG LEU A 250 17.215 10.646 -11.808 1.00 14.27 C
+ANISOU 2099 CG LEU A 250 1998 1957 1467 -288 -113 -14 C
+ATOM 2100 CD1 LEU A 250 17.430 12.094 -11.372 1.00 14.67 C
+ANISOU 2100 CD1 LEU A 250 1986 2022 1567 -275 -148 13 C
+ATOM 2101 CD2 LEU A 250 15.762 10.236 -11.577 1.00 14.78 C
+ANISOU 2101 CD2 LEU A 250 2085 2031 1500 -320 -152 -24 C
+ATOM 2102 N GLY A 251 18.940 8.525 -15.843 1.00 17.02 N
+ANISOU 2102 N GLY A 251 2570 2248 1650 -307 94 -36 N
+ATOM 2103 CA GLY A 251 19.134 8.385 -17.284 1.00 18.15 C
+ANISOU 2103 CA GLY A 251 2790 2382 1725 -327 142 -36 C
+ATOM 2104 C GLY A 251 17.975 7.739 -18.021 1.00 19.09 C
+ANISOU 2104 C GLY A 251 3006 2497 1753 -393 116 -62 C
+ATOM 2105 O GLY A 251 17.410 8.357 -18.923 1.00 19.38 O
+ANISOU 2105 O GLY A 251 3064 2557 1743 -440 85 -49 O
+ATOM 2106 N PRO A 252 17.540 6.528 -17.623 1.00 19.11 N
+ANISOU 2106 N PRO A 252 3063 2471 1729 -404 118 -95 N
+ATOM 2107 CA PRO A 252 16.394 5.908 -18.309 1.00 19.24 C
+ANISOU 2107 CA PRO A 252 3173 2481 1658 -477 81 -113 C
+ATOM 2108 C PRO A 252 15.110 6.745 -18.294 1.00 18.83 C
+ANISOU 2108 C PRO A 252 3076 2475 1604 -534 -17 -86 C
+ATOM 2109 O PRO A 252 14.431 6.798 -19.315 1.00 19.47 O
+ANISOU 2109 O PRO A 252 3219 2563 1613 -599 -47 -78 O
+ATOM 2110 CB PRO A 252 16.246 4.562 -17.589 1.00 20.19 C
+ANISOU 2110 CB PRO A 252 3331 2562 1776 -468 95 -146 C
+ATOM 2111 CG PRO A 252 17.626 4.268 -17.093 1.00 20.99 C
+ANISOU 2111 CG PRO A 252 3405 2637 1935 -389 180 -148 C
+ATOM 2112 CD PRO A 252 18.109 5.617 -16.617 1.00 19.33 C
+ANISOU 2112 CD PRO A 252 3076 2467 1802 -356 156 -111 C
+ATOM 2113 N LEU A 253 14.785 7.429 -17.181 1.00 18.06 N
+ANISOU 2113 N LEU A 253 2874 2407 1582 -512 -65 -66 N
+ATOM 2114 CA LEU A 253 13.586 8.275 -17.140 1.00 17.83 C
+ANISOU 2114 CA LEU A 253 2797 2418 1560 -557 -145 -31 C
+ATOM 2115 C LEU A 253 13.741 9.519 -18.012 1.00 18.44 C
+ANISOU 2115 C LEU A 253 2847 2525 1635 -570 -153 1 C
+ATOM 2116 O LEU A 253 12.785 9.977 -18.635 1.00 19.17 O
+ANISOU 2116 O LEU A 253 2944 2644 1698 -629 -206 32 O
+ATOM 2117 CB LEU A 253 13.221 8.666 -15.706 1.00 17.36 C
+ANISOU 2117 CB LEU A 253 2645 2373 1577 -522 -181 -20 C
+ATOM 2118 CG LEU A 253 12.642 7.523 -14.882 1.00 18.39 C
+ANISOU 2118 CG LEU A 253 2797 2484 1705 -525 -193 -40 C
+ATOM 2119 CD1 LEU A 253 12.522 7.914 -13.415 1.00 18.47 C
+ANISOU 2119 CD1 LEU A 253 2723 2503 1790 -479 -212 -33 C
+ATOM 2120 CD2 LEU A 253 11.285 7.102 -15.419 1.00 19.76 C
+ANISOU 2120 CD2 LEU A 253 3014 2666 1826 -600 -251 -21 C
+ATOM 2121 N SER A 254 14.956 10.052 -18.077 1.00 18.35 N
+ANISOU 2121 N SER A 254 2804 2509 1657 -518 -101 1 N
+ATOM 2122 CA SER A 254 15.269 11.190 -18.918 1.00 18.83 C
+ANISOU 2122 CA SER A 254 2840 2596 1720 -525 -100 32 C
+ATOM 2123 C SER A 254 15.130 10.789 -20.399 1.00 19.74 C
+ANISOU 2123 C SER A 254 3057 2704 1738 -578 -82 29 C
+ATOM 2124 O SER A 254 14.617 11.567 -21.210 1.00 20.29 O
+ANISOU 2124 O SER A 254 3123 2805 1782 -624 -119 61 O
+ATOM 2125 CB SER A 254 16.703 11.640 -18.638 1.00 19.93 C
+ANISOU 2125 CB SER A 254 2930 2724 1917 -456 -43 35 C
+ATOM 2126 OG SER A 254 17.063 12.706 -19.494 1.00 22.09 O
+ANISOU 2126 OG SER A 254 3179 3022 2193 -461 -39 68 O
+ATOM 2127 N ALA A 255 15.585 9.585 -20.748 1.00 19.75 N
+ANISOU 2127 N ALA A 255 3155 2664 1685 -573 -23 -8 N
+ATOM 2128 CA ALA A 255 15.515 9.100 -22.123 1.00 20.73 C
+ANISOU 2128 CA ALA A 255 3400 2771 1707 -623 2 -17 C
+ATOM 2129 C ALA A 255 14.080 8.868 -22.550 1.00 22.35 C
+ANISOU 2129 C ALA A 255 3655 2991 1848 -715 -82 -7 C
+ATOM 2130 O ALA A 255 13.724 9.175 -23.692 1.00 22.53 O
+ANISOU 2130 O ALA A 255 3732 3025 1802 -774 -103 12 O
+ATOM 2131 CB ALA A 255 16.321 7.819 -22.267 1.00 20.66 C
+ANISOU 2131 CB ALA A 255 3488 2704 1658 -590 91 -60 C
+ATOM 2132 N GLN A 256 13.260 8.330 -21.643 1.00 22.99 N
+ANISOU 2132 N GLN A 256 3714 3069 1952 -729 -131 -13 N
+ATOM 2133 CA GLN A 256 11.861 8.039 -21.931 1.00 24.03 C
+ANISOU 2133 CA GLN A 256 3882 3212 2036 -818 -217 9 C
+ATOM 2134 C GLN A 256 11.033 9.298 -22.174 1.00 23.74 C
+ANISOU 2134 C GLN A 256 3764 3230 2027 -857 -289 71 C
+ATOM 2135 O GLN A 256 10.254 9.350 -23.132 1.00 24.91 O
+ANISOU 2135 O GLN A 256 3964 3390 2109 -941 -342 102 O
+ATOM 2136 CB GLN A 256 11.252 7.200 -20.805 1.00 26.63 C
+ANISOU 2136 CB GLN A 256 4192 3527 2398 -813 -246 -4 C
+ATOM 2137 CG GLN A 256 9.818 6.770 -21.073 1.00 31.24 C
+ANISOU 2137 CG GLN A 256 4812 4119 2938 -905 -335 28 C
+ATOM 2138 CD GLN A 256 9.199 6.054 -19.898 1.00 36.62 C
+ANISOU 2138 CD GLN A 256 5459 4792 3663 -894 -364 25 C
+ATOM 2139 OE1 GLN A 256 9.885 5.560 -18.983 1.00 38.38 O
+ANISOU 2139 OE1 GLN A 256 5664 4991 3928 -825 -312 -15 O
+ATOM 2140 NE2 GLN A 256 7.876 5.983 -19.902 1.00 37.67 N
+ANISOU 2140 NE2 GLN A 256 5577 4944 3791 -964 -450 75 N
+ATOM 2141 N THR A 257 11.226 10.325 -21.350 1.00 21.63 N
+ANISOU 2141 N THR A 257 3374 2991 1853 -801 -291 93 N
+ATOM 2142 CA THR A 257 10.447 11.552 -21.456 1.00 20.74 C
+ANISOU 2142 CA THR A 257 3177 2924 1780 -828 -352 154 C
+ATOM 2143 C THR A 257 11.055 12.627 -22.354 1.00 20.66 C
+ANISOU 2143 C THR A 257 3148 2937 1766 -824 -332 176 C
+ATOM 2144 O THR A 257 10.367 13.578 -22.708 1.00 21.25 O
+ANISOU 2144 O THR A 257 3169 3048 1857 -860 -382 231 O
+ATOM 2145 CB THR A 257 10.244 12.132 -20.061 1.00 21.06 C
+ANISOU 2145 CB THR A 257 3105 2976 1920 -770 -364 167 C
+ATOM 2146 OG1 THR A 257 11.535 12.470 -19.536 1.00 21.29 O
+ANISOU 2146 OG1 THR A 257 3100 2992 1997 -691 -302 135 O
+ATOM 2147 CG2 THR A 257 9.565 11.151 -19.127 1.00 21.27 C
+ANISOU 2147 CG2 THR A 257 3140 2985 1956 -772 -386 155 C
+ATOM 2148 N GLY A 258 12.336 12.508 -22.660 1.00 19.65 N
+ANISOU 2148 N GLY A 258 3055 2787 1625 -777 -256 140 N
+ATOM 2149 CA GLY A 258 13.033 13.522 -23.440 1.00 19.47 C
+ANISOU 2149 CA GLY A 258 3007 2784 1606 -763 -230 162 C
+ATOM 2150 C GLY A 258 13.360 14.765 -22.637 1.00 18.75 C
+ANISOU 2150 C GLY A 258 2790 2716 1619 -707 -237 188 C
+ATOM 2151 O GLY A 258 13.782 15.770 -23.207 1.00 18.83 O
+ANISOU 2151 O GLY A 258 2760 2747 1645 -699 -229 217 O
+ATOM 2152 N ILE A 259 13.206 14.712 -21.284 1.00 17.30 N
+ANISOU 2152 N ILE A 259 2544 2524 1504 -664 -249 176 N
+ATOM 2153 CA ILE A 259 13.516 15.858 -20.450 1.00 17.01 C
+ANISOU 2153 CA ILE A 259 2404 2499 1558 -614 -257 196 C
+ATOM 2154 C ILE A 259 14.840 15.605 -19.784 1.00 16.46 C
+ANISOU 2154 C ILE A 259 2324 2402 1529 -544 -200 163 C
+ATOM 2155 O ILE A 259 14.980 14.653 -19.015 1.00 16.95 O
+ANISOU 2155 O ILE A 259 2410 2438 1594 -521 -183 128 O
+ATOM 2156 CB ILE A 259 12.396 16.138 -19.416 1.00 18.00 C
+ANISOU 2156 CB ILE A 259 2472 2634 1733 -617 -310 216 C
+ATOM 2157 CG1 ILE A 259 11.064 16.389 -20.148 1.00 19.63 C
+ANISOU 2157 CG1 ILE A 259 2679 2870 1908 -690 -367 267 C
+ATOM 2158 CG2 ILE A 259 12.766 17.336 -18.557 1.00 18.35 C
+ANISOU 2158 CG2 ILE A 259 2428 2682 1863 -565 -312 231 C
+ATOM 2159 CD1 ILE A 259 9.876 16.454 -19.229 1.00 21.54 C
+ANISOU 2159 CD1 ILE A 259 2874 3119 2193 -695 -411 296 C
+ATOM 2160 N ALA A 260 15.837 16.436 -20.095 1.00 15.60 N
+ANISOU 2160 N ALA A 260 2177 2297 1452 -512 -172 179 N
+ATOM 2161 CA ALA A 260 17.170 16.324 -19.512 1.00 15.26 C
+ANISOU 2161 CA ALA A 260 2111 2229 1457 -449 -123 165 C
+ATOM 2162 C ALA A 260 17.099 16.416 -17.996 1.00 14.60 C
+ANISOU 2162 C ALA A 260 1974 2133 1439 -416 -150 154 C
+ATOM 2163 O ALA A 260 16.278 17.168 -17.463 1.00 14.60 O
+ANISOU 2163 O ALA A 260 1930 2148 1470 -426 -201 169 O
+ATOM 2164 CB ALA A 260 18.067 17.431 -20.055 1.00 16.18 C
+ANISOU 2164 CB ALA A 260 2178 2359 1611 -428 -106 202 C
+ATOM 2165 N VAL A 261 17.925 15.638 -17.296 1.00 13.65 N
+ANISOU 2165 N VAL A 261 1862 1984 1340 -375 -114 130 N
+ATOM 2166 CA VAL A 261 17.923 15.636 -15.837 1.00 13.86 C
+ANISOU 2166 CA VAL A 261 1849 1997 1422 -346 -140 118 C
+ATOM 2167 C VAL A 261 18.078 17.028 -15.244 1.00 13.55 C
+ANISOU 2167 C VAL A 261 1738 1965 1447 -331 -179 145 C
+ATOM 2168 O VAL A 261 17.313 17.391 -14.351 1.00 14.19 O
+ANISOU 2168 O VAL A 261 1797 2045 1548 -332 -219 141 O
+ATOM 2169 CB VAL A 261 18.954 14.647 -15.258 1.00 15.10 C
+ANISOU 2169 CB VAL A 261 2018 2123 1596 -306 -94 99 C
+ATOM 2170 CG1 VAL A 261 19.013 14.754 -13.744 1.00 14.97 C
+ANISOU 2170 CG1 VAL A 261 1959 2093 1635 -281 -127 92 C
+ATOM 2171 CG2 VAL A 261 18.624 13.214 -15.680 1.00 16.65 C
+ANISOU 2171 CG2 VAL A 261 2294 2303 1728 -321 -58 66 C
+ATOM 2172 N LEU A 262 19.005 17.831 -15.794 1.00 13.28 N
+ANISOU 2172 N LEU A 262 1670 1935 1440 -319 -165 175 N
+ATOM 2173 CA LEU A 262 19.208 19.180 -15.273 1.00 13.56 C
+ANISOU 2173 CA LEU A 262 1643 1971 1536 -308 -205 201 C
+ATOM 2174 C LEU A 262 18.028 20.109 -15.552 1.00 13.51 C
+ANISOU 2174 C LEU A 262 1622 1988 1522 -338 -245 217 C
+ATOM 2175 O LEU A 262 17.795 21.025 -14.755 1.00 13.73 O
+ANISOU 2175 O LEU A 262 1616 2008 1595 -329 -281 226 O
+ATOM 2176 CB LEU A 262 20.526 19.768 -15.738 1.00 13.70 C
+ANISOU 2176 CB LEU A 262 1625 1988 1594 -288 -184 237 C
+ATOM 2177 CG LEU A 262 21.765 19.061 -15.162 1.00 15.11 C
+ANISOU 2177 CG LEU A 262 1797 2140 1806 -252 -152 239 C
+ATOM 2178 CD1 LEU A 262 23.038 19.609 -15.783 1.00 15.85 C
+ANISOU 2178 CD1 LEU A 262 1849 2233 1941 -233 -126 290 C
+ATOM 2179 CD2 LEU A 262 21.832 19.171 -13.652 1.00 15.29 C
+ANISOU 2179 CD2 LEU A 262 1798 2139 1872 -239 -195 228 C
+ATOM 2180 N ASP A 263 17.252 19.857 -16.630 1.00 13.50 N
+ANISOU 2180 N ASP A 263 1652 2012 1467 -376 -240 223 N
+ATOM 2181 CA ASP A 263 16.044 20.647 -16.866 1.00 13.09 C
+ANISOU 2181 CA ASP A 263 1578 1982 1413 -407 -279 249 C
+ATOM 2182 C ASP A 263 15.008 20.287 -15.786 1.00 14.28 C
+ANISOU 2182 C ASP A 263 1734 2122 1570 -405 -304 233 C
+ATOM 2183 O ASP A 263 14.352 21.181 -15.249 1.00 15.00 O
+ANISOU 2183 O ASP A 263 1790 2213 1698 -400 -331 254 O
+ATOM 2184 CB ASP A 263 15.460 20.397 -18.251 1.00 13.77 C
+ANISOU 2184 CB ASP A 263 1698 2097 1437 -457 -277 267 C
+ATOM 2185 CG ASP A 263 16.333 20.842 -19.408 1.00 14.89 C
+ANISOU 2185 CG ASP A 263 1838 2253 1567 -461 -250 288 C
+ATOM 2186 OD1 ASP A 263 17.440 21.396 -19.156 1.00 14.07 O
+ANISOU 2186 OD1 ASP A 263 1696 2137 1512 -423 -234 296 O
+ATOM 2187 OD2 ASP A 263 15.912 20.661 -20.549 1.00 16.19 O
+ANISOU 2187 OD2 ASP A 263 2039 2440 1674 -504 -248 302 O
+ATOM 2188 N MET A 264 14.883 18.991 -15.442 1.00 13.23 N
+ANISOU 2188 N MET A 264 1646 1978 1403 -405 -289 199 N
+ATOM 2189 CA MET A 264 13.973 18.598 -14.358 1.00 12.75 C
+ANISOU 2189 CA MET A 264 1588 1907 1351 -398 -309 187 C
+ATOM 2190 C MET A 264 14.443 19.193 -13.029 1.00 13.28 C
+ANISOU 2190 C MET A 264 1625 1947 1475 -352 -315 177 C
+ATOM 2191 O MET A 264 13.626 19.638 -12.230 1.00 14.09 O
+ANISOU 2191 O MET A 264 1712 2041 1599 -342 -334 186 O
+ATOM 2192 CB MET A 264 13.808 17.085 -14.252 1.00 13.83 C
+ANISOU 2192 CB MET A 264 1777 2035 1444 -407 -293 155 C
+ATOM 2193 CG MET A 264 12.620 16.710 -13.385 1.00 14.70 C
+ANISOU 2193 CG MET A 264 1885 2142 1558 -409 -317 157 C
+ATOM 2194 SD MET A 264 11.043 17.204 -14.145 1.00 16.49 S
+ANISOU 2194 SD MET A 264 2095 2401 1771 -463 -356 214 S
+ATOM 2195 CE MET A 264 10.741 15.784 -15.174 1.00 18.99 C
+ANISOU 2195 CE MET A 264 2483 2724 2007 -520 -357 202 C
+ATOM 2196 N CYS A 265 15.767 19.296 -12.823 1.00 12.88 N
+ANISOU 2196 N CYS A 265 1567 1879 1448 -327 -301 165 N
+ATOM 2197 CA CYS A 265 16.310 19.936 -11.623 1.00 13.13 C
+ANISOU 2197 CA CYS A 265 1578 1883 1529 -294 -318 160 C
+ATOM 2198 C CYS A 265 15.888 21.399 -11.572 1.00 13.37 C
+ANISOU 2198 C CYS A 265 1576 1912 1591 -295 -343 189 C
+ATOM 2199 O CYS A 265 15.599 21.895 -10.489 1.00 13.84 O
+ANISOU 2199 O CYS A 265 1637 1946 1675 -276 -360 183 O
+ATOM 2200 CB CYS A 265 17.828 19.815 -11.597 1.00 13.18 C
+ANISOU 2200 CB CYS A 265 1574 1875 1559 -276 -304 160 C
+ATOM 2201 SG CYS A 265 18.430 18.150 -11.239 1.00 13.95 S
+ANISOU 2201 SG CYS A 265 1704 1959 1636 -262 -268 129 S
+ATOM 2202 N ALA A 266 15.814 22.076 -12.734 1.00 13.18 N
+ANISOU 2202 N ALA A 266 1530 1913 1565 -317 -343 220 N
+ATOM 2203 CA ALA A 266 15.388 23.477 -12.773 1.00 14.34 C
+ANISOU 2203 CA ALA A 266 1644 2059 1747 -318 -364 252 C
+ATOM 2204 C ALA A 266 13.907 23.600 -12.453 1.00 15.13 C
+ANISOU 2204 C ALA A 266 1744 2162 1842 -323 -370 266 C
+ATOM 2205 O ALA A 266 13.510 24.582 -11.826 1.00 16.07 O
+ANISOU 2205 O ALA A 266 1850 2259 1996 -305 -379 280 O
+ATOM 2206 CB ALA A 266 15.692 24.101 -14.119 1.00 15.34 C
+ANISOU 2206 CB ALA A 266 1742 2213 1873 -342 -362 287 C
+ATOM 2207 N SER A 267 13.093 22.600 -12.841 1.00 14.73 N
+ANISOU 2207 N SER A 267 1711 2133 1750 -346 -364 266 N
+ATOM 2208 CA SER A 267 11.680 22.574 -12.475 1.00 15.16 C
+ANISOU 2208 CA SER A 267 1762 2192 1808 -350 -370 290 C
+ATOM 2209 C SER A 267 11.573 22.402 -10.957 1.00 14.35 C
+ANISOU 2209 C SER A 267 1678 2053 1723 -308 -364 261 C
+ATOM 2210 O SER A 267 10.788 23.086 -10.302 1.00 14.65 O
+ANISOU 2210 O SER A 267 1705 2073 1788 -287 -360 283 O
+ATOM 2211 CB SER A 267 10.953 21.421 -13.163 1.00 17.63 C
+ANISOU 2211 CB SER A 267 2095 2533 2072 -390 -373 297 C
+ATOM 2212 OG SER A 267 10.610 21.744 -14.499 1.00 21.64 O
+ANISOU 2212 OG SER A 267 2588 3075 2561 -436 -386 337 O
+ATOM 2213 N LEU A 268 12.371 21.488 -10.401 1.00 13.19 N
+ANISOU 2213 N LEU A 268 1561 1892 1560 -295 -358 216 N
+ATOM 2214 CA LEU A 268 12.359 21.248 -8.965 1.00 13.02 C
+ANISOU 2214 CA LEU A 268 1563 1837 1548 -260 -354 188 C
+ATOM 2215 C LEU A 268 12.836 22.482 -8.205 1.00 13.76 C
+ANISOU 2215 C LEU A 268 1657 1895 1678 -233 -363 187 C
+ATOM 2216 O LEU A 268 12.237 22.854 -7.203 1.00 13.46 O
+ANISOU 2216 O LEU A 268 1637 1828 1651 -206 -357 187 O
+ATOM 2217 CB LEU A 268 13.191 20.007 -8.611 1.00 12.54 C
+ANISOU 2217 CB LEU A 268 1529 1770 1465 -255 -348 147 C
+ATOM 2218 CG LEU A 268 13.338 19.701 -7.124 1.00 13.38 C
+ANISOU 2218 CG LEU A 268 1661 1844 1579 -223 -349 118 C
+ATOM 2219 CD1 LEU A 268 11.961 19.546 -6.450 1.00 14.09 C
+ANISOU 2219 CD1 LEU A 268 1760 1930 1665 -209 -341 130 C
+ATOM 2220 CD2 LEU A 268 14.098 18.421 -6.934 1.00 13.76 C
+ANISOU 2220 CD2 LEU A 268 1727 1891 1609 -223 -341 87 C
+ATOM 2221 N LYS A 269 13.869 23.160 -8.705 1.00 12.82 N
+ANISOU 2221 N LYS A 269 1523 1773 1577 -241 -375 191 N
+ATOM 2222 CA LYS A 269 14.363 24.389 -8.097 1.00 12.60 C
+ANISOU 2222 CA LYS A 269 1498 1707 1582 -225 -392 194 C
+ATOM 2223 C LYS A 269 13.255 25.446 -8.026 1.00 13.34 C
+ANISOU 2223 C LYS A 269 1584 1790 1695 -214 -383 224 C
+ATOM 2224 O LYS A 269 13.062 26.038 -6.976 1.00 13.99 O
+ANISOU 2224 O LYS A 269 1699 1828 1789 -188 -381 215 O
+ATOM 2225 CB LYS A 269 15.546 24.917 -8.911 1.00 13.63 C
+ANISOU 2225 CB LYS A 269 1600 1846 1732 -242 -407 208 C
+ATOM 2226 CG LYS A 269 16.062 26.292 -8.492 1.00 17.21 C
+ANISOU 2226 CG LYS A 269 2053 2261 2223 -235 -433 219 C
+ATOM 2227 CD LYS A 269 17.254 26.664 -9.357 1.00 20.23 C
+ANISOU 2227 CD LYS A 269 2400 2659 2629 -252 -448 241 C
+ATOM 2228 CE LYS A 269 17.557 28.150 -9.315 1.00 23.68 C
+ANISOU 2228 CE LYS A 269 2824 3067 3105 -255 -474 265 C
+ATOM 2229 NZ LYS A 269 18.553 28.518 -10.362 1.00 25.16 N
+ANISOU 2229 NZ LYS A 269 2965 3278 3318 -272 -484 298 N
+ATOM 2230 N GLU A 270 12.479 25.616 -9.107 1.00 13.60 N
+ANISOU 2230 N GLU A 270 1579 1859 1729 -234 -374 264 N
+ATOM 2231 CA GLU A 270 11.380 26.581 -9.098 1.00 14.67 C
+ANISOU 2231 CA GLU A 270 1697 1985 1891 -223 -360 306 C
+ATOM 2232 C GLU A 270 10.288 26.174 -8.115 1.00 15.62 C
+ANISOU 2232 C GLU A 270 1841 2088 2007 -194 -335 309 C
+ATOM 2233 O GLU A 270 9.749 27.026 -7.415 1.00 16.25 O
+ANISOU 2233 O GLU A 270 1935 2128 2111 -162 -315 324 O
+ATOM 2234 CB GLU A 270 10.813 26.806 -10.505 1.00 17.51 C
+ANISOU 2234 CB GLU A 270 2006 2393 2255 -258 -363 358 C
+ATOM 2235 CG GLU A 270 11.804 27.456 -11.453 1.00 24.81 C
+ANISOU 2235 CG GLU A 270 2905 3331 3190 -280 -381 365 C
+ATOM 2236 CD GLU A 270 12.368 28.793 -11.016 1.00 32.43 C
+ANISOU 2236 CD GLU A 270 3871 4255 4198 -259 -388 367 C
+ATOM 2237 OE1 GLU A 270 11.568 29.730 -10.794 1.00 33.99 O
+ANISOU 2237 OE1 GLU A 270 4059 4431 4426 -243 -375 400 O
+ATOM 2238 OE2 GLU A 270 13.611 28.907 -10.900 1.00 33.71 O
+ANISOU 2238 OE2 GLU A 270 4043 4403 4364 -260 -407 342 O
+ATOM 2239 N LEU A 271 9.974 24.877 -8.043 1.00 15.19 N
+ANISOU 2239 N LEU A 271 1794 2056 1921 -203 -333 295 N
+ATOM 2240 CA LEU A 271 8.984 24.384 -7.082 1.00 15.27 C
+ANISOU 2240 CA LEU A 271 1824 2050 1928 -174 -309 300 C
+ATOM 2241 C LEU A 271 9.434 24.628 -5.646 1.00 15.62 C
+ANISOU 2241 C LEU A 271 1924 2041 1972 -133 -299 258 C
+ATOM 2242 O LEU A 271 8.598 24.933 -4.792 1.00 17.11 O
+ANISOU 2242 O LEU A 271 2133 2197 2169 -95 -268 273 O
+ATOM 2243 CB LEU A 271 8.749 22.894 -7.289 1.00 15.27 C
+ANISOU 2243 CB LEU A 271 1825 2083 1894 -196 -316 289 C
+ATOM 2244 CG LEU A 271 7.915 22.555 -8.510 1.00 16.49 C
+ANISOU 2244 CG LEU A 271 1939 2284 2042 -240 -327 340 C
+ATOM 2245 CD1 LEU A 271 7.962 21.084 -8.777 1.00 16.95 C
+ANISOU 2245 CD1 LEU A 271 2015 2366 2060 -269 -339 316 C
+ATOM 2246 CD2 LEU A 271 6.477 23.030 -8.321 1.00 17.56 C
+ANISOU 2246 CD2 LEU A 271 2042 2418 2211 -226 -308 409 C
+ATOM 2247 N LEU A 272 10.737 24.490 -5.367 1.00 14.10 N
+ANISOU 2247 N LEU A 272 1758 1833 1766 -139 -325 211 N
+ATOM 2248 CA LEU A 272 11.233 24.723 -4.011 1.00 14.76 C
+ANISOU 2248 CA LEU A 272 1901 1864 1843 -111 -327 173 C
+ATOM 2249 C LEU A 272 11.164 26.195 -3.655 1.00 16.26 C
+ANISOU 2249 C LEU A 272 2116 2007 2057 -91 -319 186 C
+ATOM 2250 O LEU A 272 10.760 26.536 -2.543 1.00 17.01 O
+ANISOU 2250 O LEU A 272 2267 2053 2144 -57 -297 175 O
+ATOM 2251 CB LEU A 272 12.669 24.214 -3.869 1.00 14.74 C
+ANISOU 2251 CB LEU A 272 1912 1860 1829 -130 -362 135 C
+ATOM 2252 CG LEU A 272 12.797 22.705 -3.843 1.00 16.78 C
+ANISOU 2252 CG LEU A 272 2166 2148 2063 -139 -361 114 C
+ATOM 2253 CD1 LEU A 272 14.257 22.274 -3.868 1.00 17.63 C
+ANISOU 2253 CD1 LEU A 272 2272 2256 2170 -157 -389 91 C
+ATOM 2254 CD2 LEU A 272 12.062 22.119 -2.657 1.00 18.76 C
+ANISOU 2254 CD2 LEU A 272 2454 2379 2294 -109 -341 99 C
+ATOM 2255 N GLN A 273 11.531 27.061 -4.599 1.00 16.06 N
+ANISOU 2255 N GLN A 273 2054 1992 2057 -112 -335 209 N
+ATOM 2256 CA GLN A 273 11.587 28.499 -4.374 1.00 17.33 C
+ANISOU 2256 CA GLN A 273 2237 2105 2243 -99 -332 221 C
+ATOM 2257 C GLN A 273 10.240 29.180 -4.375 1.00 19.69 C
+ANISOU 2257 C GLN A 273 2527 2390 2565 -68 -283 266 C
+ATOM 2258 O GLN A 273 10.080 30.197 -3.708 1.00 20.97 O
+ANISOU 2258 O GLN A 273 2737 2493 2739 -40 -263 267 O
+ATOM 2259 CB GLN A 273 12.515 29.162 -5.409 1.00 17.71 C
+ANISOU 2259 CB GLN A 273 2243 2171 2315 -133 -367 234 C
+ATOM 2260 CG GLN A 273 13.968 28.758 -5.252 1.00 19.36 C
+ANISOU 2260 CG GLN A 273 2464 2378 2515 -156 -413 202 C
+ATOM 2261 CD GLN A 273 14.860 29.396 -6.286 1.00 22.80 C
+ANISOU 2261 CD GLN A 273 2852 2832 2979 -185 -442 225 C
+ATOM 2262 OE1 GLN A 273 14.437 29.745 -7.391 1.00 24.43 O
+ANISOU 2262 OE1 GLN A 273 3006 3075 3202 -196 -430 261 O
+ATOM 2263 NE2 GLN A 273 16.125 29.546 -5.950 1.00 23.28 N
+ANISOU 2263 NE2 GLN A 273 2929 2871 3048 -200 -483 211 N
+ATOM 2264 N ASN A 274 9.280 28.656 -5.133 1.00 20.29 N
+ANISOU 2264 N ASN A 274 2545 2516 2649 -75 -264 309 N
+ATOM 2265 CA ASN A 274 7.976 29.304 -5.249 1.00 21.83 C
+ANISOU 2265 CA ASN A 274 2714 2704 2878 -49 -218 371 C
+ATOM 2266 C ASN A 274 6.801 28.527 -4.690 1.00 22.69 C
+ANISOU 2266 C ASN A 274 2823 2817 2981 -20 -178 397 C
+ATOM 2267 O ASN A 274 5.697 29.063 -4.637 1.00 23.59 O
+ANISOU 2267 O ASN A 274 2916 2917 3129 10 -132 457 O
+ATOM 2268 CB ASN A 274 7.716 29.658 -6.695 1.00 23.76 C
+ANISOU 2268 CB ASN A 274 2879 2999 3149 -86 -232 426 C
+ATOM 2269 CG ASN A 274 8.780 30.577 -7.217 1.00 29.54 C
+ANISOU 2269 CG ASN A 274 3608 3720 3895 -106 -263 411 C
+ATOM 2270 OD1 ASN A 274 8.793 31.778 -6.927 1.00 32.28 O
+ANISOU 2270 OD1 ASN A 274 3974 4019 4271 -83 -247 422 O
+ATOM 2271 ND2 ASN A 274 9.721 30.023 -7.954 1.00 30.78 N
+ANISOU 2271 ND2 ASN A 274 3745 3917 4032 -146 -305 387 N
+ATOM 2272 N GLY A 275 7.023 27.287 -4.285 1.00 22.59 N
+ANISOU 2272 N GLY A 275 2828 2823 2932 -28 -193 359 N
+ATOM 2273 CA GLY A 275 5.948 26.444 -3.791 1.00 22.92 C
+ANISOU 2273 CA GLY A 275 2865 2874 2970 -5 -161 386 C
+ATOM 2274 C GLY A 275 5.080 25.943 -4.929 1.00 23.41 C
+ANISOU 2274 C GLY A 275 2849 2996 3049 -41 -171 452 C
+ATOM 2275 O GLY A 275 5.379 26.177 -6.111 1.00 23.66 O
+ANISOU 2275 O GLY A 275 2838 3064 3087 -85 -203 469 O
+ATOM 2276 N AMET A 276 3.995 25.255 -4.586 0.75 23.76 N
+ANISOU 2276 N AMET A 276 2877 3051 3100 -24 -146 494 N
+ATOM 2277 N BMET A 276 3.999 25.241 -4.587 0.25 23.17 N
+ANISOU 2277 N BMET A 276 2802 2977 3025 -25 -147 494 N
+ATOM 2278 CA AMET A 276 3.106 24.713 -5.607 0.75 24.64 C
+ANISOU 2278 CA AMET A 276 2918 3217 3226 -67 -165 565 C
+ATOM 2279 CA BMET A 276 3.087 24.717 -5.599 0.25 23.44 C
+ANISOU 2279 CA BMET A 276 2766 3065 3075 -66 -165 566 C
+ATOM 2280 C AMET A 276 1.887 25.618 -5.902 0.75 25.05 C
+ANISOU 2280 C AMET A 276 2913 3266 3338 -49 -128 668 C
+ATOM 2281 C BMET A 276 1.968 25.686 -5.984 0.25 24.43 C
+ANISOU 2281 C BMET A 276 2834 3188 3259 -52 -132 666 C
+ATOM 2282 O AMET A 276 1.113 25.299 -6.801 0.75 25.20 O
+ANISOU 2282 O AMET A 276 2868 3330 3374 -92 -151 741 O
+ATOM 2283 O BMET A 276 1.294 25.437 -6.974 0.25 24.50 O
+ANISOU 2283 O BMET A 276 2781 3245 3285 -99 -158 734 O
+ATOM 2284 CB AMET A 276 2.723 23.269 -5.272 0.75 25.92 C
+ANISOU 2284 CB AMET A 276 3085 3402 3362 -77 -176 558 C
+ATOM 2285 CB BMET A 276 2.506 23.358 -5.181 0.25 23.19 C
+ANISOU 2285 CB BMET A 276 2735 3053 3025 -70 -168 572 C
+ATOM 2286 CG AMET A 276 3.943 22.341 -5.362 0.75 28.07 C
+ANISOU 2286 CG AMET A 276 3395 3688 3581 -109 -218 471 C
+ATOM 2287 CG BMET A 276 3.463 22.203 -5.391 0.25 23.17 C
+ANISOU 2287 CG BMET A 276 2760 3074 2968 -110 -214 498 C
+ATOM 2288 SD AMET A 276 3.789 20.735 -4.570 0.75 35.78 S
+ANISOU 2288 SD AMET A 276 4400 4671 4525 -105 -223 438 S
+ATOM 2289 SD BMET A 276 2.590 20.634 -5.587 0.25 19.97 S
+ANISOU 2289 SD BMET A 276 2332 2709 2548 -145 -237 531 S
+ATOM 2290 CE AMET A 276 2.500 20.047 -5.545 0.75 30.19 C
+ANISOU 2290 CE AMET A 276 3629 4010 3831 -152 -244 528 C
+ATOM 2291 CE BMET A 276 3.918 19.512 -5.312 0.25 18.54 C
+ANISOU 2291 CE BMET A 276 2208 2526 2310 -159 -263 426 C
+ATOM 2292 N ASN A 277 1.774 26.783 -5.227 1.00 24.94 N
+ANISOU 2292 N ASN A 277 2923 3197 3354 8 -75 678 N
+ATOM 2293 CA ASN A 277 0.711 27.772 -5.473 1.00 25.60 C
+ANISOU 2293 CA ASN A 277 2954 3270 3503 34 -29 778 C
+ATOM 2294 C ASN A 277 -0.709 27.189 -5.412 1.00 25.41 C
+ANISOU 2294 C ASN A 277 2873 3268 3515 43 -4 878 C
+ATOM 2295 O ASN A 277 -1.567 27.570 -6.209 1.00 26.11 O
+ANISOU 2295 O ASN A 277 2883 3383 3654 22 -4 980 O
+ATOM 2296 CB ASN A 277 0.942 28.527 -6.787 1.00 27.55 C
+ANISOU 2296 CB ASN A 277 3146 3549 3771 -16 -66 811 C
+ATOM 2297 CG ASN A 277 2.030 29.565 -6.712 1.00 32.36 C
+ANISOU 2297 CG ASN A 277 3801 4120 4375 -4 -67 749 C
+ATOM 2298 OD1 ASN A 277 3.087 29.452 -7.353 1.00 34.44 O
+ANISOU 2298 OD1 ASN A 277 4070 4407 4607 -50 -120 694 O
+ATOM 2299 ND2 ASN A 277 1.795 30.607 -5.933 1.00 32.85 N
+ANISOU 2299 ND2 ASN A 277 3897 4116 4467 58 -5 760 N
+ATOM 2300 N GLY A 278 -0.939 26.258 -4.495 1.00 24.04 N
+ANISOU 2300 N GLY A 278 2732 3084 3318 70 13 856 N
+ATOM 2301 CA GLY A 278 -2.250 25.630 -4.362 1.00 23.26 C
+ANISOU 2301 CA GLY A 278 2576 3004 3255 80 34 955 C
+ATOM 2302 C GLY A 278 -2.558 24.555 -5.391 1.00 22.48 C
+ANISOU 2302 C GLY A 278 2420 2976 3147 -3 -42 992 C
+ATOM 2303 O GLY A 278 -3.689 24.070 -5.468 1.00 22.88 O
+ANISOU 2303 O GLY A 278 2411 3048 3234 -11 -39 1091 O
+ATOM 2304 N AARG A 279 -1.553 24.151 -6.167 0.50 21.95 N
+ANISOU 2304 N AARG A 279 2374 2940 3026 -66 -109 916 N
+ATOM 2305 N BARG A 279 -1.550 24.164 -6.183 0.50 21.71 N
+ANISOU 2305 N BARG A 279 2343 2909 2996 -67 -110 916 N
+ATOM 2306 CA AARG A 279 -1.722 23.116 -7.173 0.50 21.79 C
+ANISOU 2306 CA AARG A 279 2322 2977 2981 -149 -181 936 C
+ATOM 2307 CA BARG A 279 -1.691 23.135 -7.207 0.50 21.30 C
+ANISOU 2307 CA BARG A 279 2260 2915 2918 -151 -183 935 C
+ATOM 2308 C AARG A 279 -1.216 21.759 -6.668 0.50 21.02 C
+ANISOU 2308 C AARG A 279 2276 2883 2826 -159 -206 856 C
+ATOM 2309 C BARG A 279 -1.203 21.769 -6.683 0.50 20.81 C
+ANISOU 2309 C BARG A 279 2250 2857 2799 -160 -206 856 C
+ATOM 2310 O AARG A 279 -0.595 21.677 -5.602 0.50 20.83 O
+ANISOU 2310 O AARG A 279 2311 2822 2782 -106 -172 780 O
+ATOM 2311 O BARG A 279 -0.560 21.694 -5.629 0.50 20.66 O
+ANISOU 2311 O BARG A 279 2290 2801 2759 -107 -173 778 O
+ATOM 2312 CB AARG A 279 -1.035 23.533 -8.485 0.50 23.35 C
+ANISOU 2312 CB AARG A 279 2510 3206 3158 -214 -232 918 C
+ATOM 2313 CB BARG A 279 -0.911 23.540 -8.475 0.50 22.14 C
+ANISOU 2313 CB BARG A 279 2362 3051 2999 -213 -233 907 C
+ATOM 2314 CG AARG A 279 -1.623 24.814 -9.067 0.50 27.22 C
+ANISOU 2314 CG AARG A 279 2938 3698 3709 -211 -214 1010 C
+ATOM 2315 CG BARG A 279 -1.238 24.939 -9.002 0.50 24.89 C
+ANISOU 2315 CG BARG A 279 2661 3395 3403 -205 -212 976 C
+ATOM 2316 CD AARG A 279 -1.199 25.050 -10.505 0.50 31.04 C
+ANISOU 2316 CD AARG A 279 3399 4224 4173 -287 -273 1016 C
+ATOM 2317 CD BARG A 279 -0.110 25.483 -9.868 0.50 27.42 C
+ANISOU 2317 CD BARG A 279 2998 3726 3693 -240 -245 916 C
+ATOM 2318 NE AARG A 279 -1.606 23.954 -11.383 0.50 34.59 N
+ANISOU 2318 NE AARG A 279 3833 4723 4588 -371 -340 1049 N
+ATOM 2319 NE BARG A 279 -0.302 26.894 -10.206 0.50 30.09 N
+ANISOU 2319 NE BARG A 279 3295 4052 4085 -223 -219 973 N
+ATOM 2320 CZ AARG A 279 -2.790 23.867 -11.981 0.50 37.85 C
+ANISOU 2320 CZ AARG A 279 4179 5167 5037 -417 -368 1170 C
+ATOM 2321 CZ BARG A 279 0.680 27.785 -10.306 0.50 31.90 C
+ANISOU 2321 CZ BARG A 279 3550 4260 4310 -209 -213 917 C
+ATOM 2322 NH1AARG A 279 -3.697 24.824 -11.819 0.50 37.97 N
+ANISOU 2322 NH1AARG A 279 4125 5171 5131 -382 -327 1276 N
+ATOM 2323 NH1BARG A 279 1.940 27.424 -10.088 0.50 31.04 N
+ANISOU 2323 NH1BARG A 279 3504 4141 4149 -210 -232 809 N
+ATOM 2324 NH2AARG A 279 -3.068 22.834 -12.764 0.50 38.37 N
+ANISOU 2324 NH2AARG A 279 4248 5272 5060 -501 -437 1190 N
+ATOM 2325 NH2BARG A 279 0.413 29.041 -10.636 0.50 31.90 N
+ANISOU 2325 NH2BARG A 279 3509 4248 4364 -195 -189 976 N
+ATOM 2326 N THR A 280 -1.531 20.684 -7.398 1.00 20.29 N
+ANISOU 2326 N THR A 280 2166 2832 2709 -228 -264 879 N
+ATOM 2327 CA THR A 280 -1.107 19.344 -7.010 1.00 19.70 C
+ANISOU 2327 CA THR A 280 2139 2762 2585 -242 -287 810 C
+ATOM 2328 C THR A 280 -0.346 18.658 -8.148 1.00 18.60 C
+ANISOU 2328 C THR A 280 2026 2653 2386 -320 -349 758 C
+ATOM 2329 O THR A 280 -0.473 19.032 -9.320 1.00 18.37 O
+ANISOU 2329 O THR A 280 1972 2652 2356 -377 -384 798 O
+ATOM 2330 CB THR A 280 -2.305 18.475 -6.574 1.00 21.75 C
+ANISOU 2330 CB THR A 280 2364 3030 2869 -242 -288 887 C
+ATOM 2331 OG1 THR A 280 -3.207 18.341 -7.675 1.00 22.42 O
+ANISOU 2331 OG1 THR A 280 2391 3154 2973 -315 -340 988 O
+ATOM 2332 CG2 THR A 280 -3.016 19.017 -5.348 1.00 22.81 C
+ANISOU 2332 CG2 THR A 280 2482 3129 3057 -154 -213 936 C
+ATOM 2333 N ILE A 281 0.475 17.669 -7.786 1.00 17.32 N
+ANISOU 2333 N ILE A 281 1921 2483 2175 -321 -358 669 N
+ATOM 2334 CA ILE A 281 1.241 16.844 -8.713 1.00 17.17 C
+ANISOU 2334 CA ILE A 281 1942 2484 2097 -384 -402 613 C
+ATOM 2335 C ILE A 281 0.971 15.413 -8.307 1.00 17.06 C
+ANISOU 2335 C ILE A 281 1954 2471 2059 -398 -418 598 C
+ATOM 2336 O ILE A 281 1.194 15.057 -7.152 1.00 16.72 O
+ANISOU 2336 O ILE A 281 1929 2404 2021 -344 -387 558 O
+ATOM 2337 CB ILE A 281 2.749 17.150 -8.631 1.00 17.81 C
+ANISOU 2337 CB ILE A 281 2069 2547 2150 -359 -385 514 C
+ATOM 2338 CG1 ILE A 281 3.047 18.602 -9.014 1.00 18.05 C
+ANISOU 2338 CG1 ILE A 281 2075 2576 2209 -346 -371 531 C
+ATOM 2339 CG2 ILE A 281 3.527 16.160 -9.502 1.00 18.38 C
+ANISOU 2339 CG2 ILE A 281 2187 2634 2162 -414 -415 459 C
+ATOM 2340 CD1 ILE A 281 4.518 19.020 -8.861 1.00 18.34 C
+ANISOU 2340 CD1 ILE A 281 2148 2592 2228 -321 -358 447 C
+ATOM 2341 N LEU A 282 0.390 14.603 -9.206 1.00 17.24 N
+ANISOU 2341 N LEU A 282 1976 2518 2056 -474 -470 638 N
+ATOM 2342 CA LEU A 282 0.041 13.212 -8.889 1.00 17.35 C
+ANISOU 2342 CA LEU A 282 2014 2530 2048 -495 -492 632 C
+ATOM 2343 C LEU A 282 -0.763 13.066 -7.587 1.00 18.42 C
+ANISOU 2343 C LEU A 282 2114 2652 2233 -435 -461 674 C
+ATOM 2344 O LEU A 282 -0.449 12.228 -6.754 1.00 19.49 O
+ANISOU 2344 O LEU A 282 2279 2771 2354 -406 -446 622 O
+ATOM 2345 CB LEU A 282 1.267 12.292 -8.890 1.00 16.82 C
+ANISOU 2345 CB LEU A 282 2020 2448 1923 -498 -488 523 C
+ATOM 2346 CG LEU A 282 1.936 12.047 -10.240 1.00 17.52 C
+ANISOU 2346 CG LEU A 282 2157 2547 1952 -564 -518 488 C
+ATOM 2347 CD1 LEU A 282 3.136 11.159 -10.080 1.00 17.37 C
+ANISOU 2347 CD1 LEU A 282 2203 2506 1889 -551 -497 390 C
+ATOM 2348 CD2 LEU A 282 0.969 11.447 -11.235 1.00 18.50 C
+ANISOU 2348 CD2 LEU A 282 2288 2691 2051 -654 -580 555 C
+ATOM 2349 N GLY A 283 -1.725 13.970 -7.411 1.00 19.57 N
+ANISOU 2349 N GLY A 283 2195 2802 2437 -412 -443 767 N
+ATOM 2350 CA GLY A 283 -2.606 13.998 -6.248 1.00 20.20 C
+ANISOU 2350 CA GLY A 283 2237 2868 2570 -349 -402 826 C
+ATOM 2351 C GLY A 283 -1.975 14.425 -4.940 1.00 20.33 C
+ANISOU 2351 C GLY A 283 2283 2848 2593 -257 -334 759 C
+ATOM 2352 O GLY A 283 -2.567 14.232 -3.877 1.00 21.64 O
+ANISOU 2352 O GLY A 283 2436 2998 2788 -202 -296 791 O
+ATOM 2353 N ASER A 284 -0.758 14.973 -4.996 0.75 19.07 N
+ANISOU 2353 N ASER A 284 2168 2675 2403 -242 -321 668 N
+ATOM 2354 N BSER A 284 -0.757 14.979 -4.998 0.25 19.33 N
+ANISOU 2354 N BSER A 284 2200 2707 2436 -242 -321 669 N
+ATOM 2355 CA ASER A 284 -0.061 15.413 -3.798 0.75 18.29 C
+ANISOU 2355 CA ASER A 284 2108 2539 2303 -166 -269 603 C
+ATOM 2356 CA BSER A 284 -0.033 15.409 -3.809 0.25 18.82 C
+ANISOU 2356 CA BSER A 284 2176 2606 2369 -167 -270 601 C
+ATOM 2357 C ASER A 284 0.123 16.915 -3.823 0.75 18.11 C
+ANISOU 2357 C ASER A 284 2077 2497 2305 -132 -236 613 C
+ATOM 2358 C BSER A 284 0.197 16.911 -3.813 0.25 18.48 C
+ANISOU 2358 C BSER A 284 2128 2543 2350 -132 -236 607 C
+ATOM 2359 O ASER A 284 0.390 17.488 -4.872 0.75 17.64 O
+ANISOU 2359 O ASER A 284 2003 2455 2245 -173 -261 621 O
+ATOM 2360 O BSER A 284 0.554 17.481 -4.841 0.25 18.38 O
+ANISOU 2360 O BSER A 284 2104 2546 2333 -172 -261 607 O
+ATOM 2361 CB ASER A 284 1.311 14.752 -3.713 0.75 18.83 C
+ANISOU 2361 CB ASER A 284 2234 2600 2319 -177 -285 493 C
+ATOM 2362 CB BSER A 284 1.319 14.705 -3.725 0.25 19.61 C
+ANISOU 2362 CB BSER A 284 2334 2699 2416 -179 -287 492 C
+ATOM 2363 OG ASER A 284 2.022 15.192 -2.566 0.75 20.77 O
+ANISOU 2363 OG ASER A 284 2520 2810 2562 -114 -246 435 O
+ATOM 2364 OG BSER A 284 1.181 13.310 -3.519 0.25 21.27 O
+ANISOU 2364 OG BSER A 284 2558 2918 2605 -199 -308 477 O
+ATOM 2365 N ALA A 285 0.040 17.547 -2.650 1.00 18.03 N
+ANISOU 2365 N ALA A 285 2088 2447 2314 -58 -178 607 N
+ATOM 2366 CA ALA A 285 0.290 18.982 -2.522 1.00 18.74 C
+ANISOU 2366 CA ALA A 285 2189 2508 2425 -20 -141 606 C
+ATOM 2367 C ALA A 285 1.728 19.259 -1.985 1.00 18.86 C
+ANISOU 2367 C ALA A 285 2274 2492 2400 -3 -142 498 C
+ATOM 2368 O ALA A 285 2.067 20.400 -1.676 1.00 20.19 O
+ANISOU 2368 O ALA A 285 2469 2625 2578 30 -114 483 O
+ATOM 2369 CB ALA A 285 -0.755 19.620 -1.623 1.00 19.27 C
+ANISOU 2369 CB ALA A 285 2244 2542 2537 51 -71 676 C
+ATOM 2370 N LEU A 286 2.561 18.233 -1.874 1.00 17.88 N
+ANISOU 2370 N LEU A 286 2180 2377 2235 -26 -174 429 N
+ATOM 2371 CA LEU A 286 3.951 18.373 -1.497 1.00 18.08 C
+ANISOU 2371 CA LEU A 286 2259 2381 2229 -22 -186 342 C
+ATOM 2372 C LEU A 286 4.832 17.526 -2.431 1.00 17.12 C
+ANISOU 2372 C LEU A 286 2134 2293 2079 -80 -234 299 C
+ATOM 2373 O LEU A 286 4.316 16.735 -3.234 1.00 17.43 O
+ANISOU 2373 O LEU A 286 2143 2366 2113 -123 -257 329 O
+ATOM 2374 CB LEU A 286 4.191 18.099 -0.005 1.00 19.14 C
+ANISOU 2374 CB LEU A 286 2449 2477 2345 28 -159 300 C
+ATOM 2375 CG LEU A 286 3.662 16.806 0.562 1.00 21.28 C
+ANISOU 2375 CG LEU A 286 2717 2762 2607 35 -156 307 C
+ATOM 2376 CD1 LEU A 286 4.491 15.630 0.105 1.00 22.70 C
+ANISOU 2376 CD1 LEU A 286 2898 2969 2759 -12 -201 258 C
+ATOM 2377 CD2 LEU A 286 3.721 16.839 2.088 1.00 22.17 C
+ANISOU 2377 CD2 LEU A 286 2887 2833 2704 92 -120 279 C
+ATOM 2378 N LEU A 287 6.135 17.757 -2.402 1.00 15.55 N
+ANISOU 2378 N LEU A 287 1966 2080 1863 -85 -248 238 N
+ATOM 2379 CA LEU A 287 7.059 17.031 -3.258 1.00 15.39 C
+ANISOU 2379 CA LEU A 287 1945 2084 1818 -129 -280 201 C
+ATOM 2380 C LEU A 287 7.339 15.664 -2.641 1.00 15.22 C
+ANISOU 2380 C LEU A 287 1947 2063 1774 -127 -283 165 C
+ATOM 2381 O LEU A 287 7.958 15.571 -1.591 1.00 16.81 O
+ANISOU 2381 O LEU A 287 2180 2238 1970 -98 -277 127 O
+ATOM 2382 CB LEU A 287 8.323 17.863 -3.459 1.00 16.06 C
+ANISOU 2382 CB LEU A 287 2044 2153 1904 -131 -290 166 C
+ATOM 2383 CG LEU A 287 8.026 19.223 -4.104 1.00 18.18 C
+ANISOU 2383 CG LEU A 287 2287 2422 2198 -134 -287 204 C
+ATOM 2384 CD1 LEU A 287 9.204 20.138 -3.991 1.00 18.93 C
+ANISOU 2384 CD1 LEU A 287 2400 2492 2299 -128 -297 172 C
+ATOM 2385 CD2 LEU A 287 7.575 19.068 -5.566 1.00 19.33 C
+ANISOU 2385 CD2 LEU A 287 2392 2611 2341 -183 -304 244 C
+ATOM 2386 N AGLU A 288 6.855 14.602 -3.286 0.50 13.98 N
+ANISOU 2386 N AGLU A 288 1777 1933 1603 -162 -297 179 N
+ATOM 2387 N BGLU A 288 6.866 14.610 -3.293 0.50 14.00 N
+ANISOU 2387 N BGLU A 288 1778 1935 1605 -162 -297 179 N
+ATOM 2388 CA AGLU A 288 6.993 13.231 -2.776 0.50 13.48 C
+ANISOU 2388 CA AGLU A 288 1732 1869 1521 -162 -299 150 C
+ATOM 2389 CA BGLU A 288 6.991 13.233 -2.807 0.50 13.54 C
+ANISOU 2389 CA BGLU A 288 1739 1877 1528 -164 -299 151 C
+ATOM 2390 C AGLU A 288 8.376 12.638 -2.986 0.50 13.16 C
+ANISOU 2390 C AGLU A 288 1716 1824 1461 -175 -305 93 C
+ATOM 2391 C BGLU A 288 8.390 12.654 -2.992 0.50 13.22 C
+ANISOU 2391 C BGLU A 288 1723 1831 1468 -175 -305 93 C
+ATOM 2392 O AGLU A 288 8.883 12.653 -4.105 0.50 13.26 O
+ANISOU 2392 O AGLU A 288 1728 1850 1461 -209 -314 87 O
+ATOM 2393 O BGLU A 288 8.917 12.689 -4.102 0.50 13.37 O
+ANISOU 2393 O BGLU A 288 1742 1863 1476 -208 -314 86 O
+ATOM 2394 CB AGLU A 288 5.916 12.318 -3.382 0.50 14.44 C
+ANISOU 2394 CB AGLU A 288 1836 2015 1635 -199 -314 192 C
+ATOM 2395 CB BGLU A 288 5.938 12.358 -3.504 0.50 14.59 C
+ANISOU 2395 CB BGLU A 288 1855 2036 1653 -203 -316 192 C
+ATOM 2396 CG AGLU A 288 4.495 12.789 -3.115 0.50 16.46 C
+ANISOU 2396 CG AGLU A 288 2056 2277 1921 -185 -306 266 C
+ATOM 2397 CG BGLU A 288 6.026 10.881 -3.187 0.50 16.96 C
+ANISOU 2397 CG BGLU A 288 2176 2336 1934 -213 -322 166 C
+ATOM 2398 CD AGLU A 288 3.946 12.471 -1.736 0.50 20.85 C
+ANISOU 2398 CD AGLU A 288 2616 2815 2492 -134 -280 276 C
+ATOM 2399 CD BGLU A 288 5.638 10.508 -1.773 0.50 19.50 C
+ANISOU 2399 CD BGLU A 288 2499 2642 2269 -166 -304 167 C
+ATOM 2400 OE1AGLU A 288 4.624 11.747 -0.972 0.50 22.15 O
+ANISOU 2400 OE1AGLU A 288 2810 2966 2640 -115 -275 224 O
+ATOM 2401 OE1BGLU A 288 6.458 9.855 -1.089 0.50 16.00 O
+ANISOU 2401 OE1BGLU A 288 2080 2184 1815 -149 -297 118 O
+ATOM 2402 OE2AGLU A 288 2.824 12.931 -1.426 0.50 21.03 O
+ANISOU 2402 OE2AGLU A 288 2609 2838 2546 -111 -261 343 O
+ATOM 2403 OE2BGLU A 288 4.514 10.867 -1.350 0.50 22.07 O
+ANISOU 2403 OE2BGLU A 288 2800 2969 2618 -145 -293 222 O
+ATOM 2404 N ASP A 289 8.971 12.078 -1.927 1.00 12.93 N
+ANISOU 2404 N ASP A 289 1707 1775 1429 -148 -298 58 N
+ATOM 2405 CA ASP A 289 10.310 11.516 -2.024 1.00 12.60 C
+ANISOU 2405 CA ASP A 289 1681 1727 1380 -155 -300 16 C
+ATOM 2406 C ASP A 289 10.423 10.047 -1.666 1.00 13.43 C
+ANISOU 2406 C ASP A 289 1799 1831 1473 -156 -295 -4 C
+ATOM 2407 O ASP A 289 11.543 9.594 -1.414 1.00 13.88 O
+ANISOU 2407 O ASP A 289 1866 1876 1533 -150 -290 -33 O
+ATOM 2408 CB ASP A 289 11.323 12.330 -1.215 1.00 12.56 C
+ANISOU 2408 CB ASP A 289 1686 1696 1389 -129 -303 -4 C
+ATOM 2409 CG ASP A 289 11.288 12.143 0.274 1.00 14.92 C
+ANISOU 2409 CG ASP A 289 2007 1974 1689 -96 -302 -16 C
+ATOM 2410 OD1 ASP A 289 10.301 11.554 0.778 1.00 14.82 O
+ANISOU 2410 OD1 ASP A 289 1995 1965 1670 -83 -291 -4 O
+ATOM 2411 OD2 ASP A 289 12.243 12.583 0.934 1.00 15.48 O
+ANISOU 2411 OD2 ASP A 289 2094 2023 1766 -86 -313 -34 O
+ATOM 2412 N GLU A 290 9.296 9.306 -1.633 1.00 13.33 N
+ANISOU 2412 N GLU A 290 1783 1828 1452 -165 -297 17 N
+ATOM 2413 CA GLU A 290 9.409 7.892 -1.299 1.00 13.90 C
+ANISOU 2413 CA GLU A 290 1869 1897 1516 -168 -293 -2 C
+ATOM 2414 C GLU A 290 9.082 6.995 -2.504 1.00 14.27 C
+ANISOU 2414 C GLU A 290 1929 1955 1537 -215 -299 2 C
+ATOM 2415 O GLU A 290 8.544 5.902 -2.363 1.00 14.58 O
+ANISOU 2415 O GLU A 290 1977 1993 1568 -227 -304 5 O
+ATOM 2416 CB GLU A 290 8.658 7.524 -0.006 1.00 14.67 C
+ANISOU 2416 CB GLU A 290 1961 1989 1623 -136 -289 10 C
+ATOM 2417 CG GLU A 290 9.218 8.275 1.202 1.00 16.76 C
+ANISOU 2417 CG GLU A 290 2235 2234 1899 -94 -282 -5 C
+ATOM 2418 CD GLU A 290 8.875 7.717 2.576 1.00 18.56 C
+ANISOU 2418 CD GLU A 290 2471 2452 2128 -61 -274 -5 C
+ATOM 2419 OE1 GLU A 290 7.986 6.840 2.655 1.00 16.60 O
+ANISOU 2419 OE1 GLU A 290 2213 2215 1880 -64 -272 16 O
+ATOM 2420 OE2 GLU A 290 9.511 8.133 3.572 1.00 19.92 O
+ANISOU 2420 OE2 GLU A 290 2664 2605 2300 -35 -273 -23 O
+ATOM 2421 N PHE A 291 9.510 7.433 -3.696 1.00 13.63 N
+ANISOU 2421 N PHE A 291 1857 1881 1443 -244 -300 -1 N
+ATOM 2422 CA PHE A 291 9.546 6.589 -4.879 1.00 14.24 C
+ANISOU 2422 CA PHE A 291 1967 1958 1484 -288 -300 -10 C
+ATOM 2423 C PHE A 291 10.925 6.730 -5.436 1.00 14.69 C
+ANISOU 2423 C PHE A 291 2040 2004 1537 -282 -273 -41 C
+ATOM 2424 O PHE A 291 11.307 7.844 -5.781 1.00 15.37 O
+ANISOU 2424 O PHE A 291 2109 2098 1633 -278 -274 -32 O
+ATOM 2425 CB PHE A 291 8.614 7.038 -5.997 1.00 14.36 C
+ANISOU 2425 CB PHE A 291 1984 1994 1479 -337 -326 28 C
+ATOM 2426 CG PHE A 291 7.153 6.969 -5.703 1.00 15.75 C
+ANISOU 2426 CG PHE A 291 2136 2184 1665 -352 -355 79 C
+ATOM 2427 CD1 PHE A 291 6.458 5.787 -5.858 1.00 16.87 C
+ANISOU 2427 CD1 PHE A 291 2299 2323 1787 -387 -375 90 C
+ATOM 2428 CD2 PHE A 291 6.457 8.100 -5.333 1.00 17.27 C
+ANISOU 2428 CD2 PHE A 291 2284 2390 1890 -331 -361 122 C
+ATOM 2429 CE1 PHE A 291 5.089 5.746 -5.646 1.00 18.29 C
+ANISOU 2429 CE1 PHE A 291 2449 2518 1984 -404 -406 152 C
+ATOM 2430 CE2 PHE A 291 5.090 8.060 -5.145 1.00 18.48 C
+ANISOU 2430 CE2 PHE A 291 2408 2556 2059 -343 -383 184 C
+ATOM 2431 CZ PHE A 291 4.414 6.885 -5.307 1.00 18.11 C
+ANISOU 2431 CZ PHE A 291 2375 2511 1997 -380 -407 202 C
+ATOM 2432 N THR A 292 11.657 5.637 -5.560 1.00 14.58 N
+ANISOU 2432 N THR A 292 2058 1971 1510 -281 -247 -71 N
+ATOM 2433 CA THR A 292 12.980 5.663 -6.157 1.00 14.64 C
+ANISOU 2433 CA THR A 292 2080 1966 1518 -272 -211 -90 C
+ATOM 2434 C THR A 292 12.849 5.681 -7.683 1.00 14.39 C
+ANISOU 2434 C THR A 292 2090 1937 1441 -315 -204 -88 C
+ATOM 2435 O THR A 292 11.814 5.278 -8.228 1.00 14.19 O
+ANISOU 2435 O THR A 292 2094 1919 1380 -358 -229 -77 O
+ATOM 2436 CB THR A 292 13.753 4.380 -5.771 1.00 15.84 C
+ANISOU 2436 CB THR A 292 2254 2090 1675 -252 -175 -115 C
+ATOM 2437 OG1 THR A 292 13.148 3.243 -6.396 1.00 17.07 O
+ANISOU 2437 OG1 THR A 292 2463 2233 1789 -286 -170 -126 O
+ATOM 2438 CG2 THR A 292 13.836 4.168 -4.275 1.00 15.86 C
+ANISOU 2438 CG2 THR A 292 2222 2088 1715 -217 -184 -116 C
+ATOM 2439 N PRO A 293 13.938 5.984 -8.406 1.00 14.84 N
+ANISOU 2439 N PRO A 293 2156 1986 1496 -306 -169 -94 N
+ATOM 2440 CA PRO A 293 13.897 5.872 -9.875 1.00 14.67 C
+ANISOU 2440 CA PRO A 293 2189 1964 1422 -345 -154 -96 C
+ATOM 2441 C PRO A 293 13.499 4.455 -10.322 1.00 15.65 C
+ANISOU 2441 C PRO A 293 2387 2063 1496 -376 -141 -118 C
+ATOM 2442 O PRO A 293 12.761 4.300 -11.296 1.00 16.06 O
+ANISOU 2442 O PRO A 293 2490 2119 1493 -430 -162 -112 O
+ATOM 2443 CB PRO A 293 15.339 6.206 -10.275 1.00 15.78 C
+ANISOU 2443 CB PRO A 293 2324 2092 1581 -312 -103 -99 C
+ATOM 2444 CG PRO A 293 15.801 7.141 -9.190 1.00 16.06 C
+ANISOU 2444 CG PRO A 293 2285 2138 1679 -274 -122 -83 C
+ATOM 2445 CD PRO A 293 15.229 6.536 -7.942 1.00 14.54 C
+ANISOU 2445 CD PRO A 293 2079 1941 1504 -263 -145 -92 C
+ATOM 2446 N PHE A 294 13.961 3.420 -9.593 1.00 16.05 N
+ANISOU 2446 N PHE A 294 2447 2087 1564 -347 -111 -139 N
+ATOM 2447 CA APHE A 294 13.614 2.037 -9.947 0.60 17.63 C
+ANISOU 2447 CA APHE A 294 2722 2257 1719 -374 -97 -162 C
+ATOM 2448 CA BPHE A 294 13.625 2.042 -9.943 0.40 17.39 C
+ANISOU 2448 CA BPHE A 294 2692 2227 1690 -374 -96 -162 C
+ATOM 2449 C PHE A 294 12.129 1.806 -9.755 1.00 17.49 C
+ANISOU 2449 C PHE A 294 2707 2255 1683 -420 -162 -146 C
+ATOM 2450 O PHE A 294 11.509 1.147 -10.587 1.00 18.53 O
+ANISOU 2450 O PHE A 294 2910 2372 1757 -475 -177 -150 O
+ATOM 2451 CB APHE A 294 14.414 1.007 -9.126 0.60 18.71 C
+ANISOU 2451 CB APHE A 294 2858 2362 1888 -329 -50 -182 C
+ATOM 2452 CB BPHE A 294 14.457 1.057 -9.109 0.40 18.14 C
+ANISOU 2452 CB BPHE A 294 2783 2291 1819 -327 -49 -181 C
+ATOM 2453 CG APHE A 294 15.839 0.729 -9.559 0.60 20.73 C
+ANISOU 2453 CG APHE A 294 3135 2587 2155 -291 29 -192 C
+ATOM 2454 CG BPHE A 294 14.453 -0.377 -9.584 0.40 19.78 C
+ANISOU 2454 CG BPHE A 294 3077 2455 1983 -345 -13 -209 C
+ATOM 2455 CD1APHE A 294 16.370 1.325 -10.689 0.60 22.07 C
+ANISOU 2455 CD1APHE A 294 3332 2756 2298 -297 61 -187 C
+ATOM 2456 CD1BPHE A 294 14.237 -0.685 -10.916 0.40 21.21 C
+ANISOU 2456 CD1BPHE A 294 3351 2616 2092 -392 0 -222 C
+ATOM 2457 CD2APHE A 294 16.668 -0.076 -8.794 0.60 22.36 C
+ANISOU 2457 CD2APHE A 294 3325 2768 2404 -247 74 -197 C
+ATOM 2458 CD2BPHE A 294 14.733 -1.411 -8.711 0.40 21.02 C
+ANISOU 2458 CD2BPHE A 294 3229 2587 2170 -316 11 -221 C
+ATOM 2459 CE1APHE A 294 17.685 1.092 -11.061 0.60 23.04 C
+ANISOU 2459 CE1APHE A 294 3467 2849 2437 -255 141 -185 C
+ATOM 2460 CE1BPHE A 294 14.239 -2.002 -11.348 0.40 22.18 C
+ANISOU 2460 CE1BPHE A 294 3569 2690 2170 -411 34 -250 C
+ATOM 2461 CE2APHE A 294 17.988 -0.290 -9.162 0.60 23.26 C
+ANISOU 2461 CE2APHE A 294 3446 2853 2539 -207 151 -191 C
+ATOM 2462 CE2BPHE A 294 14.734 -2.729 -9.147 0.40 21.90 C
+ANISOU 2462 CE2BPHE A 294 3424 2652 2243 -331 47 -246 C
+ATOM 2463 CZ APHE A 294 18.485 0.292 -10.294 0.60 23.11 C
+ANISOU 2463 CZ APHE A 294 3455 2831 2493 -209 187 -184 C
+ATOM 2464 CZ BPHE A 294 14.485 -3.015 -10.461 0.40 21.80 C
+ANISOU 2464 CZ BPHE A 294 3512 2615 2156 -379 59 -263 C
+ATOM 2465 N ASP A 295 11.540 2.357 -8.678 1.00 16.66 N
+ANISOU 2465 N ASP A 295 2529 2177 1624 -401 -201 -122 N
+ATOM 2466 CA ASP A 295 10.103 2.218 -8.410 1.00 16.33 C
+ANISOU 2466 CA ASP A 295 2476 2153 1577 -437 -259 -92 C
+ATOM 2467 C ASP A 295 9.308 2.848 -9.537 1.00 17.17 C
+ANISOU 2467 C ASP A 295 2600 2280 1646 -496 -298 -60 C
+ATOM 2468 O ASP A 295 8.307 2.286 -9.970 1.00 18.29 O
+ANISOU 2468 O ASP A 295 2774 2420 1754 -553 -340 -39 O
+ATOM 2469 CB ASP A 295 9.693 2.913 -7.106 1.00 17.12 C
+ANISOU 2469 CB ASP A 295 2495 2275 1733 -396 -279 -67 C
+ATOM 2470 CG ASP A 295 10.224 2.304 -5.838 1.00 18.41 C
+ANISOU 2470 CG ASP A 295 2638 2425 1933 -346 -256 -88 C
+ATOM 2471 OD1 ASP A 295 10.556 1.095 -5.850 1.00 19.16 O
+ANISOU 2471 OD1 ASP A 295 2773 2493 2015 -349 -234 -113 O
+ATOM 2472 OD2 ASP A 295 10.319 3.037 -4.827 1.00 18.01 O
+ANISOU 2472 OD2 ASP A 295 2535 2386 1922 -306 -260 -78 O
+ATOM 2473 N VAL A 296 9.741 4.040 -9.998 1.00 16.16 N
+ANISOU 2473 N VAL A 296 2445 2169 1525 -487 -290 -51 N
+ATOM 2474 CA VAL A 296 9.047 4.738 -11.073 1.00 16.40 C
+ANISOU 2474 CA VAL A 296 2485 2222 1524 -542 -327 -16 C
+ATOM 2475 C VAL A 296 9.068 3.925 -12.358 1.00 18.06 C
+ANISOU 2475 C VAL A 296 2792 2410 1658 -602 -325 -33 C
+ATOM 2476 O VAL A 296 8.017 3.731 -12.959 1.00 19.14 O
+ANISOU 2476 O VAL A 296 2957 2555 1759 -670 -378 0 O
+ATOM 2477 CB VAL A 296 9.581 6.179 -11.258 1.00 16.18 C
+ANISOU 2477 CB VAL A 296 2406 2216 1524 -515 -316 -3 C
+ATOM 2478 CG1 VAL A 296 8.940 6.830 -12.468 1.00 16.59 C
+ANISOU 2478 CG1 VAL A 296 2471 2291 1541 -575 -351 35 C
+ATOM 2479 CG2 VAL A 296 9.293 7.003 -10.012 1.00 16.05 C
+ANISOU 2479 CG2 VAL A 296 2309 2216 1572 -468 -328 19 C
+ATOM 2480 N VAL A 297 10.238 3.395 -12.748 1.00 18.39 N
+ANISOU 2480 N VAL A 297 2892 2421 1676 -579 -263 -80 N
+ATOM 2481 CA VAL A 297 10.337 2.563 -13.952 1.00 19.89 C
+ANISOU 2481 CA VAL A 297 3194 2578 1784 -631 -248 -103 C
+ATOM 2482 C VAL A 297 9.473 1.298 -13.807 1.00 20.88 C
+ANISOU 2482 C VAL A 297 3375 2679 1878 -677 -283 -106 C
+ATOM 2483 O VAL A 297 8.737 0.942 -14.739 1.00 21.36 O
+ANISOU 2483 O VAL A 297 3512 2732 1873 -755 -325 -93 O
+ATOM 2484 CB VAL A 297 11.811 2.192 -14.251 1.00 21.55 C
+ANISOU 2484 CB VAL A 297 3451 2753 1985 -581 -158 -147 C
+ATOM 2485 CG1 VAL A 297 11.910 1.180 -15.391 1.00 22.49 C
+ANISOU 2485 CG1 VAL A 297 3705 2827 2015 -628 -129 -176 C
+ATOM 2486 CG2 VAL A 297 12.640 3.438 -14.563 1.00 22.68 C
+ANISOU 2486 CG2 VAL A 297 3543 2919 2157 -545 -128 -135 C
+ATOM 2487 N ARG A 298 9.549 0.644 -12.641 1.00 21.24 N
+ANISOU 2487 N ARG A 298 3385 2714 1970 -634 -271 -119 N
+ATOM 2488 CA ARG A 298 8.807 -0.585 -12.372 1.00 22.55 C
+ANISOU 2488 CA ARG A 298 3595 2855 2117 -670 -301 -122 C
+ATOM 2489 C ARG A 298 7.308 -0.361 -12.501 1.00 22.93 C
+ANISOU 2489 C ARG A 298 3621 2932 2158 -738 -391 -63 C
+ATOM 2490 O ARG A 298 6.636 -1.115 -13.208 1.00 22.97 O
+ANISOU 2490 O ARG A 298 3706 2916 2105 -814 -433 -54 O
+ATOM 2491 CB ARG A 298 9.156 -1.144 -10.976 1.00 25.03 C
+ANISOU 2491 CB ARG A 298 3855 3161 2494 -605 -274 -137 C
+ATOM 2492 CG ARG A 298 8.689 -2.583 -10.744 1.00 29.79 C
+ANISOU 2492 CG ARG A 298 4514 3728 3077 -632 -286 -150 C
+ATOM 2493 CD ARG A 298 8.979 -3.085 -9.331 1.00 34.67 C
+ANISOU 2493 CD ARG A 298 5071 4343 3760 -568 -263 -159 C
+ATOM 2494 NE ARG A 298 10.404 -3.075 -8.999 1.00 39.16 N
+ANISOU 2494 NE ARG A 298 5627 4894 4357 -499 -184 -195 N
+ATOM 2495 CZ ARG A 298 10.970 -2.244 -8.127 1.00 42.47 C
+ANISOU 2495 CZ ARG A 298 5959 5340 4836 -439 -169 -186 C
+ATOM 2496 NH1 ARG A 298 12.272 -2.306 -7.894 1.00 43.09 N
+ANISOU 2496 NH1 ARG A 298 6028 5401 4942 -386 -104 -208 N
+ATOM 2497 NH2 ARG A 298 10.237 -1.347 -7.482 1.00 42.21 N
+ANISOU 2497 NH2 ARG A 298 5851 5349 4837 -434 -218 -151 N
+ATOM 2498 N GLN A 299 6.784 0.674 -11.846 1.00 23.07 N
+ANISOU 2498 N GLN A 299 3535 2995 2235 -715 -421 -16 N
+ATOM 2499 CA GLN A 299 5.354 0.958 -11.884 1.00 23.81 C
+ANISOU 2499 CA GLN A 299 3590 3118 2339 -770 -499 56 C
+ATOM 2500 C GLN A 299 4.900 1.427 -13.238 1.00 25.68 C
+ANISOU 2500 C GLN A 299 3870 3366 2520 -848 -542 88 C
+ATOM 2501 O GLN A 299 3.853 0.988 -13.714 1.00 26.69 O
+ANISOU 2501 O GLN A 299 4029 3494 2619 -928 -611 134 O
+ATOM 2502 CB GLN A 299 4.957 1.970 -10.809 1.00 23.65 C
+ANISOU 2502 CB GLN A 299 3452 3136 2398 -713 -503 98 C
+ATOM 2503 CG GLN A 299 3.447 2.122 -10.708 1.00 23.14 C
+ANISOU 2503 CG GLN A 299 3338 3097 2356 -760 -573 184 C
+ATOM 2504 CD GLN A 299 2.957 2.977 -9.576 1.00 22.18 C
+ANISOU 2504 CD GLN A 299 3113 3003 2311 -699 -567 229 C
+ATOM 2505 OE1 GLN A 299 1.844 3.497 -9.627 1.00 22.38 O
+ANISOU 2505 OE1 GLN A 299 3085 3054 2364 -726 -610 310 O
+ATOM 2506 NE2 GLN A 299 3.758 3.156 -8.534 1.00 20.10 N
+ANISOU 2506 NE2 GLN A 299 2821 2734 2084 -618 -513 185 N
+ATOM 2507 N CYS A 300 5.691 2.286 -13.886 1.00 26.06 N
+ANISOU 2507 N CYS A 300 3924 3424 2554 -831 -507 68 N
+ATOM 2508 CA CYS A 300 5.337 2.786 -15.204 1.00 27.01 C
+ANISOU 2508 CA CYS A 300 4087 3556 2619 -905 -545 98 C
+ATOM 2509 C CYS A 300 5.445 1.714 -16.315 1.00 28.98 C
+ANISOU 2509 C CYS A 300 4480 3763 2769 -979 -552 65 C
+ATOM 2510 O CYS A 300 4.855 1.899 -17.375 1.00 29.26 O
+ANISOU 2510 O CYS A 300 4564 3806 2748 -1063 -607 101 O
+ATOM 2511 CB CYS A 300 6.127 4.045 -15.545 1.00 26.34 C
+ANISOU 2511 CB CYS A 300 3963 3494 2550 -864 -505 91 C
+ATOM 2512 SG CYS A 300 5.721 5.471 -14.500 1.00 27.90 S
+ANISOU 2512 SG CYS A 300 4013 3739 2849 -804 -515 145 S
+ATOM 2513 N SER A 301 6.132 0.583 -16.063 1.00 30.28 N
+ANISOU 2513 N SER A 301 4716 3880 2911 -951 -500 1 N
+ATOM 2514 CA SER A 301 6.245 -0.481 -17.069 1.00 32.04 C
+ANISOU 2514 CA SER A 301 5089 4050 3035 -1017 -498 -35 C
+ATOM 2515 C SER A 301 5.465 -1.768 -16.734 1.00 33.71 C
+ANISOU 2515 C SER A 301 5350 4229 3229 -1066 -546 -31 C
+ATOM 2516 O SER A 301 5.292 -2.617 -17.604 1.00 34.43 O
+ANISOU 2516 O SER A 301 5574 4275 3234 -1139 -565 -50 O
+ATOM 2517 CB SER A 301 7.705 -0.806 -17.369 1.00 33.84 C
+ANISOU 2517 CB SER A 301 5388 4236 3234 -957 -391 -109 C
+ATOM 2518 OG SER A 301 8.315 -1.500 -16.296 1.00 36.40 O
+ANISOU 2518 OG SER A 301 5687 4535 3609 -883 -335 -146 O
+ATOM 2519 N GLY A 302 5.019 -1.910 -15.491 1.00 34.12 N
+ANISOU 2519 N GLY A 302 5305 4300 3361 -1026 -563 -6 N
+ATOM 2520 CA GLY A 302 4.222 -3.058 -15.071 1.00 35.05 C
+ANISOU 2520 CA GLY A 302 5449 4392 3475 -1069 -613 10 C
+ATOM 2521 C GLY A 302 4.997 -4.334 -14.820 1.00 35.61 C
+ANISOU 2521 C GLY A 302 5606 4402 3523 -1038 -550 -62 C
+ATOM 2522 O GLY A 302 4.571 -5.413 -15.243 1.00 36.15 O
+ANISOU 2522 O GLY A 302 5777 4425 3534 -1106 -585 -70 O
+ATOM 2523 N VAL A 303 6.128 -4.228 -14.109 1.00 35.32 N
+ANISOU 2523 N VAL A 303 5526 4361 3534 -937 -459 -110 N
+ATOM 2524 CA VAL A 303 6.954 -5.389 -13.780 1.00 35.32 C
+ANISOU 2524 CA VAL A 303 5589 4304 3526 -896 -389 -171 C
+ATOM 2525 C VAL A 303 6.215 -6.275 -12.784 1.00 34.93 C
+ANISOU 2525 C VAL A 303 5504 4249 3518 -901 -431 -151 C
+ATOM 2526 O VAL A 303 5.658 -5.767 -11.815 1.00 34.71 O
+ANISOU 2526 O VAL A 303 5357 4270 3563 -873 -466 -105 O
+ATOM 2527 CB VAL A 303 8.320 -4.942 -13.211 1.00 36.13 C
+ANISOU 2527 CB VAL A 303 5633 4412 3684 -789 -291 -207 C
+ATOM 2528 CG1 VAL A 303 9.179 -6.136 -12.804 1.00 36.86 C
+ANISOU 2528 CG1 VAL A 303 5777 4448 3782 -742 -215 -257 C
+ATOM 2529 CG2 VAL A 303 9.059 -4.069 -14.209 1.00 36.62 C
+ANISOU 2529 CG2 VAL A 303 5724 4479 3709 -782 -248 -220 C
+ATOM 2530 N ATHR A 304 6.200 -7.599 -13.004 0.50 34.73 N
+ANISOU 2530 N ATHR A 304 5584 4163 3449 -934 -424 -183 N
+ATOM 2531 N BTHR A 304 6.201 -7.585 -13.044 0.50 34.72 N
+ANISOU 2531 N BTHR A 304 5585 4161 3445 -936 -424 -183 N
+ATOM 2532 CA ATHR A 304 5.514 -8.516 -12.093 0.50 34.97 C
+ANISOU 2532 CA ATHR A 304 5583 4185 3519 -940 -464 -162 C
+ATOM 2533 CA BTHR A 304 5.553 -8.566 -12.184 0.50 34.96 C
+ANISOU 2533 CA BTHR A 304 5595 4178 3510 -944 -461 -167 C
+ATOM 2534 C ATHR A 304 6.476 -9.352 -11.246 0.50 35.09 C
+ANISOU 2534 C ATHR A 304 5592 4165 3575 -859 -379 -212 C
+ATOM 2535 C BTHR A 304 6.556 -9.620 -11.706 0.50 35.18 C
+ANISOU 2535 C BTHR A 304 5665 4152 3551 -881 -372 -228 C
+ATOM 2536 O ATHR A 304 6.038 -10.116 -10.384 0.50 34.91 O
+ANISOU 2536 O ATHR A 304 5537 4136 3592 -853 -403 -199 O
+ATOM 2537 O BTHR A 304 7.751 -9.347 -11.597 0.50 35.09 O
+ANISOU 2537 O BTHR A 304 5641 4134 3558 -806 -281 -266 O
+ATOM 2538 CB ATHR A 304 4.532 -9.384 -12.868 0.50 36.14 C
+ANISOU 2538 CB ATHR A 304 5841 4294 3596 -1053 -545 -143 C
+ATOM 2539 CB BTHR A 304 4.394 -9.205 -12.939 0.50 35.98 C
+ANISOU 2539 CB BTHR A 304 5814 4283 3575 -1062 -558 -133 C
+ATOM 2540 OG1ATHR A 304 5.255 -10.142 -13.839 0.50 37.13 O
+ANISOU 2540 OG1ATHR A 304 6127 4346 3633 -1078 -490 -209 O
+ATOM 2541 OG1BTHR A 304 4.903 -9.804 -14.134 0.50 36.92 O
+ANISOU 2541 OG1BTHR A 304 6100 4336 3593 -1110 -526 -187 O
+ATOM 2542 CG2ATHR A 304 3.471 -8.559 -13.555 0.50 36.53 C
+ANISOU 2542 CG2ATHR A 304 5871 4386 3622 -1137 -643 -73 C
+ATOM 2543 CG2BTHR A 304 3.329 -8.196 -13.297 0.50 36.25 C
+ANISOU 2543 CG2BTHR A 304 5784 4376 3615 -1123 -651 -54 C
+TER 2544 THR A 304
+HETATM 2545 S DMS A 401 6.882 -28.125 21.472 1.00 20.06 S
+ANISOU 2545 S DMS A 401 2030 2530 3059 142 -223 422 S
+HETATM 2546 O DMS A 401 7.674 -27.206 22.316 1.00 20.48 O
+ANISOU 2546 O DMS A 401 2067 2623 3090 170 -213 422 O
+HETATM 2547 C1 DMS A 401 5.955 -27.138 20.370 1.00 19.79 C
+ANISOU 2547 C1 DMS A 401 2054 2497 2971 117 -247 398 C
+HETATM 2548 C2 DMS A 401 5.581 -28.752 22.497 1.00 19.86 C
+ANISOU 2548 C2 DMS A 401 1948 2540 3057 159 -255 493 C
+HETATM 2549 S DMS A 402 7.044 -21.256 28.847 1.00 48.64 S
+ANISOU 2549 S DMS A 402 5726 6429 6328 331 -250 516 S
+HETATM 2550 O DMS A 402 6.922 -22.717 28.688 1.00 48.54 O
+ANISOU 2550 O DMS A 402 5645 6411 6389 324 -251 544 O
+HETATM 2551 C1 DMS A 402 5.390 -20.729 29.206 1.00 48.61 C
+ANISOU 2551 C1 DMS A 402 5741 6444 6284 381 -224 551 C
+HETATM 2552 C2 DMS A 402 7.732 -21.050 30.463 1.00 48.75 C
+ANISOU 2552 C2 DMS A 402 5761 6466 6296 338 -265 540 C
+HETATM 2553 S DMS A 403 6.261 -1.076 -6.323 1.00 29.95 S
+ANISOU 2553 S DMS A 403 4191 3868 3321 -512 -390 -11 S
+HETATM 2554 O DMS A 403 5.958 -2.533 -6.360 1.00 30.71 O
+ANISOU 2554 O DMS A 403 4341 3934 3396 -547 -404 -21 O
+HETATM 2555 C1 DMS A 403 7.022 -0.725 -7.858 1.00 30.37 C
+ANISOU 2555 C1 DMS A 403 4314 3907 3317 -546 -369 -43 C
+HETATM 2556 C2 DMS A 403 7.596 -0.894 -5.175 1.00 30.14 C
+ANISOU 2556 C2 DMS A 403 4176 3886 3391 -424 -329 -54 C
+HETATM 2557 S DMS A 404 2.371 -18.855 7.984 1.00 36.23 S
+ANISOU 2557 S DMS A 404 4677 4488 4601 -274 -432 179 S
+HETATM 2558 O DMS A 404 1.975 -20.201 7.546 1.00 36.88 O
+ANISOU 2558 O DMS A 404 4800 4523 4688 -326 -462 186 O
+HETATM 2559 C1 DMS A 404 3.628 -19.160 9.196 1.00 36.02 C
+ANISOU 2559 C1 DMS A 404 4613 4467 4607 -200 -367 144 C
+HETATM 2560 C2 DMS A 404 1.058 -18.333 9.062 1.00 36.25 C
+ANISOU 2560 C2 DMS A 404 4585 4549 4639 -243 -465 272 C
+HETATM 2561 O HOH A 501 16.168 1.473 -5.859 1.00 46.52 O
+HETATM 2562 O HOH A 502 14.078 -19.491 32.277 1.00 41.46 O
+HETATM 2563 O HOH A 503 6.880 13.380 21.324 1.00 29.25 O
+HETATM 2564 O HOH A 504 13.998 -10.881 31.006 1.00 35.36 O
+HETATM 2565 O HOH A 505 -0.912 17.057 -19.539 1.00 38.93 O
+HETATM 2566 O HOH A 506 -3.061 10.895 -16.794 1.00 40.86 O
+HETATM 2567 O HOH A 507 6.044 5.803 1.306 1.00 24.97 O
+HETATM 2568 O HOH A 508 2.799 4.893 20.226 1.00 34.61 O
+HETATM 2569 O HOH A 509 24.406 -5.758 8.993 1.00 17.99 O
+HETATM 2570 O HOH A 510 21.426 -20.287 30.771 1.00 23.30 O
+HETATM 2571 O HOH A 511 11.397 31.677 -2.156 1.00 25.90 O
+HETATM 2572 O HOH A 512 12.195 -27.051 22.943 1.00 19.83 O
+HETATM 2573 O HOH A 513 19.756 10.134 -2.112 1.00 30.96 O
+HETATM 2574 O HOH A 514 5.478 -17.689 1.918 1.00 19.67 O
+HETATM 2575 O HOH A 515 8.621 24.377 -11.854 1.00 26.34 O
+HETATM 2576 O HOH A 516 0.090 -17.755 15.613 1.00 35.61 O
+HETATM 2577 O HOH A 517 9.022 -26.606 14.754 1.00 40.22 O
+HETATM 2578 O HOH A 518 9.601 -23.263 23.053 1.00 21.34 O
+HETATM 2579 O HOH A 519 7.168 -26.153 0.208 1.00 33.81 O
+HETATM 2580 O HOH A 520 16.939 -5.562 33.520 1.00 37.83 O
+HETATM 2581 O HOH A 521 8.175 -31.641 17.026 1.00 31.45 O
+HETATM 2582 O HOH A 522 20.485 8.740 25.153 1.00 39.46 O
+HETATM 2583 O HOH A 523 6.032 -8.497 8.633 1.00 14.96 O
+HETATM 2584 O HOH A 524 13.232 10.946 19.529 1.00 48.19 O
+HETATM 2585 O HOH A 525 3.638 22.182 -0.621 1.00 34.15 O
+HETATM 2586 O HOH A 526 6.136 4.320 21.727 1.00 40.25 O
+HETATM 2587 O HOH A 527 24.549 4.929 18.980 1.00 27.73 O
+HETATM 2588 O HOH A 528 21.248 -12.985 34.361 1.00 37.99 O
+HETATM 2589 O HOH A 529 4.472 26.774 -8.479 1.00 30.69 O
+HETATM 2590 O HOH A 530 16.252 12.230 7.025 1.00 30.97 O
+HETATM 2591 O HOH A 531 6.267 8.345 11.973 1.00 33.79 O
+HETATM 2592 O HOH A 532 14.837 -9.578 -4.136 1.00 34.69 O
+HETATM 2593 O HOH A 533 23.775 -14.714 27.189 1.00 19.51 O
+HETATM 2594 O HOH A 534 12.117 31.027 -8.579 1.00 28.22 O
+HETATM 2595 O HOH A 535 10.798 -24.784 2.844 1.00 18.90 O
+HETATM 2596 O HOH A 536 18.416 -28.970 20.813 1.00 44.66 O
+HETATM 2597 O HOH A 537 13.207 23.157 -18.628 1.00 23.28 O
+HETATM 2598 O HOH A 538 1.305 22.918 -1.525 1.00 39.57 O
+HETATM 2599 O HOH A 539 13.733 -16.538 32.742 1.00 42.72 O
+HETATM 2600 O HOH A 540 20.769 -13.106 10.684 1.00 24.31 O
+HETATM 2601 O HOH A 541 8.621 5.486 22.418 1.00 37.97 O
+HETATM 2602 O HOH A 542 19.369 9.113 0.911 0.50 21.92 O
+HETATM 2603 O HOH A 543 20.059 10.278 15.617 1.00 20.33 O
+HETATM 2604 O HOH A 544 13.595 0.797 -5.476 1.00 24.59 O
+HETATM 2605 O HOH A 545 15.233 18.533 -21.978 1.00 20.38 O
+HETATM 2606 O HOH A 546 4.305 7.616 10.196 1.00 32.91 O
+HETATM 2607 O HOH A 547 28.704 8.986 -11.711 1.00 37.15 O
+HETATM 2608 O HOH A 548 20.309 -18.432 26.843 1.00 19.13 O
+HETATM 2609 O HOH A 549 -0.916 1.911 13.421 1.00 31.81 O
+HETATM 2610 O HOH A 550 22.855 27.060 -0.065 1.00 31.20 O
+HETATM 2611 O HOH A 551 14.655 26.081 4.261 1.00 21.96 O
+HETATM 2612 O HOH A 552 3.751 4.190 -18.169 1.00 34.28 O
+HETATM 2613 O HOH A 553 13.326 -24.508 3.825 1.00 22.78 O
+HETATM 2614 O HOH A 554 27.169 26.220 -11.432 1.00 21.90 O
+HETATM 2615 O HOH A 555 9.882 19.723 -0.456 1.00 21.00 O
+HETATM 2616 O HOH A 556 -3.265 28.392 -8.099 1.00 21.52 O
+HETATM 2617 O HOH A 557 20.738 21.420 4.165 1.00 27.07 O
+HETATM 2618 O HOH A 558 6.867 -23.050 20.986 1.00 15.42 O
+HETATM 2619 O HOH A 559 8.877 28.045 -1.387 1.00 22.94 O
+HETATM 2620 O HOH A 560 0.113 -1.132 12.039 1.00 27.87 O
+HETATM 2621 O HOH A 561 2.365 -8.994 18.707 1.00 22.91 O
+HETATM 2622 O HOH A 562 4.775 24.485 -18.488 1.00 38.08 O
+HETATM 2623 O HOH A 563 11.512 21.778 -17.020 1.00 21.35 O
+HETATM 2624 O HOH A 564 -1.260 -19.317 22.131 1.00 37.41 O
+HETATM 2625 O HOH A 565 23.016 1.706 15.920 1.00 19.55 O
+HETATM 2626 O HOH A 566 22.194 19.573 0.676 1.00 26.37 O
+HETATM 2627 O HOH A 567 8.161 -17.907 28.320 1.00 34.19 O
+HETATM 2628 O HOH A 568 7.958 3.525 -3.456 1.00 17.12 O
+HETATM 2629 O HOH A 569 15.855 -27.834 12.287 1.00 23.48 O
+HETATM 2630 O HOH A 570 16.709 28.254 -20.308 1.00 19.84 O
+HETATM 2631 O HOH A 571 8.450 15.959 1.017 1.00 29.83 O
+HETATM 2632 O HOH A 572 9.777 6.249 5.698 1.00 15.43 O
+HETATM 2633 O HOH A 573 17.679 -25.053 30.209 1.00 30.30 O
+HETATM 2634 O HOH A 574 -5.912 -4.357 9.377 1.00 39.55 O
+HETATM 2635 O HOH A 575 25.363 9.442 -4.945 1.00 28.46 O
+HETATM 2636 O HOH A 576 16.878 6.559 -3.938 1.00 17.95 O
+HETATM 2637 O HOH A 577 12.105 -32.691 16.980 1.00 31.58 O
+HETATM 2638 O HOH A 578 12.237 21.928 2.499 1.00 20.92 O
+HETATM 2639 O HOH A 579 9.918 -25.725 22.117 1.00 14.76 O
+HETATM 2640 O HOH A 580 21.216 28.768 -6.698 1.00 41.88 O
+HETATM 2641 O HOH A 581 10.267 17.926 1.520 1.00 26.08 O
+HETATM 2642 O HOH A 582 24.873 29.260 -8.891 1.00 23.50 O
+HETATM 2643 O HOH A 583 18.869 10.206 13.140 1.00 19.66 O
+HETATM 2644 O HOH A 584 -1.740 -15.236 2.695 1.00 33.35 O
+HETATM 2645 O HOH A 585 10.507 -0.544 -3.024 1.00 21.42 O
+HETATM 2646 O HOH A 586 23.489 22.748 -17.286 1.00 16.05 O
+HETATM 2647 O HOH A 587 13.322 21.382 -20.851 1.00 26.01 O
+HETATM 2648 O HOH A 588 18.541 -8.076 -3.408 1.00 40.63 O
+HETATM 2649 O HOH A 589 8.071 3.586 30.056 1.00 37.79 O
+HETATM 2650 O HOH A 590 -1.477 3.593 -1.801 1.00 42.67 O
+HETATM 2651 O HOH A 591 3.602 22.218 -19.191 1.00 32.60 O
+HETATM 2652 O HOH A 592 9.993 -17.767 -3.963 1.00 21.80 O
+HETATM 2653 O HOH A 593 22.259 16.293 3.670 1.00 37.29 O
+HETATM 2654 O HOH A 594 10.599 32.889 -5.240 1.00 50.44 O
+HETATM 2655 O HOH A 595 13.521 12.427 17.221 1.00 36.62 O
+HETATM 2656 O HOH A 596 -3.864 -12.103 2.544 1.00 20.32 O
+HETATM 2657 O HOH A 597 26.359 -5.686 17.729 1.00 34.04 O
+HETATM 2658 O HOH A 598 0.896 -16.433 2.082 1.00 39.32 O
+HETATM 2659 O HOH A 599 28.921 9.379 -15.273 1.00 32.13 O
+HETATM 2660 O HOH A 600 24.011 13.123 -1.655 1.00 31.18 O
+HETATM 2661 O HOH A 601 21.433 21.717 -18.735 1.00 17.60 O
+HETATM 2662 O HOH A 602 1.773 1.863 0.024 1.00 26.63 O
+HETATM 2663 O HOH A 603 7.494 -28.340 15.770 1.00 33.19 O
+HETATM 2664 O HOH A 604 15.633 -5.640 20.179 1.00 12.60 O
+HETATM 2665 O HOH A 605 22.115 9.845 5.153 1.00 29.86 O
+HETATM 2666 O HOH A 606 24.327 -8.927 20.642 1.00 20.53 O
+HETATM 2667 O HOH A 607 16.826 -18.849 7.693 1.00 18.59 O
+HETATM 2668 O HOH A 608 28.679 18.724 -8.356 1.00 35.42 O
+HETATM 2669 O HOH A 609 24.424 -0.652 12.999 1.00 27.63 O
+HETATM 2670 O HOH A 610 -0.724 22.828 -3.129 1.00 39.81 O
+HETATM 2671 O HOH A 611 19.959 5.204 -1.851 1.00 27.89 O
+HETATM 2672 O HOH A 612 15.062 26.996 -12.204 1.00 18.02 O
+HETATM 2673 O HOH A 613 8.199 -28.395 6.565 1.00 25.90 O
+HETATM 2674 O HOH A 614 7.788 -24.522 25.639 1.00 18.95 O
+HETATM 2675 O HOH A 615 10.042 -5.817 25.008 1.00 36.65 O
+HETATM 2676 O HOH A 616 22.116 2.055 5.700 1.00 36.41 O
+HETATM 2677 O HOH A 617 3.693 -17.399 20.860 1.00 18.97 O
+HETATM 2678 O HOH A 618 26.732 23.577 -4.772 1.00 19.11 O
+HETATM 2679 O HOH A 619 9.585 10.091 -4.896 1.00 12.16 O
+HETATM 2680 O HOH A 620 1.295 -21.833 9.645 1.00 55.13 O
+HETATM 2681 O HOH A 621 22.839 -7.292 34.441 1.00 27.63 O
+HETATM 2682 O HOH A 622 18.961 -27.689 9.426 1.00 43.04 O
+HETATM 2683 O HOH A 623 21.521 10.599 -17.013 1.00 25.46 O
+HETATM 2684 O HOH A 624 13.990 14.918 12.502 1.00 32.85 O
+HETATM 2685 O HOH A 625 1.918 -11.990 25.974 1.00 35.35 O
+HETATM 2686 O HOH A 626 -4.038 -9.431 16.969 1.00 48.81 O
+HETATM 2687 O HOH A 627 13.366 19.059 3.371 1.00 28.20 O
+HETATM 2688 O HOH A 628 24.678 1.909 12.377 1.00 46.47 O
+HETATM 2689 O HOH A 629 14.580 -25.790 26.928 1.00 17.27 O
+HETATM 2690 O HOH A 630 15.757 -12.840 31.816 1.00 22.74 O
+HETATM 2691 O HOH A 631 14.529 -20.206 0.077 1.00 29.75 O
+HETATM 2692 O HOH A 632 10.744 -23.544 0.343 1.00 18.47 O
+HETATM 2693 O HOH A 633 2.570 13.675 -20.732 1.00 43.65 O
+HETATM 2694 O HOH A 634 5.372 -6.477 21.881 1.00 27.60 O
+HETATM 2695 O HOH A 635 3.140 9.142 -21.338 1.00 30.01 O
+HETATM 2696 O HOH A 636 19.977 -21.182 28.743 1.00 32.10 O
+HETATM 2697 O HOH A 637 7.570 12.013 0.722 1.00 33.53 O
+HETATM 2698 O HOH A 638 12.447 11.173 10.477 1.00 26.80 O
+HETATM 2699 O HOH A 639 15.757 6.369 -14.440 1.00 24.76 O
+HETATM 2700 O HOH A 640 17.547 27.500 -12.889 1.00 19.19 O
+HETATM 2701 O HOH A 641 5.057 -17.229 28.359 1.00 47.39 O
+HETATM 2702 O HOH A 642 -2.486 12.802 -14.220 1.00 42.13 O
+HETATM 2703 O HOH A 643 -4.994 23.645 -3.052 1.00 32.21 O
+HETATM 2704 O HOH A 644 -0.389 -15.332 10.266 1.00 36.06 O
+HETATM 2705 O HOH A 645 5.665 2.461 -4.750 1.00 17.90 O
+HETATM 2706 O HOH A 646 5.266 -27.778 14.491 1.00 36.75 O
+HETATM 2707 O HOH A 647 2.594 25.678 -16.824 1.00 30.95 O
+HETATM 2708 O HOH A 648 22.547 8.950 -2.317 1.00 43.74 O
+HETATM 2709 O HOH A 649 15.056 -5.071 0.319 1.00 20.13 O
+HETATM 2710 O HOH A 650 18.804 -7.696 6.107 1.00 16.54 O
+HETATM 2711 O HOH A 651 6.258 2.386 -7.542 1.00 22.14 O
+HETATM 2712 O HOH A 652 25.440 -15.867 12.089 1.00 45.56 O
+HETATM 2713 O HOH A 653 13.858 31.054 -2.000 1.00 31.40 O
+HETATM 2714 O HOH A 654 3.992 -22.184 7.072 1.00 17.77 O
+HETATM 2715 O HOH A 655 16.781 4.789 30.472 1.00 57.67 O
+HETATM 2716 O HOH A 656 14.653 -22.055 31.952 1.00 32.65 O
+HETATM 2717 O HOH A 657 13.879 4.396 -20.671 1.00 28.86 O
+HETATM 2718 O HOH A 658 27.708 -4.709 14.373 1.00 45.60 O
+HETATM 2719 O HOH A 659 -2.375 19.163 -11.398 1.00 31.14 O
+HETATM 2720 O HOH A 660 9.946 -10.999 28.175 1.00 34.34 O
+HETATM 2721 O HOH A 661 16.584 2.526 12.374 1.00 14.44 O
+HETATM 2722 O HOH A 662 7.870 23.887 -2.281 1.00 26.01 O
+HETATM 2723 O HOH A 663 15.076 11.269 -25.013 1.00 30.97 O
+HETATM 2724 O HOH A 664 12.776 -3.174 -5.257 1.00 33.42 O
+HETATM 2725 O HOH A 665 17.673 16.856 14.835 1.00 35.96 O
+HETATM 2726 O HOH A 666 -5.618 24.316 -7.513 1.00 20.87 O
+HETATM 2727 O HOH A 667 29.467 15.778 -12.676 1.00 32.03 O
+HETATM 2728 O HOH A 668 -2.615 16.225 -9.453 1.00 26.89 O
+HETATM 2729 O HOH A 669 20.970 6.298 19.867 1.00 27.96 O
+HETATM 2730 O HOH A 670 22.051 -18.298 38.812 1.00 31.27 O
+HETATM 2731 O HOH A 671 22.550 7.382 -17.399 1.00 24.21 O
+HETATM 2732 O HOH A 672 20.505 18.890 3.164 1.00 33.29 O
+HETATM 2733 O HOH A 673 21.340 -1.629 20.448 1.00 16.34 O
+HETATM 2734 O HOH A 674 -0.741 -15.736 14.250 1.00 30.76 O
+HETATM 2735 O HOH A 675 23.323 20.417 -1.600 1.00 29.58 O
+HETATM 2736 O HOH A 676 1.456 8.663 -6.092 1.00 38.82 O
+HETATM 2737 O HOH A 677 17.887 4.741 -6.103 1.00 34.71 O
+HETATM 2738 O HOH A 678 14.269 5.280 22.766 1.00 24.58 O
+HETATM 2739 O HOH A 679 27.355 20.815 -5.391 1.00 24.25 O
+HETATM 2740 O HOH A 680 9.720 -1.209 21.229 1.00 30.93 O
+HETATM 2741 O HOH A 681 2.024 11.322 -5.624 1.00 22.74 O
+HETATM 2742 O HOH A 682 9.861 24.688 -0.545 1.00 22.75 O
+HETATM 2743 O HOH A 683 20.486 -1.656 24.001 1.00 24.64 O
+HETATM 2744 O HOH A 684 23.225 2.694 9.309 1.00 22.82 O
+HETATM 2745 O HOH A 685 27.418 16.923 -6.933 1.00 31.40 O
+HETATM 2746 O HOH A 686 16.157 -27.895 23.992 1.00 21.03 O
+HETATM 2747 O HOH A 687 18.371 -16.308 -2.702 1.00 39.26 O
+HETATM 2748 O HOH A 688 25.461 -11.702 20.577 1.00 40.43 O
+HETATM 2749 O HOH A 689 22.395 -0.560 18.161 1.00 15.98 O
+HETATM 2750 O HOH A 690 11.106 -22.190 32.650 1.00 28.72 O
+HETATM 2751 O HOH A 691 13.906 15.879 -26.087 1.00 40.25 O
+HETATM 2752 O HOH A 692 3.233 28.434 -3.275 1.00 28.74 O
+HETATM 2753 O HOH A 693 22.874 -2.369 16.096 1.00 16.71 O
+HETATM 2754 O HOH A 694 5.924 -4.719 19.944 1.00 29.98 O
+HETATM 2755 O HOH A 695 13.872 17.335 10.417 1.00 36.01 O
+HETATM 2756 O HOH A 696 -3.730 23.139 -15.560 1.00 97.94 O
+HETATM 2757 O HOH A 697 8.299 -10.717 30.288 1.00 47.50 O
+HETATM 2758 O HOH A 698 21.543 -1.801 26.438 1.00 47.98 O
+HETATM 2759 O HOH A 699 18.028 -23.973 26.108 1.00 19.47 O
+HETATM 2760 O HOH A 700 12.908 18.528 -23.180 1.00 41.68 O
+HETATM 2761 O HOH A 701 2.949 30.284 -11.274 1.00 37.62 O
+HETATM 2762 O HOH A 702 20.081 -20.090 16.613 1.00 22.76 O
+HETATM 2763 O HOH A 703 18.378 30.888 -7.178 1.00 34.12 O
+HETATM 2764 O HOH A 704 5.351 -31.635 18.500 1.00 40.71 O
+HETATM 2765 O HOH A 705 0.701 25.514 -2.225 1.00 36.15 O
+HETATM 2766 O HOH A 706 25.191 16.426 -14.367 1.00 24.82 O
+HETATM 2767 O HOH A 707 21.234 -13.358 2.280 1.00 27.41 O
+HETATM 2768 O HOH A 708 7.239 19.679 -0.526 1.00 19.53 O
+HETATM 2769 O HOH A 709 26.231 -10.821 18.148 1.00 29.32 O
+HETATM 2770 O HOH A 710 18.272 24.759 5.918 1.00 42.75 O
+HETATM 2771 O HOH A 711 23.954 -16.170 21.645 1.00 23.30 O
+HETATM 2772 O HOH A 712 10.555 -16.892 30.368 1.00 33.54 O
+HETATM 2773 O HOH A 713 -3.214 21.063 -9.741 1.00 34.02 O
+HETATM 2774 O HOH A 714 -2.136 9.260 -10.450 1.00 40.46 O
+HETATM 2775 O HOH A 715 11.910 -29.685 8.498 1.00 34.74 O
+HETATM 2776 O HOH A 716 1.343 -16.891 12.512 1.00 27.31 O
+HETATM 2777 O HOH A 717 13.914 19.690 7.284 1.00 37.82 O
+HETATM 2778 O HOH A 718 -0.234 16.076 -0.146 0.50 11.47 O
+HETATM 2779 O HOH A 719 24.548 -7.687 26.198 1.00 36.32 O
+HETATM 2780 O HOH A 720 18.171 27.334 4.952 1.00 53.03 O
+HETATM 2781 O HOH A 721 11.863 12.861 14.635 1.00 54.98 O
+HETATM 2782 O HOH A 722 19.214 -6.192 32.419 1.00 25.40 O
+HETATM 2783 O HOH A 723 -0.227 7.570 -3.969 1.00 37.09 O
+HETATM 2784 O HOH A 724 19.243 12.398 -3.622 1.00 19.12 O
+HETATM 2785 O HOH A 725 23.410 -6.008 1.926 1.00 25.91 O
+HETATM 2786 O HOH A 726 7.624 -8.536 -15.424 1.00 46.55 O
+HETATM 2787 O HOH A 727 23.169 -8.425 4.161 1.00 50.23 O
+HETATM 2788 O HOH A 728 20.967 16.913 -17.778 1.00 17.97 O
+HETATM 2789 O HOH A 729 3.435 -8.065 24.643 1.00 37.20 O
+HETATM 2790 O HOH A 730 2.421 -19.701 21.721 1.00 19.80 O
+HETATM 2791 O HOH A 731 20.354 -26.799 18.082 1.00 35.93 O
+HETATM 2792 O HOH A 732 26.885 -9.220 10.443 1.00 44.15 O
+HETATM 2793 O HOH A 733 1.564 -8.119 21.531 1.00 37.29 O
+HETATM 2794 O HOH A 734 15.456 24.744 7.786 1.00 37.81 O
+HETATM 2795 O HOH A 735 27.760 21.772 -11.674 1.00 17.55 O
+HETATM 2796 O HOH A 736 -5.506 20.181 -8.002 1.00 40.32 O
+HETATM 2797 O HOH A 737 11.915 15.221 4.229 1.00 32.50 O
+HETATM 2798 O HOH A 738 30.151 25.265 -10.687 1.00 30.25 O
+HETATM 2799 O HOH A 739 20.827 -22.801 22.064 1.00 21.95 O
+HETATM 2800 O HOH A 740 13.583 -14.012 33.010 1.00 38.07 O
+HETATM 2801 O HOH A 741 0.455 1.284 20.771 1.00 47.74 O
+HETATM 2802 O HOH A 742 -0.514 19.449 -15.740 1.00 36.34 O
+HETATM 2803 O HOH A 743 23.836 -4.507 23.876 1.00 50.45 O
+HETATM 2804 O HOH A 744 3.878 20.684 -21.337 1.00 32.39 O
+HETATM 2805 O HOH A 745 24.290 -15.929 16.833 1.00 38.93 O
+HETATM 2806 O HOH A 746 23.201 -5.397 26.412 1.00 24.88 O
+HETATM 2807 O HOH A 747 26.273 20.548 -14.032 1.00 22.96 O
+HETATM 2808 O HOH A 748 2.975 2.530 24.921 1.00 30.68 O
+HETATM 2809 O HOH A 749 10.919 -11.853 30.486 1.00 37.95 O
+HETATM 2810 O HOH A 750 20.396 13.586 9.082 1.00 33.87 O
+HETATM 2811 O HOH A 751 11.865 4.048 22.653 1.00 33.22 O
+HETATM 2812 O HOH A 752 27.729 -7.194 12.023 1.00 36.54 O
+HETATM 2813 O HOH A 753 17.618 22.329 9.554 1.00 40.97 O
+HETATM 2814 O HOH A 754 8.941 -7.897 -8.369 1.00 32.94 O
+HETATM 2815 O HOH A 755 11.761 -29.800 22.589 1.00 19.37 O
+HETATM 2816 O HOH A 756 28.635 10.717 -8.101 1.00 30.16 O
+HETATM 2817 O HOH A 757 9.498 1.361 21.295 1.00 24.46 O
+HETATM 2818 O HOH A 758 9.182 28.999 -17.474 1.00 26.72 O
+HETATM 2819 O HOH A 759 16.203 30.204 -2.976 1.00 42.95 O
+HETATM 2820 O HOH A 760 11.088 -31.620 10.226 1.00 43.15 O
+HETATM 2821 O HOH A 761 20.093 -25.462 22.433 1.00 26.03 O
+HETATM 2822 O HOH A 762 28.829 14.538 -8.128 1.00 34.41 O
+HETATM 2823 O HOH A 763 3.441 24.795 -1.613 1.00 34.84 O
+HETATM 2824 O HOH A 764 20.202 14.527 -19.039 1.00 33.34 O
+HETATM 2825 O HOH A 765 0.115 -27.182 17.907 1.00 30.24 O
+HETATM 2826 O HOH A 766 1.044 -16.222 23.465 1.00 44.28 O
+HETATM 2827 O HOH A 767 -2.627 17.627 -15.519 1.00 60.97 O
+HETATM 2828 O HOH A 768 16.474 3.496 -7.806 1.00 29.34 O
+HETATM 2829 O HOH A 769 24.409 -4.330 16.668 1.00 28.43 O
+HETATM 2830 O HOH A 770 16.789 -18.630 -0.780 1.00 27.06 O
+HETATM 2831 O HOH A 771 25.012 13.875 -17.225 1.00 25.24 O
+HETATM 2832 O HOH A 772 6.492 -8.329 -7.853 1.00 39.75 O
+HETATM 2833 O HOH A 773 20.068 -0.155 -1.012 1.00 35.16 O
+HETATM 2834 O HOH A 774 0.000 -0.407 0.000 0.50 24.99 O
+HETATM 2835 O HOH A 775 11.274 -2.559 -16.545 1.00 43.12 O
+HETATM 2836 O HOH A 776 -1.568 6.148 -2.378 1.00 39.83 O
+HETATM 2837 O HOH A 777 -4.782 26.408 -9.310 1.00 22.16 O
+HETATM 2838 O HOH A 778 16.309 -2.605 -2.855 1.00 41.31 O
+HETATM 2839 O HOH A 779 30.825 20.967 -5.604 1.00 39.69 O
+HETATM 2840 O HOH A 780 15.578 -19.046 34.790 1.00 41.80 O
+HETATM 2841 O HOH A 781 -2.125 -3.200 18.826 1.00 41.36 O
+HETATM 2842 O HOH A 782 23.956 -20.421 20.945 1.00 45.16 O
+HETATM 2843 O HOH A 783 12.859 22.637 6.077 1.00 35.21 O
+HETATM 2844 O HOH A 784 25.214 -7.886 22.805 1.00 37.18 O
+HETATM 2845 O HOH A 785 6.955 -15.138 -8.159 1.00 53.30 O
+HETATM 2846 O HOH A 786 26.675 27.198 -8.963 1.00 30.23 O
+HETATM 2847 O HOH A 787 5.969 2.060 28.913 1.00 39.92 O
+HETATM 2848 O HOH A 788 3.824 -29.082 18.300 1.00 39.98 O
+HETATM 2849 O HOH A 789 5.982 -23.035 -1.144 1.00 38.34 O
+HETATM 2850 O HOH A 790 2.922 -18.050 1.197 1.00 32.81 O
+HETATM 2851 O HOH A 791 21.637 -7.541 6.163 1.00 28.51 O
+HETATM 2852 O HOH A 792 20.695 25.668 5.052 1.00 48.77 O
+HETATM 2853 O HOH A 793 21.965 -17.907 23.656 1.00 32.28 O
+HETATM 2854 O HOH A 794 3.738 9.887 14.440 1.00 38.47 O
+HETATM 2855 O HOH A 795 7.546 -34.937 19.762 1.00 35.53 O
+HETATM 2856 O HOH A 796 19.252 -11.117 34.347 1.00 37.85 O
+HETATM 2857 O HOH A 797 17.203 15.425 -23.516 1.00 36.42 O
+HETATM 2858 O HOH A 798 25.973 23.296 -2.028 1.00 29.90 O
+HETATM 2859 O HOH A 799 17.194 -10.402 -5.842 1.00 42.68 O
+HETATM 2860 O HOH A 800 8.784 -4.353 26.547 1.00 44.39 O
+HETATM 2861 O HOH A 801 17.638 -17.925 37.524 1.00 49.93 O
+HETATM 2862 O HOH A 802 12.370 32.802 -12.287 1.00 44.37 O
+HETATM 2863 O HOH A 803 2.872 -1.757 -11.757 1.00 38.02 O
+HETATM 2864 O HOH A 804 20.613 4.079 -5.766 1.00 40.55 O
+HETATM 2865 O HOH A 805 14.640 -29.204 9.936 1.00 30.84 O
+HETATM 2866 O HOH A 806 17.978 -19.808 33.834 1.00 31.41 O
+HETATM 2867 O HOH A 807 15.789 -25.802 6.748 1.00 34.39 O
+HETATM 2868 O HOH A 808 5.765 11.051 11.864 1.00 47.77 O
+HETATM 2869 O HOH A 809 20.630 8.871 18.299 1.00 34.56 O
+HETATM 2870 O HOH A 810 28.704 24.207 -12.425 1.00 28.48 O
+HETATM 2871 O HOH A 811 0.105 -17.197 4.667 1.00 37.28 O
+HETATM 2872 O HOH A 812 22.401 -22.767 19.930 1.00 34.52 O
+HETATM 2873 O HOH A 813 18.717 -18.428 1.379 1.00 41.70 O
+HETATM 2874 O HOH A 814 17.792 -22.269 33.181 1.00 42.81 O
+HETATM 2875 O HOH A 815 20.668 -22.530 17.546 1.00 24.89 O
+HETATM 2876 O HOH A 816 7.721 -5.547 22.694 1.00 46.81 O
+HETATM 2877 O HOH A 817 20.766 5.826 -19.089 1.00 39.70 O
+HETATM 2878 O HOH A 818 28.111 9.358 -5.026 1.00 37.59 O
+HETATM 2879 O HOH A 819 25.908 -14.886 15.182 1.00 37.07 O
+HETATM 2880 O HOH A 820 14.701 -6.924 -4.448 1.00 39.83 O
+HETATM 2881 O HOH A 821 21.178 6.636 -5.226 1.00 32.30 O
+HETATM 2882 O HOH A 822 24.874 10.464 -2.477 1.00 28.16 O
+HETATM 2883 O HOH A 823 -2.947 28.034 -1.971 1.00 40.10 O
+HETATM 2884 O HOH A 824 14.364 20.232 9.961 1.00 64.02 O
+HETATM 2885 O HOH A 825 1.998 9.130 -3.466 1.00 43.88 O
+HETATM 2886 O HOH A 826 11.115 20.848 -19.436 1.00 28.04 O
+HETATM 2887 O HOH A 827 10.569 -34.359 21.224 1.00 30.05 O
+HETATM 2888 O HOH A 828 7.992 2.820 22.784 1.00 30.45 O
+HETATM 2889 O HOH A 829 23.890 6.960 -5.408 1.00 41.41 O
+HETATM 2890 O HOH A 830 -4.860 -11.927 5.027 1.00 34.53 O
+HETATM 2891 O HOH A 831 -5.504 22.417 -9.461 1.00 35.31 O
+HETATM 2892 O HOH A 832 21.823 -25.766 20.312 1.00 35.08 O
+HETATM 2893 O HOH A 833 24.913 4.376 10.687 1.00 37.92 O
+HETATM 2894 O HOH A 834 1.269 20.703 -21.897 1.00 32.97 O
+HETATM 2895 O HOH A 835 3.771 11.637 -21.977 1.00 31.92 O
+HETATM 2896 O HOH A 836 12.626 24.742 -22.470 1.00 40.86 O
+HETATM 2897 O HOH A 837 16.595 -4.924 -1.942 1.00 35.09 O
+HETATM 2898 O HOH A 838 11.940 -2.105 -13.997 1.00 81.21 O
+HETATM 2899 O HOH A 839 22.261 -14.167 8.754 1.00 42.15 O
+HETATM 2900 O HOH A 840 25.901 3.885 16.892 1.00 35.17 O
+HETATM 2901 O HOH A 841 6.955 0.869 24.448 1.00 37.90 O
+HETATM 2902 O HOH A 842 19.400 7.494 -3.277 1.00 24.50 O
+HETATM 2903 O HOH A 843 22.943 -1.301 22.523 1.00 28.74 O
+HETATM 2904 O HOH A 844 -4.289 9.192 -7.451 1.00 33.71 O
+HETATM 2905 O HOH A 845 24.338 2.535 6.965 1.00 50.58 O
+HETATM 2906 O HOH A 846 12.482 24.156 3.931 1.00 27.61 O
+HETATM 2907 O HOH A 847 13.627 -27.685 25.198 1.00 17.11 O
+HETATM 2908 O HOH A 848 21.105 -20.304 14.193 1.00 35.35 O
+HETATM 2909 O HOH A 849 22.677 -16.948 26.065 1.00 22.28 O
+HETATM 2910 O HOH A 850 8.193 2.892 -22.627 1.00 55.19 O
+HETATM 2911 O HOH A 851 17.203 -26.064 27.384 1.00 25.61 O
+HETATM 2912 O HOH A 852 6.147 21.871 -1.733 1.00 31.41 O
+HETATM 2913 O HOH A 853 20.037 -8.416 33.885 1.00 27.89 O
+HETATM 2914 O HOH A 854 15.046 17.762 14.001 1.00 56.06 O
+HETATM 2915 O HOH A 855 25.051 -3.698 20.136 1.00 53.04 O
+HETATM 2916 O HOH A 856 10.109 25.184 -23.031 1.00 38.82 O
+HETATM 2917 O HOH A 857 27.648 -2.076 15.145 1.00 34.17 O
+HETATM 2918 O HOH A 858 19.976 14.798 -21.747 1.00 35.44 O
+HETATM 2919 O HOH A 859 11.374 -33.896 23.985 1.00 24.95 O
+HETATM 2920 O HOH A 860 25.999 20.692 -1.475 1.00 31.16 O
+HETATM 2921 O HOH A 861 8.111 -2.686 22.688 1.00 44.34 O
+HETATM 2922 O HOH A 862 10.912 0.306 23.988 1.00 62.89 O
+HETATM 2923 O HOH A 863 0.810 22.459 -19.140 1.00 42.26 O
+HETATM 2924 O HOH A 864 9.569 31.573 -18.134 1.00 44.74 O
+HETATM 2925 O HOH A 865 4.943 1.282 26.322 1.00 29.80 O
+HETATM 2926 O HOH A 866 8.400 -28.634 3.942 1.00 32.60 O
+HETATM 2927 O HOH A 867 13.703 12.434 22.929 1.00 44.31 O
+HETATM 2928 O HOH A 868 10.378 -27.381 2.773 1.00 30.68 O
+HETATM 2929 O HOH A 869 28.747 25.438 -4.710 1.00 33.95 O
+HETATM 2930 O HOH A 870 16.308 -29.927 22.132 1.00 41.46 O
+HETATM 2931 O HOH A 871 20.530 -15.652 4.907 1.00 37.96 O
+HETATM 2932 O HOH A 872 1.363 -29.462 16.883 1.00 43.05 O
+HETATM 2933 O HOH A 873 28.290 -3.921 16.901 1.00 33.06 O
+HETATM 2934 O HOH A 874 21.119 -26.362 24.834 1.00 28.95 O
+HETATM 2935 O HOH A 875 27.101 14.413 -1.879 1.00 33.91 O
+HETATM 2936 O HOH A 876 25.873 21.448 -16.628 1.00 22.36 O
+HETATM 2937 O HOH A 877 25.161 31.405 -7.246 1.00 39.01 O
+HETATM 2938 O HOH A 878 25.157 -0.742 15.399 1.00 32.15 O
+HETATM 2939 O HOH A 879 18.090 -7.289 35.812 1.00 56.43 O
+HETATM 2940 O HOH A 880 16.073 13.714 23.421 1.00 31.52 O
+HETATM 2941 O HOH A 881 21.892 0.520 24.913 1.00 47.37 O
+HETATM 2942 O HOH A 882 10.432 22.183 0.548 1.00 21.18 O
+HETATM 2943 O HOH A 883 16.365 -11.946 34.322 1.00 44.91 O
+HETATM 2944 O HOH A 884 14.946 -32.152 15.788 1.00 37.75 O
+HETATM 2945 O HOH A 885 21.901 12.848 -18.345 1.00 27.03 O
+HETATM 2946 O HOH A 886 23.819 16.236 -16.712 1.00 22.25 O
+HETATM 2947 O HOH A 887 24.099 18.963 2.615 1.00 30.17 O
+HETATM 2948 O HOH A 888 13.977 -31.276 21.409 1.00 26.57 O
+HETATM 2949 O HOH A 889 24.747 17.900 -18.867 1.00 37.61 O
+HETATM 2950 O HOH A 890 26.570 31.349 -4.896 1.00 34.25 O
+HETATM 2951 O HOH A 891 25.523 16.140 -20.792 1.00 39.96 O
+CONECT 2545 2546 2547 2548
+CONECT 2546 2545
+CONECT 2547 2545
+CONECT 2548 2545
+CONECT 2549 2550 2551 2552
+CONECT 2550 2549
+CONECT 2551 2549
+CONECT 2552 2549
+CONECT 2553 2554 2555 2556
+CONECT 2554 2553
+CONECT 2555 2553
+CONECT 2556 2553
+CONECT 2557 2558 2559 2560
+CONECT 2558 2557
+CONECT 2559 2557
+CONECT 2560 2557
+MASTER 307 0 4 11 15 0 7 6 2754 1 16 24
+END