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*** ***elNémo ID: 2607232355593928074Job options:ID = 2607232355593928074 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = on DORMSD = on NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:CRYST1 53.300 57.300 75.000 90.00 90.00 90.00 P 21 21 21 1 ATOM 1 N MET A 1 -22.717 23.528 1.845 1.00 14.97 N ATOM 2 CA MET A 1 -21.465 24.190 1.374 1.00 15.16 C ATOM 3 C MET A 1 -20.444 23.118 1.035 1.00 14.57 C ATOM 4 O MET A 1 -20.515 22.004 1.545 1.00 15.23 O ATOM 5 CB MET A 1 -20.926 25.151 2.448 1.00 15.52 C ATOM 6 CG MET A 1 -19.763 26.053 2.021 1.00 16.59 C ATOM 7 SD MET A 1 -20.080 27.075 0.573 1.00 19.48 S ATOM 8 CE MET A 1 -21.512 28.042 1.080 1.00 19.53 C ATOM 9 N PHE A 2 -19.511 23.439 0.144 1.00 13.89 N ATOM 10 CA PHE A 2 -18.427 22.515 -0.198 1.00 13.14 C ATOM 11 C PHE A 2 -17.627 22.114 1.046 1.00 12.81 C ATOM 12 O PHE A 2 -17.494 22.887 1.990 1.00 12.84 O ATOM 13 CB PHE A 2 -17.504 23.101 -1.288 1.00 12.79 C ATOM 14 CG PHE A 2 -16.837 24.401 -0.912 1.00 11.97 C ATOM 15 CD1 PHE A 2 -15.569 24.404 -0.342 1.00 10.64 C ATOM 16 CD2 PHE A 2 -17.466 25.619 -1.145 1.00 10.03 C ATOM 17 CE1 PHE A 2 -14.948 25.588 -0.004 1.00 10.84 C ATOM 18 CE2 PHE A 2 -16.854 26.809 -0.807 1.00 9.23 C ATOM 19 CZ PHE A 2 -15.586 26.791 -0.228 1.00 8.92 C ATOM 20 N LYS A 3 -17.114 20.890 1.039 1.00 12.34 N ATOM 21 CA LYS A 3 -16.423 20.327 2.195 1.00 12.50 C ATOM 22 C LYS A 3 -14.910 20.283 2.010 1.00 11.73 C ATOM 23 O LYS A 3 -14.171 20.050 2.968 1.00 11.90 O ATOM 24 CB LYS A 3 -16.961 18.923 2.467 1.00 12.48 C ATOM 25 CG LYS A 3 -18.481 18.895 2.706 1.00 14.55 C ATOM 26 CD LYS A 3 -18.842 19.298 4.128 1.00 17.97 C ATOM 27 CE LYS A 3 -20.221 19.957 4.269 1.00 20.33 C ATOM 28 NZ LYS A 3 -21.168 19.760 3.128 1.00 22.78 N1+ ATOM 29 N ALA A 4 -14.446 20.517 0.786 1.00 11.25 N ATOM 30 CA ALA A 4 -13.016 20.439 0.486 1.00 10.59 C ATOM 31 C ALA A 4 -12.630 21.307 -0.695 1.00 10.01 C ATOM 32 O ALA A 4 -13.438 21.542 -1.587 1.00 10.12 O ATOM 33 CB ALA A 4 -12.623 19.009 0.212 1.00 10.65 C ATOM 34 N VAL A 5 -11.378 21.759 -0.705 1.00 9.66 N ATOM 35 CA VAL A 5 -10.793 22.408 -1.867 1.00 9.07 C ATOM 36 C VAL A 5 -9.559 21.611 -2.323 1.00 9.23 C ATOM 37 O VAL A 5 -8.685 21.272 -1.521 1.00 8.94 O ATOM 38 CB VAL A 5 -10.457 23.910 -1.596 1.00 9.28 C ATOM 39 CG1 VAL A 5 -9.906 24.566 -2.857 1.00 8.77 C ATOM 40 CG2 VAL A 5 -11.702 24.637 -1.115 1.00 9.42 C ATOM 41 N LEU A 6 -9.535 21.278 -3.615 1.00 9.13 N ATOM 42 CA LEU A 6 -8.481 20.476 -4.214 1.00 9.35 C ATOM 43 C LEU A 6 -7.591 21.431 -5.001 1.00 9.46 C ATOM 44 O LEU A 6 -8.003 21.987 -6.018 1.00 9.47 O ATOM 45 CB LEU A 6 -9.094 19.401 -5.119 1.00 9.51 C ATOM 46 CG LEU A 6 -10.321 18.709 -4.516 1.00 9.16 C ATOM 47 CD1 LEU A 6 -10.965 17.730 -5.492 1.00 9.75 C ATOM 48 CD2 LEU A 6 -9.951 18.004 -3.199 1.00 10.56 C ATOM 49 N PHE A 7 -6.381 21.643 -4.504 1.00 9.57 N ATOM 50 CA PHE A 7 -5.450 22.609 -5.098 1.00 9.85 C ATOM 51 C PHE A 7 -4.470 21.963 -6.072 1.00 9.83 C ATOM 52 O PHE A 7 -3.720 21.063 -5.715 1.00 10.63 O ATOM 53 CB PHE A 7 -4.601 23.260 -4.009 1.00 9.54 C ATOM 54 CG PHE A 7 -5.315 24.282 -3.176 1.00 8.74 C ATOM 55 CD1 PHE A 7 -6.112 23.900 -2.119 1.00 8.63 C ATOM 56 CD2 PHE A 7 -5.116 25.635 -3.403 1.00 8.68 C ATOM 57 CE1 PHE A 7 -6.739 24.839 -1.326 1.00 8.29 C ATOM 58 CE2 PHE A 7 -5.733 26.590 -2.615 1.00 9.09 C ATOM 59 CZ PHE A 7 -6.547 26.197 -1.566 1.00 7.92 C ATOM 60 N ASP A 8 -4.450 22.460 -7.299 1.00 10.23 N ATOM 61 CA ASP A 8 -3.279 22.316 -8.156 1.00 10.04 C ATOM 62 C ASP A 8 -2.139 23.143 -7.546 1.00 10.29 C ATOM 63 O ASP A 8 -2.394 24.100 -6.798 1.00 10.51 O ATOM 64 CB ASP A 8 -3.621 22.796 -9.564 1.00 10.06 C ATOM 65 CG ASP A 8 -2.479 22.651 -10.531 1.00 10.20 C ATOM 66 OD1 ASP A 8 -2.300 23.567 -11.365 1.00 9.01 O ATOM 67 OD2 ASP A 8 -1.752 21.643 -10.458 1.00 10.39 O1- ATOM 68 N LEU A 9 -0.887 22.791 -7.856 1.00 10.69 N ATOM 69 CA LEU A 9 0.275 23.517 -7.334 1.00 11.53 C ATOM 70 C LEU A 9 0.779 24.566 -8.332 1.00 11.80 C ATOM 71 O LEU A 9 0.670 25.769 -8.093 1.00 11.43 O ATOM 72 CB LEU A 9 1.406 22.538 -6.978 1.00 11.85 C ATOM 73 CG LEU A 9 2.686 23.139 -6.390 1.00 13.68 C ATOM 74 CD1 LEU A 9 2.493 23.476 -4.942 1.00 15.81 C ATOM 75 CD2 LEU A 9 3.823 22.137 -6.574 1.00 16.31 C ATOM 76 N ASP A 10 1.339 24.112 -9.449 1.00 12.41 N ATOM 77 CA ASP A 10 1.953 25.024 -10.410 1.00 12.73 C ATOM 78 C ASP A 10 0.877 25.876 -11.085 1.00 12.41 C ATOM 79 O ASP A 10 -0.075 25.344 -11.646 1.00 12.28 O ATOM 80 CB ASP A 10 2.758 24.245 -11.453 1.00 13.20 C ATOM 81 CG ASP A 10 3.459 25.140 -12.435 1.00 16.00 C ATOM 82 OD1 ASP A 10 4.378 25.886 -12.023 1.00 17.72 O ATOM 83 OD2 ASP A 10 3.093 25.091 -13.635 1.00 19.88 O1- ATOM 84 N GLY A 11 1.036 27.194 -11.010 1.00 12.30 N ATOM 85 CA GLY A 11 0.074 28.148 -11.572 1.00 12.48 C ATOM 86 C GLY A 11 -1.075 28.550 -10.656 1.00 12.06 C ATOM 87 O GLY A 11 -1.887 29.380 -11.029 1.00 12.33 O ATOM 88 N VAL A 12 -1.143 27.958 -9.465 1.00 11.67 N ATOM 89 CA VAL A 12 -2.203 28.265 -8.487 1.00 11.15 C ATOM 90 C VAL A 12 -1.552 28.681 -7.165 1.00 11.16 C ATOM 91 O VAL A 12 -1.727 29.814 -6.709 1.00 10.27 O ATOM 92 CB VAL A 12 -3.144 27.069 -8.267 1.00 11.50 C ATOM 93 CG1 VAL A 12 -4.157 27.366 -7.153 1.00 10.45 C ATOM 94 CG2 VAL A 12 -3.859 26.690 -9.568 1.00 11.09 C ATOM 95 N ILE A 13 -0.787 27.772 -6.571 1.00 10.58 N ATOM 96 CA ILE A 13 -0.080 28.048 -5.312 1.00 10.88 C ATOM 97 C ILE A 13 1.217 28.802 -5.565 1.00 11.53 C ATOM 98 O ILE A 13 1.566 29.736 -4.835 1.00 11.30 O ATOM 99 CB ILE A 13 0.191 26.750 -4.519 1.00 10.36 C ATOM 100 CG1 ILE A 13 -1.142 26.151 -4.052 1.00 10.09 C ATOM 101 CG2 ILE A 13 1.122 27.019 -3.311 1.00 9.64 C ATOM 102 CD1 ILE A 13 -1.039 24.736 -3.474 1.00 9.78 C ATOM 103 N THR A 14 1.930 28.393 -6.608 1.00 12.68 N ATOM 104 CA THR A 14 3.190 29.012 -6.965 1.00 13.38 C ATOM 105 C THR A 14 3.482 28.715 -8.425 1.00 14.43 C ATOM 106 O THR A 14 2.652 28.125 -9.125 1.00 13.39 O ATOM 107 CB THR A 14 4.348 28.495 -6.058 1.00 13.29 C ATOM 108 CG2 THR A 14 4.657 27.019 -6.320 1.00 13.23 C ATOM 109 OG1 THR A 14 5.532 29.272 -6.261 1.00 14.50 O ATOM 110 N ASP A 15 4.644 29.164 -8.888 1.00 15.63 N ATOM 111 CA AASP A 15 5.170 28.843 -10.215 0.50 16.33 C ATOM 112 CA BASP A 15 5.129 28.700 -10.174 0.50 16.57 C ATOM 113 C ASP A 15 6.576 28.244 -10.079 1.00 16.85 C ATOM 114 O ASP A 15 7.431 28.854 -9.423 1.00 17.63 O ATOM 115 CB AASP A 15 5.223 30.124 -11.056 0.50 16.37 C ATOM 116 CB BASP A 15 4.874 29.685 -11.325 0.50 16.89 C ATOM 117 CG AASP A 15 6.100 29.989 -12.285 0.50 16.57 C ATOM 118 CG BASP A 15 5.486 31.042 -11.097 0.50 17.65 C ATOM 119 OD1AASP A 15 5.923 29.011 -13.037 0.50 16.33 O ATOM 120 OD1BASP A 15 5.856 31.363 -9.951 0.50 21.25 O ATOM 121 OD2AASP A 15 6.965 30.861 -12.494 0.50 18.10 O1- ATOM 122 OD2BASP A 15 5.581 31.798 -12.083 0.50 20.26 O1- ATOM 123 N THR A 16 6.808 27.100 -10.709 1.00 17.41 N ATOM 124 CA THR A 16 8.086 26.413 -10.697 1.00 18.30 C ATOM 125 C THR A 16 8.971 26.828 -11.890 1.00 18.46 C ATOM 126 O THR A 16 10.129 26.417 -11.982 1.00 18.53 O ATOM 127 CB THR A 16 7.839 24.880 -10.764 1.00 18.19 C ATOM 128 CG2 THR A 16 7.183 24.377 -9.483 1.00 20.08 C ATOM 129 OG1 THR A 16 6.960 24.590 -11.860 1.00 19.78 O ATOM 130 N ALA A 17 8.430 27.656 -12.787 1.00 18.80 N ATOM 131 CA ALA A 17 9.062 27.935 -14.088 1.00 18.80 C ATOM 132 C ALA A 17 10.468 28.513 -14.005 1.00 18.85 C ATOM 133 O ALA A 17 11.342 28.111 -14.772 1.00 18.86 O ATOM 134 CB ALA A 17 8.166 28.857 -14.937 1.00 18.97 C ATOM 135 N GLU A 18 10.686 29.460 -13.094 1.00 18.85 N ATOM 136 CA GLU A 18 12.004 30.058 -12.916 1.00 19.10 C ATOM 137 C GLU A 18 13.033 28.998 -12.509 1.00 18.41 C ATOM 138 O GLU A 18 14.192 29.062 -12.906 1.00 18.06 O ATOM 139 CB GLU A 18 11.947 31.180 -11.871 1.00 19.39 C ATOM 140 CG GLU A 18 13.255 31.938 -11.674 1.00 20.71 C ATOM 141 CD GLU A 18 13.666 32.754 -12.880 1.00 21.95 C ATOM 142 OE1 GLU A 18 12.807 33.026 -13.739 1.00 23.02 O ATOM 143 OE2 GLU A 18 14.850 33.135 -12.976 1.00 24.72 O1- ATOM 144 N TYR A 19 12.596 28.020 -11.719 1.00 18.05 N ATOM 145 CA TYR A 19 13.484 26.979 -11.217 1.00 17.46 C ATOM 146 C TYR A 19 13.825 25.967 -12.307 1.00 17.17 C ATOM 147 O TYR A 19 14.975 25.573 -12.438 1.00 16.70 O ATOM 148 CB TYR A 19 12.872 26.323 -9.975 1.00 17.54 C ATOM 149 CG TYR A 19 12.652 27.355 -8.895 1.00 17.25 C ATOM 150 CD1 TYR A 19 11.391 27.910 -8.675 1.00 17.97 C ATOM 151 CD2 TYR A 19 13.722 27.835 -8.143 1.00 17.71 C ATOM 152 CE1 TYR A 19 11.195 28.888 -7.705 1.00 18.01 C ATOM 153 CE2 TYR A 19 13.538 28.812 -7.172 1.00 17.78 C ATOM 154 CZ TYR A 19 12.273 29.327 -6.953 1.00 17.66 C ATOM 155 OH TYR A 19 12.106 30.300 -5.993 1.00 17.70 O ATOM 156 N HIS A 20 12.829 25.577 -13.098 1.00 17.11 N ATOM 157 CA HIS A 20 13.066 24.760 -14.289 1.00 16.76 C ATOM 158 C HIS A 20 13.992 25.483 -15.265 1.00 16.92 C ATOM 159 O HIS A 20 14.927 24.883 -15.811 1.00 16.44 O ATOM 160 CB HIS A 20 11.741 24.390 -14.970 1.00 16.57 C ATOM 161 CG HIS A 20 11.008 23.277 -14.289 1.00 15.67 C ATOM 162 CD2 HIS A 20 11.324 21.970 -14.145 1.00 14.34 C ATOM 163 ND1 HIS A 20 9.808 23.454 -13.635 1.00 16.78 N ATOM 164 CE1 HIS A 20 9.410 22.298 -13.130 1.00 14.42 C ATOM 165 NE2 HIS A 20 10.316 21.381 -13.423 1.00 16.93 N ATOM 166 N PHE A 21 13.747 26.778 -15.460 1.00 17.05 N ATOM 167 CA PHE A 21 14.601 27.616 -16.313 1.00 17.37 C ATOM 168 C PHE A 21 16.054 27.538 -15.856 1.00 16.90 C ATOM 169 O PHE A 21 16.947 27.202 -16.639 1.00 16.38 O ATOM 170 CB PHE A 21 14.090 29.070 -16.316 1.00 17.78 C ATOM 171 CG PHE A 21 15.043 30.058 -16.928 1.00 19.82 C ATOM 172 CD1 PHE A 21 15.662 29.791 -18.149 1.00 21.41 C ATOM 173 CD2 PHE A 21 15.308 31.267 -16.297 1.00 22.03 C ATOM 174 CE1 PHE A 21 16.536 30.704 -18.716 1.00 22.04 C ATOM 175 CE2 PHE A 21 16.178 32.190 -16.864 1.00 23.34 C ATOM 176 CZ PHE A 21 16.794 31.908 -18.079 1.00 22.90 C ATOM 177 N ARG A 22 16.278 27.828 -14.577 1.00 16.40 N ATOM 178 CA ARG A 22 17.616 27.781 -14.000 1.00 16.56 C ATOM 179 C ARG A 22 18.283 26.427 -14.219 1.00 15.71 C ATOM 180 O ARG A 22 19.474 26.365 -14.539 1.00 15.62 O ATOM 181 CB ARG A 22 17.562 28.100 -12.504 1.00 16.75 C ATOM 182 CG ARG A 22 17.276 29.564 -12.195 1.00 18.75 C ATOM 183 CD ARG A 22 17.011 29.768 -10.714 1.00 20.91 C ATOM 184 NE ARG A 22 16.461 31.096 -10.442 1.00 22.93 N ATOM 185 CZ ARG A 22 16.156 31.565 -9.231 1.00 25.08 C ATOM 186 NH1 ARG A 22 16.338 30.821 -8.143 1.00 25.57 N1+ ATOM 187 NH2 ARG A 22 15.666 32.794 -9.106 1.00 26.14 N ATOM 188 N ALA A 23 17.509 25.352 -14.056 1.00 14.91 N ATOM 189 CA ALA A 23 18.028 23.983 -14.198 1.00 14.43 C ATOM 190 C ALA A 23 18.445 23.675 -15.642 1.00 14.33 C ATOM 191 O ALA A 23 19.513 23.106 -15.875 1.00 14.51 O ATOM 192 CB ALA A 23 16.995 22.974 -13.727 1.00 13.83 C ATOM 193 N TRP A 24 17.593 24.028 -16.603 1.00 14.71 N ATOM 194 CA TRP A 24 17.921 23.841 -18.023 1.00 15.11 C ATOM 195 C TRP A 24 19.098 24.715 -18.455 1.00 15.69 C ATOM 196 O TRP A 24 19.958 24.271 -19.211 1.00 15.24 O ATOM 197 CB TRP A 24 16.719 24.152 -18.921 1.00 15.04 C ATOM 198 CG TRP A 24 15.654 23.118 -18.891 1.00 14.32 C ATOM 199 CD1 TRP A 24 14.360 23.295 -18.520 1.00 14.73 C ATOM 200 CD2 TRP A 24 15.782 21.737 -19.263 1.00 13.69 C ATOM 201 CE2 TRP A 24 14.521 21.138 -19.077 1.00 15.06 C ATOM 202 CE3 TRP A 24 16.843 20.950 -19.733 1.00 13.49 C ATOM 203 NE1 TRP A 24 13.672 22.109 -18.619 1.00 15.44 N ATOM 204 CZ2 TRP A 24 14.285 19.784 -19.344 1.00 15.20 C ATOM 205 CZ3 TRP A 24 16.607 19.604 -20.002 1.00 12.56 C ATOM 206 CH2 TRP A 24 15.337 19.038 -19.799 1.00 14.27 C ATOM 207 N LYS A 25 19.122 25.958 -17.980 1.00 16.45 N ATOM 208 CA LYS A 25 20.198 26.885 -18.315 1.00 17.21 C ATOM 209 C LYS A 25 21.537 26.368 -17.789 1.00 17.41 C ATOM 210 O LYS A 25 22.550 26.450 -18.485 1.00 17.42 O ATOM 211 CB LYS A 25 19.888 28.291 -17.780 1.00 17.74 C ATOM 212 CG LYS A 25 20.977 29.321 -18.056 1.00 19.34 C ATOM 213 CD LYS A 25 20.500 30.763 -17.851 1.00 21.80 C ATOM 214 CE LYS A 25 19.680 30.938 -16.586 1.00 23.75 C ATOM 215 NZ LYS A 25 19.448 32.380 -16.267 1.00 26.22 N1+ ATOM 216 N ALA A 26 21.535 25.811 -16.578 1.00 17.22 N ATOM 217 CA ALA A 26 22.743 25.213 -16.009 1.00 17.34 C ATOM 218 C ALA A 26 23.239 24.024 -16.839 1.00 17.42 C ATOM 219 O ALA A 26 24.434 23.927 -17.132 1.00 17.53 O ATOM 220 CB ALA A 26 22.501 24.796 -14.554 1.00 17.57 C ATOM 221 N LEU A 27 22.322 23.134 -17.223 1.00 17.30 N ATOM 222 CA LEU A 27 22.657 21.977 -18.060 1.00 17.74 C ATOM 223 C LEU A 27 23.168 22.412 -19.435 1.00 18.13 C ATOM 224 O LEU A 27 24.195 21.912 -19.906 1.00 18.01 O ATOM 225 CB LEU A 27 21.444 21.059 -18.235 1.00 17.74 C ATOM 226 CG LEU A 27 21.693 19.740 -18.983 1.00 18.08 C ATOM 227 CD1 LEU A 27 22.663 18.855 -18.219 1.00 18.32 C ATOM 228 CD2 LEU A 27 20.384 19.019 -19.239 1.00 18.26 C ATOM 229 N ALA A 28 22.451 23.332 -20.075 1.00 18.82 N ATOM 230 CA ALA A 28 22.843 23.821 -21.408 1.00 19.58 C ATOM 231 C ALA A 28 24.262 24.388 -21.386 1.00 20.36 C ATOM 232 O ALA A 28 25.073 24.073 -22.262 1.00 20.31 O ATOM 233 CB ALA A 28 21.853 24.869 -21.920 1.00 19.37 C ATOM 234 N GLU A 29 24.556 25.209 -20.378 1.00 21.50 N ATOM 235 CA GLU A 29 25.897 25.794 -20.217 1.00 22.52 C ATOM 236 C GLU A 29 26.989 24.742 -20.002 1.00 22.81 C ATOM 237 O GLU A 29 28.077 24.852 -20.570 1.00 23.26 O ATOM 238 CB GLU A 29 25.907 26.823 -19.080 1.00 22.79 C ATOM 239 CG GLU A 29 25.154 28.095 -19.443 1.00 24.23 C ATOM 240 CD GLU A 29 25.065 29.097 -18.306 1.00 26.28 C ATOM 241 OE1 GLU A 29 24.219 30.012 -18.402 1.00 25.95 O ATOM 242 OE2 GLU A 29 25.836 28.983 -17.326 1.00 28.61 O1- ATOM 243 N GLU A 30 26.695 23.723 -19.201 1.00 23.14 N ATOM 244 CA GLU A 30 27.622 22.607 -18.980 1.00 23.25 C ATOM 245 C GLU A 30 27.990 21.860 -20.271 1.00 22.85 C ATOM 246 O GLU A 30 29.154 21.508 -20.468 1.00 23.32 O ATOM 247 CB GLU A 30 27.033 21.639 -17.951 1.00 23.60 C ATOM 248 CG GLU A 30 27.773 20.317 -17.767 1.00 25.38 C ATOM 249 CD GLU A 30 27.025 19.372 -16.847 1.00 27.58 C ATOM 250 OE1 GLU A 30 26.482 19.845 -15.829 1.00 29.62 O ATOM 251 OE2 GLU A 30 26.974 18.157 -17.138 1.00 30.27 O1- ATOM 252 N ILE A 31 27.010 21.622 -21.142 1.00 21.73 N ATOM 253 CA ILE A 31 27.245 20.884 -22.388 1.00 20.95 C ATOM 254 C ILE A 31 27.485 21.811 -23.589 1.00 20.43 C ATOM 255 O ILE A 31 27.622 21.344 -24.716 1.00 20.73 O ATOM 256 CB ILE A 31 26.106 19.868 -22.691 1.00 21.14 C ATOM 257 CG1 ILE A 31 24.772 20.561 -22.983 1.00 20.68 C ATOM 258 CG2 ILE A 31 25.959 18.887 -21.531 1.00 21.51 C ATOM 259 CD1 ILE A 31 23.649 19.587 -23.349 1.00 20.64 C ATOM 260 N GLY A 32 27.516 23.118 -23.341 1.00 19.54 N ATOM 261 CA GLY A 32 27.939 24.104 -24.338 1.00 19.36 C ATOM 262 C GLY A 32 26.907 24.464 -25.391 1.00 18.78 C ATOM 263 O GLY A 32 27.254 24.616 -26.567 1.00 19.27 O ATOM 264 N ILE A 33 25.647 24.603 -24.970 1.00 18.24 N ATOM 265 CA ILE A 33 24.544 24.995 -25.849 1.00 17.60 C ATOM 266 C ILE A 33 24.025 26.387 -25.478 1.00 18.28 C ATOM 267 O ILE A 33 23.566 26.613 -24.352 1.00 17.95 O ATOM 268 CB ILE A 33 23.378 23.967 -25.778 1.00 17.35 C ATOM 269 CG1 ILE A 33 23.845 22.601 -26.293 1.00 16.59 C ATOM 270 CG2 ILE A 33 22.170 24.457 -26.568 1.00 16.33 C ATOM 271 CD1 ILE A 33 22.825 21.504 -26.113 1.00 17.59 C ATOM 272 N ASN A 34 24.135 27.324 -26.420 1.00 18.43 N ATOM 273 CA ASN A 34 23.602 28.678 -26.257 1.00 18.84 C ATOM 274 C ASN A 34 22.093 28.723 -26.447 1.00 18.62 C ATOM 275 O ASN A 34 21.499 27.807 -27.025 1.00 18.14 O ATOM 276 CB ASN A 34 24.194 29.630 -27.308 1.00 19.32 C ATOM 277 CG ASN A 34 25.664 29.910 -27.114 1.00 20.82 C ATOM 278 ND2 ASN A 34 26.243 30.625 -28.081 1.00 22.61 N ATOM 279 OD1 ASN A 34 26.277 29.521 -26.116 1.00 24.21 O ATOM 280 N GLY A 35 21.481 29.810 -25.982 1.00 18.44 N ATOM 281 CA GLY A 35 20.094 30.122 -26.326 1.00 18.54 C ATOM 282 C GLY A 35 19.010 29.720 -25.350 1.00 18.52 C ATOM 283 O GLY A 35 17.831 29.962 -25.610 1.00 18.79 O ATOM 284 N VAL A 36 19.379 29.113 -24.225 1.00 18.88 N ATOM 285 CA VAL A 36 18.384 28.758 -23.217 1.00 18.95 C ATOM 286 C VAL A 36 18.130 29.986 -22.344 1.00 19.39 C ATOM 287 O VAL A 36 18.747 30.142 -21.289 1.00 19.45 O ATOM 288 CB VAL A 36 18.821 27.535 -22.375 1.00 18.96 C ATOM 289 CG1 VAL A 36 17.777 27.202 -21.320 1.00 18.89 C ATOM 290 CG2 VAL A 36 19.067 26.332 -23.274 1.00 19.08 C ATOM 291 N ASP A 37 17.240 30.865 -22.812 1.00 19.97 N ATOM 292 CA ASP A 37 16.866 32.082 -22.079 1.00 20.32 C ATOM 293 C ASP A 37 15.431 31.991 -21.542 1.00 20.73 C ATOM 294 O ASP A 37 14.763 30.980 -21.725 1.00 20.25 O ATOM 295 CB ASP A 37 17.084 33.344 -22.946 1.00 20.36 C ATOM 296 CG ASP A 37 16.169 33.413 -24.175 1.00 21.22 C ATOM 297 OD1 ASP A 37 15.174 32.661 -24.268 1.00 21.60 O ATOM 298 OD2 ASP A 37 16.453 34.258 -25.057 1.00 23.11 O1- ATOM 299 N ARG A 38 14.970 33.043 -20.864 1.00 20.98 N ATOM 300 CA ARG A 38 13.643 33.031 -20.234 1.00 21.80 C ATOM 301 C ARG A 38 12.526 32.823 -21.257 1.00 21.71 C ATOM 302 O ARG A 38 11.508 32.186 -20.959 1.00 21.55 O ATOM 303 CB ARG A 38 13.415 34.334 -19.461 1.00 22.23 C ATOM 304 CG ARG A 38 12.023 34.479 -18.853 1.00 24.15 C ATOM 305 CD ARG A 38 11.934 35.669 -17.890 1.00 26.42 C ATOM 306 NE ARG A 38 13.119 35.787 -17.038 1.00 27.41 N ATOM 307 CZ ARG A 38 13.439 34.942 -16.064 1.00 27.66 C ATOM 308 NH1 ARG A 38 12.666 33.896 -15.800 1.00 29.26 N1+ ATOM 309 NH2 ARG A 38 14.544 35.139 -15.353 1.00 27.78 N ATOM 310 N GLN A 39 12.739 33.349 -22.460 1.00 21.61 N ATOM 311 CA AGLN A 39 11.778 33.249 -23.563 0.50 21.88 C ATOM 312 CA BGLN A 39 11.741 33.240 -23.514 0.50 21.65 C ATOM 313 C GLN A 39 11.668 31.802 -24.027 1.00 21.77 C ATOM 314 O GLN A 39 10.578 31.279 -24.250 1.00 21.49 O ATOM 315 CB AGLN A 39 12.215 34.110 -24.762 0.50 22.03 C ATOM 316 CB BGLN A 39 12.024 34.232 -24.645 0.50 21.62 C ATOM 317 CG AGLN A 39 12.643 35.544 -24.448 0.50 22.75 C ATOM 318 CG BGLN A 39 11.611 35.669 -24.313 0.50 21.34 C ATOM 319 CD AGLN A 39 11.523 36.374 -23.870 0.50 23.62 C ATOM 320 CD BGLN A 39 12.466 36.298 -23.225 0.50 20.89 C ATOM 321 NE2AGLN A 39 11.628 36.697 -22.585 0.50 24.65 N ATOM 322 NE2BGLN A 39 11.829 36.727 -22.139 0.50 21.34 N ATOM 323 OE1AGLN A 39 10.580 36.737 -24.574 0.50 24.98 O ATOM 324 OE1BGLN A 39 13.683 36.399 -23.363 0.50 20.71 O ATOM 325 N PHE A 40 12.823 31.163 -24.190 1.00 21.96 N ATOM 326 CA PHE A 40 12.876 29.771 -24.616 1.00 22.26 C ATOM 327 C PHE A 40 12.144 28.871 -23.616 1.00 22.89 C ATOM 328 O PHE A 40 11.393 27.989 -24.016 1.00 22.52 O ATOM 329 CB PHE A 40 14.330 29.314 -24.786 1.00 21.94 C ATOM 330 CG PHE A 40 14.468 27.868 -25.166 1.00 21.56 C ATOM 331 CD1 PHE A 40 14.440 27.477 -26.497 1.00 20.69 C ATOM 332 CD2 PHE A 40 14.612 26.894 -24.188 1.00 21.11 C ATOM 333 CE1 PHE A 40 14.559 26.134 -26.848 1.00 20.88 C ATOM 334 CE2 PHE A 40 14.732 25.560 -24.532 1.00 20.92 C ATOM 335 CZ PHE A 40 14.708 25.182 -25.865 1.00 20.51 C ATOM 336 N ASN A 41 12.361 29.109 -22.323 1.00 23.90 N ATOM 337 CA ASN A 41 11.749 28.287 -21.275 1.00 24.67 C ATOM 338 C ASN A 41 10.230 28.475 -21.164 1.00 25.61 C ATOM 339 O ASN A 41 9.530 27.556 -20.739 1.00 25.64 O ATOM 340 CB ASN A 41 12.413 28.550 -19.918 1.00 24.77 C ATOM 341 CG ASN A 41 11.902 27.623 -18.831 1.00 24.33 C ATOM 342 ND2 ASN A 41 12.342 26.367 -18.858 1.00 24.31 N ATOM 343 OD1 ASN A 41 11.097 28.029 -17.988 1.00 27.14 O ATOM 344 N GLU A 42 9.723 29.651 -21.544 1.00 26.77 N ATOM 345 CA GLU A 42 8.265 29.867 -21.635 1.00 27.58 C ATOM 346 C GLU A 42 7.601 28.848 -22.557 1.00 27.88 C ATOM 347 O GLU A 42 6.446 28.472 -22.343 1.00 27.96 O ATOM 348 CB GLU A 42 7.927 31.282 -22.121 1.00 27.95 C ATOM 349 CG GLU A 42 8.038 32.347 -21.049 1.00 28.75 C ATOM 350 CD GLU A 42 7.677 33.741 -21.539 1.00 30.62 C ATOM 351 OE1 GLU A 42 7.567 33.957 -22.771 1.00 29.22 O ATOM 352 OE2 GLU A 42 7.515 34.631 -20.674 1.00 32.08 O1- ATOM 353 N GLN A 43 8.335 28.411 -23.580 1.00 28.45 N ATOM 354 CA GLN A 43 7.840 27.421 -24.536 1.00 28.98 C ATOM 355 C GLN A 43 7.923 25.976 -24.029 1.00 29.12 C ATOM 356 O GLN A 43 7.524 25.049 -24.737 1.00 29.34 O ATOM 357 CB GLN A 43 8.612 27.528 -25.847 1.00 29.30 C ATOM 358 CG GLN A 43 8.571 28.910 -26.480 1.00 30.74 C ATOM 359 CD GLN A 43 8.324 28.850 -27.973 1.00 33.03 C ATOM 360 NE2 GLN A 43 9.243 29.412 -28.753 1.00 33.87 N ATOM 361 OE1 GLN A 43 7.309 28.309 -28.422 1.00 35.12 O ATOM 362 N LEU A 44 8.454 25.783 -22.824 1.00 29.00 N ATOM 363 CA LEU A 44 8.523 24.458 -22.208 1.00 28.87 C ATOM 364 C LEU A 44 7.447 24.285 -21.137 1.00 29.08 C ATOM 365 O LEU A 44 7.428 23.273 -20.430 1.00 29.10 O ATOM 366 CB LEU A 44 9.907 24.234 -21.590 1.00 28.65 C ATOM 367 CG LEU A 44 11.115 24.398 -22.513 1.00 28.01 C ATOM 368 CD1 LEU A 44 12.406 24.130 -21.757 1.00 27.57 C ATOM 369 CD2 LEU A 44 11.006 23.483 -23.723 1.00 27.89 C ATOM 370 N LYS A 45 6.555 25.267 -21.012 1.00 29.30 N ATOM 371 CA LYS A 45 5.485 25.202 -20.026 1.00 29.29 C ATOM 372 C LYS A 45 4.578 24.013 -20.332 1.00 28.96 C ATOM 373 O LYS A 45 4.024 23.911 -21.426 1.00 29.15 O ATOM 374 CB LYS A 45 4.678 26.502 -20.017 1.00 29.68 C ATOM 375 CG LYS A 45 3.669 26.599 -18.885 1.00 30.56 C ATOM 376 CD LYS A 45 3.068 27.992 -18.815 1.00 31.91 C ATOM 377 CE LYS A 45 1.982 28.086 -17.763 1.00 32.37 C ATOM 378 NZ LYS A 45 1.356 29.443 -17.749 1.00 33.02 N1+ ATOM 379 N GLY A 46 4.456 23.107 -19.365 1.00 28.42 N ATOM 380 CA GLY A 46 3.648 21.902 -19.522 1.00 27.89 C ATOM 381 C GLY A 46 4.319 20.773 -20.292 1.00 27.07 C ATOM 382 O GLY A 46 3.785 19.665 -20.339 1.00 27.70 O ATOM 383 N VAL A 47 5.487 21.038 -20.881 1.00 25.78 N ATOM 384 CA VAL A 47 6.176 20.060 -21.736 1.00 24.59 C ATOM 385 C VAL A 47 7.005 19.084 -20.890 1.00 23.40 C ATOM 386 O VAL A 47 7.624 19.480 -19.898 1.00 22.78 O ATOM 387 CB VAL A 47 7.089 20.769 -22.764 1.00 24.55 C ATOM 388 CG1 VAL A 47 7.815 19.757 -23.636 1.00 24.21 C ATOM 389 CG2 VAL A 47 6.278 21.729 -23.627 1.00 24.73 C ATOM 390 N SER A 48 7.014 17.809 -21.285 1.00 22.13 N ATOM 391 CA SER A 48 7.705 16.770 -20.517 1.00 21.05 C ATOM 392 C SER A 48 9.215 17.004 -20.477 1.00 20.24 C ATOM 393 O SER A 48 9.762 17.685 -21.343 1.00 19.33 O ATOM 394 CB SER A 48 7.436 15.388 -21.109 1.00 21.08 C ATOM 395 OG SER A 48 8.035 15.252 -22.386 1.00 21.24 O ATOM 396 N ARG A 49 9.869 16.415 -19.477 1.00 19.54 N ATOM 397 CA ARG A 49 11.328 16.516 -19.325 1.00 19.34 C ATOM 398 C ARG A 49 12.052 16.046 -20.578 1.00 18.60 C ATOM 399 O ARG A 49 13.016 16.676 -21.024 1.00 18.32 O ATOM 400 CB ARG A 49 11.819 15.676 -18.143 1.00 19.77 C ATOM 401 CG ARG A 49 13.230 16.042 -17.678 1.00 21.18 C ATOM 402 CD ARG A 49 13.891 14.969 -16.818 1.00 24.20 C ATOM 403 NE ARG A 49 12.947 14.052 -16.179 1.00 27.55 N ATOM 404 CZ ARG A 49 12.240 14.316 -15.078 1.00 29.92 C ATOM 405 NH1 ARG A 49 12.331 15.489 -14.462 1.00 30.52 N1+ ATOM 406 NH2 ARG A 49 11.417 13.396 -14.594 1.00 31.23 N ATOM 407 N GLU A 50 11.591 14.925 -21.122 1.00 17.95 N ATOM 408 CA GLU A 50 12.225 14.306 -22.281 1.00 17.81 C ATOM 409 C GLU A 50 12.036 15.172 -23.537 1.00 17.18 C ATOM 410 O GLU A 50 12.999 15.402 -24.287 1.00 16.73 O ATOM 411 CB GLU A 50 11.687 12.881 -22.493 1.00 18.09 C ATOM 412 CG GLU A 50 12.226 11.829 -21.498 1.00 19.58 C ATOM 413 CD GLU A 50 11.726 11.999 -20.055 1.00 21.69 C ATOM 414 OE1 GLU A 50 10.560 12.421 -19.847 1.00 22.60 O ATOM 415 OE2 GLU A 50 12.508 11.698 -19.118 1.00 23.71 O1- ATOM 416 N ASP A 51 10.813 15.664 -23.756 1.00 16.65 N ATOM 417 CA ASP A 51 10.523 16.545 -24.898 1.00 16.80 C ATOM 418 C ASP A 51 11.255 17.886 -24.775 1.00 16.25 C ATOM 419 O ASP A 51 11.718 18.440 -25.780 1.00 15.94 O ATOM 420 CB ASP A 51 9.012 16.800 -25.045 1.00 17.00 C ATOM 421 CG ASP A 51 8.247 15.610 -25.622 1.00 19.29 C ATOM 422 OD1 ASP A 51 6.998 15.657 -25.567 1.00 22.52 O ATOM 423 OD2 ASP A 51 8.858 14.647 -26.143 1.00 22.14 O1- ATOM 424 N SER A 52 11.345 18.399 -23.545 1.00 15.75 N ATOM 425 CA SER A 52 12.080 19.620 -23.248 1.00 15.36 C ATOM 426 C SER A 52 13.563 19.445 -23.580 1.00 14.59 C ATOM 427 O SER A 52 14.163 20.311 -24.213 1.00 13.85 O ATOM 428 CB SER A 52 11.914 20.016 -21.771 1.00 15.89 C ATOM 429 OG SER A 52 10.558 20.298 -21.457 1.00 16.39 O ATOM 430 N LEU A 53 14.146 18.322 -23.164 1.00 13.34 N ATOM 431 CA LEU A 53 15.565 18.064 -23.442 1.00 13.44 C ATOM 432 C LEU A 53 15.810 18.027 -24.943 1.00 13.33 C ATOM 433 O LEU A 53 16.804 18.566 -25.428 1.00 13.25 O ATOM 434 CB LEU A 53 16.033 16.749 -22.804 1.00 13.25 C ATOM 435 CG LEU A 53 17.441 16.260 -23.173 1.00 13.40 C ATOM 436 CD1 LEU A 53 18.492 17.274 -22.788 1.00 13.85 C ATOM 437 CD2 LEU A 53 17.739 14.917 -22.508 1.00 12.81 C ATOM 438 N GLN A 54 14.910 17.379 -25.679 1.00 13.63 N ATOM 439 CA GLN A 54 15.039 17.345 -27.128 1.00 13.96 C ATOM 440 C GLN A 54 15.029 18.757 -27.725 1.00 13.75 C ATOM 441 O GLN A 54 15.794 19.038 -28.643 1.00 13.36 O ATOM 442 CB GLN A 54 13.938 16.498 -27.777 1.00 14.32 C ATOM 443 CG GLN A 54 14.176 16.284 -29.259 1.00 16.15 C ATOM 444 CD GLN A 54 15.511 15.626 -29.522 1.00 17.21 C ATOM 445 NE2 GLN A 54 16.395 16.311 -30.256 1.00 18.54 N ATOM 446 OE1 GLN A 54 15.759 14.522 -29.046 1.00 21.53 O ATOM 447 N LYS A 55 14.171 19.633 -27.208 1.00 14.23 N ATOM 448 CA LYS A 55 14.134 21.027 -27.672 1.00 14.48 C ATOM 449 C LYS A 55 15.458 21.763 -27.407 1.00 14.41 C ATOM 450 O LYS A 55 15.867 22.601 -28.208 1.00 14.52 O ATOM 451 CB LYS A 55 12.958 21.786 -27.054 1.00 14.83 C ATOM 452 CG LYS A 55 11.590 21.333 -27.557 1.00 16.26 C ATOM 453 CD LYS A 55 10.473 21.944 -26.737 1.00 19.64 C ATOM 454 CE LYS A 55 9.116 21.371 -27.102 1.00 21.22 C ATOM 455 NZ LYS A 55 8.692 21.762 -28.475 1.00 22.55 N1+ ATOM 456 N ILE A 56 16.124 21.430 -26.299 1.00 14.29 N ATOM 457 CA AILE A 56 17.414 22.033 -25.980 0.50 14.24 C ATOM 458 CA BILE A 56 17.429 22.006 -25.950 0.50 14.30 C ATOM 459 C ILE A 56 18.501 21.525 -26.922 1.00 14.02 C ATOM 460 O ILE A 56 19.297 22.314 -27.434 1.00 14.04 O ATOM 461 CB AILE A 56 17.794 21.803 -24.507 0.50 14.16 C ATOM 462 CB BILE A 56 17.860 21.630 -24.503 0.50 14.35 C ATOM 463 CG1AILE A 56 16.771 22.508 -23.618 0.50 14.00 C ATOM 464 CG1BILE A 56 16.936 22.277 -23.464 0.50 14.45 C ATOM 465 CG2AILE A 56 19.200 22.330 -24.219 0.50 14.38 C ATOM 466 CG2BILE A 56 19.308 22.050 -24.243 0.50 14.33 C ATOM 467 CD1AILE A 56 17.164 22.602 -22.195 0.50 12.71 C ATOM 468 CD1BILE A 56 17.214 23.745 -23.211 0.50 15.00 C ATOM 469 N LEU A 57 18.536 20.219 -27.165 1.00 13.89 N ATOM 470 CA LEU A 57 19.486 19.660 -28.120 1.00 13.59 C ATOM 471 C LEU A 57 19.274 20.243 -29.523 1.00 13.83 C ATOM 472 O LEU A 57 20.243 20.470 -30.249 1.00 13.41 O ATOM 473 CB LEU A 57 19.389 18.129 -28.163 1.00 13.75 C ATOM 474 CG LEU A 57 19.732 17.383 -26.869 1.00 13.59 C ATOM 475 CD1 LEU A 57 19.458 15.895 -27.037 1.00 15.00 C ATOM 476 CD2 LEU A 57 21.183 17.628 -26.448 1.00 14.05 C ATOM 477 N ASP A 58 18.013 20.489 -29.883 1.00 14.00 N ATOM 478 CA ASP A 58 17.656 21.087 -31.177 1.00 14.80 C ATOM 479 C ASP A 58 18.233 22.497 -31.388 1.00 14.85 C ATOM 480 O ASP A 58 18.485 22.898 -32.534 1.00 14.88 O ATOM 481 CB ASP A 58 16.131 21.120 -31.367 1.00 14.80 C ATOM 482 CG ASP A 58 15.513 19.726 -31.551 1.00 15.85 C ATOM 483 OD1 ASP A 58 16.241 18.732 -31.760 1.00 16.15 O ATOM 484 OD2 ASP A 58 14.269 19.621 -31.481 1.00 19.09 O1- ATOM 485 N LEU A 59 18.455 23.243 -30.304 1.00 14.91 N ATOM 486 CA LEU A 59 19.131 24.546 -30.395 1.00 15.03 C ATOM 487 C LEU A 59 20.521 24.459 -31.034 1.00 15.12 C ATOM 488 O LEU A 59 21.000 25.448 -31.602 1.00 14.73 O ATOM 489 CB LEU A 59 19.254 25.219 -29.019 1.00 14.81 C ATOM 490 CG LEU A 59 17.968 25.706 -28.352 1.00 14.83 C ATOM 491 CD1 LEU A 59 18.231 26.030 -26.885 1.00 14.30 C ATOM 492 CD2 LEU A 59 17.402 26.924 -29.088 1.00 15.29 C ATOM 493 N ALA A 60 21.166 23.298 -30.928 1.00 15.38 N ATOM 494 CA ALA A 60 22.486 23.082 -31.524 1.00 15.62 C ATOM 495 C ALA A 60 22.468 21.950 -32.555 1.00 15.88 C ATOM 496 O ALA A 60 23.517 21.391 -32.877 1.00 15.34 O ATOM 497 CB ALA A 60 23.509 22.787 -30.431 1.00 15.67 C ATOM 498 N ASP A 61 21.279 21.639 -33.077 1.00 16.35 N ATOM 499 CA ASP A 61 21.068 20.519 -34.004 1.00 17.32 C ATOM 500 C ASP A 61 21.782 19.241 -33.547 1.00 17.93 C ATOM 501 O ASP A 61 22.346 18.509 -34.365 1.00 17.82 O ATOM 502 CB ASP A 61 21.511 20.910 -35.428 1.00 17.18 C ATOM 503 CG ASP A 61 20.785 20.120 -36.521 1.00 18.38 C ATOM 504 OD1 ASP A 61 21.359 19.963 -37.621 1.00 19.82 O ATOM 505 OD2 ASP A 61 19.644 19.663 -36.296 1.00 18.32 O1- ATOM 506 N LYS A 62 21.735 18.978 -32.238 1.00 18.97 N ATOM 507 CA LYS A 62 22.553 17.937 -31.608 1.00 19.55 C ATOM 508 C LYS A 62 21.809 16.612 -31.463 1.00 19.79 C ATOM 509 O LYS A 62 20.625 16.580 -31.110 1.00 19.39 O ATOM 510 CB LYS A 62 23.048 18.417 -30.235 1.00 20.05 C ATOM 511 CG LYS A 62 24.130 17.546 -29.594 1.00 21.68 C ATOM 512 CD LYS A 62 24.778 18.241 -28.388 1.00 23.98 C ATOM 513 CE LYS A 62 26.146 17.659 -28.024 1.00 25.74 C ATOM 514 NZ LYS A 62 26.059 16.523 -27.066 1.00 26.42 N1+ ATOM 515 N LYS A 63 22.529 15.529 -31.752 1.00 20.07 N ATOM 516 CA LYS A 63 22.039 14.163 -31.595 1.00 20.62 C ATOM 517 C LYS A 63 22.876 13.486 -30.519 1.00 19.99 C ATOM 518 O LYS A 63 24.088 13.695 -30.451 1.00 20.20 O ATOM 519 CB LYS A 63 22.165 13.391 -32.921 1.00 21.08 C ATOM 520 CG LYS A 63 21.888 14.215 -34.185 1.00 22.80 C ATOM 521 CD LYS A 63 20.464 14.765 -34.234 1.00 24.17 C ATOM 522 CE LYS A 63 20.248 15.660 -35.458 1.00 24.82 C ATOM 523 NZ LYS A 63 19.061 16.561 -35.302 1.00 24.88 N1+ ATOM 524 N VAL A 64 22.235 12.706 -29.651 1.00 19.51 N ATOM 525 CA VAL A 64 22.961 11.905 -28.653 1.00 18.96 C ATOM 526 C VAL A 64 22.404 10.486 -28.585 1.00 18.36 C ATOM 527 O VAL A 64 21.305 10.220 -29.077 1.00 18.41 O ATOM 528 CB VAL A 64 22.899 12.545 -27.238 1.00 18.99 C ATOM 529 CG1 VAL A 64 23.492 13.942 -27.254 1.00 19.53 C ATOM 530 CG2 VAL A 64 21.474 12.580 -26.725 1.00 19.35 C ATOM 531 N SER A 65 23.152 9.584 -27.957 1.00 17.62 N ATOM 532 CA SER A 65 22.698 8.204 -27.775 1.00 17.31 C ATOM 533 C SER A 65 21.528 8.128 -26.802 1.00 16.70 C ATOM 534 O SER A 65 21.279 9.064 -26.044 1.00 15.63 O ATOM 535 CB SER A 65 23.831 7.336 -27.242 1.00 17.13 C ATOM 536 OG SER A 65 24.140 7.677 -25.900 1.00 17.82 O ATOM 537 N ALA A 66 20.831 6.996 -26.800 1.00 16.28 N ATOM 538 CA ALA A 66 19.730 6.792 -25.858 1.00 16.54 C ATOM 539 C ALA A 66 20.226 6.884 -24.412 1.00 16.55 C ATOM 540 O ALA A 66 19.551 7.473 -23.559 1.00 15.95 O ATOM 541 CB ALA A 66 19.054 5.450 -26.104 1.00 16.59 C ATOM 542 N GLU A 67 21.400 6.305 -24.145 1.00 16.75 N ATOM 543 CA GLU A 67 21.977 6.350 -22.800 1.00 17.42 C ATOM 544 C GLU A 67 22.388 7.761 -22.407 1.00 16.88 C ATOM 545 O GLU A 67 22.134 8.177 -21.279 1.00 16.96 O ATOM 546 CB GLU A 67 23.167 5.392 -22.645 1.00 18.14 C ATOM 547 CG GLU A 67 23.690 5.293 -21.204 1.00 20.77 C ATOM 548 CD GLU A 67 22.574 5.077 -20.172 1.00 24.19 C ATOM 549 OE1 GLU A 67 21.855 4.049 -20.266 1.00 25.99 O ATOM 550 OE2 GLU A 67 22.401 5.946 -19.278 1.00 26.70 O1- ATOM 551 N GLU A 68 23.012 8.502 -23.323 1.00 16.37 N ATOM 552 CA AGLU A 68 23.414 9.879 -23.046 0.50 16.00 C ATOM 553 CA BGLU A 68 23.412 9.879 -23.019 0.50 16.17 C ATOM 554 C GLU A 68 22.185 10.757 -22.781 1.00 15.54 C ATOM 555 O GLU A 68 22.201 11.621 -21.912 1.00 15.65 O ATOM 556 CB AGLU A 68 24.253 10.441 -24.204 0.50 16.01 C ATOM 557 CB BGLU A 68 24.293 10.491 -24.117 0.50 16.33 C ATOM 558 CG AGLU A 68 25.668 9.859 -24.271 0.50 15.98 C ATOM 559 CG BGLU A 68 24.617 11.975 -23.871 0.50 17.00 C ATOM 560 CD AGLU A 68 26.387 10.148 -25.586 0.50 16.31 C ATOM 561 CD BGLU A 68 25.825 12.472 -24.639 0.50 18.57 C ATOM 562 OE1AGLU A 68 25.724 10.460 -26.599 0.50 15.93 O ATOM 563 OE1BGLU A 68 26.276 11.774 -25.569 0.50 19.48 O ATOM 564 OE2AGLU A 68 27.635 10.062 -25.602 0.50 17.26 O1- ATOM 565 OE2BGLU A 68 26.319 13.576 -24.312 0.50 20.54 O1- ATOM 566 N PHE A 69 21.123 10.527 -23.546 1.00 14.54 N ATOM 567 CA PHE A 69 19.884 11.292 -23.403 1.00 13.86 C ATOM 568 C PHE A 69 19.288 11.073 -22.005 1.00 13.35 C ATOM 569 O PHE A 69 18.908 12.022 -21.325 1.00 12.78 O ATOM 570 CB PHE A 69 18.899 10.869 -24.491 1.00 13.90 C ATOM 571 CG PHE A 69 17.676 11.723 -24.581 1.00 14.51 C ATOM 572 CD1 PHE A 69 17.647 12.823 -25.432 1.00 14.31 C ATOM 573 CD2 PHE A 69 16.545 11.426 -23.840 1.00 15.05 C ATOM 574 CE1 PHE A 69 16.518 13.604 -25.535 1.00 15.12 C ATOM 575 CE2 PHE A 69 15.411 12.214 -23.939 1.00 15.15 C ATOM 576 CZ PHE A 69 15.402 13.306 -24.784 1.00 14.45 C ATOM 577 N LYS A 70 19.231 9.813 -21.587 1.00 12.73 N ATOM 578 CA LYS A 70 18.779 9.450 -20.234 1.00 12.99 C ATOM 579 C LYS A 70 19.595 10.136 -19.143 1.00 12.32 C ATOM 580 O LYS A 70 19.041 10.611 -18.154 1.00 12.21 O ATOM 581 CB LYS A 70 18.871 7.936 -20.045 1.00 12.97 C ATOM 582 CG LYS A 70 18.185 7.397 -18.792 1.00 14.40 C ATOM 583 CD LYS A 70 18.250 5.876 -18.752 1.00 15.64 C ATOM 584 CE LYS A 70 17.612 5.319 -17.491 1.00 16.83 C ATOM 585 NZ LYS A 70 17.626 3.832 -17.469 1.00 17.12 N1+ ATOM 586 N GLU A 71 20.915 10.159 -19.314 1.00 13.09 N ATOM 587 CA GLU A 71 21.808 10.778 -18.337 1.00 13.22 C ATOM 588 C GLU A 71 21.618 12.294 -18.273 1.00 12.64 C ATOM 589 O GLU A 71 21.614 12.868 -17.187 1.00 12.37 O ATOM 590 CB GLU A 71 23.273 10.419 -18.644 1.00 14.14 C ATOM 591 CG GLU A 71 24.310 11.033 -17.697 1.00 16.98 C ATOM 592 CD GLU A 71 24.139 10.644 -16.231 1.00 20.82 C ATOM 593 OE1 GLU A 71 23.454 9.636 -15.924 1.00 23.47 O ATOM 594 OE2 GLU A 71 24.715 11.353 -15.370 1.00 24.30 O1- ATOM 595 N LEU A 72 21.448 12.932 -19.428 1.00 11.98 N ATOM 596 CA LEU A 72 21.187 14.373 -19.461 1.00 11.86 C ATOM 597 C LEU A 72 19.872 14.723 -18.772 1.00 11.78 C ATOM 598 O LEU A 72 19.806 15.719 -18.040 1.00 11.61 O ATOM 599 CB LEU A 72 21.203 14.911 -20.896 1.00 11.65 C ATOM 600 CG LEU A 72 22.591 14.979 -21.533 1.00 11.30 C ATOM 601 CD1 LEU A 72 22.481 15.275 -23.030 1.00 10.37 C ATOM 602 CD2 LEU A 72 23.478 16.017 -20.844 1.00 10.89 C ATOM 603 N ALA A 73 18.833 13.930 -19.021 1.00 12.01 N ATOM 604 CA ALA A 73 17.540 14.134 -18.361 1.00 12.28 C ATOM 605 C ALA A 73 17.682 14.014 -16.841 1.00 12.76 C ATOM 606 O ALA A 73 17.093 14.798 -16.087 1.00 13.44 O ATOM 607 CB ALA A 73 16.508 13.160 -18.883 1.00 12.24 C ATOM 608 N LYS A 74 18.480 13.049 -16.396 1.00 13.24 N ATOM 609 CA LYS A 74 18.742 12.868 -14.967 1.00 13.46 C ATOM 610 C LYS A 74 19.477 14.078 -14.384 1.00 13.80 C ATOM 611 O LYS A 74 19.090 14.603 -13.333 1.00 13.13 O ATOM 612 CB LYS A 74 19.542 11.588 -14.732 1.00 13.90 C ATOM 613 CG LYS A 74 19.915 11.350 -13.273 1.00 15.10 C ATOM 614 CD LYS A 74 21.112 10.438 -13.136 1.00 18.00 C ATOM 615 CE LYS A 74 21.517 10.280 -11.670 1.00 18.05 C ATOM 616 NZ LYS A 74 22.359 11.417 -11.211 1.00 19.33 N1+ ATOM 617 N ARG A 75 20.531 14.516 -15.072 1.00 13.59 N ATOM 618 CA ARG A 75 21.289 15.699 -14.659 1.00 14.10 C ATOM 619 C ARG A 75 20.412 16.951 -14.551 1.00 13.40 C ATOM 620 O ARG A 75 20.557 17.739 -13.616 1.00 13.31 O ATOM 621 CB ARG A 75 22.468 15.965 -15.610 1.00 14.43 C ATOM 622 CG ARG A 75 23.586 14.948 -15.543 1.00 17.71 C ATOM 623 CD ARG A 75 24.811 15.468 -16.297 1.00 21.61 C ATOM 624 NE ARG A 75 25.336 14.490 -17.240 1.00 25.73 N ATOM 625 CZ ARG A 75 26.096 14.785 -18.294 1.00 27.88 C ATOM 626 NH1 ARG A 75 26.449 16.041 -18.561 1.00 29.18 N1+ ATOM 627 NH2 ARG A 75 26.509 13.808 -19.094 1.00 29.42 N ATOM 628 N LYS A 76 19.487 17.140 -15.489 1.00 12.93 N ATOM 629 CA LYS A 76 18.579 18.276 -15.389 1.00 12.66 C ATOM 630 C LYS A 76 17.751 18.173 -14.115 1.00 12.54 C ATOM 631 O LYS A 76 17.544 19.161 -13.419 1.00 12.15 O ATOM 632 CB LYS A 76 17.643 18.379 -16.585 1.00 12.59 C ATOM 633 CG LYS A 76 16.697 19.593 -16.500 1.00 12.94 C ATOM 634 CD LYS A 76 15.332 19.211 -15.930 1.00 13.09 C ATOM 635 CE LYS A 76 14.550 20.414 -15.468 1.00 14.58 C ATOM 636 NZ LYS A 76 13.180 19.988 -15.108 1.00 14.80 N1+ ATOM 637 N ASN A 77 17.262 16.975 -13.823 1.00 12.41 N ATOM 638 CA ASN A 77 16.478 16.788 -12.610 1.00 13.06 C ATOM 639 C ASN A 77 17.312 17.040 -11.361 1.00 12.68 C ATOM 640 O ASN A 77 16.831 17.648 -10.411 1.00 13.29 O ATOM 641 CB ASN A 77 15.857 15.397 -12.548 1.00 13.13 C ATOM 642 CG ASN A 77 14.861 15.268 -11.412 1.00 14.89 C ATOM 643 ND2 ASN A 77 15.129 14.350 -10.495 1.00 16.42 N ATOM 644 OD1 ASN A 77 13.873 16.005 -11.351 1.00 17.34 O ATOM 645 N ASP A 78 18.568 16.603 -11.371 1.00 13.08 N ATOM 646 CA ASP A 78 19.476 16.877 -10.255 1.00 13.03 C ATOM 647 C ASP A 78 19.646 18.402 -10.087 1.00 12.83 C ATOM 648 O ASP A 78 19.607 18.927 -8.970 1.00 12.61 O ATOM 649 CB ASP A 78 20.842 16.207 -10.477 1.00 13.36 C ATOM 650 CG ASP A 78 20.766 14.679 -10.522 1.00 14.77 C ATOM 651 OD1 ASP A 78 19.806 14.081 -9.981 1.00 16.36 O ATOM 652 OD2 ASP A 78 21.687 14.070 -11.103 1.00 16.32 O1- ATOM 653 N ASN A 79 19.814 19.111 -11.203 1.00 12.44 N ATOM 654 CA ASN A 79 19.872 20.576 -11.188 1.00 12.68 C ATOM 655 C ASN A 79 18.595 21.194 -10.602 1.00 12.60 C ATOM 656 O ASN A 79 18.661 22.114 -9.782 1.00 13.18 O ATOM 657 CB ASN A 79 20.091 21.143 -12.605 1.00 12.73 C ATOM 658 CG ASN A 79 21.468 20.824 -13.183 1.00 13.24 C ATOM 659 ND2 ASN A 79 22.342 20.244 -12.378 1.00 11.29 N ATOM 660 OD1 ASN A 79 21.729 21.101 -14.363 1.00 15.79 O ATOM 661 N TYR A 80 17.443 20.705 -11.039 1.00 12.63 N ATOM 662 CA TYR A 80 16.155 21.234 -10.580 1.00 12.42 C ATOM 663 C TYR A 80 16.031 21.104 -9.058 1.00 12.24 C ATOM 664 O TYR A 80 15.706 22.075 -8.383 1.00 11.55 O ATOM 665 CB TYR A 80 14.996 20.531 -11.286 1.00 12.38 C ATOM 666 CG TYR A 80 13.624 21.001 -10.846 1.00 12.36 C ATOM 667 CD1 TYR A 80 13.149 22.260 -11.206 1.00 12.68 C ATOM 668 CD2 TYR A 80 12.803 20.192 -10.065 1.00 12.90 C ATOM 669 CE1 TYR A 80 11.889 22.696 -10.813 1.00 12.92 C ATOM 670 CE2 TYR A 80 11.544 20.622 -9.667 1.00 11.89 C ATOM 671 CZ TYR A 80 11.095 21.877 -10.046 1.00 11.71 C ATOM 672 OH TYR A 80 9.847 22.323 -9.656 1.00 12.83 O ATOM 673 N VAL A 81 16.327 19.915 -8.530 1.00 12.30 N ATOM 674 CA VAL A 81 16.338 19.685 -7.079 1.00 12.47 C ATOM 675 C VAL A 81 17.236 20.689 -6.335 1.00 12.69 C ATOM 676 O VAL A 81 16.844 21.212 -5.286 1.00 12.06 O ATOM 677 CB VAL A 81 16.780 18.250 -6.735 1.00 12.70 C ATOM 678 CG1 VAL A 81 17.034 18.089 -5.218 1.00 13.25 C ATOM 679 CG2 VAL A 81 15.733 17.247 -7.212 1.00 12.78 C ATOM 680 N LYS A 82 18.430 20.960 -6.870 1.00 12.94 N ATOM 681 CA LYS A 82 19.290 22.020 -6.315 1.00 13.67 C ATOM 682 C LYS A 82 18.622 23.390 -6.376 1.00 13.19 C ATOM 683 O LYS A 82 18.669 24.137 -5.404 1.00 12.84 O ATOM 684 CB LYS A 82 20.640 22.108 -7.042 1.00 14.13 C ATOM 685 CG LYS A 82 21.571 20.950 -6.789 1.00 16.97 C ATOM 686 CD LYS A 82 22.870 21.121 -7.544 1.00 20.23 C ATOM 687 CE LYS A 82 23.749 19.893 -7.407 1.00 22.51 C ATOM 688 NZ LYS A 82 25.064 20.116 -8.060 1.00 24.35 N1+ ATOM 689 N MET A 83 18.006 23.723 -7.509 1.00 13.08 N ATOM 690 CA MET A 83 17.451 25.064 -7.689 1.00 13.23 C ATOM 691 C MET A 83 16.292 25.319 -6.728 1.00 12.87 C ATOM 692 O MET A 83 16.167 26.425 -6.195 1.00 13.48 O ATOM 693 CB MET A 83 16.991 25.299 -9.131 1.00 13.26 C ATOM 694 CG MET A 83 18.082 25.224 -10.181 1.00 15.30 C ATOM 695 SD MET A 83 19.512 26.253 -9.837 1.00 18.31 S ATOM 696 CE MET A 83 20.627 25.582 -11.083 1.00 19.67 C ATOM 697 N ILE A 84 15.470 24.295 -6.484 1.00 12.33 N ATOM 698 CA ILE A 84 14.261 24.461 -5.653 1.00 11.87 C ATOM 699 C ILE A 84 14.564 24.539 -4.150 1.00 11.51 C ATOM 700 O ILE A 84 13.683 24.847 -3.356 1.00 10.16 O ATOM 701 CB ILE A 84 13.161 23.400 -5.953 1.00 11.80 C ATOM 702 CG1 ILE A 84 13.667 21.972 -5.713 1.00 12.66 C ATOM 703 CG2 ILE A 84 12.629 23.569 -7.391 1.00 12.25 C ATOM 704 CD1 ILE A 84 12.584 20.930 -5.807 1.00 11.62 C ATOM 705 N GLN A 85 15.812 24.312 -3.753 1.00 11.65 N ATOM 706 CA GLN A 85 16.211 24.625 -2.381 1.00 12.16 C ATOM 707 C GLN A 85 15.955 26.105 -2.042 1.00 12.39 C ATOM 708 O GLN A 85 15.736 26.444 -0.876 1.00 13.19 O ATOM 709 CB GLN A 85 17.692 24.284 -2.143 1.00 12.15 C ATOM 710 CG GLN A 85 18.094 22.836 -2.456 1.00 11.84 C ATOM 711 CD GLN A 85 17.289 21.799 -1.701 1.00 11.31 C ATOM 712 NE2 GLN A 85 16.650 20.902 -2.442 1.00 12.42 N ATOM 713 OE1 GLN A 85 17.239 21.798 -0.468 1.00 11.97 O ATOM 714 N ASP A 86 15.982 26.978 -3.051 1.00 12.63 N ATOM 715 CA ASP A 86 15.780 28.419 -2.840 1.00 13.43 C ATOM 716 C ASP A 86 14.307 28.849 -2.807 1.00 13.14 C ATOM 717 O ASP A 86 14.018 30.022 -2.550 1.00 13.10 O ATOM 718 CB ASP A 86 16.516 29.240 -3.907 1.00 13.56 C ATOM 719 CG ASP A 86 18.017 29.142 -3.793 1.00 16.16 C ATOM 720 OD1 ASP A 86 18.688 29.352 -4.827 1.00 20.59 O ATOM 721 OD2 ASP A 86 18.527 28.849 -2.691 1.00 18.85 O1- ATOM 722 N VAL A 87 13.389 27.918 -3.056 1.00 13.12 N ATOM 723 CA VAL A 87 11.953 28.189 -2.903 1.00 12.49 C ATOM 724 C VAL A 87 11.687 28.616 -1.448 1.00 12.27 C ATOM 725 O VAL A 87 12.318 28.110 -0.515 1.00 11.89 O ATOM 726 CB VAL A 87 11.091 26.953 -3.304 1.00 12.84 C ATOM 727 CG1 VAL A 87 9.621 27.201 -3.001 1.00 12.46 C ATOM 728 CG2 VAL A 87 11.254 26.633 -4.785 1.00 12.40 C ATOM 729 N GLY A 88 10.789 29.581 -1.262 1.00 0.00 N ATOM 730 CA GLY A 88 10.482 30.137 0.053 1.00 0.00 C ATOM 731 C GLY A 88 9.049 30.608 0.120 1.00 0.00 C ATOM 732 O GLY A 88 8.354 30.613 -0.919 1.00 0.00 O ATOM 733 N GLY A 89 8.549 31.075 1.280 1.00 0.00 N ATOM 734 CA GLY A 89 7.195 31.609 1.383 1.00 0.00 C ATOM 735 C GLY A 89 7.007 32.789 0.460 1.00 0.00 C ATOM 736 O GLY A 89 5.819 33.136 0.139 1.00 0.00 O ATOM 737 N GLY A 90 8.035 33.473 -0.026 1.00 0.00 N ATOM 738 CA GLY A 90 7.935 34.565 -0.990 1.00 0.00 C ATOM 739 C GLY A 90 7.463 34.060 -2.332 1.00 0.00 C ATOM 740 O GLY A 90 6.996 34.864 -3.153 1.00 0.00 O ATOM 741 N GLY A 91 7.542 32.759 -2.630 1.00 0.00 N ATOM 742 CA GLY A 91 7.094 32.180 -3.893 1.00 0.00 C ATOM 743 C GLY A 91 5.597 31.989 -3.899 1.00 0.00 C ATOM 744 O GLY A 91 5.012 31.775 -4.999 1.00 0.00 O ATOM 745 N VAL A 92 4.909 32.050 -2.768 1.00 11.72 N ATOM 746 CA VAL A 92 3.471 31.789 -2.707 1.00 11.98 C ATOM 747 C VAL A 92 2.700 32.881 -3.458 1.00 11.79 C ATOM 748 O VAL A 92 2.964 34.063 -3.286 1.00 11.70 O ATOM 749 CB VAL A 92 2.970 31.677 -1.244 1.00 11.86 C ATOM 750 CG1 VAL A 92 1.465 31.472 -1.205 1.00 12.16 C ATOM 751 CG2 VAL A 92 3.689 30.527 -0.512 1.00 12.37 C ATOM 752 N TYR A 93 1.743 32.470 -4.288 1.00 11.76 N ATOM 753 CA TYR A 93 0.946 33.402 -5.085 1.00 12.12 C ATOM 754 C TYR A 93 0.007 34.253 -4.221 1.00 12.22 C ATOM 755 O TYR A 93 -0.414 33.821 -3.147 1.00 11.52 O ATOM 756 CB TYR A 93 0.133 32.629 -6.127 1.00 12.43 C ATOM 757 CG TYR A 93 0.817 32.415 -7.467 1.00 13.21 C ATOM 758 CD1 TYR A 93 0.059 32.125 -8.597 1.00 15.13 C ATOM 759 CD2 TYR A 93 2.204 32.510 -7.615 1.00 14.95 C ATOM 760 CE1 TYR A 93 0.649 31.941 -9.829 1.00 14.41 C ATOM 761 CE2 TYR A 93 2.801 32.320 -8.852 1.00 14.79 C ATOM 762 CZ TYR A 93 2.011 32.040 -9.953 1.00 15.26 C ATOM 763 OH TYR A 93 2.575 31.855 -11.191 1.00 15.94 O ATOM 764 N PRO A 94 -0.333 35.469 -4.692 1.00 12.97 N ATOM 765 CA PRO A 94 -1.194 36.326 -3.882 1.00 12.79 C ATOM 766 C PRO A 94 -2.553 35.680 -3.565 1.00 12.61 C ATOM 767 O PRO A 94 -3.128 34.985 -4.416 1.00 12.71 O ATOM 768 CB PRO A 94 -1.372 37.583 -4.745 1.00 13.30 C ATOM 769 CG PRO A 94 -0.284 37.529 -5.763 1.00 14.10 C ATOM 770 CD PRO A 94 0.042 36.097 -5.971 1.00 13.13 C ATOM 771 N GLY A 95 -3.017 35.867 -2.327 1.00 11.85 N ATOM 772 CA GLY A 95 -4.335 35.396 -1.888 1.00 11.62 C ATOM 773 C GLY A 95 -4.357 33.983 -1.342 1.00 11.14 C ATOM 774 O GLY A 95 -5.252 33.617 -0.567 1.00 10.82 O ATOM 775 N ILE A 96 -3.371 33.186 -1.744 1.00 10.75 N ATOM 776 CA ILE A 96 -3.372 31.759 -1.467 1.00 10.63 C ATOM 777 C ILE A 96 -3.211 31.477 0.023 1.00 10.54 C ATOM 778 O ILE A 96 -3.939 30.642 0.568 1.00 9.85 O ATOM 779 CB ILE A 96 -2.279 31.011 -2.260 1.00 10.84 C ATOM 780 CG1 ILE A 96 -2.549 31.074 -3.768 1.00 10.40 C ATOM 781 CG2 ILE A 96 -2.200 29.552 -1.810 1.00 10.98 C ATOM 782 CD1 ILE A 96 -3.831 30.401 -4.191 1.00 10.69 C ATOM 783 N LEU A 97 -2.272 32.156 0.681 1.00 10.08 N ATOM 784 CA LEU A 97 -2.059 31.917 2.116 1.00 10.24 C ATOM 785 C LEU A 97 -3.315 32.246 2.928 1.00 9.97 C ATOM 786 O LEU A 97 -3.726 31.468 3.784 1.00 9.15 O ATOM 787 CB LEU A 97 -0.862 32.698 2.661 1.00 10.29 C ATOM 788 CG LEU A 97 -0.558 32.516 4.155 1.00 10.65 C ATOM 789 CD1 LEU A 97 -0.510 31.028 4.566 1.00 11.99 C ATOM 790 CD2 LEU A 97 0.741 33.208 4.526 1.00 10.60 C ATOM 791 N GLN A 98 -3.903 33.411 2.669 1.00 10.76 N ATOM 792 CA GLN A 98 -5.115 33.809 3.373 1.00 11.41 C ATOM 793 C GLN A 98 -6.248 32.808 3.119 1.00 11.10 C ATOM 794 O GLN A 98 -7.005 32.500 4.035 1.00 11.84 O ATOM 795 CB GLN A 98 -5.550 35.231 2.993 1.00 12.00 C ATOM 796 CG GLN A 98 -6.708 35.768 3.840 1.00 13.22 C ATOM 797 CD GLN A 98 -6.351 35.873 5.308 1.00 15.01 C ATOM 798 NE2 GLN A 98 -5.282 36.606 5.602 1.00 14.53 N ATOM 799 OE1 GLN A 98 -7.014 35.283 6.169 1.00 18.00 O ATOM 800 N LEU A 99 -6.360 32.291 1.891 1.00 10.85 N ATOM 801 CA LEU A 99 -7.385 31.292 1.575 1.00 10.37 C ATOM 802 C LEU A 99 -7.176 30.005 2.389 1.00 9.86 C ATOM 803 O LEU A 99 -8.116 29.476 2.984 1.00 9.40 O ATOM 804 CB LEU A 99 -7.395 30.950 0.075 1.00 10.22 C ATOM 805 CG LEU A 99 -8.340 29.825 -0.366 1.00 10.11 C ATOM 806 CD1 LEU A 99 -9.789 30.163 -0.046 1.00 9.39 C ATOM 807 CD2 LEU A 99 -8.188 29.495 -1.856 1.00 9.37 C ATOM 808 N LEU A 100 -5.949 29.494 2.399 1.00 9.58 N ATOM 809 CA LEU A 100 -5.631 28.296 3.177 1.00 9.44 C ATOM 810 C LEU A 100 -5.977 28.503 4.658 1.00 9.74 C ATOM 811 O LEU A 100 -6.526 27.605 5.300 1.00 10.14 O ATOM 812 CB LEU A 100 -4.153 27.916 3.029 1.00 9.27 C ATOM 813 CG LEU A 100 -3.698 27.436 1.648 1.00 9.54 C ATOM 814 CD1 LEU A 100 -2.167 27.385 1.539 1.00 8.41 C ATOM 815 CD2 LEU A 100 -4.298 26.086 1.330 1.00 9.77 C ATOM 816 N LYS A 101 -5.646 29.677 5.197 1.00 10.71 N ATOM 817 CA LYS A 101 -5.936 29.984 6.605 1.00 11.19 C ATOM 818 C LYS A 101 -7.436 29.991 6.880 1.00 11.09 C ATOM 819 O LYS A 101 -7.889 29.471 7.904 1.00 11.17 O ATOM 820 CB LYS A 101 -5.347 31.337 7.003 1.00 12.20 C ATOM 821 CG LYS A 101 -3.816 31.368 6.995 1.00 14.48 C ATOM 822 CD LYS A 101 -3.259 32.130 8.163 1.00 18.85 C ATOM 823 CE LYS A 101 -3.528 33.599 8.077 1.00 20.98 C ATOM 824 NZ LYS A 101 -2.679 34.177 7.018 1.00 24.79 N1+ ATOM 825 N ASP A 102 -8.194 30.573 5.954 1.00 11.06 N ATOM 826 CA ASP A 102 -9.654 30.703 6.087 1.00 11.52 C ATOM 827 C ASP A 102 -10.356 29.356 5.911 1.00 11.09 C ATOM 828 O ASP A 102 -11.344 29.068 6.594 1.00 11.48 O ATOM 829 CB ASP A 102 -10.213 31.729 5.090 1.00 11.62 C ATOM 830 CG ASP A 102 -9.838 33.158 5.437 1.00 14.00 C ATOM 831 OD1 ASP A 102 -10.060 34.037 4.579 1.00 15.50 O ATOM 832 OD2 ASP A 102 -9.316 33.412 6.549 1.00 17.38 O1- ATOM 833 N LEU A 103 -9.846 28.523 5.008 1.00 10.96 N ATOM 834 CA LEU A 103 -10.395 27.184 4.815 1.00 10.84 C ATOM 835 C LEU A 103 -10.170 26.352 6.074 1.00 11.54 C ATOM 836 O LEU A 103 -11.097 25.719 6.593 1.00 10.94 O ATOM 837 CB LEU A 103 -9.766 26.504 3.585 1.00 10.86 C ATOM 838 CG LEU A 103 -10.205 27.044 2.216 1.00 9.51 C ATOM 839 CD1 LEU A 103 -9.278 26.541 1.093 1.00 9.92 C ATOM 840 CD2 LEU A 103 -11.655 26.685 1.886 1.00 8.34 C ATOM 841 N ARG A 104 -8.952 26.376 6.597 1.00 11.82 N ATOM 842 CA AARG A 104 -8.666 25.541 7.749 0.50 12.52 C ATOM 843 CA BARG A 104 -8.608 25.589 7.784 0.50 12.04 C ATOM 844 C ARG A 104 -9.409 26.020 9.002 1.00 12.41 C ATOM 845 O ARG A 104 -9.907 25.187 9.754 1.00 12.51 O ATOM 846 CB AARG A 104 -7.160 25.358 7.978 0.50 12.75 C ATOM 847 CB BARG A 104 -7.117 25.702 8.108 0.50 11.97 C ATOM 848 CG AARG A 104 -6.463 26.443 8.737 0.50 14.67 C ATOM 849 CG BARG A 104 -6.722 24.991 9.413 0.50 11.70 C ATOM 850 CD AARG A 104 -5.834 25.876 10.002 0.50 16.01 C ATOM 851 CD BARG A 104 -5.221 24.982 9.639 0.50 13.02 C ATOM 852 NE AARG A 104 -4.507 25.305 9.808 0.50 17.53 N ATOM 853 NE BARG A 104 -4.872 24.423 10.946 0.50 13.89 N ATOM 854 CZ AARG A 104 -3.390 25.835 10.296 0.50 18.61 C ATOM 855 CZ BARG A 104 -4.563 23.148 11.155 0.50 15.69 C ATOM 856 NH1AARG A 104 -3.437 26.959 10.998 0.50 20.13 N1+ ATOM 857 NH1BARG A 104 -4.557 22.291 10.146 0.50 16.61 N1+ ATOM 858 NH2AARG A 104 -2.225 25.240 10.085 0.50 18.94 N ATOM 859 NH2BARG A 104 -4.261 22.728 12.376 0.50 16.52 N ATOM 860 N SER A 105 -9.520 27.339 9.200 1.00 12.32 N ATOM 861 CA SER A 105 -10.210 27.872 10.385 1.00 13.28 C ATOM 862 C SER A 105 -11.704 27.576 10.328 1.00 13.80 C ATOM 863 O SER A 105 -12.363 27.471 11.377 1.00 14.04 O ATOM 864 CB SER A 105 -9.961 29.377 10.559 1.00 13.67 C ATOM 865 OG SER A 105 -10.663 30.140 9.602 1.00 13.72 O ATOM 866 N ASN A 106 -12.232 27.415 9.114 1.00 13.93 N ATOM 867 CA ASN A 106 -13.626 27.026 8.916 1.00 14.50 C ATOM 868 C ASN A 106 -13.848 25.511 8.769 1.00 14.52 C ATOM 869 O ASN A 106 -14.948 25.065 8.438 1.00 15.61 O ATOM 870 CB ASN A 106 -14.202 27.779 7.725 1.00 14.59 C ATOM 871 CG ASN A 106 -14.520 29.211 8.065 1.00 15.18 C ATOM 872 ND2 ASN A 106 -13.625 30.119 7.721 1.00 12.67 N ATOM 873 OD1 ASN A 106 -15.562 29.492 8.660 1.00 17.58 O ATOM 874 N LYS A 107 -12.804 24.730 9.034 1.00 14.74 N ATOM 875 CA LYS A 107 -12.876 23.265 9.034 1.00 14.61 C ATOM 876 C LYS A 107 -13.241 22.685 7.665 1.00 14.30 C ATOM 877 O LYS A 107 -13.897 21.647 7.569 1.00 14.97 O ATOM 878 CB LYS A 107 -13.851 22.770 10.118 1.00 15.01 C ATOM 879 CG LYS A 107 -13.523 23.277 11.514 1.00 16.35 C ATOM 880 CD LYS A 107 -12.264 22.588 12.033 1.00 17.14 C ATOM 881 CE LYS A 107 -11.699 23.243 13.259 1.00 18.05 C ATOM 882 NZ LYS A 107 -10.343 22.699 13.568 1.00 17.36 N1+ ATOM 883 N ILE A 108 -12.795 23.363 6.612 1.00 13.08 N ATOM 884 CA ILE A 108 -12.909 22.866 5.250 1.00 12.23 C ATOM 885 C ILE A 108 -11.596 22.162 4.885 1.00 11.86 C ATOM 886 O ILE A 108 -10.498 22.687 5.122 1.00 11.47 O ATOM 887 CB ILE A 108 -13.208 24.019 4.262 1.00 12.17 C ATOM 888 CG1 ILE A 108 -14.552 24.691 4.614 1.00 12.67 C ATOM 889 CG2 ILE A 108 -13.213 23.508 2.823 1.00 12.17 C ATOM 890 CD1 ILE A 108 -14.815 25.992 3.863 1.00 11.93 C ATOM 891 N LYS A 109 -11.715 20.966 4.315 1.00 11.61 N ATOM 892 CA LYS A 109 -10.558 20.130 4.005 1.00 11.65 C ATOM 893 C LYS A 109 -9.756 20.696 2.843 1.00 10.66 C ATOM 894 O LYS A 109 -10.314 21.307 1.929 1.00 10.31 O ATOM 895 CB LYS A 109 -11.006 18.712 3.658 1.00 12.38 C ATOM 896 CG LYS A 109 -11.797 18.011 4.744 1.00 14.95 C ATOM 897 CD LYS A 109 -10.929 17.809 5.970 1.00 17.28 C ATOM 898 CE LYS A 109 -11.605 16.961 7.003 1.00 20.61 C ATOM 899 NZ LYS A 109 -10.680 16.721 8.127 1.00 21.62 N1+ ATOM 900 N ILE A 110 -8.451 20.445 2.872 1.00 10.50 N ATOM 901 CA ILE A 110 -7.505 20.991 1.892 1.00 9.98 C ATOM 902 C ILE A 110 -6.626 19.859 1.390 1.00 9.87 C ATOM 903 O ILE A 110 -6.004 19.160 2.188 1.00 9.26 O ATOM 904 CB ILE A 110 -6.615 22.070 2.540 1.00 10.13 C ATOM 905 CG1 ILE A 110 -7.446 23.299 2.916 1.00 10.71 C ATOM 906 CG2 ILE A 110 -5.453 22.511 1.596 1.00 9.58 C ATOM 907 CD1 ILE A 110 -6.801 24.154 3.972 1.00 11.85 C ATOM 908 N ALA A 111 -6.587 19.668 0.073 1.00 9.21 N ATOM 909 CA ALA A 111 -5.749 18.629 -0.526 1.00 9.76 C ATOM 910 C ALA A 111 -4.998 19.137 -1.746 1.00 10.23 C ATOM 911 O ALA A 111 -5.460 20.058 -2.434 1.00 10.18 O ATOM 912 CB ALA A 111 -6.593 17.416 -0.899 1.00 9.85 C ATOM 913 N LEU A 112 -3.835 18.541 -1.998 1.00 10.50 N ATOM 914 CA LEU A 112 -3.051 18.842 -3.180 1.00 10.30 C ATOM 915 C LEU A 112 -3.325 17.816 -4.270 1.00 10.83 C ATOM 916 O LEU A 112 -3.305 16.606 -4.019 1.00 10.94 O ATOM 917 CB LEU A 112 -1.558 18.844 -2.849 1.00 10.17 C ATOM 918 CG LEU A 112 -0.702 19.538 -3.904 1.00 9.39 C ATOM 919 CD1 LEU A 112 -0.894 21.052 -3.883 1.00 8.46 C ATOM 920 CD2 LEU A 112 0.776 19.175 -3.716 1.00 9.22 C ATOM 921 N ALA A 113 -3.566 18.323 -5.480 1.00 11.53 N ATOM 922 CA ALA A 113 -3.821 17.509 -6.670 1.00 11.97 C ATOM 923 C ALA A 113 -2.903 17.989 -7.793 1.00 12.58 C ATOM 924 O ALA A 113 -3.351 18.492 -8.834 1.00 13.26 O ATOM 925 CB ALA A 113 -5.303 17.606 -7.077 1.00 11.87 C ATOM 926 N SER A 114 -1.602 17.834 -7.554 1.00 12.61 N ATOM 927 CA SER A 114 -0.555 18.337 -8.437 1.00 13.01 C ATOM 928 C SER A 114 0.194 17.220 -9.173 1.00 13.09 C ATOM 929 O SER A 114 0.378 16.119 -8.630 1.00 13.48 O ATOM 930 CB SER A 114 0.447 19.136 -7.607 1.00 12.83 C ATOM 931 OG SER A 114 1.556 19.543 -8.378 1.00 13.19 O ATOM 932 N ALA A 115 0.646 17.521 -10.394 1.00 12.94 N ATOM 933 CA ALA A 115 1.489 16.599 -11.166 1.00 12.65 C ATOM 934 C ALA A 115 2.919 16.570 -10.640 1.00 12.78 C ATOM 935 O ALA A 115 3.688 15.703 -11.022 1.00 12.78 O ATOM 936 CB ALA A 115 1.508 16.978 -12.637 1.00 12.87 C ATOM 937 N SER A 116 3.276 17.520 -9.785 1.00 12.57 N ATOM 938 CA SER A 116 4.656 17.634 -9.317 1.00 13.06 C ATOM 939 C SER A 116 5.059 16.478 -8.414 1.00 13.26 C ATOM 940 O SER A 116 4.465 16.273 -7.359 1.00 13.28 O ATOM 941 CB SER A 116 4.874 18.943 -8.563 1.00 12.82 C ATOM 942 OG SER A 116 6.219 19.033 -8.097 1.00 14.06 O ATOM 943 N LYS A 117 6.112 15.762 -8.808 1.00 14.48 N ATOM 944 CA LYS A 117 6.731 14.760 -7.939 1.00 14.81 C ATOM 945 C LYS A 117 7.513 15.384 -6.766 1.00 14.35 C ATOM 946 O LYS A 117 7.978 14.651 -5.894 1.00 15.01 O ATOM 947 CB LYS A 117 7.643 13.818 -8.739 1.00 15.38 C ATOM 948 CG LYS A 117 6.896 12.832 -9.644 1.00 17.67 C ATOM 949 CD LYS A 117 7.868 11.841 -10.295 1.00 20.86 C ATOM 950 CE LYS A 117 7.157 10.624 -10.892 1.00 22.63 C ATOM 951 NZ LYS A 117 6.716 10.834 -12.300 1.00 24.38 N1+ ATOM 952 N ASN A 118 7.637 16.713 -6.725 1.00 13.14 N ATOM 953 CA ASN A 118 8.254 17.410 -5.578 1.00 12.74 C ATOM 954 C ASN A 118 7.249 18.229 -4.758 1.00 11.93 C ATOM 955 O ASN A 118 7.626 19.150 -4.027 1.00 11.92 O ATOM 956 CB ASN A 118 9.403 18.299 -6.052 1.00 12.60 C ATOM 957 CG ASN A 118 10.496 17.508 -6.740 1.00 12.73 C ATOM 958 ND2 ASN A 118 10.505 17.546 -8.071 1.00 8.76 N ATOM 959 OD1 ASN A 118 11.317 16.851 -6.081 1.00 15.47 O ATOM 960 N GLY A 119 5.970 17.884 -4.871 1.00 11.17 N ATOM 961 CA GLY A 119 4.911 18.619 -4.181 1.00 10.60 C ATOM 962 C GLY A 119 5.106 18.813 -2.685 1.00 9.83 C ATOM 963 O GLY A 119 5.104 19.949 -2.196 1.00 10.06 O ATOM 964 N PRO A 120 5.267 17.707 -1.938 1.00 9.74 N ATOM 965 CA PRO A 120 5.443 17.802 -0.486 1.00 9.69 C ATOM 966 C PRO A 120 6.642 18.678 -0.088 1.00 9.59 C ATOM 967 O PRO A 120 6.535 19.487 0.830 1.00 9.90 O ATOM 968 CB PRO A 120 5.653 16.342 -0.067 1.00 9.44 C ATOM 969 CG PRO A 120 4.951 15.556 -1.124 1.00 9.58 C ATOM 970 CD PRO A 120 5.133 16.309 -2.387 1.00 9.63 C ATOM 971 N PHE A 121 7.760 18.528 -0.796 1.00 10.19 N ATOM 972 CA PHE A 121 8.940 19.357 -0.553 1.00 10.21 C ATOM 973 C PHE A 121 8.651 20.828 -0.820 1.00 9.76 C ATOM 974 O PHE A 121 9.022 21.688 -0.023 1.00 9.94 O ATOM 975 CB PHE A 121 10.125 18.880 -1.403 1.00 10.52 C ATOM 976 CG PHE A 121 11.312 19.798 -1.366 1.00 12.23 C ATOM 977 CD1 PHE A 121 12.241 19.727 -0.343 1.00 14.45 C ATOM 978 CD2 PHE A 121 11.497 20.737 -2.368 1.00 14.49 C ATOM 979 CE1 PHE A 121 13.340 20.579 -0.321 1.00 15.60 C ATOM 980 CE2 PHE A 121 12.583 21.592 -2.345 1.00 14.30 C ATOM 981 CZ PHE A 121 13.507 21.505 -1.332 1.00 14.00 C ATOM 982 N LEU A 122 7.975 21.115 -1.929 1.00 9.82 N ATOM 983 CA LEU A 122 7.686 22.505 -2.293 1.00 9.85 C ATOM 984 C LEU A 122 6.761 23.143 -1.251 1.00 10.11 C ATOM 985 O LEU A 122 6.975 24.286 -0.858 1.00 9.45 O ATOM 986 CB LEU A 122 7.085 22.590 -3.699 1.00 9.87 C ATOM 987 CG LEU A 122 8.103 22.320 -4.813 1.00 9.66 C ATOM 988 CD1 LEU A 122 7.426 22.049 -6.152 1.00 8.57 C ATOM 989 CD2 LEU A 122 9.094 23.470 -4.930 1.00 10.94 C ATOM 990 N LEU A 123 5.736 22.406 -0.812 1.00 10.50 N ATOM 991 CA LEU A 123 4.865 22.892 0.259 1.00 11.45 C ATOM 992 C LEU A 123 5.650 23.180 1.539 1.00 11.99 C ATOM 993 O LEU A 123 5.366 24.158 2.232 1.00 11.26 O ATOM 994 CB LEU A 123 3.723 21.914 0.543 1.00 11.47 C ATOM 995 CG LEU A 123 2.658 21.765 -0.551 1.00 11.59 C ATOM 996 CD1 LEU A 123 1.629 20.720 -0.110 1.00 11.05 C ATOM 997 CD2 LEU A 123 1.980 23.083 -0.880 1.00 11.45 C ATOM 998 N GLU A 124 6.634 22.335 1.841 1.00 12.44 N ATOM 999 CA GLU A 124 7.482 22.531 3.019 1.00 13.33 C ATOM 1000 C GLU A 124 8.308 23.808 2.889 1.00 13.07 C ATOM 1001 O GLU A 124 8.335 24.623 3.824 1.00 12.78 O ATOM 1002 CB GLU A 124 8.377 21.308 3.282 1.00 14.02 C ATOM 1003 CG GLU A 124 8.285 20.785 4.700 1.00 17.78 C ATOM 1004 CD GLU A 124 8.882 19.401 4.865 1.00 20.78 C ATOM 1005 OE1 GLU A 124 10.058 19.215 4.486 1.00 24.43 O ATOM 1006 OE2 GLU A 124 8.170 18.500 5.366 1.00 24.59 O1- ATOM 1007 N ARG A 125 8.937 24.001 1.723 1.00 12.44 N ATOM 1008 CA AARG A 125 9.722 25.209 1.419 0.50 12.39 C ATOM 1009 CA BARG A 125 9.735 25.202 1.493 0.50 12.45 C ATOM 1010 C ARG A 125 8.903 26.486 1.564 1.00 12.06 C ATOM 1011 O ARG A 125 9.407 27.524 2.000 1.00 12.05 O ATOM 1012 CB AARG A 125 10.258 25.157 -0.020 0.50 12.37 C ATOM 1013 CB BARG A 125 10.489 25.109 0.163 0.50 12.45 C ATOM 1014 CG AARG A 125 11.318 24.112 -0.289 0.50 13.13 C ATOM 1015 CG BARG A 125 11.688 24.184 0.220 0.50 13.49 C ATOM 1016 CD AARG A 125 12.692 24.569 0.157 0.50 13.40 C ATOM 1017 CD BARG A 125 12.651 24.582 1.323 0.50 14.66 C ATOM 1018 NE AARG A 125 13.003 24.143 1.517 0.50 14.07 N ATOM 1019 NE BARG A 125 12.986 26.001 1.260 0.50 15.67 N ATOM 1020 CZ AARG A 125 14.148 24.411 2.137 0.50 13.94 C ATOM 1021 CZ BARG A 125 13.767 26.627 2.133 0.50 17.19 C ATOM 1022 NH1AARG A 125 15.089 25.108 1.521 0.50 14.62 N1+ ATOM 1023 NH1BARG A 125 14.304 25.960 3.146 0.50 17.63 N1+ ATOM 1024 NH2AARG A 125 14.352 23.983 3.374 0.50 13.40 N ATOM 1025 NH2BARG A 125 14.003 27.927 1.996 0.50 17.60 N ATOM 1026 N MET A 126 7.636 26.418 1.159 1.00 11.26 N ATOM 1027 CA MET A 126 6.753 27.589 1.201 1.00 10.56 C ATOM 1028 C MET A 126 6.026 27.750 2.556 1.00 10.68 C ATOM 1029 O MET A 126 5.226 28.681 2.719 1.00 10.66 O ATOM 1030 CB MET A 126 5.730 27.510 0.057 1.00 10.48 C ATOM 1031 CG MET A 126 6.365 27.684 -1.310 1.00 9.06 C ATOM 1032 SD MET A 126 5.206 27.704 -2.685 1.00 11.53 S ATOM 1033 CE MET A 126 4.691 25.994 -2.716 1.00 8.95 C ATOM 1034 N ASN A 127 6.325 26.858 3.508 1.00 10.82 N ATOM 1035 CA ASN A 127 5.773 26.889 4.869 1.00 10.97 C ATOM 1036 C ASN A 127 4.267 26.629 4.877 1.00 10.92 C ATOM 1037 O ASN A 127 3.544 27.178 5.719 1.00 11.33 O ATOM 1038 CB ASN A 127 6.092 28.223 5.565 1.00 10.98 C ATOM 1039 CG ASN A 127 5.885 28.171 7.081 1.00 11.91 C ATOM 1040 ND2 ASN A 127 5.304 29.230 7.639 1.00 13.92 N ATOM 1041 OD1 ASN A 127 6.232 27.190 7.731 1.00 11.06 O ATOM 1042 N LEU A 128 3.802 25.780 3.955 1.00 11.24 N ATOM 1043 CA LEU A 128 2.367 25.529 3.776 1.00 11.03 C ATOM 1044 C LEU A 128 1.912 24.136 4.227 1.00 11.34 C ATOM 1045 O LEU A 128 0.719 23.839 4.195 1.00 10.84 O ATOM 1046 CB LEU A 128 1.970 25.733 2.305 1.00 10.95 C ATOM 1047 CG LEU A 128 2.224 27.108 1.677 1.00 11.33 C ATOM 1048 CD1 LEU A 128 1.710 27.153 0.240 1.00 11.97 C ATOM 1049 CD2 LEU A 128 1.578 28.190 2.505 1.00 10.07 C ATOM 1050 N THR A 129 2.845 23.294 4.659 1.00 11.56 N ATOM 1051 CA THR A 129 2.534 21.894 4.953 1.00 12.31 C ATOM 1052 C THR A 129 1.412 21.725 5.972 1.00 12.35 C ATOM 1053 O THR A 129 0.585 20.822 5.840 1.00 12.05 O ATOM 1054 CB THR A 129 3.773 21.156 5.466 1.00 12.67 C ATOM 1055 CG2 THR A 129 3.448 19.722 5.836 1.00 14.08 C ATOM 1056 OG1 THR A 129 4.770 21.159 4.441 1.00 14.70 O ATOM 1057 N GLY A 130 1.395 22.597 6.976 1.00 12.13 N ATOM 1058 CA GLY A 130 0.454 22.487 8.085 1.00 12.61 C ATOM 1059 C GLY A 130 -0.990 22.744 7.698 1.00 12.65 C ATOM 1060 O GLY A 130 -1.896 22.406 8.460 1.00 12.80 O ATOM 1061 N TYR A 131 -1.214 23.361 6.539 1.00 12.23 N ATOM 1062 CA TYR A 131 -2.584 23.594 6.056 1.00 11.90 C ATOM 1063 C TYR A 131 -3.170 22.403 5.285 1.00 12.22 C ATOM 1064 O TYR A 131 -4.387 22.303 5.161 1.00 12.47 O ATOM 1065 CB TYR A 131 -2.652 24.864 5.202 1.00 11.97 C ATOM 1066 CG TYR A 131 -2.229 26.105 5.953 1.00 12.30 C ATOM 1067 CD1 TYR A 131 -0.983 26.676 5.743 1.00 12.91 C ATOM 1068 CD2 TYR A 131 -3.071 26.694 6.891 1.00 12.74 C ATOM 1069 CE1 TYR A 131 -0.587 27.817 6.434 1.00 13.39 C ATOM 1070 CE2 TYR A 131 -2.687 27.846 7.589 1.00 14.20 C ATOM 1071 CZ TYR A 131 -1.434 28.391 7.364 1.00 14.40 C ATOM 1072 OH TYR A 131 -1.037 29.515 8.058 1.00 16.00 O ATOM 1073 N PHE A 132 -2.332 21.486 4.804 1.00 12.40 N ATOM 1074 CA PHE A 132 -2.801 20.403 3.931 1.00 12.24 C ATOM 1075 C PHE A 132 -3.208 19.150 4.695 1.00 12.51 C ATOM 1076 O PHE A 132 -2.456 18.656 5.523 1.00 13.10 O ATOM 1077 CB PHE A 132 -1.768 20.098 2.846 1.00 12.10 C ATOM 1078 CG PHE A 132 -1.793 21.098 1.741 1.00 11.64 C ATOM 1079 CD1 PHE A 132 -1.257 22.360 1.933 1.00 10.97 C ATOM 1080 CD2 PHE A 132 -2.416 20.811 0.538 1.00 11.26 C ATOM 1081 CE1 PHE A 132 -1.315 23.316 0.939 1.00 11.40 C ATOM 1082 CE2 PHE A 132 -2.478 21.767 -0.466 1.00 10.83 C ATOM 1083 CZ PHE A 132 -1.929 23.018 -0.265 1.00 10.88 C ATOM 1084 N ASP A 133 -4.425 18.668 4.427 1.00 12.58 N ATOM 1085 CA ASP A 133 -4.936 17.430 5.021 1.00 12.76 C ATOM 1086 C ASP A 133 -4.499 16.184 4.252 1.00 12.84 C ATOM 1087 O ASP A 133 -4.425 15.090 4.823 1.00 13.47 O ATOM 1088 CB ASP A 133 -6.469 17.461 5.090 1.00 12.67 C ATOM 1089 CG ASP A 133 -6.988 18.546 6.001 1.00 13.38 C ATOM 1090 OD1 ASP A 133 -6.697 18.499 7.221 1.00 15.15 O ATOM 1091 OD2 ASP A 133 -7.698 19.440 5.504 1.00 13.54 O1- ATOM 1092 N ALA A 134 -4.228 16.340 2.958 1.00 12.27 N ATOM 1093 CA ALA A 134 -3.732 15.247 2.136 1.00 12.82 C ATOM 1094 C ALA A 134 -3.002 15.761 0.905 1.00 12.56 C ATOM 1095 O ALA A 134 -3.214 16.893 0.465 1.00 13.08 O ATOM 1096 CB ALA A 134 -4.879 14.339 1.715 1.00 12.78 C ATOM 1097 N ILE A 135 -2.116 14.926 0.376 1.00 13.11 N ATOM 1098 CA ILE A 135 -1.477 15.171 -0.905 1.00 13.26 C ATOM 1099 C ILE A 135 -1.723 13.914 -1.735 1.00 13.88 C ATOM 1100 O ILE A 135 -1.366 12.813 -1.308 1.00 13.33 O ATOM 1101 CB ILE A 135 0.042 15.462 -0.757 1.00 13.59 C ATOM 1102 CG1 ILE A 135 0.272 16.796 -0.025 1.00 13.67 C ATOM 1103 CG2 ILE A 135 0.711 15.488 -2.130 1.00 13.17 C ATOM 1104 CD1 ILE A 135 1.744 17.073 0.339 1.00 15.21 C ATOM 1105 N ALA A 136 -2.406 14.065 -2.869 1.00 14.12 N ATOM 1106 CA ALA A 136 -2.578 12.971 -3.816 1.00 14.51 C ATOM 1107 C ALA A 136 -1.256 12.753 -4.527 1.00 15.22 C ATOM 1108 O ALA A 136 -0.698 13.687 -5.099 1.00 14.61 O ATOM 1109 CB ALA A 136 -3.662 13.302 -4.829 1.00 14.56 C ATOM 1110 N ASP A 137 -0.751 11.548 -4.515 1.00 15.85 N ATOM 1111 CA ASP A 137 0.555 11.209 -5.073 1.00 17.18 C ATOM 1112 C ASP A 137 0.499 10.961 -6.556 1.00 18.27 C ATOM 1113 O ASP A 137 -0.110 10.054 -6.944 1.00 18.75 O ATOM 1114 CB ASP A 137 1.061 9.950 -4.385 1.00 17.14 C ATOM 1115 CG ASP A 137 2.504 9.534 -4.774 1.00 17.23 C ATOM 1116 OD1 ASP A 137 2.922 8.604 -4.134 1.00 18.50 O ATOM 1117 OD2 ASP A 137 3.124 10.089 -5.644 1.00 17.83 O1- ATOM 1118 N PRO A 138 1.142 11.783 -7.364 1.00 19.62 N ATOM 1119 CA PRO A 138 1.059 11.585 -8.795 1.00 20.71 C ATOM 1120 C PRO A 138 1.640 10.278 -9.244 1.00 22.26 C ATOM 1121 O PRO A 138 1.365 9.862 -10.323 1.00 22.37 O ATOM 1122 CB PRO A 138 1.859 12.734 -9.369 1.00 20.63 C ATOM 1123 CG PRO A 138 2.585 13.266 -8.345 1.00 19.82 C ATOM 1124 CD PRO A 138 1.956 12.953 -7.076 1.00 19.96 C ATOM 1125 N ALA A 139 2.434 9.643 -8.410 1.00 24.04 N ATOM 1126 CA ALA A 139 3.122 8.455 -8.862 1.00 25.58 C ATOM 1127 C ALA A 139 2.225 7.258 -8.800 1.00 26.64 C ATOM 1128 O ALA A 139 2.584 6.231 -9.298 1.00 27.14 O ATOM 1129 CB ALA A 139 4.352 8.226 -8.118 1.00 25.99 C ATOM 1130 N GLU A 140 1.028 7.481 -8.248 1.00 27.79 N ATOM 1131 CA GLU A 140 -0.008 6.534 -7.852 1.00 28.06 C ATOM 1132 C GLU A 140 -1.253 6.490 -8.775 1.00 27.82 C ATOM 1133 O GLU A 140 -1.983 5.541 -8.698 1.00 28.16 O ATOM 1134 CB GLU A 140 -0.459 6.861 -6.415 1.00 28.75 C ATOM 1135 CG GLU A 140 -1.939 6.611 -5.974 1.00 30.00 C ATOM 1136 CD GLU A 140 -3.086 7.696 -6.303 1.00 32.10 C ATOM 1137 OE1 GLU A 140 -4.194 7.216 -6.672 1.00 32.71 O ATOM 1138 OE2 GLU A 140 -2.909 8.968 -6.159 1.00 32.52 O1- ATOM 1139 N VAL A 141 -1.454 7.499 -9.624 1.00 27.10 N ATOM 1140 CA VAL A 141 -2.559 7.606 -10.553 1.00 26.86 C ATOM 1141 C VAL A 141 -2.236 6.789 -11.796 1.00 26.17 C ATOM 1142 O VAL A 141 -1.097 6.793 -12.276 1.00 26.24 O ATOM 1143 CB VAL A 141 -2.801 9.092 -10.988 1.00 27.08 C ATOM 1144 CG1 VAL A 141 -4.027 9.659 -10.266 1.00 27.87 C ATOM 1145 CG2 VAL A 141 -1.573 9.969 -10.688 1.00 27.48 C ATOM 1146 N ALA A 142 -3.244 6.097 -12.313 1.00 25.46 N ATOM 1147 CA ALA A 142 -3.108 5.319 -13.547 1.00 24.72 C ATOM 1148 C ALA A 142 -3.021 6.223 -14.779 1.00 24.16 C ATOM 1149 O ALA A 142 -2.396 5.857 -15.784 1.00 23.88 O ATOM 1150 CB ALA A 142 -4.275 4.356 -13.682 1.00 24.99 C ATOM 1151 N ALA A 143 -3.651 7.397 -14.699 1.00 22.98 N ATOM 1152 CA ALA A 143 -3.680 8.351 -15.805 1.00 22.29 C ATOM 1153 C ALA A 143 -3.512 9.793 -15.318 1.00 21.78 C ATOM 1154 O ALA A 143 -4.125 10.202 -14.334 1.00 21.88 O ATOM 1155 CB ALA A 143 -4.984 8.210 -16.581 1.00 22.20 C ATOM 1156 N SER A 144 -2.679 10.549 -16.024 1.00 21.09 N ATOM 1157 CA SER A 144 -2.452 11.963 -15.735 1.00 20.64 C ATOM 1158 C SER A 144 -3.603 12.828 -16.251 1.00 19.82 C ATOM 1159 O SER A 144 -4.436 12.375 -17.037 1.00 19.52 O ATOM 1160 CB SER A 144 -1.147 12.407 -16.391 1.00 20.94 C ATOM 1161 OG SER A 144 -1.212 12.217 -17.795 1.00 22.32 O ATOM 1162 N LYS A 145 -3.642 14.082 -15.802 1.00 18.45 N ATOM 1163 CA LYS A 145 -4.591 15.063 -16.320 1.00 17.77 C ATOM 1164 C LYS A 145 -4.442 15.114 -17.846 1.00 16.82 C ATOM 1165 O LYS A 145 -3.320 15.134 -18.344 1.00 16.93 O ATOM 1166 CB LYS A 145 -4.300 16.448 -15.741 1.00 17.31 C ATOM 1167 CG LYS A 145 -4.358 16.543 -14.208 1.00 17.22 C ATOM 1168 CD LYS A 145 -3.759 17.859 -13.710 1.00 16.47 C ATOM 1169 CE LYS A 145 -3.482 17.824 -12.197 1.00 16.84 C ATOM 1170 NZ LYS A 145 -3.166 19.177 -11.635 1.00 15.81 N1+ ATOM 1171 N PRO A 146 -5.557 15.169 -18.588 1.00 16.27 N ATOM 1172 CA PRO A 146 -6.934 15.450 -18.192 1.00 15.84 C ATOM 1173 C PRO A 146 -7.751 14.313 -17.555 1.00 15.51 C ATOM 1174 O PRO A 146 -8.939 14.505 -17.297 1.00 15.48 O ATOM 1175 CB PRO A 146 -7.576 15.874 -19.515 1.00 16.02 C ATOM 1176 CG PRO A 146 -6.877 15.060 -20.518 1.00 16.02 C ATOM 1177 CD PRO A 146 -5.458 14.932 -20.045 1.00 16.21 C ATOM 1178 N ALA A 147 -7.154 13.147 -17.315 1.00 15.53 N ATOM 1179 CA ALA A 147 -7.847 12.088 -16.579 1.00 15.47 C ATOM 1180 C ALA A 147 -8.174 12.630 -15.180 1.00 15.50 C ATOM 1181 O ALA A 147 -7.358 13.340 -14.609 1.00 15.79 O ATOM 1182 CB ALA A 147 -6.976 10.835 -16.483 1.00 15.85 C ATOM 1183 N PRO A 148 -9.366 12.303 -14.635 1.00 15.43 N ATOM 1184 CA PRO A 148 -9.773 12.842 -13.334 1.00 14.96 C ATOM 1185 C PRO A 148 -9.119 12.172 -12.124 1.00 14.92 C ATOM 1186 O PRO A 148 -9.334 12.626 -10.993 1.00 14.40 O ATOM 1187 CB PRO A 148 -11.283 12.589 -13.309 1.00 15.00 C ATOM 1188 CG PRO A 148 -11.477 11.389 -14.168 1.00 15.48 C ATOM 1189 CD PRO A 148 -10.429 11.488 -15.249 1.00 15.43 C ATOM 1190 N ASP A 149 -8.338 11.117 -12.375 1.00 14.54 N ATOM 1191 CA ASP A 149 -7.771 10.254 -11.331 1.00 14.55 C ATOM 1192 C ASP A 149 -7.189 11.007 -10.136 1.00 13.69 C ATOM 1193 O ASP A 149 -7.468 10.654 -8.994 1.00 13.78 O ATOM 1194 CB ASP A 149 -6.661 9.367 -11.896 1.00 14.81 C ATOM 1195 CG ASP A 149 -7.118 8.471 -13.036 1.00 16.07 C ATOM 1196 OD1 ASP A 149 -6.503 7.395 -13.199 1.00 19.44 O ATOM 1197 OD2 ASP A 149 -8.048 8.842 -13.778 1.00 16.78 O1- ATOM 1198 N ILE A 150 -6.363 12.022 -10.399 1.00 13.09 N ATOM 1199 CA AILE A 150 -5.656 12.748 -9.335 0.50 12.81 C ATOM 1200 CA BILE A 150 -5.661 12.727 -9.320 0.50 12.76 C ATOM 1201 C ILE A 150 -6.611 13.548 -8.440 1.00 12.61 C ATOM 1202 O ILE A 150 -6.395 13.655 -7.226 1.00 12.09 O ATOM 1203 CB AILE A 150 -4.545 13.670 -9.917 0.50 12.73 C ATOM 1204 CB BILE A 150 -4.496 13.603 -9.848 0.50 12.64 C ATOM 1205 CG1AILE A 150 -3.600 14.160 -8.813 0.50 12.84 C ATOM 1206 CG1BILE A 150 -3.601 14.050 -8.686 0.50 12.61 C ATOM 1207 CG2AILE A 150 -5.149 14.846 -10.669 0.50 12.86 C ATOM 1208 CG2BILE A 150 -5.017 14.800 -10.627 0.50 12.68 C ATOM 1209 CD1AILE A 150 -2.806 13.058 -8.157 0.50 13.13 C ATOM 1210 CD1BILE A 150 -2.366 14.795 -9.121 0.50 12.64 C ATOM 1211 N PHE A 151 -7.666 14.111 -9.030 1.00 12.06 N ATOM 1212 CA PHE A 151 -8.643 14.880 -8.242 1.00 12.26 C ATOM 1213 C PHE A 151 -9.546 13.960 -7.426 1.00 12.45 C ATOM 1214 O PHE A 151 -9.877 14.275 -6.280 1.00 12.32 O ATOM 1215 CB PHE A 151 -9.441 15.849 -9.124 1.00 12.35 C ATOM 1216 CG PHE A 151 -8.637 17.034 -9.567 1.00 12.10 C ATOM 1217 CD1 PHE A 151 -8.042 17.062 -10.822 1.00 12.62 C ATOM 1218 CD2 PHE A 151 -8.424 18.099 -8.699 1.00 11.36 C ATOM 1219 CE1 PHE A 151 -7.284 18.150 -11.222 1.00 11.83 C ATOM 1220 CE2 PHE A 151 -7.654 19.183 -9.083 1.00 12.20 C ATOM 1221 CZ PHE A 151 -7.088 19.211 -10.349 1.00 12.92 C ATOM 1222 N ILE A 152 -9.901 12.809 -8.001 1.00 11.95 N ATOM 1223 CA ILE A 152 -10.658 11.789 -7.283 1.00 11.83 C ATOM 1224 C ILE A 152 -9.847 11.324 -6.078 1.00 11.20 C ATOM 1225 O ILE A 152 -10.368 11.231 -4.969 1.00 11.57 O ATOM 1226 CB ILE A 152 -11.027 10.572 -8.184 1.00 11.68 C ATOM 1227 CG1 ILE A 152 -11.933 11.008 -9.336 1.00 11.98 C ATOM 1228 CG2 ILE A 152 -11.722 9.488 -7.367 1.00 12.18 C ATOM 1229 CD1 ILE A 152 -12.213 9.903 -10.366 1.00 12.58 C ATOM 1230 N ALA A 153 -8.565 11.050 -6.306 1.00 10.79 N ATOM 1231 CA ALA A 153 -7.666 10.622 -5.239 1.00 10.54 C ATOM 1232 C ALA A 153 -7.541 11.674 -4.136 1.00 10.07 C ATOM 1233 O ALA A 153 -7.542 11.336 -2.955 1.00 10.70 O ATOM 1234 CB ALA A 153 -6.297 10.273 -5.804 1.00 10.35 C ATOM 1235 N ALA A 154 -7.448 12.943 -4.521 1.00 10.15 N ATOM 1236 CA ALA A 154 -7.331 14.044 -3.559 1.00 9.82 C ATOM 1237 C ALA A 154 -8.583 14.185 -2.688 1.00 9.77 C ATOM 1238 O ALA A 154 -8.496 14.389 -1.474 1.00 10.14 O ATOM 1239 CB ALA A 154 -7.062 15.335 -4.283 1.00 9.94 C ATOM 1240 N ALA A 155 -9.746 14.114 -3.319 1.00 9.75 N ATOM 1241 CA ALA A 155 -11.003 14.174 -2.591 1.00 9.95 C ATOM 1242 C ALA A 155 -11.091 13.011 -1.609 1.00 9.81 C ATOM 1243 O ALA A 155 -11.307 13.213 -0.404 1.00 9.42 O ATOM 1244 CB ALA A 155 -12.192 14.160 -3.568 1.00 10.11 C ATOM 1245 N HIS A 156 -10.877 11.798 -2.114 1.00 9.89 N ATOM 1246 CA HIS A 156 -10.978 10.602 -1.282 1.00 10.52 C ATOM 1247 C HIS A 156 -10.022 10.614 -0.099 1.00 10.35 C ATOM 1248 O HIS A 156 -10.396 10.217 1.001 1.00 10.30 O ATOM 1249 CB HIS A 156 -10.782 9.333 -2.120 1.00 10.61 C ATOM 1250 CG HIS A 156 -11.951 9.013 -3.006 1.00 12.52 C ATOM 1251 CD2 HIS A 156 -13.190 9.554 -3.076 1.00 15.69 C ATOM 1252 ND1 HIS A 156 -11.912 8.026 -3.968 1.00 16.07 N ATOM 1253 CE1 HIS A 156 -13.079 7.967 -4.584 1.00 15.75 C ATOM 1254 NE2 HIS A 156 -13.872 8.888 -4.065 1.00 16.07 N ATOM 1255 N ALA A 157 -8.803 11.090 -0.334 1.00 10.29 N ATOM 1256 CA ALA A 157 -7.783 11.190 0.711 1.00 10.78 C ATOM 1257 C ALA A 157 -8.175 12.090 1.895 1.00 10.78 C ATOM 1258 O ALA A 157 -7.602 11.944 2.983 1.00 11.92 O ATOM 1259 CB ALA A 157 -6.470 11.670 0.111 1.00 10.47 C ATOM 1260 N VAL A 158 -9.128 13.007 1.700 1.00 10.43 N ATOM 1261 CA VAL A 158 -9.648 13.821 2.800 1.00 10.07 C ATOM 1262 C VAL A 158 -11.083 13.445 3.216 1.00 10.33 C ATOM 1263 O VAL A 158 -11.735 14.172 3.969 1.00 10.37 O ATOM 1264 CB VAL A 158 -9.516 15.353 2.497 1.00 10.03 C ATOM 1265 CG1 VAL A 158 -8.044 15.710 2.292 1.00 10.82 C ATOM 1266 CG2 VAL A 158 -10.351 15.751 1.288 1.00 10.86 C ATOM 1267 N GLY A 159 -11.545 12.281 2.762 1.00 9.96 N ATOM 1268 CA GLY A 159 -12.813 11.731 3.218 1.00 10.01 C ATOM 1269 C GLY A 159 -14.060 12.304 2.570 1.00 10.22 C ATOM 1270 O GLY A 159 -15.147 12.206 3.143 1.00 9.78 O ATOM 1271 N VAL A 160 -13.921 12.879 1.375 1.00 10.39 N ATOM 1272 CA VAL A 160 -15.060 13.479 0.686 1.00 10.88 C ATOM 1273 C VAL A 160 -15.217 12.897 -0.711 1.00 10.92 C ATOM 1274 O VAL A 160 -14.263 12.402 -1.309 1.00 11.01 O ATOM 1275 CB VAL A 160 -14.977 15.041 0.616 1.00 10.83 C ATOM 1276 CG1 VAL A 160 -14.638 15.622 1.983 1.00 11.74 C ATOM 1277 CG2 VAL A 160 -13.964 15.507 -0.423 1.00 10.47 C ATOM 1278 N ALA A 161 -16.440 12.954 -1.221 1.00 11.27 N ATOM 1279 CA ALA A 161 -16.685 12.661 -2.622 1.00 11.19 C ATOM 1280 C ALA A 161 -16.269 13.903 -3.415 1.00 11.45 C ATOM 1281 O ALA A 161 -16.401 15.032 -2.919 1.00 11.11 O ATOM 1282 CB ALA A 161 -18.160 12.335 -2.842 1.00 11.65 C ATOM 1283 N PRO A 162 -15.759 13.714 -4.648 1.00 12.01 N ATOM 1284 CA PRO A 162 -15.427 14.879 -5.474 1.00 12.35 C ATOM 1285 C PRO A 162 -16.585 15.867 -5.633 1.00 12.89 C ATOM 1286 O PRO A 162 -16.347 17.068 -5.700 1.00 13.09 O ATOM 1287 CB PRO A 162 -15.048 14.264 -6.825 1.00 12.65 C ATOM 1288 CG PRO A 162 -14.626 12.881 -6.512 1.00 12.41 C ATOM 1289 CD PRO A 162 -15.389 12.449 -5.304 1.00 11.93 C ATOM 1290 N SER A 163 -17.826 15.369 -5.650 1.00 13.24 N ATOM 1291 CA SER A 163 -19.013 16.227 -5.752 1.00 13.57 C ATOM 1292 C SER A 163 -19.175 17.219 -4.589 1.00 13.29 C ATOM 1293 O SER A 163 -19.960 18.150 -4.687 1.00 13.52 O ATOM 1294 CB SER A 163 -20.282 15.374 -5.880 1.00 13.86 C ATOM 1295 OG SER A 163 -20.411 14.482 -4.784 1.00 15.22 O ATOM 1296 N GLU A 164 -18.446 17.008 -3.493 1.00 12.94 N ATOM 1297 CA GLU A 164 -18.467 17.915 -2.342 1.00 13.17 C ATOM 1298 C GLU A 164 -17.343 18.941 -2.404 1.00 12.73 C ATOM 1299 O GLU A 164 -17.135 19.687 -1.439 1.00 12.80 O ATOM 1300 CB GLU A 164 -18.290 17.121 -1.047 1.00 13.11 C ATOM 1301 CG GLU A 164 -19.350 16.090 -0.773 1.00 13.75 C ATOM 1302 CD GLU A 164 -19.072 15.344 0.505 1.00 14.28 C ATOM 1303 OE1 GLU A 164 -19.558 15.780 1.562 1.00 15.80 O ATOM 1304 OE2 GLU A 164 -18.344 14.336 0.457 1.00 13.80 O1- ATOM 1305 N SER A 165 -16.620 18.979 -3.524 1.00 12.23 N ATOM 1306 CA SER A 165 -15.336 19.661 -3.575 1.00 11.82 C ATOM 1307 C SER A 165 -15.287 20.693 -4.693 1.00 11.49 C ATOM 1308 O SER A 165 -15.998 20.571 -5.710 1.00 10.63 O ATOM 1309 CB SER A 165 -14.202 18.658 -3.792 1.00 12.01 C ATOM 1310 OG SER A 165 -14.239 17.611 -2.834 1.00 11.47 O ATOM 1311 N ILE A 166 -14.422 21.689 -4.490 1.00 10.83 N ATOM 1312 CA ILE A 166 -14.015 22.634 -5.522 1.00 10.39 C ATOM 1313 C ILE A 166 -12.577 22.330 -5.924 1.00 10.32 C ATOM 1314 O ILE A 166 -11.739 22.073 -5.064 1.00 10.32 O ATOM 1315 CB ILE A 166 -14.107 24.088 -5.009 1.00 9.76 C ATOM 1316 CG1 ILE A 166 -15.573 24.497 -4.865 1.00 10.52 C ATOM 1317 CG2 ILE A 166 -13.383 25.071 -5.953 1.00 11.86 C ATOM 1318 CD1 ILE A 166 -15.773 25.801 -4.119 1.00 10.19 C ATOM 1319 N GLY A 167 -12.311 22.333 -7.229 1.00 10.12 N ATOM 1320 CA GLY A 167 -10.942 22.230 -7.753 1.00 9.74 C ATOM 1321 C GLY A 167 -10.459 23.554 -8.320 1.00 9.62 C ATOM 1322 O GLY A 167 -11.200 24.235 -9.024 1.00 9.67 O ATOM 1323 N LEU A 168 -9.212 23.920 -8.015 1.00 9.42 N ATOM 1324 CA LEU A 168 -8.596 25.150 -8.541 1.00 9.49 C ATOM 1325 C LEU A 168 -7.443 24.785 -9.475 1.00 10.20 C ATOM 1326 O LEU A 168 -6.545 24.030 -9.090 1.00 10.77 O ATOM 1327 CB LEU A 168 -8.090 26.040 -7.403 1.00 9.91 C ATOM 1328 CG LEU A 168 -9.088 26.379 -6.290 1.00 9.06 C ATOM 1329 CD1 LEU A 168 -8.435 27.314 -5.281 1.00 10.06 C ATOM 1330 CD2 LEU A 168 -10.382 26.991 -6.842 1.00 8.71 C ATOM 1331 N GLU A 169 -7.496 25.303 -10.705 1.00 10.34 N ATOM 1332 CA GLU A 169 -6.562 24.919 -11.774 1.00 10.79 C ATOM 1333 C GLU A 169 -6.245 26.082 -12.719 1.00 10.96 C ATOM 1334 O GLU A 169 -7.072 26.978 -12.924 1.00 10.84 O ATOM 1335 CB GLU A 169 -7.135 23.743 -12.581 1.00 10.95 C ATOM 1336 CG GLU A 169 -6.614 22.364 -12.186 1.00 11.61 C ATOM 1337 CD GLU A 169 -5.211 22.092 -12.695 1.00 13.72 C ATOM 1338 OE1 GLU A 169 -4.674 22.916 -13.478 1.00 13.52 O ATOM 1339 OE2 GLU A 169 -4.660 21.025 -12.341 1.00 13.07 O1- ATOM 1340 N ASP A 170 -5.041 26.039 -13.288 1.00 10.95 N ATOM 1341 CA ASP A 170 -4.578 27.032 -14.266 1.00 11.38 C ATOM 1342 C ASP A 170 -4.478 26.471 -15.693 1.00 11.59 C ATOM 1343 O ASP A 170 -4.154 27.215 -16.629 1.00 10.88 O ATOM 1344 CB ASP A 170 -3.203 27.575 -13.859 1.00 11.42 C ATOM 1345 CG ASP A 170 -2.111 26.536 -13.980 1.00 12.37 C ATOM 1346 OD1 ASP A 170 -2.345 25.377 -13.562 1.00 11.36 O ATOM 1347 OD2 ASP A 170 -1.023 26.858 -14.514 1.00 11.41 O1- ATOM 1348 N SER A 171 -4.700 25.170 -15.853 1.00 11.70 N ATOM 1349 CA SER A 171 -4.529 24.505 -17.149 1.00 12.98 C ATOM 1350 C SER A 171 -5.848 23.945 -17.680 1.00 13.15 C ATOM 1351 O SER A 171 -6.715 23.541 -16.910 1.00 13.76 O ATOM 1352 CB SER A 171 -3.498 23.377 -17.044 1.00 12.78 C ATOM 1353 OG SER A 171 -4.022 22.212 -16.430 1.00 14.75 O ATOM 1354 N GLN A 172 -5.982 23.897 -19.003 1.00 14.05 N ATOM 1355 CA GLN A 172 -7.178 23.325 -19.610 1.00 14.53 C ATOM 1356 C GLN A 172 -7.331 21.848 -19.255 1.00 14.22 C ATOM 1357 O GLN A 172 -8.436 21.408 -18.929 1.00 14.06 O ATOM 1358 CB GLN A 172 -7.166 23.497 -21.130 1.00 14.92 C ATOM 1359 CG GLN A 172 -8.499 23.155 -21.788 1.00 16.45 C ATOM 1360 CD GLN A 172 -8.684 21.661 -22.044 1.00 17.89 C ATOM 1361 NE2 GLN A 172 -9.922 21.196 -21.951 1.00 19.51 N ATOM 1362 OE1 GLN A 172 -7.723 20.941 -22.322 1.00 21.36 O ATOM 1363 N ALA A 173 -6.231 21.094 -19.319 1.00 14.35 N ATOM 1364 CA ALA A 173 -6.242 19.666 -18.975 1.00 14.06 C ATOM 1365 C ALA A 173 -6.698 19.469 -17.530 1.00 13.94 C ATOM 1366 O ALA A 173 -7.501 18.576 -17.230 1.00 14.30 O ATOM 1367 CB ALA A 173 -4.866 19.060 -19.177 1.00 14.28 C ATOM 1368 N GLY A 174 -6.188 20.322 -16.649 1.00 13.19 N ATOM 1369 CA GLY A 174 -6.590 20.333 -15.244 1.00 13.00 C ATOM 1370 C GLY A 174 -8.067 20.596 -15.039 1.00 13.16 C ATOM 1371 O GLY A 174 -8.712 19.925 -14.236 1.00 12.86 O ATOM 1372 N ILE A 175 -8.610 21.586 -15.743 1.00 13.17 N ATOM 1373 CA ILE A 175 -10.046 21.871 -15.664 1.00 13.64 C ATOM 1374 C ILE A 175 -10.879 20.674 -16.114 1.00 13.70 C ATOM 1375 O ILE A 175 -11.887 20.328 -15.487 1.00 13.25 O ATOM 1376 CB ILE A 175 -10.423 23.096 -16.519 1.00 13.73 C ATOM 1377 CG1 ILE A 175 -9.807 24.367 -15.932 1.00 13.82 C ATOM 1378 CG2 ILE A 175 -11.952 23.258 -16.625 1.00 14.71 C ATOM 1379 CD1 ILE A 175 -10.372 24.785 -14.588 1.00 13.34 C ATOM 1380 N GLN A 176 -10.464 20.035 -17.201 1.00 14.20 N ATOM 1381 CA GLN A 176 -11.156 18.839 -17.673 1.00 14.57 C ATOM 1382 C GLN A 176 -11.155 17.735 -16.605 1.00 14.37 C ATOM 1383 O GLN A 176 -12.190 17.123 -16.353 1.00 14.51 O ATOM 1384 CB GLN A 176 -10.545 18.333 -18.984 1.00 15.11 C ATOM 1385 CG GLN A 176 -11.344 17.222 -19.661 1.00 16.44 C ATOM 1386 CD GLN A 176 -12.740 17.657 -20.068 1.00 18.19 C ATOM 1387 NE2 GLN A 176 -12.825 18.755 -20.800 1.00 18.80 N ATOM 1388 OE1 GLN A 176 -13.734 17.018 -19.714 1.00 21.66 O ATOM 1389 N ALA A 177 -10.003 17.505 -15.977 1.00 14.27 N ATOM 1390 CA ALA A 177 -9.874 16.502 -14.915 1.00 13.93 C ATOM 1391 C ALA A 177 -10.836 16.787 -13.760 1.00 13.98 C ATOM 1392 O ALA A 177 -11.502 15.884 -13.275 1.00 14.10 O ATOM 1393 CB ALA A 177 -8.433 16.443 -14.411 1.00 14.00 C ATOM 1394 N ILE A 178 -10.925 18.052 -13.346 1.00 13.67 N ATOM 1395 CA ILE A 178 -11.845 18.453 -12.273 1.00 13.54 C ATOM 1396 C ILE A 178 -13.304 18.187 -12.677 1.00 14.14 C ATOM 1397 O ILE A 178 -14.067 17.599 -11.916 1.00 14.37 O ATOM 1398 CB ILE A 178 -11.680 19.940 -11.913 1.00 13.39 C ATOM 1399 CG1 ILE A 178 -10.276 20.211 -11.351 1.00 12.41 C ATOM 1400 CG2 ILE A 178 -12.735 20.367 -10.894 1.00 12.83 C ATOM 1401 CD1 ILE A 178 -9.960 21.703 -11.224 1.00 12.01 C ATOM 1402 N LYS A 179 -13.677 18.615 -13.879 1.00 14.99 N ATOM 1403 CA LYS A 179 -15.025 18.353 -14.401 1.00 15.76 C ATOM 1404 C LYS A 179 -15.348 16.846 -14.390 1.00 15.40 C ATOM 1405 O LYS A 179 -16.372 16.421 -13.858 1.00 15.64 O ATOM 1406 CB LYS A 179 -15.184 18.936 -15.814 1.00 16.14 C ATOM 1407 CG LYS A 179 -15.143 20.468 -15.871 1.00 18.58 C ATOM 1408 CD LYS A 179 -14.909 20.998 -17.294 1.00 21.44 C ATOM 1409 CE LYS A 179 -16.149 21.620 -17.917 1.00 22.67 C ATOM 1410 NZ LYS A 179 -15.997 21.820 -19.401 1.00 23.88 N1+ ATOM 1411 N ASP A 180 -14.453 16.037 -14.933 1.00 15.68 N ATOM 1412 CA ASP A 180 -14.704 14.601 -15.031 1.00 15.84 C ATOM 1413 C ASP A 180 -14.590 13.857 -13.700 1.00 15.65 C ATOM 1414 O ASP A 180 -14.993 12.699 -13.614 1.00 15.79 O ATOM 1415 CB ASP A 180 -13.810 13.987 -16.107 1.00 16.13 C ATOM 1416 CG ASP A 180 -14.222 14.423 -17.514 1.00 17.55 C ATOM 1417 OD1 ASP A 180 -13.371 14.449 -18.422 1.00 19.38 O ATOM 1418 OD2 ASP A 180 -15.413 14.750 -17.702 1.00 19.63 O1- ATOM 1419 N SER A 181 -14.060 14.520 -12.668 1.00 15.05 N ATOM 1420 CA SER A 181 -14.061 13.966 -11.305 1.00 14.73 C ATOM 1421 C SER A 181 -15.421 14.115 -10.626 1.00 14.56 C ATOM 1422 O SER A 181 -15.753 13.321 -9.742 1.00 14.53 O ATOM 1423 CB SER A 181 -12.989 14.635 -10.429 1.00 14.31 C ATOM 1424 OG SER A 181 -13.426 15.894 -9.915 1.00 14.31 O ATOM 1425 N GLY A 182 -16.182 15.146 -11.019 1.00 13.90 N ATOM 1426 CA GLY A 182 -17.442 15.515 -10.357 1.00 13.61 C ATOM 1427 C GLY A 182 -17.342 16.760 -9.483 1.00 13.05 C ATOM 1428 O GLY A 182 -18.354 17.272 -9.006 1.00 13.30 O ATOM 1429 N ALA A 183 -16.125 17.256 -9.261 1.00 12.24 N ATOM 1430 CA ALA A 183 -15.926 18.476 -8.481 1.00 11.80 C ATOM 1431 C ALA A 183 -16.263 19.719 -9.304 1.00 11.49 C ATOM 1432 O ALA A 183 -16.390 19.647 -10.532 1.00 12.06 O ATOM 1433 CB ALA A 183 -14.490 18.552 -7.980 1.00 11.49 C ATOM 1434 N LEU A 184 -16.395 20.853 -8.625 1.00 11.06 N ATOM 1435 CA LEU A 184 -16.644 22.135 -9.292 1.00 11.33 C ATOM 1436 C LEU A 184 -15.336 22.866 -9.595 1.00 10.94 C ATOM 1437 O LEU A 184 -14.595 23.208 -8.675 1.00 10.88 O ATOM 1438 CB LEU A 184 -17.537 23.028 -8.429 1.00 11.61 C ATOM 1439 CG LEU A 184 -17.905 24.381 -9.053 1.00 12.54 C ATOM 1440 CD1 LEU A 184 -18.950 24.192 -10.142 1.00 14.51 C ATOM 1441 CD2 LEU A 184 -18.403 25.347 -7.981 1.00 14.59 C ATOM 1442 N PRO A 185 -15.055 23.133 -10.883 1.00 11.28 N ATOM 1443 CA PRO A 185 -13.847 23.869 -11.245 1.00 10.92 C ATOM 1444 C PRO A 185 -13.983 25.395 -11.129 1.00 10.89 C ATOM 1445 O PRO A 185 -15.009 25.969 -11.514 1.00 11.12 O ATOM 1446 CB PRO A 185 -13.635 23.480 -12.704 1.00 11.18 C ATOM 1447 CG PRO A 185 -14.990 23.240 -13.220 1.00 11.76 C ATOM 1448 CD PRO A 185 -15.845 22.772 -12.079 1.00 11.27 C ATOM 1449 N ILE A 186 -12.963 26.039 -10.578 1.00 9.88 N ATOM 1450 CA ILE A 186 -12.818 27.498 -10.722 1.00 9.84 C ATOM 1451 C ILE A 186 -11.412 27.718 -11.267 1.00 10.37 C ATOM 1452 O ILE A 186 -10.422 27.432 -10.582 1.00 10.26 O ATOM 1453 CB ILE A 186 -13.021 28.269 -9.404 1.00 9.54 C ATOM 1454 CG1 ILE A 186 -14.365 27.909 -8.752 1.00 10.85 C ATOM 1455 CG2 ILE A 186 -12.938 29.788 -9.665 1.00 9.19 C ATOM 1456 CD1 ILE A 186 -14.602 28.590 -7.414 1.00 11.79 C ATOM 1457 N GLY A 187 -11.326 28.187 -12.506 1.00 10.71 N ATOM 1458 CA GLY A 187 -10.048 28.343 -13.179 1.00 10.61 C ATOM 1459 C GLY A 187 -9.399 29.676 -12.881 1.00 11.28 C ATOM 1460 O GLY A 187 -10.069 30.606 -12.452 1.00 10.92 O ATOM 1461 N VAL A 188 -8.086 29.752 -13.080 1.00 11.95 N ATOM 1462 CA VAL A 188 -7.354 31.012 -13.009 1.00 12.40 C ATOM 1463 C VAL A 188 -6.598 31.196 -14.326 1.00 13.41 C ATOM 1464 O VAL A 188 -5.796 30.345 -14.717 1.00 13.21 O ATOM 1465 CB VAL A 188 -6.396 31.095 -11.782 1.00 12.02 C ATOM 1466 CG1 VAL A 188 -5.487 29.866 -11.697 1.00 11.80 C ATOM 1467 CG2 VAL A 188 -5.589 32.398 -11.804 1.00 12.30 C ATOM 1468 N GLY A 189 -6.876 32.313 -14.997 1.00 14.86 N ATOM 1469 CA GLY A 189 -6.370 32.573 -16.340 1.00 15.84 C ATOM 1470 C GLY A 189 -7.436 33.199 -17.229 1.00 16.75 C ATOM 1471 O GLY A 189 -8.181 34.078 -16.791 1.00 17.37 O ATOM 1472 N ARG A 190 -7.496 32.733 -18.477 1.00 17.76 N ATOM 1473 CA ARG A 190 -8.383 33.288 -19.503 1.00 18.68 C ATOM 1474 C ARG A 190 -9.244 32.210 -20.163 1.00 18.35 C ATOM 1475 O ARG A 190 -8.803 31.069 -20.321 1.00 17.98 O ATOM 1476 CB ARG A 190 -7.557 34.004 -20.576 1.00 19.49 C ATOM 1477 CG ARG A 190 -7.765 35.509 -20.621 1.00 22.73 C ATOM 1478 CD ARG A 190 -7.071 36.128 -21.821 1.00 26.40 C ATOM 1479 NE ARG A 190 -5.652 36.338 -21.557 1.00 29.03 N ATOM 1480 CZ ARG A 190 -5.138 37.412 -20.956 1.00 31.39 C ATOM 1481 NH1 ARG A 190 -5.918 38.409 -20.539 1.00 32.49 N1+ ATOM 1482 NH2 ARG A 190 -3.825 37.491 -20.768 1.00 32.08 N ATOM 1483 N PRO A 191 -10.477 32.575 -20.571 1.00 18.16 N ATOM 1484 CA PRO A 191 -11.350 31.594 -21.209 1.00 18.15 C ATOM 1485 C PRO A 191 -10.802 31.064 -22.533 1.00 18.09 C ATOM 1486 O PRO A 191 -11.067 29.920 -22.880 1.00 17.73 O ATOM 1487 CB PRO A 191 -12.667 32.358 -21.416 1.00 18.19 C ATOM 1488 CG PRO A 191 -12.306 33.796 -21.339 1.00 18.40 C ATOM 1489 CD PRO A 191 -11.140 33.881 -20.407 1.00 18.15 C ATOM 1490 N GLU A 192 -10.028 31.881 -23.245 1.00 18.29 N ATOM 1491 CA GLU A 192 -9.357 31.431 -24.468 1.00 18.63 C ATOM 1492 C GLU A 192 -8.512 30.170 -24.227 1.00 18.32 C ATOM 1493 O GLU A 192 -8.403 29.325 -25.111 1.00 18.33 O ATOM 1494 CB GLU A 192 -8.486 32.550 -25.059 1.00 19.09 C ATOM 1495 CG GLU A 192 -9.262 33.755 -25.623 1.00 20.79 C ATOM 1496 CD GLU A 192 -9.560 34.842 -24.601 1.00 22.69 C ATOM 1497 OE1 GLU A 192 -9.411 34.596 -23.384 1.00 22.97 O ATOM 1498 OE2 GLU A 192 -9.949 35.958 -25.020 1.00 23.53 O1- ATOM 1499 N ASP A 193 -7.934 30.045 -23.029 1.00 17.73 N ATOM 1500 CA ASP A 193 -7.083 28.901 -22.671 1.00 17.62 C ATOM 1501 C ASP A 193 -7.826 27.780 -21.938 1.00 17.00 C ATOM 1502 O ASP A 193 -7.547 26.602 -22.169 1.00 16.53 O ATOM 1503 CB ASP A 193 -5.921 29.360 -21.781 1.00 17.81 C ATOM 1504 CG ASP A 193 -5.013 30.369 -22.464 1.00 19.35 C ATOM 1505 OD1 ASP A 193 -4.780 30.240 -23.687 1.00 19.04 O ATOM 1506 OD2 ASP A 193 -4.532 31.293 -21.770 1.00 21.20 O1- ATOM 1507 N LEU A 194 -8.737 28.145 -21.036 1.00 16.36 N ATOM 1508 CA LEU A 194 -9.341 27.179 -20.114 1.00 16.16 C ATOM 1509 C LEU A 194 -10.739 26.688 -20.514 1.00 16.12 C ATOM 1510 O LEU A 194 -11.193 25.636 -20.037 1.00 16.09 O ATOM 1511 CB LEU A 194 -9.400 27.780 -18.700 1.00 16.18 C ATOM 1512 CG LEU A 194 -8.070 28.262 -18.108 1.00 16.61 C ATOM 1513 CD1 LEU A 194 -8.254 28.778 -16.684 1.00 16.54 C ATOM 1514 CD2 LEU A 194 -7.035 27.154 -18.133 1.00 15.86 C ATOM 1515 N GLY A 195 -11.420 27.446 -21.370 1.00 15.86 N ATOM 1516 CA GLY A 195 -12.790 27.120 -21.766 1.00 15.88 C ATOM 1517 C GLY A 195 -13.772 28.199 -21.367 1.00 15.81 C ATOM 1518 O GLY A 195 -13.519 28.986 -20.452 1.00 14.87 O ATOM 1519 N ASP A 196 -14.914 28.219 -22.048 1.00 15.83 N ATOM 1520 CA ASP A 196 -15.887 29.289 -21.901 1.00 16.46 C ATOM 1521 C ASP A 196 -17.080 28.881 -21.035 1.00 16.25 C ATOM 1522 O ASP A 196 -18.027 29.648 -20.899 1.00 17.08 O ATOM 1523 CB ASP A 196 -16.365 29.726 -23.297 1.00 16.54 C ATOM 1524 CG ASP A 196 -16.945 31.126 -23.314 1.00 17.32 C ATOM 1525 OD1 ASP A 196 -17.883 31.363 -24.104 1.00 18.11 O ATOM 1526 OD2 ASP A 196 -16.476 31.990 -22.543 1.00 17.36 O1- ATOM 1527 N ASP A 197 -17.023 27.686 -20.439 1.00 16.61 N ATOM 1528 CA ASP A 197 -18.153 27.120 -19.693 1.00 16.94 C ATOM 1529 C ASP A 197 -17.890 26.911 -18.195 1.00 16.84 C ATOM 1530 O ASP A 197 -18.651 26.198 -17.528 1.00 17.88 O ATOM 1531 CB ASP A 197 -18.582 25.793 -20.334 1.00 17.35 C ATOM 1532 CG ASP A 197 -17.480 24.740 -20.314 1.00 19.32 C ATOM 1533 OD1 ASP A 197 -16.289 25.098 -20.163 1.00 21.24 O ATOM 1534 OD2 ASP A 197 -17.808 23.542 -20.460 1.00 24.28 O1- ATOM 1535 N ILE A 198 -16.827 27.519 -17.669 1.00 16.07 N ATOM 1536 CA ILE A 198 -16.552 27.465 -16.226 1.00 15.14 C ATOM 1537 C ILE A 198 -16.308 28.866 -15.670 1.00 14.53 C ATOM 1538 O ILE A 198 -16.058 29.806 -16.427 1.00 13.91 O ATOM 1539 CB ILE A 198 -15.380 26.485 -15.864 1.00 15.22 C ATOM 1540 CG1 ILE A 198 -14.007 27.015 -16.305 1.00 15.00 C ATOM 1541 CG2 ILE A 198 -15.627 25.084 -16.445 1.00 15.46 C ATOM 1542 CD1 ILE A 198 -13.771 26.999 -17.776 1.00 14.66 C ATOM 1543 N VAL A 199 -16.411 29.008 -14.349 1.00 13.58 N ATOM 1544 CA VAL A 199 -16.049 30.262 -13.691 1.00 13.40 C ATOM 1545 C VAL A 199 -14.521 30.379 -13.695 1.00 13.05 C ATOM 1546 O VAL A 199 -13.821 29.430 -13.347 1.00 13.17 O ATOM 1547 CB VAL A 199 -16.596 30.344 -12.246 1.00 13.20 C ATOM 1548 CG1 VAL A 199 -16.104 31.612 -11.566 1.00 13.57 C ATOM 1549 CG2 VAL A 199 -18.125 30.306 -12.252 1.00 13.39 C ATOM 1550 N ILE A 200 -14.024 31.537 -14.115 1.00 12.96 N ATOM 1551 CA ILE A 200 -12.592 31.815 -14.168 1.00 13.04 C ATOM 1552 C ILE A 200 -12.324 33.163 -13.521 1.00 13.45 C ATOM 1553 O ILE A 200 -13.085 34.110 -13.718 1.00 14.11 O ATOM 1554 CB ILE A 200 -12.083 31.866 -15.630 1.00 12.99 C ATOM 1555 CG1 ILE A 200 -12.367 30.552 -16.360 1.00 12.65 C ATOM 1556 CG2 ILE A 200 -10.576 32.160 -15.673 1.00 12.89 C ATOM 1557 CD1 ILE A 200 -12.054 30.626 -17.850 1.00 12.48 C ATOM 1558 N VAL A 201 -11.246 33.245 -12.747 1.00 13.37 N ATOM 1559 CA VAL A 201 -10.764 34.516 -12.221 1.00 13.40 C ATOM 1560 C VAL A 201 -9.451 34.857 -12.925 1.00 13.68 C ATOM 1561 O VAL A 201 -8.746 33.960 -13.372 1.00 13.34 O ATOM 1562 CB VAL A 201 -10.559 34.470 -10.692 1.00 13.80 C ATOM 1563 CG1 VAL A 201 -11.889 34.211 -9.989 1.00 13.61 C ATOM 1564 CG2 VAL A 201 -9.521 33.418 -10.310 1.00 13.00 C ATOM 1565 N PRO A 202 -9.125 36.157 -13.046 1.00 14.16 N ATOM 1566 CA PRO A 202 -7.943 36.517 -13.822 1.00 14.32 C ATOM 1567 C PRO A 202 -6.625 36.209 -13.115 1.00 14.19 C ATOM 1568 O PRO A 202 -5.632 35.972 -13.779 1.00 14.41 O ATOM 1569 CB PRO A 202 -8.098 38.031 -14.025 1.00 14.49 C ATOM 1570 CG PRO A 202 -9.026 38.480 -12.973 1.00 15.41 C ATOM 1571 CD PRO A 202 -9.915 37.339 -12.648 1.00 14.51 C ATOM 1572 N ASP A 203 -6.637 36.234 -11.784 1.00 13.83 N ATOM 1573 CA ASP A 203 -5.468 35.902 -10.980 1.00 14.19 C ATOM 1574 C ASP A 203 -5.897 35.411 -9.599 1.00 13.67 C ATOM 1575 O ASP A 203 -7.079 35.480 -9.239 1.00 13.03 O ATOM 1576 CB ASP A 203 -4.528 37.100 -10.867 1.00 14.55 C ATOM 1577 CG ASP A 203 -5.125 38.250 -10.082 1.00 16.20 C ATOM 1578 OD1 ASP A 203 -5.202 38.145 -8.843 1.00 19.42 O ATOM 1579 OD2 ASP A 203 -5.495 39.273 -10.700 1.00 20.71 O1- ATOM 1580 N THR A 204 -4.931 34.909 -8.836 1.00 13.10 N ATOM 1581 CA THR A 204 -5.237 34.198 -7.592 1.00 12.82 C ATOM 1582 C THR A 204 -5.670 35.093 -6.429 1.00 12.74 C ATOM 1583 O THR A 204 -6.197 34.593 -5.442 1.00 12.57 O ATOM 1584 CB THR A 204 -4.056 33.304 -7.144 1.00 12.50 C ATOM 1585 CG2 THR A 204 -3.787 32.198 -8.175 1.00 13.09 C ATOM 1586 OG1 THR A 204 -2.875 34.094 -6.976 1.00 12.18 O ATOM 1587 N SER A 205 -5.476 36.412 -6.531 1.00 12.77 N ATOM 1588 CA SER A 205 -5.994 37.313 -5.498 1.00 13.03 C ATOM 1589 C SER A 205 -7.525 37.256 -5.419 1.00 12.96 C ATOM 1590 O SER A 205 -8.118 37.645 -4.412 1.00 13.06 O ATOM 1591 CB SER A 205 -5.520 38.752 -5.724 1.00 13.35 C ATOM 1592 OG SER A 205 -6.201 39.367 -6.799 1.00 14.53 O ATOM 1593 N HIS A 206 -8.162 36.766 -6.480 1.00 13.12 N ATOM 1594 CA HIS A 206 -9.610 36.604 -6.509 1.00 12.99 C ATOM 1595 C HIS A 206 -10.109 35.307 -5.853 1.00 12.65 C ATOM 1596 O HIS A 206 -11.315 35.131 -5.665 1.00 13.17 O ATOM 1597 CB HIS A 206 -10.101 36.701 -7.953 1.00 13.72 C ATOM 1598 CG HIS A 206 -9.920 38.065 -8.547 1.00 15.53 C ATOM 1599 CD2 HIS A 206 -10.751 39.131 -8.606 1.00 18.51 C ATOM 1600 ND1 HIS A 206 -8.745 38.462 -9.149 1.00 17.53 N ATOM 1601 CE1 HIS A 206 -8.867 39.709 -9.570 1.00 17.77 C ATOM 1602 NE2 HIS A 206 -10.076 40.137 -9.254 1.00 19.55 N ATOM 1603 N TYR A 207 -9.190 34.410 -5.515 1.00 12.53 N ATOM 1604 CA TYR A 207 -9.536 33.159 -4.836 1.00 12.31 C ATOM 1605 C TYR A 207 -9.709 33.424 -3.329 1.00 12.60 C ATOM 1606 O TYR A 207 -8.823 33.141 -2.520 1.00 12.67 O ATOM 1607 CB TYR A 207 -8.436 32.114 -5.038 1.00 12.45 C ATOM 1608 CG TYR A 207 -8.416 31.323 -6.337 1.00 11.58 C ATOM 1609 CD1 TYR A 207 -7.201 30.865 -6.851 1.00 10.98 C ATOM 1610 CD2 TYR A 207 -9.577 30.986 -7.027 1.00 10.68 C ATOM 1611 CE1 TYR A 207 -7.137 30.108 -7.999 1.00 10.61 C ATOM 1612 CE2 TYR A 207 -9.520 30.212 -8.196 1.00 10.69 C ATOM 1613 CZ TYR A 207 -8.294 29.779 -8.670 1.00 11.11 C ATOM 1614 OH TYR A 207 -8.205 29.010 -9.810 1.00 10.16 O ATOM 1615 N THR A 208 -10.850 33.985 -2.957 1.00 12.53 N ATOM 1616 CA THR A 208 -11.158 34.242 -1.554 1.00 12.87 C ATOM 1617 C THR A 208 -12.216 33.242 -1.110 1.00 12.66 C ATOM 1618 O THR A 208 -12.971 32.744 -1.935 1.00 12.43 O ATOM 1619 CB THR A 208 -11.683 35.676 -1.352 1.00 13.29 C ATOM 1620 CG2 THR A 208 -10.711 36.680 -1.957 1.00 14.23 C ATOM 1621 OG1 THR A 208 -12.968 35.810 -1.975 1.00 14.47 O ATOM 1622 N LEU A 209 -12.281 32.959 0.191 1.00 12.77 N ATOM 1623 CA LEU A 209 -13.316 32.062 0.716 1.00 12.64 C ATOM 1624 C LEU A 209 -14.705 32.600 0.372 1.00 13.13 C ATOM 1625 O LEU A 209 -15.581 31.842 -0.033 1.00 13.00 O ATOM 1626 CB LEU A 209 -13.180 31.847 2.231 1.00 12.88 C ATOM 1627 CG LEU A 209 -14.217 30.911 2.873 1.00 13.54 C ATOM 1628 CD1 LEU A 209 -14.186 29.528 2.225 1.00 13.61 C ATOM 1629 CD2 LEU A 209 -13.984 30.806 4.381 1.00 15.08 C ATOM 1630 N GLU A 210 -14.889 33.915 0.500 1.00 13.80 N ATOM 1631 CA GLU A 210 -16.161 34.546 0.153 1.00 14.60 C ATOM 1632 C GLU A 210 -16.546 34.264 -1.304 1.00 13.87 C ATOM 1633 O GLU A 210 -17.685 33.899 -1.595 1.00 13.31 O ATOM 1634 CB GLU A 210 -16.091 36.058 0.405 1.00 15.47 C ATOM 1635 CG GLU A 210 -17.396 36.800 0.149 1.00 18.51 C ATOM 1636 CD GLU A 210 -17.313 38.286 0.470 1.00 23.13 C ATOM 1637 OE1 GLU A 210 -16.279 38.918 0.164 1.00 26.72 O ATOM 1638 OE2 GLU A 210 -18.300 38.831 1.011 1.00 26.43 O1- ATOM 1639 N PHE A 211 -15.592 34.408 -2.217 1.00 13.25 N ATOM 1640 CA PHE A 211 -15.865 34.162 -3.629 1.00 13.02 C ATOM 1641 C PHE A 211 -16.192 32.692 -3.893 1.00 12.47 C ATOM 1642 O PHE A 211 -17.170 32.386 -4.576 1.00 11.82 O ATOM 1643 CB PHE A 211 -14.700 34.606 -4.509 1.00 13.26 C ATOM 1644 CG PHE A 211 -14.981 34.470 -5.981 1.00 15.23 C ATOM 1645 CD1 PHE A 211 -15.938 35.271 -6.594 1.00 17.66 C ATOM 1646 CD2 PHE A 211 -14.316 33.525 -6.748 1.00 16.12 C ATOM 1647 CE1 PHE A 211 -16.212 35.149 -7.949 1.00 17.29 C ATOM 1648 CE2 PHE A 211 -14.589 33.393 -8.113 1.00 16.79 C ATOM 1649 CZ PHE A 211 -15.537 34.208 -8.711 1.00 17.33 C ATOM 1650 N LEU A 212 -15.390 31.782 -3.344 1.00 12.17 N ATOM 1651 CA LEU A 212 -15.667 30.345 -3.499 1.00 12.38 C ATOM 1652 C LEU A 212 -17.069 29.970 -3.007 1.00 12.47 C ATOM 1653 O LEU A 212 -17.739 29.137 -3.624 1.00 11.70 O ATOM 1654 CB LEU A 212 -14.643 29.471 -2.772 1.00 12.94 C ATOM 1655 CG LEU A 212 -13.142 29.539 -3.070 1.00 14.87 C ATOM 1656 CD1 LEU A 212 -12.480 28.159 -2.903 1.00 15.48 C ATOM 1657 CD2 LEU A 212 -12.836 30.127 -4.421 1.00 15.64 C ATOM 1658 N LYS A 213 -17.494 30.568 -1.894 1.00 12.44 N ATOM 1659 CA LYS A 213 -18.817 30.275 -1.326 1.00 13.50 C ATOM 1660 C LYS A 213 -19.923 30.799 -2.228 1.00 13.57 C ATOM 1661 O LYS A 213 -20.919 30.120 -2.451 1.00 13.41 O ATOM 1662 CB LYS A 213 -18.959 30.850 0.090 1.00 14.00 C ATOM 1663 CG LYS A 213 -18.228 30.032 1.161 1.00 15.50 C ATOM 1664 CD LYS A 213 -18.570 30.498 2.585 1.00 18.81 C ATOM 1665 CE LYS A 213 -18.233 29.444 3.633 1.00 20.95 C ATOM 1666 NZ LYS A 213 -18.947 29.652 4.944 1.00 23.34 N1+ ATOM 1667 N GLU A 214 -19.736 32.005 -2.757 1.00 13.58 N ATOM 1668 CA GLU A 214 -20.708 32.597 -3.683 1.00 14.18 C ATOM 1669 C GLU A 214 -20.853 31.742 -4.936 1.00 13.91 C ATOM 1670 O GLU A 214 -21.966 31.504 -5.409 1.00 13.29 O ATOM 1671 CB GLU A 214 -20.290 34.018 -4.065 1.00 14.65 C ATOM 1672 CG GLU A 214 -20.403 35.030 -2.928 1.00 16.91 C ATOM 1673 CD GLU A 214 -19.690 36.342 -3.208 1.00 20.31 C ATOM 1674 OE1 GLU A 214 -19.164 36.525 -4.331 1.00 25.43 O ATOM 1675 OE2 GLU A 214 -19.666 37.206 -2.303 1.00 22.14 O1- ATOM 1676 N VAL A 215 -19.729 31.284 -5.479 1.00 13.92 N ATOM 1677 CA VAL A 215 -19.753 30.458 -6.681 1.00 13.93 C ATOM 1678 C VAL A 215 -20.442 29.122 -6.415 1.00 14.47 C ATOM 1679 O VAL A 215 -21.257 28.682 -7.219 1.00 13.99 O ATOM 1680 CB VAL A 215 -18.346 30.238 -7.256 1.00 14.04 C ATOM 1681 CG1 VAL A 215 -18.376 29.192 -8.363 1.00 13.99 C ATOM 1682 CG2 VAL A 215 -17.801 31.557 -7.779 1.00 13.38 C ATOM 1683 N TRP A 216 -20.140 28.500 -5.277 1.00 14.83 N ATOM 1684 CA TRP A 216 -20.795 27.247 -4.891 1.00 15.50 C ATOM 1685 C TRP A 216 -22.311 27.403 -4.848 1.00 16.63 C ATOM 1686 O TRP A 216 -23.041 26.581 -5.399 1.00 15.70 O ATOM 1687 CB TRP A 216 -20.295 26.769 -3.524 1.00 15.31 C ATOM 1688 CG TRP A 216 -20.760 25.397 -3.158 1.00 14.63 C ATOM 1689 CD1 TRP A 216 -21.788 25.075 -2.325 1.00 14.15 C ATOM 1690 CD2 TRP A 216 -20.198 24.155 -3.603 1.00 13.95 C ATOM 1691 CE2 TRP A 216 -20.943 23.121 -3.003 1.00 13.89 C ATOM 1692 CE3 TRP A 216 -19.147 23.820 -4.464 1.00 13.97 C ATOM 1693 NE1 TRP A 216 -21.908 23.707 -2.227 1.00 14.50 N ATOM 1694 CZ2 TRP A 216 -20.661 21.768 -3.229 1.00 13.88 C ATOM 1695 CZ3 TRP A 216 -18.862 22.483 -4.682 1.00 13.81 C ATOM 1696 CH2 TRP A 216 -19.625 21.471 -4.073 1.00 14.35 C ATOM 1697 N LEU A 217 -22.774 28.468 -4.197 1.00 17.99 N ATOM 1698 CA LEU A 217 -24.214 28.709 -4.052 1.00 19.87 C ATOM 1699 C LEU A 217 -24.871 29.019 -5.395 1.00 21.41 C ATOM 1700 O LEU A 217 -25.967 28.531 -5.675 1.00 21.91 O ATOM 1701 CB LEU A 217 -24.476 29.839 -3.052 1.00 19.78 C ATOM 1702 CG LEU A 217 -24.160 29.502 -1.592 1.00 20.40 C ATOM 1703 CD1 LEU A 217 -24.250 30.741 -0.723 1.00 21.35 C ATOM 1704 CD2 LEU A 217 -25.085 28.406 -1.075 1.00 21.85 C ATOM 1705 N GLN A 218 -24.191 29.812 -6.223 1.00 23.41 N ATOM 1706 CA GLN A 218 -24.681 30.142 -7.568 1.00 24.92 C ATOM 1707 C GLN A 218 -24.774 28.919 -8.484 1.00 26.68 C ATOM 1708 O GLN A 218 -25.655 28.851 -9.342 1.00 26.76 O ATOM 1709 CB GLN A 218 -23.782 31.205 -8.215 1.00 24.71 C ATOM 1710 CG GLN A 218 -23.949 32.598 -7.616 1.00 24.42 C ATOM 1711 CD GLN A 218 -22.733 33.499 -7.791 1.00 24.51 C ATOM 1712 NE2 GLN A 218 -22.580 34.449 -6.873 1.00 23.85 N ATOM 1713 OE1 GLN A 218 -21.946 33.355 -8.737 1.00 24.10 O ATOM 1714 N LYS A 219 -23.869 27.960 -8.288 1.00 28.87 N ATOM 1715 CA LYS A 219 -23.741 26.797 -9.175 1.00 30.67 C ATOM 1716 C LYS A 219 -24.739 25.675 -8.872 1.00 32.31 C ATOM 1717 O LYS A 219 -24.930 24.783 -9.696 1.00 32.72 O ATOM 1718 CB LYS A 219 -22.306 26.245 -9.131 1.00 30.68 C ATOM 1719 CG LYS A 219 -21.310 26.869 -10.128 1.00 31.08 C ATOM 1720 CD LYS A 219 -21.413 28.396 -10.296 1.00 31.91 C ATOM 1721 CE LYS A 219 -22.026 28.771 -11.641 1.00 32.93 C ATOM 1722 NZ LYS A 219 -22.137 30.245 -11.845 1.00 33.27 N1+ ATOM 1723 N GLN A 220 -25.362 25.702 -7.697 1.00 34.20 N ATOM 1724 CA GLN A 220 -26.435 24.756 -7.391 1.00 35.76 C ATOM 1725 C GLN A 220 -27.784 25.481 -7.388 1.00 36.73 C ATOM 1726 O GLN A 220 -28.592 25.352 -6.469 1.00 37.38 O ATOM 1727 CB GLN A 220 -26.131 23.999 -6.097 1.00 35.86 C ATOM 1728 CG GLN A 220 -25.157 22.830 -6.326 1.00 36.74 C ATOM 1729 CD GLN A 220 -24.023 22.785 -5.322 1.00 37.26 C ATOM 1730 NE2 GLN A 220 -22.796 22.937 -5.810 1.00 37.04 N ATOM 1731 OE1 GLN A 220 -24.244 22.604 -4.125 1.00 38.39 O ATOM 1732 N LYS A 221 -27.984 26.264 -8.447 1.00 37.92 N ATOM 1733 CA LYS A 221 -29.273 26.842 -8.801 1.00 38.57 C ATOM 1734 C LYS A 221 -29.469 26.620 -10.304 1.00 38.85 C ATOM 1735 O LYS A 221 -29.605 25.484 -10.760 1.00 39.14 O ATOM 1736 CB LYS A 221 -29.308 28.338 -8.474 1.00 38.80 C ATOM 1737 CG LYS A 221 -30.652 29.003 -8.777 1.00 39.46 C ATOM 1738 CD LYS A 221 -30.496 30.251 -9.645 1.00 40.23 C ATOM 1739 CE LYS A 221 -31.839 30.704 -10.211 1.00 40.57 C ATOM 1740 NZ LYS A 221 -32.457 29.683 -11.107 1.00 40.79 N1+ ATOM 1741 OXT LYS A 221 -29.477 27.553 -11.111 1.00 39.13 O1- TER HETATM 1742 MG MG A1222 -1.005 23.999 -12.865 1.00 11.80 MG HETATM 1743 BE BEF A1223 -0.179 21.344 -11.189 1.00 13.23 BE HETATM 1744 F1 BEF A1223 -0.235 19.922 -11.780 1.00 12.50 F HETATM 1745 F2 BEF A1223 0.874 21.443 -10.033 1.00 12.75 F HETATM 1746 F3 BEF A1223 0.088 22.419 -12.289 1.00 13.58 F HETATM 1747 O HOH A2001 -23.405 21.865 -0.249 1.00 27.83 O HETATM 1748 O HOH A2002 -21.233 19.553 -0.341 1.00 23.40 O HETATM 1749 O HOH A2003 -20.330 22.811 6.017 1.00 21.50 O HETATM 1750 O HOH A2004 -18.236 26.046 5.757 1.00 22.90 O HETATM 1751 O HOH A2005 -18.134 23.676 4.630 1.00 14.00 O HETATM 1752 O HOH A2006 -23.859 16.263 1.654 1.00 21.03 O HETATM 1753 O HOH A2007 -15.110 19.548 5.566 1.00 21.40 O HETATM 1754 O HOH A2008 -21.505 17.758 1.546 1.00 19.11 O HETATM 1755 O HOH A2009 -2.246 33.914 -11.604 1.00 23.04 O HETATM 1756 O HOH A2010 -1.720 31.364 -12.717 1.00 13.06 O HETATM 1757 O HOH A2011 5.999 32.736 -7.481 1.00 22.98 O HETATM 1758 O HOH A2012 9.105 30.355 -10.946 1.00 30.20 O HETATM 1759 O HOH A2013 6.675 21.971 -11.846 1.00 23.87 O HETATM 1760 O HOH A2014 14.428 31.808 -5.718 1.00 28.05 O HETATM 1761 O HOH A2015 13.910 7.423 -18.528 1.00 36.95 O HETATM 1762 O HOH A2016 14.274 24.018 -33.789 1.00 26.11 O HETATM 1763 O HOH A2017 21.105 28.369 -13.890 1.00 30.53 O HETATM 1764 O HOH A2018 10.927 21.369 -18.819 1.00 19.14 O HETATM 1765 O HOH A2019 15.279 8.875 -21.669 1.00 18.46 O HETATM 1766 O HOH A2020 26.333 25.321 -15.716 1.00 34.80 O HETATM 1767 O HOH A2021 16.139 11.503 -12.862 1.00 24.63 O HETATM 1768 O HOH A2022 24.452 20.987 -15.242 1.00 23.73 O HETATM 1769 O HOH A2023 26.318 24.108 -29.029 1.00 20.40 O HETATM 1770 O HOH A2024 22.049 28.429 -23.020 1.00 20.57 O HETATM 1771 O HOH A2025 26.089 28.169 -23.630 1.00 37.99 O HETATM 1772 O HOH A2026 1.744 34.747 0.992 1.00 11.49 O HETATM 1773 O HOH A2027 -7.396 37.129 0.164 1.00 21.65 O HETATM 1774 O HOH A2028 1.551 37.867 -1.783 1.00 28.67 O HETATM 1775 O HOH A2029 16.357 30.482 -27.769 1.00 30.31 O HETATM 1776 O HOH A2030 23.026 31.909 -24.535 1.00 29.67 O HETATM 1777 O HOH A2031 20.804 31.849 -21.078 1.00 35.49 O HETATM 1778 O HOH A2032 -1.532 36.513 3.274 1.00 26.68 O HETATM 1779 O HOH A2033 -4.423 37.743 0.890 1.00 29.38 O HETATM 1780 O HOH A2034 14.511 32.411 -26.955 1.00 23.52 O HETATM 1781 O HOH A2035 -4.754 30.666 10.965 1.00 22.88 O HETATM 1782 O HOH A2036 16.762 35.378 -20.188 1.00 25.89 O HETATM 1783 O HOH A2037 -9.936 21.303 9.065 1.00 20.54 O HETATM 1784 O HOH A2038 -18.909 20.956 7.753 1.00 31.23 O HETATM 1785 O HOH A2039 9.889 35.717 -27.452 1.00 30.74 O HETATM 1786 O HOH A2040 3.273 13.686 -3.876 1.00 16.89 O HETATM 1787 O HOH A2041 7.915 27.434 -18.636 1.00 24.37 O HETATM 1788 O HOH A2042 9.607 26.022 -17.051 1.00 31.22 O HETATM 1789 O HOH A2043 9.225 36.422 -21.531 1.00 26.28 O HETATM 1790 O HOH A2044 11.723 21.843 7.376 1.00 30.31 O HETATM 1791 O HOH A2045 11.248 29.466 5.656 1.00 29.72 O HETATM 1792 O HOH A2046 -1.045 27.885 -18.805 1.00 42.57 O HETATM 1793 O HOH A2047 3.967 16.272 -19.806 1.00 45.15 O HETATM 1794 O HOH A2048 7.618 10.323 -7.395 1.00 20.52 O HETATM 1795 O HOH A2049 7.740 12.758 -23.231 1.00 22.77 O HETATM 1796 O HOH A2050 12.849 17.792 -13.401 1.00 21.53 O HETATM 1797 O HOH A2051 12.027 11.774 -12.236 1.00 36.63 O HETATM 1798 O HOH A2052 8.235 14.932 -17.503 1.00 32.98 O HETATM 1799 O HOH A2053 8.111 11.640 -20.753 1.00 29.20 O HETATM 1800 O HOH A2054 14.844 9.780 -19.290 1.00 26.56 O HETATM 1801 O HOH A2055 5.546 16.992 -23.730 1.00 25.03 O HETATM 1802 O HOH A2056 10.786 17.711 -28.528 1.00 32.33 O HETATM 1803 O HOH A2057 -5.730 7.836 2.667 1.00 31.00 O HETATM 1804 O HOH A2058 13.489 12.914 -28.155 1.00 32.75 O HETATM 1805 O HOH A2059 14.329 24.029 -30.016 1.00 17.82 O HETATM 1806 O HOH A2060 13.058 22.434 -31.529 1.00 26.35 O HETATM 1807 O HOH A2061 18.748 18.110 -32.684 1.00 26.71 O HETATM 1808 O HOH A2062 14.493 17.101 -33.093 1.00 29.27 O HETATM 1809 O HOH A2063 15.867 25.105 -32.006 1.00 30.62 O HETATM 1810 O HOH A2064 17.478 21.827 -34.886 1.00 27.12 O HETATM 1811 O HOH A2065 25.414 20.548 -34.759 1.00 21.75 O HETATM 1812 O HOH A2066 20.164 19.811 -40.027 1.00 26.63 O HETATM 1813 O HOH A2067 23.490 21.456 -38.586 1.00 15.09 O HETATM 1814 O HOH A2068 -10.318 14.320 -21.432 1.00 30.21 O HETATM 1815 O HOH A2069 18.635 14.941 -31.183 1.00 31.18 O HETATM 1816 O HOH A2070 -18.634 20.137 -14.113 1.00 33.75 O HETATM 1817 O HOH A2071 -20.834 20.729 -11.180 1.00 33.92 O HETATM 1818 O HOH A2072 25.198 15.773 -33.005 1.00 30.51 O HETATM 1819 O HOH A2073 19.188 12.795 -29.592 1.00 34.34 O HETATM 1820 O HOH A2074 -10.689 36.978 -19.383 1.00 39.60 O HETATM 1821 O HOH A2075 23.617 9.186 -31.988 1.00 36.71 O HETATM 1822 O HOH A2076 16.926 7.296 -23.249 1.00 20.36 O HETATM 1823 O HOH A2077 -18.074 26.439 -24.067 1.00 35.54 O HETATM 1824 O HOH A2078 -1.145 37.682 -9.350 1.00 27.63 O HETATM 1825 O HOH A2079 16.680 10.181 -17.041 1.00 17.46 O HETATM 1826 O HOH A2080 21.431 7.899 -16.484 1.00 26.24 O HETATM 1827 O HOH A2081 23.297 9.325 -8.732 1.00 28.62 O HETATM 1828 O HOH A2082 11.313 19.114 -17.112 1.00 17.37 O HETATM 1829 O HOH A2083 13.554 14.024 -8.433 1.00 45.49 O HETATM 1830 O HOH A2084 18.299 14.460 -7.524 1.00 18.63 O HETATM 1831 O HOH A2085 20.681 17.410 -6.667 1.00 14.54 O HETATM 1832 O HOH A2086 17.701 12.628 -10.674 1.00 15.86 O HETATM 1833 O HOH A2087 23.903 15.293 -11.585 1.00 26.66 O HETATM 1834 O HOH A2088 3.700 32.987 2.030 1.00 10.86 O HETATM 1835 O HOH A2089 8.062 31.224 -7.887 1.00 19.57 O HETATM 1836 O HOH A2090 12.234 32.225 -2.864 1.00 17.03 O HETATM 1837 O HOH A2091 3.583 35.984 -5.070 1.00 30.27 O HETATM 1838 O HOH A2092 -0.565 34.386 -0.438 1.00 12.68 O HETATM 1839 O HOH A2093 1.199 31.372 -13.313 1.00 25.39 O HETATM 1840 O HOH A2094 -1.580 37.879 -0.972 1.00 26.87 O HETATM 1841 O HOH A2095 -7.581 34.705 -0.437 1.00 13.83 O HETATM 1842 O HOH A2096 -2.653 35.555 0.956 1.00 13.80 O HETATM 1843 O HOH A2097 -6.185 28.898 9.998 1.00 15.29 O HETATM 1844 O HOH A2098 -2.556 35.562 5.375 1.00 29.93 O HETATM 1845 O HOH A2099 -8.730 32.528 9.178 1.00 23.80 O HETATM 1846 O HOH A2100 -5.656 20.477 8.693 1.00 28.81 O HETATM 1847 O HOH A2101 -17.734 25.513 8.513 1.00 22.32 O HETATM 1848 O HOH A2102 -13.584 33.074 8.315 1.00 35.19 O HETATM 1849 O HOH A2103 -16.548 21.809 6.386 1.00 26.42 O HETATM 1850 O HOH A2104 -8.550 21.710 6.746 1.00 15.92 O HETATM 1851 O HOH A2105 -11.726 19.383 9.278 1.00 29.27 O HETATM 1852 O HOH A2106 3.172 20.662 -11.660 1.00 34.96 O HETATM 1853 O HOH A2107 3.521 13.673 -12.706 1.00 30.96 O HETATM 1854 O HOH A2108 7.848 20.418 -9.699 1.00 17.97 O HETATM 1855 O HOH A2109 2.581 16.154 -5.164 1.00 14.94 O HETATM 1856 O HOH A2110 7.404 16.119 -11.213 1.00 25.54 O HETATM 1857 O HOH A2111 10.891 12.685 -5.416 1.00 29.12 O HETATM 1858 O HOH A2112 11.668 15.908 -9.795 1.00 27.61 O HETATM 1859 O HOH A2113 11.294 19.212 7.013 1.00 22.84 O HETATM 1860 O HOH A2114 11.491 28.028 3.467 1.00 26.47 O HETATM 1861 O HOH A2115 3.764 30.843 3.702 1.00 15.40 O HETATM 1862 O HOH A2116 8.985 26.842 7.428 1.00 31.20 O HETATM 1863 O HOH A2117 2.618 29.751 6.119 1.00 17.52 O HETATM 1864 O HOH A2118 5.474 23.801 6.182 1.00 25.43 O HETATM 1865 O HOH A2119 4.747 19.025 2.820 1.00 22.81 O HETATM 1866 O HOH A2120 2.284 25.218 7.541 1.00 21.02 O HETATM 1867 O HOH A2121 -2.248 30.162 10.370 1.00 28.68 O HETATM 1868 O HOH A2122 -5.926 22.687 7.335 1.00 15.71 O HETATM 1869 O HOH A2123 1.530 30.685 8.455 1.00 17.46 O HETATM 1870 O HOH A2124 -3.853 14.857 7.486 1.00 30.55 O HETATM 1871 O HOH A2125 -8.606 18.417 9.005 1.00 23.78 O HETATM 1872 O HOH A2126 -5.351 16.547 8.583 1.00 19.33 O HETATM 1873 O HOH A2127 -2.977 10.383 0.503 1.00 33.93 O HETATM 1874 O HOH A2128 -1.786 12.367 1.965 1.00 21.36 O HETATM 1875 O HOH A2129 -0.108 16.166 -5.774 1.00 13.20 O HETATM 1876 O HOH A2130 5.308 11.431 -6.403 1.00 30.62 O HETATM 1877 O HOH A2131 4.118 6.136 -4.591 1.00 22.65 O HETATM 1878 O HOH A2132 0.338 12.275 -12.831 1.00 35.24 O HETATM 1879 O HOH A2133 5.024 5.444 -10.514 1.00 25.17 O HETATM 1880 O HOH A2134 -2.474 9.337 -3.454 1.00 24.85 O HETATM 1881 O HOH A2135 -5.877 6.905 -8.480 1.00 35.51 O HETATM 1882 O HOH A2136 -5.566 5.786 -10.881 1.00 23.50 O HETATM 1883 O HOH A2137 -5.268 12.318 -13.052 1.00 11.69 O HETATM 1884 O HOH A2138 -4.371 11.095 -19.473 1.00 21.47 O HETATM 1885 O HOH A2139 -0.792 19.917 -14.290 1.00 24.83 O HETATM 1886 O HOH A2140 -1.387 15.059 -14.001 1.00 20.41 O HETATM 1887 O HOH A2141 -8.211 8.046 -8.262 1.00 23.15 O HETATM 1888 O HOH A2142 -6.329 8.846 -2.311 1.00 23.45 O HETATM 1889 O HOH A2143 -5.976 10.316 4.104 1.00 19.86 O HETATM 1890 O HOH A2144 -6.960 13.323 5.489 1.00 24.56 O HETATM 1891 O HOH A2145 -13.644 14.208 5.932 1.00 14.63 O HETATM 1892 O HOH A2146 -22.125 18.685 -2.898 1.00 31.98 O HETATM 1893 O HOH A2147 -22.314 15.780 -3.229 1.00 29.09 O HETATM 1894 O HOH A2148 -18.541 12.786 -6.534 1.00 21.13 O HETATM 1895 O HOH A2149 -20.857 11.937 -4.912 1.00 23.91 O HETATM 1896 O HOH A2150 -18.015 12.458 2.538 1.00 12.01 O HETATM 1897 O HOH A2151 -20.451 15.398 4.075 1.00 25.72 O HETATM 1898 O HOH A2152 -2.029 22.583 -14.038 1.00 14.94 O HETATM 1899 O HOH A2153 -4.169 29.576 -16.990 1.00 24.48 O HETATM 1900 O HOH A2154 0.436 24.439 -14.426 1.00 12.43 O HETATM 1901 O HOH A2155 -3.709 25.151 -20.536 1.00 22.67 O HETATM 1902 O HOH A2156 -7.655 18.181 -21.935 1.00 25.38 O HETATM 1903 O HOH A2157 -3.634 21.898 -20.614 1.00 18.88 O HETATM 1904 O HOH A2158 -12.948 21.153 -19.686 1.00 27.89 O HETATM 1905 O HOH A2159 -18.701 13.959 -14.085 1.00 32.53 O HETATM 1906 O HOH A2160 -10.929 13.507 -18.800 1.00 21.68 O HETATM 1907 O HOH A2161 -20.747 16.115 -9.501 1.00 22.22 O HETATM 1908 O HOH A2162 -17.827 18.334 -12.323 1.00 26.59 O HETATM 1909 O HOH A2163 -17.311 26.789 -12.767 1.00 13.75 O HETATM 1910 O HOH A2164 -2.804 31.222 -15.285 1.00 28.26 O HETATM 1911 O HOH A2165 -10.006 35.991 -16.964 1.00 25.03 O HETATM 1912 O HOH A2166 -8.970 29.481 -27.746 1.00 20.63 O HETATM 1913 O HOH A2167 -5.052 26.024 -23.097 1.00 28.77 O HETATM 1914 O HOH A2168 -4.994 31.322 -18.976 1.00 20.11 O HETATM 1915 O HOH A2169 -13.114 23.708 -20.144 1.00 32.56 O HETATM 1916 O HOH A2170 -19.598 29.710 -25.163 1.00 21.74 O HETATM 1917 O HOH A2171 -15.374 26.082 -23.882 1.00 20.92 O HETATM 1918 O HOH A2172 -18.817 23.057 -17.484 1.00 42.01 O HETATM 1919 O HOH A2173 -21.016 27.354 -14.501 1.00 46.97 O HETATM 1920 O HOH A2174 -15.220 30.609 -18.893 1.00 17.78 O HETATM 1921 O HOH A2175 -12.164 36.077 -15.675 1.00 28.86 O HETATM 1922 O HOH A2176 -16.187 33.328 -15.434 1.00 19.68 O HETATM 1923 O HOH A2177 -15.047 35.566 -12.200 1.00 22.89 O HETATM 1924 O HOH A2178 -5.671 36.522 -16.523 1.00 24.07 O HETATM 1925 O HOH A2179 -3.002 35.406 -13.675 1.00 19.64 O HETATM 1926 O HOH A2180 -1.873 35.112 -9.264 1.00 18.91 O HETATM 1927 O HOH A2181 -7.157 38.250 -2.058 1.00 24.33 O HETATM 1928 O HOH A2182 -14.194 37.975 -2.116 1.00 27.13 O HETATM 1929 O HOH A2183 -9.896 33.727 1.621 1.00 24.05 O HETATM 1930 O HOH A2184 -13.098 35.565 2.107 1.00 17.56 O HETATM 1931 O HOH A2185 -17.075 32.726 5.496 1.00 36.61 O HETATM 1932 O HOH A2186 -16.686 38.134 -3.514 1.00 34.56 O HETATM 1933 O HOH A2187 -20.248 36.350 -7.078 1.00 30.31 O HETATM 1934 O HOH A2188 -22.700 33.031 -11.613 1.00 18.96 O CONECT 67 1743 CONECT 1743 67 1744 1745 1746 CONECT 1744 1743 CONECT 1745 1743 CONECT 1746 1743 END A second structure was input as follows:CRYST1 32.100 72.700 85.200 90.00 90.00 90.00 P 21 21 21 1 ATOM 1 N MET A 1 -10.304 16.771 31.244 1.00 14.40 N ANISOU 1 N MET A 1 1800 1882 1786 -9 2 -2 N ATOM 2 CA AMET A 1 -9.077 16.559 30.404 0.50 14.12 C ANISOU 2 CA AMET A 1 1771 1822 1771 -2 -2 4 C ATOM 3 CA BMET A 1 -9.098 16.526 30.390 0.50 13.84 C ANISOU 3 CA BMET A 1 1741 1778 1737 -5 -2 2 C ATOM 4 C MET A 1 -9.375 17.111 29.017 1.00 13.60 C ANISOU 4 C MET A 1 1700 1753 1712 -14 1 4 C ATOM 5 O MET A 1 -10.501 17.036 28.536 1.00 13.96 O ANISOU 5 O MET A 1 1690 1849 1762 -16 17 14 O ATOM 6 CB AMET A 1 -8.659 15.084 30.340 0.50 14.50 C ANISOU 6 CB AMET A 1 1826 1857 1824 0 4 0 C ATOM 7 CB BMET A 1 -8.831 15.018 30.294 0.50 14.02 C ANISOU 7 CB BMET A 1 1769 1792 1766 -5 2 -4 C ATOM 8 CG AMET A 1 -7.176 14.825 30.566 0.50 15.20 C ANISOU 8 CG AMET A 1 1901 1957 1915 23 2 1 C ATOM 9 CG BMET A 1 -7.735 14.589 29.320 0.50 13.81 C ANISOU 9 CG BMET A 1 1776 1734 1736 -11 8 8 C ATOM 10 SD AMET A 1 -6.107 16.211 30.135 0.50 16.45 S ANISOU 10 SD AMET A 1 2077 2161 2010 15 72 105 S ATOM 11 SD BMET A 1 -6.068 15.127 29.754 0.50 13.38 S ANISOU 11 SD BMET A 1 1812 1585 1684 -47 94 -9 S ATOM 12 CE AMET A 1 -5.078 15.404 28.913 0.50 16.70 C ANISOU 12 CE AMET A 1 2102 2134 2107 8 23 5 C ATOM 13 CE BMET A 1 -5.211 14.713 28.234 0.50 13.30 C ANISOU 13 CE BMET A 1 1721 1654 1675 -28 39 -11 C ATOM 14 N PHE A 2 -8.362 17.701 28.387 1.00 12.26 N ANISOU 14 N PHE A 2 1545 1581 1528 -11 -13 -7 N ATOM 15 CA PHE A 2 -8.547 18.241 27.038 1.00 11.27 C ANISOU 15 CA PHE A 2 1426 1433 1422 -9 2 -18 C ATOM 16 C PHE A 2 -8.741 17.101 26.041 1.00 10.53 C ANISOU 16 C PHE A 2 1329 1326 1346 -14 2 -8 C ATOM 17 O PHE A 2 -8.216 16.002 26.228 1.00 10.55 O ANISOU 17 O PHE A 2 1345 1336 1327 -2 -28 10 O ATOM 18 CB PHE A 2 -7.401 19.181 26.605 1.00 11.07 C ANISOU 18 CB PHE A 2 1405 1403 1396 -8 -13 -15 C ATOM 19 CG PHE A 2 -6.024 18.561 26.638 1.00 10.55 C ANISOU 19 CG PHE A 2 1346 1354 1307 -21 -1 -50 C ATOM 20 CD1 PHE A 2 -5.471 17.990 25.496 1.00 9.94 C ANISOU 20 CD1 PHE A 2 1265 1270 1240 -25 -2 -22 C ATOM 21 CD2 PHE A 2 -5.258 18.595 27.796 1.00 10.18 C ANISOU 21 CD2 PHE A 2 1315 1288 1263 -19 11 4 C ATOM 22 CE1 PHE A 2 -4.200 17.436 25.521 1.00 9.98 C ANISOU 22 CE1 PHE A 2 1298 1254 1239 -52 17 -5 C ATOM 23 CE2 PHE A 2 -3.987 18.045 27.826 1.00 10.46 C ANISOU 23 CE2 PHE A 2 1328 1319 1324 -32 9 -7 C ATOM 24 CZ PHE A 2 -3.460 17.461 26.688 1.00 10.13 C ANISOU 24 CZ PHE A 2 1239 1271 1336 -20 -4 -33 C ATOM 25 N LYS A 3 -9.515 17.376 24.997 1.00 9.53 N ANISOU 25 N LYS A 3 1201 1199 1220 -19 11 -26 N ATOM 26 CA LYS A 3 -9.858 16.381 23.976 1.00 9.09 C ANISOU 26 CA LYS A 3 1153 1154 1147 -23 21 -23 C ATOM 27 C LYS A 3 -9.077 16.547 22.672 1.00 8.29 C ANISOU 27 C LYS A 3 1037 1037 1076 -33 44 -39 C ATOM 28 O LYS A 3 -9.084 15.646 21.829 1.00 8.42 O ANISOU 28 O LYS A 3 1067 1024 1105 -102 60 -80 O ATOM 29 CB LYS A 3 -11.348 16.458 23.651 1.00 9.39 C ANISOU 29 CB LYS A 3 1172 1206 1188 -14 25 -18 C ATOM 30 CG LYS A 3 -12.264 16.028 24.774 1.00 11.13 C ANISOU 30 CG LYS A 3 1424 1416 1390 -16 78 10 C ATOM 31 CD LYS A 3 -13.706 16.003 24.291 1.00 13.76 C ANISOU 31 CD LYS A 3 1699 1763 1763 -9 2 -16 C ATOM 32 CE LYS A 3 -14.634 15.386 25.319 1.00 15.58 C ANISOU 32 CE LYS A 3 1965 1980 1973 -14 52 40 C ATOM 33 NZ LYS A 3 -14.525 16.066 26.630 1.00 17.27 N1+ ANISOU 33 NZ LYS A 3 2198 2181 2184 -34 -2 -33 N1+ ATOM 34 N ALA A 4 -8.414 17.688 22.495 1.00 7.51 N ANISOU 34 N ALA A 4 966 937 950 -23 45 -30 N ATOM 35 CA ALA A 4 -7.708 17.976 21.247 1.00 6.97 C ANISOU 35 CA ALA A 4 883 878 887 -18 43 -45 C ATOM 36 C ALA A 4 -6.565 18.949 21.453 1.00 6.45 C ANISOU 36 C ALA A 4 821 815 814 -25 55 -30 C ATOM 37 O ALA A 4 -6.597 19.774 22.363 1.00 6.52 O ANISOU 37 O ALA A 4 811 844 820 -43 115 -50 O ATOM 38 CB ALA A 4 -8.665 18.539 20.217 1.00 6.98 C ANISOU 38 CB ALA A 4 879 905 867 -19 35 -45 C ATOM 39 N VAL A 5 -5.560 18.846 20.588 1.00 5.86 N ANISOU 39 N VAL A 5 743 703 779 -10 59 -20 N ATOM 40 CA VAL A 5 -4.496 19.837 20.515 1.00 5.55 C ANISOU 40 CA VAL A 5 717 671 717 -2 9 -28 C ATOM 41 C VAL A 5 -4.478 20.387 19.098 1.00 5.46 C ANISOU 41 C VAL A 5 704 661 709 -5 19 -33 C ATOM 42 O VAL A 5 -4.482 19.624 18.118 1.00 5.34 O ANISOU 42 O VAL A 5 696 635 697 -4 16 -23 O ATOM 43 CB VAL A 5 -3.121 19.261 20.902 1.00 5.52 C ANISOU 43 CB VAL A 5 690 689 717 -8 28 -13 C ATOM 44 CG1 VAL A 5 -2.052 20.342 20.823 1.00 5.53 C ANISOU 44 CG1 VAL A 5 702 738 658 -57 30 18 C ATOM 45 CG2 VAL A 5 -3.168 18.675 22.308 1.00 5.79 C ANISOU 45 CG2 VAL A 5 756 751 690 47 -26 2 C ATOM 46 N LEU A 6 -4.494 21.714 19.007 1.00 5.35 N ANISOU 46 N LEU A 6 716 648 668 10 5 -19 N ATOM 47 CA LEU A 6 -4.568 22.430 17.744 1.00 5.17 C ANISOU 47 CA LEU A 6 664 646 650 23 5 -17 C ATOM 48 C LEU A 6 -3.201 23.060 17.489 1.00 5.04 C ANISOU 48 C LEU A 6 646 624 641 11 -2 -18 C ATOM 49 O LEU A 6 -2.779 23.962 18.212 1.00 5.26 O ANISOU 49 O LEU A 6 668 695 634 -2 37 -67 O ATOM 50 CB LEU A 6 -5.677 23.496 17.799 1.00 5.00 C ANISOU 50 CB LEU A 6 645 638 616 16 -15 -5 C ATOM 51 CG LEU A 6 -6.993 23.071 18.475 1.00 5.47 C ANISOU 51 CG LEU A 6 718 669 689 5 9 -23 C ATOM 52 CD1 LEU A 6 -7.931 24.261 18.576 1.00 6.45 C ANISOU 52 CD1 LEU A 6 743 866 840 87 38 -26 C ATOM 53 CD2 LEU A 6 -7.667 21.899 17.760 1.00 6.47 C ANISOU 53 CD2 LEU A 6 828 853 774 -60 -10 -28 C ATOM 54 N PHE A 7 -2.503 22.547 16.479 1.00 5.06 N ANISOU 54 N PHE A 7 619 670 631 2 -1 -33 N ATOM 55 CA PHE A 7 -1.122 22.940 16.187 1.00 4.94 C ANISOU 55 CA PHE A 7 600 657 618 4 9 -25 C ATOM 56 C PHE A 7 -1.027 24.002 15.107 1.00 4.97 C ANISOU 56 C PHE A 7 565 675 644 16 7 -16 C ATOM 57 O PHE A 7 -1.477 23.794 13.989 1.00 5.16 O ANISOU 57 O PHE A 7 592 732 636 5 -2 -33 O ATOM 58 CB PHE A 7 -0.316 21.743 15.663 1.00 5.09 C ANISOU 58 CB PHE A 7 624 675 634 22 11 -11 C ATOM 59 CG PHE A 7 0.032 20.721 16.701 1.00 5.26 C ANISOU 59 CG PHE A 7 651 661 684 45 4 -1 C ATOM 60 CD1 PHE A 7 1.306 20.682 17.253 1.00 6.28 C ANISOU 60 CD1 PHE A 7 761 883 743 -53 -35 -9 C ATOM 61 CD2 PHE A 7 -0.902 19.777 17.112 1.00 5.56 C ANISOU 61 CD2 PHE A 7 646 747 719 -20 -17 2 C ATOM 62 CE1 PHE A 7 1.642 19.724 18.197 1.00 6.59 C ANISOU 62 CE1 PHE A 7 765 862 875 22 9 19 C ATOM 63 CE2 PHE A 7 -0.565 18.812 18.059 1.00 6.17 C ANISOU 63 CE2 PHE A 7 743 764 835 -28 9 27 C ATOM 64 CZ PHE A 7 0.705 18.793 18.607 1.00 7.04 C ANISOU 64 CZ PHE A 7 893 838 941 2 -4 -11 C ATOM 65 N ASP A 8 -0.385 25.117 15.422 1.00 4.91 N ANISOU 65 N ASP A 8 595 665 605 30 0 -21 N ATOM 66 CA ASP A 8 0.204 25.949 14.389 1.00 5.52 C ANISOU 66 CA ASP A 8 691 714 688 16 -15 -5 C ATOM 67 C ASP A 8 1.359 25.148 13.757 1.00 5.59 C ANISOU 67 C ASP A 8 678 732 712 19 -23 2 C ATOM 68 O ASP A 8 1.863 24.206 14.365 1.00 5.33 O ANISOU 68 O ASP A 8 702 704 618 2 -56 2 O ATOM 69 CB ASP A 8 0.689 27.252 15.013 1.00 5.60 C ANISOU 69 CB ASP A 8 706 719 701 19 -2 -10 C ATOM 70 CG ASP A 8 1.356 28.162 14.024 1.00 6.49 C ANISOU 70 CG ASP A 8 804 840 819 -9 -18 32 C ATOM 71 OD1 ASP A 8 0.837 28.323 12.894 1.00 6.63 O ANISOU 71 OD1 ASP A 8 832 927 759 -21 -28 59 O ATOM 72 OD2 ASP A 8 2.407 28.725 14.379 1.00 7.93 O1- ANISOU 72 OD2 ASP A 8 909 980 1124 -15 -31 18 O1- ATOM 73 N LEU A 9 1.752 25.493 12.533 1.00 5.62 N ANISOU 73 N LEU A 9 695 731 708 33 -28 1 N ATOM 74 CA LEU A 9 2.846 24.799 11.848 1.00 6.30 C ANISOU 74 CA LEU A 9 772 824 796 16 -17 -8 C ATOM 75 C LEU A 9 4.171 25.546 12.009 1.00 6.46 C ANISOU 75 C LEU A 9 783 853 816 19 -18 2 C ATOM 76 O LEU A 9 5.069 25.061 12.702 1.00 6.44 O ANISOU 76 O LEU A 9 724 874 846 22 -15 28 O ATOM 77 CB LEU A 9 2.508 24.596 10.367 1.00 6.61 C ANISOU 77 CB LEU A 9 801 885 824 23 -11 -4 C ATOM 78 CG LEU A 9 3.510 23.819 9.514 1.00 8.28 C ANISOU 78 CG LEU A 9 1007 1148 988 43 -5 -68 C ATOM 79 CD1 LEU A 9 3.497 22.359 9.878 1.00 10.65 C ANISOU 79 CD1 LEU A 9 1278 1383 1384 47 18 17 C ATOM 80 CD2 LEU A 9 3.184 24.015 8.034 1.00 10.86 C ANISOU 80 CD2 LEU A 9 1409 1526 1189 87 -56 -23 C ATOM 81 N ASP A 10 4.292 26.714 11.380 1.00 6.60 N ANISOU 81 N ASP A 10 827 849 830 33 -43 -11 N ATOM 82 CA ASP A 10 5.548 27.461 11.387 1.00 7.32 C ANISOU 82 CA ASP A 10 908 912 958 16 -15 21 C ATOM 83 C ASP A 10 5.890 27.945 12.794 1.00 7.11 C ANISOU 83 C ASP A 10 884 882 935 15 5 1 C ATOM 84 O ASP A 10 5.105 28.649 13.432 1.00 7.28 O ANISOU 84 O ASP A 10 869 864 1032 39 0 7 O ATOM 85 CB ASP A 10 5.503 28.647 10.412 1.00 7.68 C ANISOU 85 CB ASP A 10 968 949 999 23 -7 44 C ATOM 86 CG ASP A 10 6.795 29.458 10.406 1.00 10.61 C ANISOU 86 CG ASP A 10 1234 1303 1490 -16 -47 44 C ATOM 87 OD1 ASP A 10 7.896 28.860 10.412 1.00 14.02 O ANISOU 87 OD1 ASP A 10 1555 1743 2027 76 86 86 O ATOM 88 OD2 ASP A 10 6.711 30.703 10.394 1.00 15.09 O1- ANISOU 88 OD2 ASP A 10 1897 1626 2209 -43 -19 38 O1- ATOM 89 N GLY A 11 7.064 27.547 13.272 1.00 6.95 N ANISOU 89 N GLY A 11 880 869 892 -9 -37 19 N ATOM 90 CA GLY A 11 7.529 27.908 14.605 1.00 6.74 C ANISOU 90 CA GLY A 11 868 852 840 -1 -8 -8 C ATOM 91 C GLY A 11 7.067 26.984 15.721 1.00 6.58 C ANISOU 91 C GLY A 11 840 821 838 -11 -13 0 C ATOM 92 O GLY A 11 7.403 27.207 16.883 1.00 7.05 O ANISOU 92 O GLY A 11 942 881 853 -62 -5 -5 O ATOM 93 N VAL A 12 6.299 25.950 15.381 1.00 6.28 N ANISOU 93 N VAL A 12 798 796 789 -2 -26 -4 N ATOM 94 CA VAL A 12 5.847 24.963 16.362 1.00 6.34 C ANISOU 94 CA VAL A 12 792 815 801 11 -23 -5 C ATOM 95 C VAL A 12 6.264 23.561 15.908 1.00 6.26 C ANISOU 95 C VAL A 12 780 809 787 15 -14 -27 C ATOM 96 O VAL A 12 7.018 22.873 16.598 1.00 6.16 O ANISOU 96 O VAL A 12 769 786 786 56 1 -37 O ATOM 97 CB VAL A 12 4.318 25.036 16.582 1.00 6.27 C ANISOU 97 CB VAL A 12 806 774 801 22 -13 -35 C ATOM 98 CG1 VAL A 12 3.854 23.923 17.509 1.00 7.30 C ANISOU 98 CG1 VAL A 12 906 920 948 11 -32 36 C ATOM 99 CG2 VAL A 12 3.925 26.407 17.136 1.00 6.82 C ANISOU 99 CG2 VAL A 12 873 816 900 31 -31 -77 C ATOM 100 N ILE A 13 5.783 23.142 14.742 1.00 6.28 N ANISOU 100 N ILE A 13 798 801 783 43 -28 -17 N ATOM 101 CA ILE A 13 6.149 21.836 14.184 1.00 6.63 C ANISOU 101 CA ILE A 13 842 856 818 49 -13 -33 C ATOM 102 C ILE A 13 7.475 21.891 13.428 1.00 7.20 C ANISOU 102 C ILE A 13 909 935 892 53 -15 -28 C ATOM 103 O ILE A 13 8.271 20.951 13.500 1.00 7.01 O ANISOU 103 O ILE A 13 896 954 811 111 -15 -7 O ATOM 104 CB ILE A 13 5.040 21.308 13.250 1.00 6.39 C ANISOU 104 CB ILE A 13 816 809 800 28 -21 -39 C ATOM 105 CG1 ILE A 13 3.756 21.080 14.044 1.00 6.70 C ANISOU 105 CG1 ILE A 13 842 886 815 47 -37 -31 C ATOM 106 CG2 ILE A 13 5.469 20.012 12.563 1.00 6.46 C ANISOU 106 CG2 ILE A 13 851 782 820 23 18 -53 C ATOM 107 CD1 ILE A 13 2.573 20.711 13.190 1.00 7.69 C ANISOU 107 CD1 ILE A 13 844 1043 1033 -34 -52 -63 C ATOM 108 N THR A 14 7.701 22.985 12.705 1.00 7.90 N ANISOU 108 N THR A 14 995 1015 990 32 7 -19 N ATOM 109 CA THR A 14 8.937 23.195 11.948 1.00 9.27 C ANISOU 109 CA THR A 14 1155 1194 1172 11 2 -4 C ATOM 110 C THR A 14 9.123 24.684 11.660 1.00 10.50 C ANISOU 110 C THR A 14 1330 1317 1339 32 -30 -16 C ATOM 111 O THR A 14 8.265 25.496 12.002 1.00 10.40 O ANISOU 111 O THR A 14 1265 1333 1351 46 -10 -42 O ATOM 112 CB THR A 14 8.932 22.384 10.624 1.00 9.23 C ANISOU 112 CB THR A 14 1158 1165 1182 5 -10 7 C ATOM 113 CG2 THR A 14 7.957 22.981 9.603 1.00 9.87 C ANISOU 113 CG2 THR A 14 1277 1242 1229 -7 -28 26 C ATOM 114 OG1 THR A 14 10.252 22.348 10.063 1.00 9.63 O ANISOU 114 OG1 THR A 14 1249 1197 1212 91 91 -19 O ATOM 115 N ASP A 15 10.252 25.032 11.047 1.00 12.17 N ANISOU 115 N ASP A 15 1531 1554 1539 13 -2 -5 N ATOM 116 CA ASP A 15 10.553 26.408 10.651 1.00 13.97 C ANISOU 116 CA ASP A 15 1774 1760 1774 0 10 11 C ATOM 117 C ASP A 15 10.503 26.464 9.143 1.00 14.91 C ANISOU 117 C ASP A 15 1907 1877 1880 -16 2 5 C ATOM 118 O ASP A 15 11.234 25.737 8.475 1.00 15.55 O ANISOU 118 O ASP A 15 2001 1986 1917 -5 20 -4 O ATOM 119 CB ASP A 15 11.954 26.819 11.123 1.00 14.46 C ANISOU 119 CB ASP A 15 1827 1833 1832 -10 15 11 C ATOM 120 CG ASP A 15 12.331 28.244 10.720 1.00 15.65 C ANISOU 120 CG ASP A 15 1971 1970 2002 -22 16 51 C ATOM 121 OD1 ASP A 15 11.436 29.097 10.532 1.00 16.54 O ANISOU 121 OD1 ASP A 15 2160 2019 2104 -31 31 115 O ATOM 122 OD2 ASP A 15 13.549 28.515 10.616 1.00 18.40 O1- ANISOU 122 OD2 ASP A 15 2223 2380 2385 -53 -2 32 O1- ATOM 123 N THR A 16 9.626 27.319 8.629 1.00 15.73 N ANISOU 123 N THR A 16 2013 1978 1985 -26 -11 15 N ATOM 124 CA ATHR A 16 9.497 27.558 7.193 0.50 16.20 C ANISOU 124 CA ATHR A 16 2084 2034 2036 -31 -23 10 C ATOM 125 CA BTHR A 16 9.508 27.549 7.202 0.50 16.26 C ANISOU 125 CA BTHR A 16 2090 2041 2047 -30 -21 10 C ATOM 126 C THR A 16 10.037 28.941 6.824 1.00 16.31 C ANISOU 126 C THR A 16 2110 2038 2047 -35 -28 9 C ATOM 127 O THR A 16 10.110 29.295 5.644 1.00 16.31 O ANISOU 127 O THR A 16 2124 2026 2044 -78 -49 31 O ATOM 128 CB ATHR A 16 8.015 27.472 6.740 0.50 16.31 C ANISOU 128 CB ATHR A 16 2080 2050 2065 -20 -20 15 C ATOM 129 CB BTHR A 16 8.041 27.429 6.764 0.50 16.41 C ANISOU 129 CB BTHR A 16 2087 2061 2084 -15 -18 11 C ATOM 130 CG2ATHR A 16 7.445 26.079 7.000 0.50 16.65 C ANISOU 130 CG2ATHR A 16 2146 2079 2099 -28 -37 7 C ATOM 131 CG2BTHR A 16 7.978 27.235 5.297 0.50 16.59 C ANISOU 131 CG2BTHR A 16 2103 2093 2105 -28 0 1 C ATOM 132 OG1ATHR A 16 7.230 28.445 7.446 0.50 15.93 O ANISOU 132 OG1ATHR A 16 2061 2034 1956 -34 -23 -1 O ATOM 133 OG1BTHR A 16 7.419 26.308 7.413 0.50 17.03 O ANISOU 133 OG1BTHR A 16 2214 2119 2136 -20 -18 27 O ATOM 134 N ALA A 17 10.434 29.715 7.833 1.00 16.33 N ANISOU 134 N ALA A 17 2115 2034 2053 -46 -46 16 N ATOM 135 CA ALA A 17 10.754 31.137 7.654 1.00 16.24 C ANISOU 135 CA ALA A 17 2105 2019 2044 -32 -46 11 C ATOM 136 C ALA A 17 11.898 31.463 6.693 1.00 16.40 C ANISOU 136 C ALA A 17 2117 2052 2061 -28 -50 -4 C ATOM 137 O ALA A 17 11.821 32.453 5.967 1.00 16.12 O ANISOU 137 O ALA A 17 2082 1981 2060 -47 -64 23 O ATOM 138 CB ALA A 17 11.014 31.787 9.011 1.00 16.32 C ANISOU 138 CB ALA A 17 2126 2015 2057 -47 -57 1 C ATOM 139 N GLU A 18 12.956 30.662 6.683 1.00 16.54 N ANISOU 139 N GLU A 18 2124 2080 2078 -25 -43 2 N ATOM 140 CA GLU A 18 14.072 30.929 5.777 1.00 16.85 C ANISOU 140 CA GLU A 18 2145 2121 2134 -26 -30 2 C ATOM 141 C GLU A 18 13.672 30.710 4.315 1.00 16.41 C ANISOU 141 C GLU A 18 2074 2079 2079 -27 -27 16 C ATOM 142 O GLU A 18 14.126 31.437 3.428 1.00 16.34 O ANISOU 142 O GLU A 18 2053 2094 2061 -49 -42 20 O ATOM 143 CB GLU A 18 15.289 30.076 6.128 1.00 17.43 C ANISOU 143 CB GLU A 18 2200 2184 2237 -16 -39 0 C ATOM 144 CG GLU A 18 16.500 30.380 5.275 1.00 19.68 C ANISOU 144 CG GLU A 18 2428 2577 2469 40 0 20 C ATOM 145 CD GLU A 18 17.047 31.790 5.452 1.00 16.90 C ANISOU 145 CD GLU A 18 2669 2340 1413 -219 313 -68 C ATOM 146 OE1 GLU A 18 16.971 32.340 6.572 1.00 24.69 O ANISOU 146 OE1 GLU A 18 2846 3047 3487 -83 -123 261 O ATOM 147 OE2 GLU A 18 17.564 32.345 4.457 1.00 25.77 O1- ANISOU 147 OE2 GLU A 18 3108 3163 3520 111 -227 -158 O1- ATOM 148 N TYR A 19 12.828 29.707 4.071 1.00 16.00 N ANISOU 148 N TYR A 19 2019 2030 2028 -23 -32 17 N ATOM 149 CA TYR A 19 12.324 29.436 2.726 1.00 15.71 C ANISOU 149 CA TYR A 19 1971 1996 2000 -7 -28 16 C ATOM 150 C TYR A 19 11.441 30.585 2.251 1.00 14.84 C ANISOU 150 C TYR A 19 1847 1901 1890 -18 -21 7 C ATOM 151 O TYR A 19 11.587 31.071 1.126 1.00 14.31 O ANISOU 151 O TYR A 19 1702 1882 1850 -20 -56 19 O ATOM 152 CB TYR A 19 11.506 28.144 2.692 1.00 16.04 C ANISOU 152 CB TYR A 19 2022 2039 2030 -17 -26 14 C ATOM 153 CG TYR A 19 12.268 26.875 3.008 1.00 17.88 C ANISOU 153 CG TYR A 19 2264 2239 2291 11 -40 13 C ATOM 154 CD1 TYR A 19 13.210 26.363 2.124 1.00 19.23 C ANISOU 154 CD1 TYR A 19 2445 2432 2430 90 23 47 C ATOM 155 CD2 TYR A 19 12.013 26.165 4.177 1.00 19.13 C ANISOU 155 CD2 TYR A 19 2424 2436 2408 23 2 41 C ATOM 156 CE1 TYR A 19 13.897 25.183 2.406 1.00 21.71 C ANISOU 156 CE1 TYR A 19 2697 2672 2879 31 -49 -35 C ATOM 157 CE2 TYR A 19 12.690 24.990 4.467 1.00 21.01 C ANISOU 157 CE2 TYR A 19 2665 2648 2669 -26 -71 15 C ATOM 158 CZ TYR A 19 13.630 24.504 3.583 1.00 19.45 C ANISOU 158 CZ TYR A 19 2488 2419 2481 140 74 84 C ATOM 159 OH TYR A 19 14.296 23.335 3.884 1.00 22.76 O ANISOU 159 OH TYR A 19 2869 2856 2920 -2 26 18 O ATOM 160 N HIS A 20 10.520 31.008 3.115 1.00 14.13 N ANISOU 160 N HIS A 20 1775 1801 1791 -30 -35 11 N ATOM 161 CA HIS A 20 9.641 32.137 2.815 1.00 13.87 C ANISOU 161 CA HIS A 20 1760 1747 1760 -28 -25 9 C ATOM 162 C HIS A 20 10.443 33.409 2.556 1.00 13.89 C ANISOU 162 C HIS A 20 1770 1746 1762 -38 -28 14 C ATOM 163 O HIS A 20 10.132 34.163 1.635 1.00 13.79 O ANISOU 163 O HIS A 20 1779 1703 1756 -57 -23 28 O ATOM 164 CB HIS A 20 8.642 32.380 3.951 1.00 13.71 C ANISOU 164 CB HIS A 20 1750 1724 1734 -25 -37 0 C ATOM 165 CG HIS A 20 7.479 31.436 3.948 1.00 13.17 C ANISOU 165 CG HIS A 20 1686 1671 1644 -27 -17 30 C ATOM 166 CD2 HIS A 20 7.037 30.559 4.881 1.00 13.37 C ANISOU 166 CD2 HIS A 20 1715 1729 1635 -18 16 0 C ATOM 167 ND1 HIS A 20 6.606 31.337 2.887 1.00 12.71 N ANISOU 167 ND1 HIS A 20 1627 1608 1593 -1 23 17 N ATOM 168 CE1 HIS A 20 5.679 30.438 3.162 1.00 13.01 C ANISOU 168 CE1 HIS A 20 1590 1674 1676 -15 -17 32 C ATOM 169 NE2 HIS A 20 5.917 29.950 4.366 1.00 12.96 N ANISOU 169 NE2 HIS A 20 1621 1695 1605 -13 54 27 N ATOM 170 N PHE A 21 11.472 33.637 3.370 1.00 14.02 N ANISOU 170 N PHE A 21 1785 1772 1767 -31 -30 26 N ATOM 171 CA PHE A 21 12.324 34.814 3.222 1.00 14.37 C ANISOU 171 CA PHE A 21 1838 1807 1814 -28 -39 14 C ATOM 172 C PHE A 21 13.000 34.870 1.859 1.00 14.21 C ANISOU 172 C PHE A 21 1810 1789 1800 -30 -47 7 C ATOM 173 O PHE A 21 12.910 35.881 1.158 1.00 14.21 O ANISOU 173 O PHE A 21 1845 1813 1738 -65 -86 42 O ATOM 174 CB PHE A 21 13.395 34.855 4.315 1.00 14.60 C ANISOU 174 CB PHE A 21 1860 1847 1838 -21 -39 16 C ATOM 175 CG PHE A 21 14.345 36.014 4.179 1.00 15.67 C ANISOU 175 CG PHE A 21 1993 1967 1994 -51 -11 23 C ATOM 176 CD1 PHE A 21 13.865 37.317 4.168 1.00 16.45 C ANISOU 176 CD1 PHE A 21 2095 2054 2098 -42 -23 5 C ATOM 177 CD2 PHE A 21 15.711 35.804 4.050 1.00 16.79 C ANISOU 177 CD2 PHE A 21 2095 2083 2199 -32 1 25 C ATOM 178 CE1 PHE A 21 14.730 38.395 4.037 1.00 16.99 C ANISOU 178 CE1 PHE A 21 2169 2120 2164 -57 10 34 C ATOM 179 CE2 PHE A 21 16.587 36.881 3.920 1.00 17.41 C ANISOU 179 CE2 PHE A 21 2175 2157 2280 -51 -15 10 C ATOM 180 CZ PHE A 21 16.090 38.177 3.913 1.00 17.43 C ANISOU 180 CZ PHE A 21 2197 2176 2247 -16 -18 14 C ATOM 181 N ARG A 22 13.684 33.791 1.490 1.00 14.13 N ANISOU 181 N ARG A 22 1778 1797 1790 -34 -44 18 N ATOM 182 CA ARG A 22 14.364 33.731 0.198 1.00 14.08 C ANISOU 182 CA ARG A 22 1768 1797 1782 -18 -37 23 C ATOM 183 C ARG A 22 13.397 33.969 -0.965 1.00 13.37 C ANISOU 183 C ARG A 22 1654 1719 1704 -14 -23 38 C ATOM 184 O ARG A 22 13.736 34.658 -1.927 1.00 13.24 O ANISOU 184 O ARG A 22 1630 1691 1708 -2 -56 82 O ATOM 185 CB ARG A 22 15.088 32.393 0.020 1.00 14.52 C ANISOU 185 CB ARG A 22 1836 1848 1831 -8 -21 10 C ATOM 186 CG ARG A 22 16.313 32.233 0.911 1.00 16.04 C ANISOU 186 CG ARG A 22 1995 2069 2029 -18 -43 14 C ATOM 187 CD ARG A 22 17.339 31.299 0.292 1.00 18.02 C ANISOU 187 CD ARG A 22 2281 2300 2263 51 -4 -14 C ATOM 188 NE ARG A 22 16.864 29.919 0.183 1.00 19.34 N ANISOU 188 NE ARG A 22 2504 2398 2447 -1 -28 42 N ATOM 189 CZ ARG A 22 16.856 29.032 1.180 1.00 22.44 C ANISOU 189 CZ ARG A 22 2770 2883 2873 52 46 11 C ATOM 190 NH1 ARG A 22 17.281 29.363 2.394 1.00 21.03 N1+ ANISOU 190 NH1 ARG A 22 2797 2564 2627 -52 -87 -32 N1+ ATOM 191 NH2 ARG A 22 16.412 27.797 0.967 1.00 21.33 N ANISOU 191 NH2 ARG A 22 2925 2602 2575 -104 -107 -15 N ATOM 192 N ALA A 23 12.196 33.405 -0.858 1.00 12.62 N ANISOU 192 N ALA A 23 1572 1612 1610 -14 -27 45 N ATOM 193 CA ALA A 23 11.185 33.535 -1.901 1.00 12.00 C ANISOU 193 CA ALA A 23 1492 1537 1528 -15 -2 40 C ATOM 194 C ALA A 23 10.643 34.962 -2.004 1.00 11.65 C ANISOU 194 C ALA A 23 1453 1487 1486 -19 -2 27 C ATOM 195 O ALA A 23 10.528 35.498 -3.107 1.00 11.33 O ANISOU 195 O ALA A 23 1411 1467 1426 -43 18 47 O ATOM 196 CB ALA A 23 10.048 32.539 -1.669 1.00 11.71 C ANISOU 196 CB ALA A 23 1467 1496 1485 -15 -2 38 C ATOM 197 N TRP A 24 10.316 35.580 -0.869 1.00 11.35 N ANISOU 197 N TRP A 24 1419 1452 1441 -20 -14 28 N ATOM 198 CA TRP A 24 9.829 36.969 -0.872 1.00 11.41 C ANISOU 198 CA TRP A 24 1439 1441 1452 -31 -14 28 C ATOM 199 C TRP A 24 10.914 37.951 -1.322 1.00 11.77 C ANISOU 199 C TRP A 24 1470 1482 1519 -42 -23 30 C ATOM 200 O TRP A 24 10.627 38.907 -2.039 1.00 11.81 O ANISOU 200 O TRP A 24 1480 1501 1504 -92 -26 74 O ATOM 201 CB TRP A 24 9.309 37.399 0.505 1.00 11.29 C ANISOU 201 CB TRP A 24 1419 1422 1445 -34 -13 25 C ATOM 202 CG TRP A 24 7.955 36.856 0.889 1.00 10.67 C ANISOU 202 CG TRP A 24 1388 1326 1339 -22 17 21 C ATOM 203 CD1 TRP A 24 7.650 36.152 2.017 1.00 11.03 C ANISOU 203 CD1 TRP A 24 1417 1385 1387 -37 -8 1 C ATOM 204 CD2 TRP A 24 6.724 37.009 0.167 1.00 10.21 C ANISOU 204 CD2 TRP A 24 1335 1269 1275 -17 49 35 C ATOM 205 CE2 TRP A 24 5.719 36.351 0.912 1.00 10.24 C ANISOU 205 CE2 TRP A 24 1323 1260 1307 -35 15 32 C ATOM 206 CE3 TRP A 24 6.374 37.620 -1.045 1.00 10.48 C ANISOU 206 CE3 TRP A 24 1329 1325 1327 -4 16 51 C ATOM 207 NE1 TRP A 24 6.312 35.847 2.040 1.00 10.76 N ANISOU 207 NE1 TRP A 24 1402 1327 1358 -18 9 40 N ATOM 208 CZ2 TRP A 24 4.390 36.297 0.493 1.00 10.43 C ANISOU 208 CZ2 TRP A 24 1356 1319 1288 9 43 4 C ATOM 209 CZ3 TRP A 24 5.050 37.560 -1.464 1.00 10.27 C ANISOU 209 CZ3 TRP A 24 1296 1291 1314 7 42 31 C ATOM 210 CH2 TRP A 24 4.075 36.901 -0.696 1.00 10.37 C ANISOU 210 CH2 TRP A 24 1305 1295 1337 -2 0 47 C ATOM 211 N LYS A 25 12.150 37.720 -0.887 1.00 12.22 N ANISOU 211 N LYS A 25 1530 1539 1572 -49 -21 38 N ATOM 212 CA LYS A 25 13.277 38.568 -1.283 1.00 12.61 C ANISOU 212 CA LYS A 25 1577 1590 1624 -45 -15 37 C ATOM 213 C LYS A 25 13.484 38.506 -2.793 1.00 12.44 C ANISOU 213 C LYS A 25 1544 1577 1605 -49 -23 35 C ATOM 214 O LYS A 25 13.655 39.540 -3.443 1.00 12.43 O ANISOU 214 O LYS A 25 1540 1580 1602 -88 -40 67 O ATOM 215 CB LYS A 25 14.556 38.140 -0.553 1.00 13.09 C ANISOU 215 CB LYS A 25 1641 1663 1666 -42 -28 43 C ATOM 216 CG LYS A 25 15.739 39.089 -0.724 1.00 14.49 C ANISOU 216 CG LYS A 25 1824 1824 1855 -62 -17 18 C ATOM 217 CD LYS A 25 16.906 38.671 0.167 1.00 16.56 C ANISOU 217 CD LYS A 25 2081 2114 2096 -2 -59 40 C ATOM 218 CE LYS A 25 18.053 39.669 0.112 1.00 18.13 C ANISOU 218 CE LYS A 25 2272 2294 2321 -37 -21 23 C ATOM 219 NZ LYS A 25 17.662 41.003 0.652 1.00 19.75 N1+ ANISOU 219 NZ LYS A 25 2535 2454 2515 -10 2 -17 N1+ ATOM 220 N ALA A 26 13.472 37.292 -3.344 1.00 12.17 N ANISOU 220 N ALA A 26 1507 1560 1557 -31 -4 28 N ATOM 221 CA ALA A 26 13.595 37.095 -4.789 1.00 11.94 C ANISOU 221 CA ALA A 26 1481 1537 1517 -25 -8 25 C ATOM 222 C ALA A 26 12.490 37.829 -5.547 1.00 11.77 C ANISOU 222 C ALA A 26 1462 1529 1479 -22 2 26 C ATOM 223 O ALA A 26 12.750 38.462 -6.572 1.00 11.81 O ANISOU 223 O ALA A 26 1481 1553 1454 -31 -14 63 O ATOM 224 CB ALA A 26 13.579 35.611 -5.134 1.00 12.13 C ANISOU 224 CB ALA A 26 1492 1562 1554 -23 2 19 C ATOM 225 N LEU A 27 11.263 37.754 -5.038 1.00 11.16 N ANISOU 225 N LEU A 27 1387 1456 1397 -9 -1 15 N ATOM 226 CA LEU A 27 10.141 38.464 -5.650 1.00 10.96 C ANISOU 226 CA LEU A 27 1374 1423 1366 0 5 27 C ATOM 227 C LEU A 27 10.340 39.978 -5.592 1.00 11.14 C ANISOU 227 C LEU A 27 1407 1441 1384 -4 -1 27 C ATOM 228 O LEU A 27 10.176 40.663 -6.599 1.00 11.03 O ANISOU 228 O LEU A 27 1390 1455 1345 -21 27 61 O ATOM 229 CB LEU A 27 8.816 38.084 -4.977 1.00 10.89 C ANISOU 229 CB LEU A 27 1361 1421 1355 -5 -9 28 C ATOM 230 CG LEU A 27 7.571 38.673 -5.649 1.00 11.00 C ANISOU 230 CG LEU A 27 1397 1398 1385 42 -23 11 C ATOM 231 CD1 LEU A 27 7.322 38.007 -6.995 1.00 11.46 C ANISOU 231 CD1 LEU A 27 1409 1511 1434 21 1 -32 C ATOM 232 CD2 LEU A 27 6.352 38.540 -4.755 1.00 11.87 C ANISOU 232 CD2 LEU A 27 1435 1583 1489 23 20 -23 C ATOM 233 N ALA A 28 10.692 40.493 -4.416 1.00 11.38 N ANISOU 233 N ALA A 28 1452 1462 1409 -11 5 20 N ATOM 234 CA ALA A 28 10.964 41.920 -4.233 1.00 11.84 C ANISOU 234 CA ALA A 28 1532 1511 1452 -23 2 23 C ATOM 235 C ALA A 28 12.050 42.423 -5.191 1.00 12.39 C ANISOU 235 C ALA A 28 1602 1569 1534 -32 2 27 C ATOM 236 O ALA A 28 11.898 43.471 -5.822 1.00 12.54 O ANISOU 236 O ALA A 28 1656 1571 1537 -67 25 49 O ATOM 237 CB ALA A 28 11.358 42.198 -2.785 1.00 11.84 C ANISOU 237 CB ALA A 28 1553 1492 1451 -31 7 14 C ATOM 238 N GLU A 29 13.131 41.661 -5.314 1.00 12.90 N ANISOU 238 N GLU A 29 1646 1659 1593 -36 14 38 N ATOM 239 CA GLU A 29 14.225 42.024 -6.218 1.00 13.64 C ANISOU 239 CA GLU A 29 1734 1750 1696 -43 19 30 C ATOM 240 C GLU A 29 13.801 41.977 -7.685 1.00 13.88 C ANISOU 240 C GLU A 29 1772 1787 1712 -47 7 39 C ATOM 241 O GLU A 29 14.278 42.774 -8.497 1.00 13.98 O ANISOU 241 O GLU A 29 1792 1802 1714 -88 13 63 O ATOM 242 CB GLU A 29 15.434 41.122 -5.980 1.00 13.98 C ANISOU 242 CB GLU A 29 1776 1787 1748 -32 28 32 C ATOM 243 CG GLU A 29 16.152 41.425 -4.671 1.00 15.35 C ANISOU 243 CG GLU A 29 1941 1969 1921 -47 -13 11 C ATOM 244 CD GLU A 29 17.232 40.417 -4.325 1.00 17.61 C ANISOU 244 CD GLU A 29 2178 2214 2297 -13 13 76 C ATOM 245 OE1 GLU A 29 17.476 39.484 -5.119 1.00 18.71 O ANISOU 245 OE1 GLU A 29 2383 2337 2389 69 -33 -41 O ATOM 246 OE2 GLU A 29 17.841 40.564 -3.245 1.00 19.39 O1- ANISOU 246 OE2 GLU A 29 2451 2543 2372 -27 -126 57 O1- ATOM 247 N GLU A 30 12.905 41.048 -8.015 1.00 14.17 N ANISOU 247 N GLU A 30 1797 1822 1761 -47 7 38 N ATOM 248 CA GLU A 30 12.368 40.917 -9.372 1.00 14.60 C ANISOU 248 CA GLU A 30 1853 1883 1811 -23 5 26 C ATOM 249 C GLU A 30 11.558 42.143 -9.795 1.00 14.64 C ANISOU 249 C GLU A 30 1845 1893 1824 -26 -1 37 C ATOM 250 O GLU A 30 11.596 42.544 -10.958 1.00 14.53 O ANISOU 250 O GLU A 30 1809 1941 1770 -46 4 80 O ATOM 251 CB GLU A 30 11.499 39.655 -9.471 1.00 14.84 C ANISOU 251 CB GLU A 30 1888 1897 1850 -28 5 17 C ATOM 252 CG GLU A 30 10.827 39.413 -10.824 1.00 16.25 C ANISOU 252 CG GLU A 30 2074 2106 1993 0 -2 -8 C ATOM 253 CD GLU A 30 9.900 38.210 -10.794 1.00 18.64 C ANISOU 253 CD GLU A 30 2404 2357 2320 -59 -9 -28 C ATOM 254 OE1 GLU A 30 10.357 37.117 -10.401 1.00 20.64 O ANISOU 254 OE1 GLU A 30 2675 2519 2646 11 -22 -28 O ATOM 255 OE2 GLU A 30 8.714 38.358 -11.159 1.00 20.83 O1- ANISOU 255 OE2 GLU A 30 2523 2746 2646 -27 17 -30 O1- ATOM 256 N ILE A 31 10.817 42.729 -8.860 1.00 14.91 N ANISOU 256 N ILE A 31 1884 1904 1876 -7 -8 45 N ATOM 257 CA ILE A 31 9.973 43.886 -9.176 1.00 15.42 C ANISOU 257 CA ILE A 31 1949 1946 1961 -2 5 30 C ATOM 258 C ILE A 31 10.629 45.216 -8.793 1.00 15.62 C ANISOU 258 C ILE A 31 1967 1967 1998 -9 10 32 C ATOM 259 O ILE A 31 10.052 46.275 -9.016 1.00 15.76 O ANISOU 259 O ILE A 31 1983 1944 2060 -31 31 75 O ATOM 260 CB ILE A 31 8.557 43.752 -8.560 1.00 15.62 C ANISOU 260 CB ILE A 31 1961 1966 2005 0 -2 31 C ATOM 261 CG1 ILE A 31 8.603 43.770 -7.027 1.00 15.79 C ANISOU 261 CG1 ILE A 31 1968 2009 2019 -10 19 14 C ATOM 262 CG2 ILE A 31 7.890 42.480 -9.076 1.00 16.13 C ANISOU 262 CG2 ILE A 31 2027 2038 2062 -20 -4 0 C ATOM 263 CD1 ILE A 31 7.272 43.429 -6.368 1.00 16.92 C ANISOU 263 CD1 ILE A 31 2070 2184 2172 -23 65 0 C ATOM 264 N GLY A 32 11.836 45.155 -8.233 1.00 15.80 N ANISOU 264 N GLY A 32 1991 1989 2022 -11 -1 28 N ATOM 265 CA GLY A 32 12.633 46.352 -7.971 1.00 16.15 C ANISOU 265 CA GLY A 32 2051 2023 2061 -18 7 30 C ATOM 266 C GLY A 32 12.297 47.071 -6.679 1.00 16.66 C ANISOU 266 C GLY A 32 2121 2087 2120 -15 10 11 C ATOM 267 O GLY A 32 12.424 48.294 -6.596 1.00 16.61 O ANISOU 267 O GLY A 32 2125 2068 2119 -33 23 40 O ATOM 268 N ILE A 33 11.878 46.315 -5.665 1.00 17.34 N ANISOU 268 N ILE A 33 2215 2177 2197 -34 15 22 N ATOM 269 CA ILE A 33 11.552 46.881 -4.357 1.00 18.24 C ANISOU 269 CA ILE A 33 2325 2302 2299 -26 21 5 C ATOM 270 C ILE A 33 12.694 46.649 -3.373 1.00 19.27 C ANISOU 270 C ILE A 33 2444 2448 2428 -20 11 13 C ATOM 271 O ILE A 33 13.201 45.532 -3.251 1.00 19.25 O ANISOU 271 O ILE A 33 2440 2457 2414 -36 20 8 O ATOM 272 CB ILE A 33 10.256 46.266 -3.777 1.00 18.06 C ANISOU 272 CB ILE A 33 2296 2290 2275 -21 16 2 C ATOM 273 CG1 ILE A 33 9.039 46.746 -4.571 1.00 18.07 C ANISOU 273 CG1 ILE A 33 2310 2269 2283 -13 17 4 C ATOM 274 CG2 ILE A 33 10.094 46.637 -2.298 1.00 18.09 C ANISOU 274 CG2 ILE A 33 2309 2310 2254 -36 20 1 C ATOM 275 CD1 ILE A 33 7.751 46.035 -4.206 1.00 18.00 C ANISOU 275 CD1 ILE A 33 2271 2316 2249 0 28 9 C ATOM 276 N ASN A 34 13.089 47.719 -2.681 1.00 20.58 N ANISOU 276 N ASN A 34 2619 2599 2599 -33 5 2 N ATOM 277 CA ASN A 34 14.067 47.651 -1.598 1.00 21.70 C ANISOU 277 CA ASN A 34 2752 2753 2740 -21 -4 7 C ATOM 278 C ASN A 34 13.378 47.487 -0.254 1.00 22.21 C ANISOU 278 C ASN A 34 2817 2818 2800 -28 5 7 C ATOM 279 O ASN A 34 12.253 47.954 -0.069 1.00 22.60 O ANISOU 279 O ASN A 34 2872 2867 2844 -15 0 22 O ATOM 280 CB ASN A 34 14.904 48.933 -1.547 1.00 22.05 C ANISOU 280 CB ASN A 34 2801 2784 2792 -28 -11 5 C ATOM 281 CG ASN A 34 16.040 48.932 -2.539 1.00 23.37 C ANISOU 281 CG ASN A 34 2952 2983 2940 -11 11 -13 C ATOM 282 ND2 ASN A 34 16.172 50.021 -3.289 1.00 24.68 N ANISOU 282 ND2 ASN A 34 3152 3126 3100 -14 -11 42 N ATOM 283 OD1 ASN A 34 16.809 47.973 -2.617 1.00 25.76 O ANISOU 283 OD1 ASN A 34 3239 3226 3322 73 -4 -28 O ATOM 284 N GLY A 35 14.063 46.837 0.685 1.00 22.86 N ANISOU 284 N GLY A 35 2902 2884 2896 -21 -5 11 N ATOM 285 CA GLY A 35 13.616 46.796 2.077 1.00 23.33 C ANISOU 285 CA GLY A 35 2970 2950 2943 -23 2 5 C ATOM 286 C GLY A 35 13.310 45.422 2.642 1.00 23.81 C ANISOU 286 C GLY A 35 3033 3000 3012 -28 0 11 C ATOM 287 O GLY A 35 13.194 45.273 3.858 1.00 23.84 O ANISOU 287 O GLY A 35 3045 3009 3002 -51 9 2 O ATOM 288 N VAL A 36 13.175 44.417 1.777 1.00 24.45 N ANISOU 288 N VAL A 36 3119 3096 3073 -27 -2 1 N ATOM 289 CA VAL A 36 12.877 43.058 2.231 1.00 24.95 C ANISOU 289 CA VAL A 36 3186 3148 3145 -32 5 2 C ATOM 290 C VAL A 36 14.156 42.391 2.741 1.00 25.69 C ANISOU 290 C VAL A 36 3269 3242 3247 -23 5 11 C ATOM 291 O VAL A 36 14.801 41.619 2.030 1.00 25.58 O ANISOU 291 O VAL A 36 3270 3219 3227 -34 7 23 O ATOM 292 CB VAL A 36 12.217 42.203 1.117 1.00 24.87 C ANISOU 292 CB VAL A 36 3180 3139 3131 -31 5 2 C ATOM 293 CG1 VAL A 36 11.875 40.808 1.637 1.00 24.89 C ANISOU 293 CG1 VAL A 36 3177 3147 3132 -45 17 -10 C ATOM 294 CG2 VAL A 36 10.969 42.887 0.597 1.00 24.91 C ANISOU 294 CG2 VAL A 36 3178 3141 3144 -42 2 -5 C ATOM 295 N ASP A 37 14.518 42.719 3.980 1.00 26.69 N ANISOU 295 N ASP A 37 3398 3379 3365 -28 5 2 N ATOM 296 CA ASP A 37 15.693 42.142 4.640 1.00 27.54 C ANISOU 296 CA ASP A 37 3489 3493 3479 -14 -1 4 C ATOM 297 C ASP A 37 15.257 41.308 5.847 1.00 28.31 C ANISOU 297 C ASP A 37 3590 3590 3575 -16 8 11 C ATOM 298 O ASP A 37 14.061 41.189 6.120 1.00 28.34 O ANISOU 298 O ASP A 37 3580 3602 3584 -21 2 11 O ATOM 299 CB ASP A 37 16.697 43.240 5.038 1.00 27.61 C ANISOU 299 CB ASP A 37 3498 3500 3491 -21 0 5 C ATOM 300 CG ASP A 37 16.089 44.323 5.925 1.00 27.99 C ANISOU 300 CG ASP A 37 3555 3548 3530 -18 2 -7 C ATOM 301 OD1 ASP A 37 14.992 44.122 6.489 1.00 28.15 O ANISOU 301 OD1 ASP A 37 3555 3580 3559 -52 0 -11 O ATOM 302 OD2 ASP A 37 16.724 45.392 6.059 1.00 28.67 O1- ANISOU 302 OD2 ASP A 37 3621 3635 3634 -66 5 -2 O1- ATOM 303 N ARG A 38 16.221 40.733 6.563 1.00 29.21 N ANISOU 303 N ARG A 38 3694 3714 3690 -8 -2 7 N ATOM 304 CA ARG A 38 15.917 39.834 7.681 1.00 30.02 C ANISOU 304 CA ARG A 38 3804 3808 3792 -8 1 11 C ATOM 305 C ARG A 38 15.155 40.517 8.827 1.00 30.34 C ANISOU 305 C ARG A 38 3842 3856 3827 -4 2 4 C ATOM 306 O ARG A 38 14.424 39.853 9.567 1.00 30.48 O ANISOU 306 O ARG A 38 3856 3880 3844 -5 13 4 O ATOM 307 CB ARG A 38 17.196 39.150 8.194 1.00 30.22 C ANISOU 307 CB ARG A 38 3824 3837 3817 -1 4 11 C ATOM 308 CG ARG A 38 18.190 40.062 8.914 1.00 31.23 C ANISOU 308 CG ARG A 38 3946 3953 3966 -10 -5 -2 C ATOM 309 CD ARG A 38 18.114 39.952 10.442 1.00 32.69 C ANISOU 309 CD ARG A 38 4142 4184 4093 -13 5 -5 C ATOM 310 NE ARG A 38 18.611 38.671 10.955 1.00 33.70 N ANISOU 310 NE ARG A 38 4341 4184 4277 10 0 42 N ATOM 311 CZ ARG A 38 17.853 37.644 11.349 1.00 35.19 C ANISOU 311 CZ ARG A 38 4416 4517 4435 -54 26 -44 C ATOM 312 NH1 ARG A 38 16.524 37.701 11.299 1.00 36.71 N1+ ANISOU 312 NH1 ARG A 38 4565 4897 4486 33 -11 -119 N1+ ATOM 313 NH2 ARG A 38 18.432 36.538 11.800 1.00 33.23 N ANISOU 313 NH2 ARG A 38 4035 4122 4469 7 -2 117 N ATOM 314 N GLN A 39 15.313 41.834 8.956 1.00 30.73 N ANISOU 314 N GLN A 39 3895 3902 3877 -2 -1 8 N ATOM 315 CA GLN A 39 14.582 42.608 9.967 1.00 30.94 C ANISOU 315 CA GLN A 39 3923 3928 3901 5 -5 16 C ATOM 316 C GLN A 39 13.111 42.702 9.564 1.00 31.06 C ANISOU 316 C GLN A 39 3937 3950 3912 -5 2 5 C ATOM 317 O GLN A 39 12.217 42.451 10.372 1.00 31.07 O ANISOU 317 O GLN A 39 3946 3952 3908 -16 2 7 O ATOM 318 CB GLN A 39 15.152 44.030 10.138 1.00 31.38 C ANISOU 318 CB GLN A 39 3988 3962 3973 0 -19 -2 C ATOM 319 CG GLN A 39 16.667 44.199 9.966 1.00 33.36 C ANISOU 319 CG GLN A 39 4164 4244 4266 -150 115 -166 C ATOM 320 CD GLN A 39 17.495 43.294 10.861 1.00 25.52 C ANISOU 320 CD GLN A 39 3008 3793 2893 51 649 792 C ATOM 321 NE2 GLN A 39 18.772 43.150 10.525 1.00 36.57 N ANISOU 321 NE2 GLN A 39 5286 4128 4480 -182 -416 -14 N ATOM 322 OE1 GLN A 39 17.002 42.738 11.845 1.00 39.50 O ANISOU 322 OE1 GLN A 39 4767 4728 5511 343 -487 -525 O ATOM 323 N PHE A 40 12.879 43.076 8.307 1.00 31.06 N ANISOU 323 N PHE A 40 3937 3953 3910 -7 -1 4 N ATOM 324 CA PHE A 40 11.530 43.182 7.748 1.00 31.00 C ANISOU 324 CA PHE A 40 3928 3947 3903 -2 -1 2 C ATOM 325 C PHE A 40 10.802 41.837 7.755 1.00 31.16 C ANISOU 325 C PHE A 40 3952 3968 3920 -8 -2 2 C ATOM 326 O PHE A 40 9.597 41.785 7.997 1.00 31.19 O ANISOU 326 O PHE A 40 3956 3983 3911 -9 -9 2 O ATOM 327 CB PHE A 40 11.596 43.734 6.317 1.00 30.96 C ANISOU 327 CB PHE A 40 3926 3936 3900 -5 -1 5 C ATOM 328 CG PHE A 40 10.259 43.819 5.628 1.00 30.55 C ANISOU 328 CG PHE A 40 3886 3873 3847 -19 15 2 C ATOM 329 CD1 PHE A 40 9.413 44.896 5.856 1.00 29.37 C ANISOU 329 CD1 PHE A 40 3647 3785 3726 -5 -92 -30 C ATOM 330 CD2 PHE A 40 9.854 42.827 4.742 1.00 29.72 C ANISOU 330 CD2 PHE A 40 3678 3832 3780 18 -53 21 C ATOM 331 CE1 PHE A 40 8.179 44.980 5.219 1.00 32.37 C ANISOU 331 CE1 PHE A 40 4019 4266 4011 -57 121 250 C ATOM 332 CE2 PHE A 40 8.622 42.905 4.101 1.00 31.87 C ANISOU 332 CE2 PHE A 40 4162 4086 3859 -145 86 122 C ATOM 333 CZ PHE A 40 7.785 43.983 4.341 1.00 27.04 C ANISOU 333 CZ PHE A 40 3386 3326 3562 97 -109 -171 C ATOM 334 N ASN A 41 11.538 40.757 7.499 1.00 31.43 N ANISOU 334 N ASN A 41 3986 4001 3955 -2 -4 5 N ATOM 335 CA ASN A 41 10.958 39.412 7.432 1.00 31.72 C ANISOU 335 CA ASN A 41 4022 4030 3997 -7 0 4 C ATOM 336 C ASN A 41 10.287 38.968 8.737 1.00 32.04 C ANISOU 336 C ASN A 41 4066 4071 4034 -8 5 4 C ATOM 337 O ASN A 41 9.376 38.140 8.716 1.00 32.01 O ANISOU 337 O ASN A 41 4068 4072 4021 -16 5 2 O ATOM 338 CB ASN A 41 12.024 38.387 7.025 1.00 31.71 C ANISOU 338 CB ASN A 41 4023 4027 3996 -7 -2 7 C ATOM 339 CG ASN A 41 11.429 37.048 6.622 1.00 31.69 C ANISOU 339 CG ASN A 41 4010 4032 3996 -7 -9 14 C ATOM 340 ND2 ASN A 41 10.531 37.068 5.642 1.00 31.38 N ANISOU 340 ND2 ASN A 41 3953 4001 3968 -31 7 16 N ATOM 341 OD1 ASN A 41 11.770 36.010 7.187 1.00 31.87 O ANISOU 341 OD1 ASN A 41 4019 4052 4036 -30 5 23 O ATOM 342 N GLU A 42 10.737 39.520 9.862 1.00 32.43 N ANISOU 342 N GLU A 42 4114 4119 4088 -11 1 2 N ATOM 343 CA GLU A 42 10.117 39.246 11.163 1.00 32.60 C ANISOU 343 CA GLU A 42 4137 4142 4106 -11 -2 -7 C ATOM 344 C GLU A 42 8.659 39.714 11.219 1.00 32.60 C ANISOU 344 C GLU A 42 4139 4135 4112 -8 4 0 C ATOM 345 O GLU A 42 7.829 39.080 11.873 1.00 32.73 O ANISOU 345 O GLU A 42 4157 4151 4125 -16 13 4 O ATOM 346 CB GLU A 42 10.923 39.896 12.292 1.00 33.07 C ANISOU 346 CB GLU A 42 4198 4207 4157 -23 -5 9 C ATOM 347 CG GLU A 42 12.313 39.292 12.477 1.00 34.74 C ANISOU 347 CG GLU A 42 4351 4375 4471 68 129 135 C ATOM 348 CD GLU A 42 13.134 39.986 13.552 1.00 26.27 C ANISOU 348 CD GLU A 42 3176 3051 3750 748 62 -713 C ATOM 349 OE1 GLU A 42 12.612 40.910 14.215 1.00 41.54 O ANISOU 349 OE1 GLU A 42 4956 5712 5113 -660 -383 672 O ATOM 350 OE2 GLU A 42 14.310 39.604 13.733 1.00 38.14 O1- ANISOU 350 OE2 GLU A 42 5480 4735 4277 -479 222 -27 O1- ATOM 351 N GLN A 43 8.353 40.811 10.527 1.00 32.41 N ANISOU 351 N GLN A 43 4107 4105 4099 -10 4 -2 N ATOM 352 CA GLN A 43 6.977 41.314 10.424 1.00 32.17 C ANISOU 352 CA GLN A 43 4077 4078 4067 -5 4 -11 C ATOM 353 C GLN A 43 6.057 40.360 9.654 1.00 31.69 C ANISOU 353 C GLN A 43 4013 4010 4015 -2 8 -11 C ATOM 354 O GLN A 43 4.844 40.365 9.864 1.00 31.82 O ANISOU 354 O GLN A 43 4029 4023 4036 -10 10 -16 O ATOM 355 CB GLN A 43 6.951 42.690 9.746 1.00 32.42 C ANISOU 355 CB GLN A 43 4122 4096 4099 -10 7 -9 C ATOM 356 CG GLN A 43 7.620 43.807 10.542 1.00 33.55 C ANISOU 356 CG GLN A 43 4254 4183 4310 -36 -70 27 C ATOM 357 CD GLN A 43 6.810 44.246 11.752 1.00 30.69 C ANISOU 357 CD GLN A 43 3477 4364 3817 152 -110 -87 C ATOM 358 NE2 GLN A 43 5.529 44.538 11.540 1.00 35.22 N ANISOU 358 NE2 GLN A 43 4760 4290 4331 -162 121 -23 N ATOM 359 OE1 GLN A 43 7.333 44.324 12.865 1.00 35.57 O ANISOU 359 OE1 GLN A 43 4571 4259 4685 7 151 5 O ATOM 360 N LEU A 44 6.637 39.558 8.761 1.00 30.98 N ANISOU 360 N LEU A 44 3922 3925 3924 -11 -1 -8 N ATOM 361 CA LEU A 44 5.880 38.601 7.947 1.00 30.31 C ANISOU 361 CA LEU A 44 3837 3836 3839 -2 2 0 C ATOM 362 C LEU A 44 5.676 37.248 8.642 1.00 29.61 C ANISOU 362 C LEU A 44 3745 3758 3748 -5 -4 -7 C ATOM 363 O LEU A 44 4.991 36.373 8.110 1.00 29.60 O ANISOU 363 O LEU A 44 3735 3754 3757 -4 1 -10 O ATOM 364 CB LEU A 44 6.590 38.381 6.607 1.00 30.29 C ANISOU 364 CB LEU A 44 3837 3832 3837 0 0 -5 C ATOM 365 CG LEU A 44 6.920 39.635 5.792 1.00 30.30 C ANISOU 365 CG LEU A 44 3837 3841 3832 0 0 -2 C ATOM 366 CD1 LEU A 44 7.717 39.269 4.548 1.00 30.28 C ANISOU 366 CD1 LEU A 44 3841 3836 3827 8 1 -4 C ATOM 367 CD2 LEU A 44 5.653 40.389 5.418 1.00 30.30 C ANISOU 367 CD2 LEU A 44 3842 3822 3845 9 2 0 C ATOM 368 N LYS A 45 6.270 37.082 9.824 1.00 28.73 N ANISOU 368 N LYS A 45 3630 3633 3653 -7 2 2 N ATOM 369 CA LYS A 45 6.193 35.830 10.579 1.00 27.97 C ANISOU 369 CA LYS A 45 3527 3547 3551 -9 2 -5 C ATOM 370 C LYS A 45 4.758 35.535 11.018 1.00 26.66 C ANISOU 370 C LYS A 45 3376 3367 3384 -10 -7 -14 C ATOM 371 O LYS A 45 4.149 36.317 11.749 1.00 26.64 O ANISOU 371 O LYS A 45 3362 3366 3391 -16 2 -15 O ATOM 372 CB LYS A 45 7.111 35.907 11.802 1.00 28.28 C ANISOU 372 CB LYS A 45 3570 3585 3587 -4 -5 -8 C ATOM 373 CG LYS A 45 7.222 34.623 12.615 1.00 29.22 C ANISOU 373 CG LYS A 45 3706 3687 3706 -2 2 7 C ATOM 374 CD LYS A 45 8.299 34.765 13.683 1.00 30.36 C ANISOU 374 CD LYS A 45 3829 3864 3840 0 -26 -5 C ATOM 375 CE LYS A 45 8.278 33.608 14.661 1.00 30.99 C ANISOU 375 CE LYS A 45 3927 3926 3919 -2 -11 7 C ATOM 376 NZ LYS A 45 9.283 33.774 15.748 1.00 31.70 N1+ ANISOU 376 NZ LYS A 45 3994 4051 3997 -2 -34 0 N1+ ATOM 377 N GLY A 46 4.222 34.405 10.560 1.00 25.10 N ANISOU 377 N GLY A 46 3164 3189 3181 -1 5 2 N ATOM 378 CA GLY A 46 2.849 34.013 10.879 1.00 23.81 C ANISOU 378 CA GLY A 46 3024 3014 3007 1 0 1 C ATOM 379 C GLY A 46 1.782 34.708 10.046 1.00 22.62 C ANISOU 379 C GLY A 46 2881 2863 2848 -10 16 5 C ATOM 380 O GLY A 46 0.595 34.418 10.195 1.00 22.46 O ANISOU 380 O GLY A 46 2867 2854 2813 1 25 10 O ATOM 381 N VAL A 47 2.199 35.609 9.155 1.00 21.29 N ANISOU 381 N VAL A 47 2696 2708 2683 0 13 -4 N ATOM 382 CA VAL A 47 1.276 36.408 8.348 1.00 20.18 C ANISOU 382 CA VAL A 47 2569 2567 2530 -11 18 -7 C ATOM 383 C VAL A 47 0.905 35.664 7.066 1.00 19.31 C ANISOU 383 C VAL A 47 2445 2456 2433 -5 22 13 C ATOM 384 O VAL A 47 1.723 34.932 6.510 1.00 18.93 O ANISOU 384 O VAL A 47 2417 2413 2361 -11 36 23 O ATOM 385 CB VAL A 47 1.905 37.776 7.991 1.00 20.20 C ANISOU 385 CB VAL A 47 2572 2567 2534 -2 14 -8 C ATOM 386 CG1 VAL A 47 0.964 38.609 7.135 1.00 20.14 C ANISOU 386 CG1 VAL A 47 2577 2567 2506 1 17 -7 C ATOM 387 CG2 VAL A 47 2.282 38.529 9.263 1.00 20.08 C ANISOU 387 CG2 VAL A 47 2558 2552 2519 -30 11 -10 C ATOM 388 N SER A 48 -0.328 35.858 6.599 1.00 18.26 N ANISOU 388 N SER A 48 2321 2325 2291 -2 26 5 N ATOM 389 CA SER A 48 -0.812 35.188 5.391 1.00 17.60 C ANISOU 389 CA SER A 48 2221 2240 2226 -2 33 22 C ATOM 390 C SER A 48 -0.017 35.627 4.162 1.00 16.84 C ANISOU 390 C SER A 48 2129 2148 2121 -2 25 13 C ATOM 391 O SER A 48 0.657 36.658 4.181 1.00 16.57 O ANISOU 391 O SER A 48 2095 2105 2096 11 37 28 O ATOM 392 CB SER A 48 -2.303 35.467 5.167 1.00 17.66 C ANISOU 392 CB SER A 48 2224 2243 2241 -8 22 13 C ATOM 393 OG SER A 48 -2.512 36.769 4.639 1.00 17.89 O ANISOU 393 OG SER A 48 2274 2291 2233 13 62 31 O ATOM 394 N ARG A 49 -0.107 34.832 3.101 1.00 16.20 N ANISOU 394 N ARG A 49 2038 2064 2051 -5 47 28 N ATOM 395 CA ARG A 49 0.600 35.112 1.847 1.00 15.67 C ANISOU 395 CA ARG A 49 1973 1995 1983 0 31 14 C ATOM 396 C ARG A 49 0.206 36.471 1.273 1.00 15.99 C ANISOU 396 C ARG A 49 2013 2023 2037 4 25 9 C ATOM 397 O ARG A 49 1.061 37.254 0.855 1.00 15.59 O ANISOU 397 O ARG A 49 1969 1944 2007 5 35 11 O ATOM 398 CB ARG A 49 0.298 34.016 0.823 1.00 15.40 C ANISOU 398 CB ARG A 49 1931 1969 1949 4 36 25 C ATOM 399 CG ARG A 49 1.199 34.037 -0.410 1.00 14.22 C ANISOU 399 CG ARG A 49 1815 1789 1797 -8 11 26 C ATOM 400 CD ARG A 49 0.801 32.955 -1.409 1.00 13.32 C ANISOU 400 CD ARG A 49 1681 1669 1707 19 11 44 C ATOM 401 NE ARG A 49 0.715 31.642 -0.774 1.00 12.83 N ANISOU 401 NE ARG A 49 1573 1626 1675 -25 0 34 N ATOM 402 CZ ARG A 49 0.215 30.549 -1.345 1.00 12.35 C ANISOU 402 CZ ARG A 49 1555 1557 1578 27 16 9 C ATOM 403 NH1 ARG A 49 -0.252 30.575 -2.589 1.00 12.77 N1+ ANISOU 403 NH1 ARG A 49 1610 1620 1621 28 4 19 N1+ ATOM 404 NH2 ARG A 49 0.177 29.413 -0.658 1.00 11.29 N ANISOU 404 NH2 ARG A 49 1424 1460 1405 -27 2 0 N ATOM 405 N GLU A 50 -1.094 36.747 1.274 1.00 16.51 N ANISOU 405 N GLU A 50 2079 2088 2105 1 14 4 N ATOM 406 CA GLU A 50 -1.627 37.953 0.654 1.00 17.06 C ANISOU 406 CA GLU A 50 2157 2149 2175 7 4 -2 C ATOM 407 C GLU A 50 -1.273 39.186 1.483 1.00 17.11 C ANISOU 407 C GLU A 50 2166 2154 2179 8 4 5 C ATOM 408 O GLU A 50 -0.857 40.209 0.937 1.00 17.14 O ANISOU 408 O GLU A 50 2183 2128 2199 20 11 2 O ATOM 409 CB GLU A 50 -3.144 37.830 0.468 1.00 17.46 C ANISOU 409 CB GLU A 50 2185 2206 2241 18 -1 4 C ATOM 410 CG GLU A 50 -3.569 36.761 -0.559 1.00 19.20 C ANISOU 410 CG GLU A 50 2422 2455 2417 -2 -10 -43 C ATOM 411 CD GLU A 50 -3.352 35.318 -0.086 1.00 19.86 C ANISOU 411 CD GLU A 50 2696 2513 2336 31 11 -15 C ATOM 412 OE1 GLU A 50 -3.405 35.055 1.139 1.00 22.29 O ANISOU 412 OE1 GLU A 50 2713 2816 2936 -59 11 -14 O ATOM 413 OE2 GLU A 50 -3.129 34.439 -0.949 1.00 23.58 O1- ANISOU 413 OE2 GLU A 50 2934 2970 3053 -8 -21 -5 O1- ATOM 414 N ASP A 51 -1.414 39.075 2.801 1.00 17.27 N ANISOU 414 N ASP A 51 2192 2173 2197 19 23 -4 N ATOM 415 CA ASP A 51 -1.035 40.157 3.709 1.00 17.26 C ANISOU 415 CA ASP A 51 2197 2184 2175 11 14 0 C ATOM 416 C ASP A 51 0.474 40.418 3.671 1.00 16.83 C ANISOU 416 C ASP A 51 2162 2117 2115 15 26 1 C ATOM 417 O ASP A 51 0.907 41.561 3.796 1.00 16.95 O ANISOU 417 O ASP A 51 2197 2120 2123 27 46 -8 O ATOM 418 CB ASP A 51 -1.489 39.854 5.145 1.00 17.63 C ANISOU 418 CB ASP A 51 2256 2222 2218 15 32 0 C ATOM 419 CG ASP A 51 -3.006 39.916 5.318 1.00 18.90 C ANISOU 419 CG ASP A 51 2371 2427 2383 21 16 0 C ATOM 420 OD1 ASP A 51 -3.716 40.376 4.398 1.00 20.28 O ANISOU 420 OD1 ASP A 51 2466 2642 2592 108 -5 -1 O ATOM 421 OD2 ASP A 51 -3.492 39.502 6.393 1.00 20.80 O1- ANISOU 421 OD2 ASP A 51 2650 2697 2554 -10 87 25 O1- ATOM 422 N SER A 52 1.267 39.361 3.491 1.00 16.32 N ANISOU 422 N SER A 52 2093 2063 2044 8 25 15 N ATOM 423 CA SER A 52 2.718 39.500 3.354 1.00 15.96 C ANISOU 423 CA SER A 52 2063 2011 1988 -2 21 11 C ATOM 424 C SER A 52 3.082 40.281 2.088 1.00 15.94 C ANISOU 424 C SER A 52 2050 2009 1996 -1 28 9 C ATOM 425 O SER A 52 3.903 41.197 2.136 1.00 15.75 O ANISOU 425 O SER A 52 2063 1964 1954 -1 54 2 O ATOM 426 CB SER A 52 3.399 38.126 3.332 1.00 15.79 C ANISOU 426 CB SER A 52 2047 1988 1962 -7 23 21 C ATOM 427 OG SER A 52 3.346 37.501 4.607 1.00 15.27 O ANISOU 427 OG SER A 52 2034 1886 1878 -5 34 16 O ATOM 428 N LEU A 53 2.473 39.917 0.961 1.00 16.01 N ANISOU 428 N LEU A 53 2053 2017 2013 -1 27 10 N ATOM 429 CA LEU A 53 2.714 40.629 -0.299 1.00 16.22 C ANISOU 429 CA LEU A 53 2080 2046 2034 0 23 8 C ATOM 430 C LEU A 53 2.323 42.097 -0.180 1.00 16.87 C ANISOU 430 C LEU A 53 2169 2120 2119 2 23 0 C ATOM 431 O LEU A 53 3.036 42.971 -0.668 1.00 16.80 O ANISOU 431 O LEU A 53 2207 2104 2072 -2 25 -13 O ATOM 432 CB LEU A 53 1.946 39.985 -1.458 1.00 15.88 C ANISOU 432 CB LEU A 53 2034 2006 1993 0 28 17 C ATOM 433 CG LEU A 53 2.052 40.686 -2.822 1.00 15.10 C ANISOU 433 CG LEU A 53 1912 1885 1937 0 20 9 C ATOM 434 CD1 LEU A 53 3.512 40.857 -3.241 1.00 15.02 C ANISOU 434 CD1 LEU A 53 1896 1874 1937 27 38 5 C ATOM 435 CD2 LEU A 53 1.281 39.919 -3.875 1.00 14.70 C ANISOU 435 CD2 LEU A 53 1873 1869 1843 2 22 32 C ATOM 436 N GLN A 54 1.193 42.365 0.470 1.00 17.79 N ANISOU 436 N GLN A 54 2281 2246 2233 1 35 4 N ATOM 437 CA GLN A 54 0.728 43.737 0.653 1.00 18.67 C ANISOU 437 CA GLN A 54 2394 2337 2360 11 18 11 C ATOM 438 C GLN A 54 1.735 44.571 1.449 1.00 19.22 C ANISOU 438 C GLN A 54 2464 2408 2431 0 10 2 C ATOM 439 O GLN A 54 1.986 45.727 1.114 1.00 19.53 O ANISOU 439 O GLN A 54 2541 2427 2453 -1 5 9 O ATOM 440 CB GLN A 54 -0.642 43.761 1.341 1.00 18.82 C ANISOU 440 CB GLN A 54 2404 2368 2378 8 25 9 C ATOM 441 CG GLN A 54 -1.309 45.133 1.370 1.00 19.97 C ANISOU 441 CG GLN A 54 2514 2474 2597 25 38 -27 C ATOM 442 CD GLN A 54 -1.577 45.680 -0.021 1.00 18.72 C ANISOU 442 CD GLN A 54 2363 2257 2492 -227 -82 32 C ATOM 443 NE2 GLN A 54 -0.860 46.735 -0.392 1.00 23.32 N ANISOU 443 NE2 GLN A 54 3030 3033 2796 183 -23 -61 N ATOM 444 OE1 GLN A 54 -2.418 45.158 -0.753 1.00 23.27 O ANISOU 444 OE1 GLN A 54 3020 2902 2919 141 80 35 O ATOM 445 N LYS A 55 2.315 43.977 2.490 1.00 19.78 N ANISOU 445 N LYS A 55 2542 2486 2486 5 11 9 N ATOM 446 CA LYS A 55 3.353 44.638 3.288 1.00 20.32 C ANISOU 446 CA LYS A 55 2599 2558 2560 -2 7 -1 C ATOM 447 C LYS A 55 4.596 44.968 2.455 1.00 20.43 C ANISOU 447 C LYS A 55 2625 2570 2567 -9 11 -5 C ATOM 448 O LYS A 55 5.218 46.014 2.647 1.00 20.76 O ANISOU 448 O LYS A 55 2693 2599 2591 -30 16 -23 O ATOM 449 CB LYS A 55 3.757 43.760 4.478 1.00 20.57 C ANISOU 449 CB LYS A 55 2635 2595 2585 0 1 0 C ATOM 450 CG LYS A 55 2.662 43.559 5.524 1.00 21.73 C ANISOU 450 CG LYS A 55 2741 2762 2754 -8 26 19 C ATOM 451 CD LYS A 55 2.744 44.577 6.651 1.00 23.32 C ANISOU 451 CD LYS A 55 2975 2932 2950 -1 -4 -11 C ATOM 452 CE LYS A 55 1.801 44.222 7.796 1.00 24.18 C ANISOU 452 CE LYS A 55 3068 3071 3047 0 11 11 C ATOM 453 NZ LYS A 55 2.127 42.901 8.413 1.00 24.97 N1+ ANISOU 453 NZ LYS A 55 3202 3106 3177 -23 -2 42 N1+ ATOM 454 N ILE A 56 4.956 44.070 1.539 1.00 20.52 N ANISOU 454 N ILE A 56 2635 2574 2586 -4 7 -8 N ATOM 455 CA ILE A 56 6.119 44.268 0.671 1.00 20.68 C ANISOU 455 CA ILE A 56 2651 2597 2606 -2 8 -5 C ATOM 456 C ILE A 56 5.875 45.390 -0.336 1.00 21.25 C ANISOU 456 C ILE A 56 2732 2671 2669 -5 10 -2 C ATOM 457 O ILE A 56 6.759 46.209 -0.587 1.00 21.15 O ANISOU 457 O ILE A 56 2726 2661 2647 -18 -1 -11 O ATOM 458 CB ILE A 56 6.488 42.973 -0.083 1.00 20.43 C ANISOU 458 CB ILE A 56 2624 2566 2571 -7 5 -11 C ATOM 459 CG1 ILE A 56 7.030 41.931 0.896 1.00 20.16 C ANISOU 459 CG1 ILE A 56 2572 2528 2557 -7 5 -9 C ATOM 460 CG2 ILE A 56 7.529 43.251 -1.163 1.00 20.23 C ANISOU 460 CG2 ILE A 56 2609 2528 2548 -10 -2 1 C ATOM 461 CD1 ILE A 56 7.119 40.543 0.312 1.00 19.97 C ANISOU 461 CD1 ILE A 56 2556 2514 2515 -20 -14 -34 C ATOM 462 N LEU A 57 4.677 45.425 -0.909 1.00 21.99 N ANISOU 462 N LEU A 57 2813 2762 2779 -4 7 -4 N ATOM 463 CA LEU A 57 4.305 46.495 -1.835 1.00 22.79 C ANISOU 463 CA LEU A 57 2919 2868 2872 -2 0 8 C ATOM 464 C LEU A 57 4.270 47.870 -1.157 1.00 23.87 C ANISOU 464 C LEU A 57 3064 2983 3019 5 4 -5 C ATOM 465 O LEU A 57 4.431 48.883 -1.830 1.00 23.97 O ANISOU 465 O LEU A 57 3103 2999 3005 -10 14 -5 O ATOM 466 CB LEU A 57 2.953 46.199 -2.492 1.00 22.67 C ANISOU 466 CB LEU A 57 2898 2843 2870 5 7 7 C ATOM 467 CG LEU A 57 2.918 44.987 -3.429 1.00 22.30 C ANISOU 467 CG LEU A 57 2837 2811 2823 -2 4 19 C ATOM 468 CD1 LEU A 57 1.485 44.652 -3.822 1.00 22.26 C ANISOU 468 CD1 LEU A 57 2828 2804 2823 2 0 1 C ATOM 469 CD2 LEU A 57 3.776 45.219 -4.670 1.00 22.26 C ANISOU 469 CD2 LEU A 57 2857 2785 2816 2 13 -2 C ATOM 470 N ASP A 58 4.060 47.895 0.162 1.00 25.15 N ANISOU 470 N ASP A 58 3225 3162 3165 0 11 -2 N ATOM 471 CA ASP A 58 4.058 49.144 0.942 1.00 26.18 C ANISOU 471 CA ASP A 58 3353 3283 3311 2 7 -13 C ATOM 472 C ASP A 58 5.458 49.619 1.344 1.00 27.03 C ANISOU 472 C ASP A 58 3444 3406 3417 -5 2 -11 C ATOM 473 O ASP A 58 5.605 50.747 1.828 1.00 27.34 O ANISOU 473 O ASP A 58 3494 3415 3478 -5 7 -26 O ATOM 474 CB ASP A 58 3.223 48.998 2.214 1.00 26.35 C ANISOU 474 CB ASP A 58 3369 3306 3333 9 7 -7 C ATOM 475 CG ASP A 58 1.780 48.625 1.938 1.00 26.71 C ANISOU 475 CG ASP A 58 3417 3333 3394 10 5 -19 C ATOM 476 OD1 ASP A 58 1.272 48.901 0.830 1.00 27.30 O ANISOU 476 OD1 ASP A 58 3524 3409 3439 44 -8 -19 O ATOM 477 OD2 ASP A 58 1.146 48.051 2.847 1.00 27.69 O1- ANISOU 477 OD2 ASP A 58 3573 3456 3492 33 43 2 O1- ATOM 478 N LEU A 59 6.474 48.767 1.181 1.00 27.86 N ANISOU 478 N LEU A 59 3540 3511 3533 5 5 -2 N ATOM 479 CA LEU A 59 7.867 49.227 1.219 1.00 28.47 C ANISOU 479 CA LEU A 59 3608 3600 3605 -2 -2 -4 C ATOM 480 C LEU A 59 7.895 50.391 0.236 1.00 28.93 C ANISOU 480 C LEU A 59 3673 3652 3667 2 -4 0 C ATOM 481 O LEU A 59 8.193 51.530 0.601 1.00 29.07 O ANISOU 481 O LEU A 59 3705 3662 3677 -1 -17 -2 O ATOM 482 CB LEU A 59 8.837 48.112 0.807 1.00 28.55 C ANISOU 482 CB LEU A 59 3621 3605 3620 0 0 2 C ATOM 483 CG LEU A 59 9.234 47.095 1.886 1.00 28.62 C ANISOU 483 CG LEU A 59 3633 3629 3612 -10 -5 5 C ATOM 484 CD1 LEU A 59 10.084 45.986 1.300 1.00 28.85 C ANISOU 484 CD1 LEU A 59 3662 3631 3666 -2 -4 11 C ATOM 485 CD2 LEU A 59 9.967 47.777 3.029 1.00 28.88 C ANISOU 485 CD2 LEU A 59 3683 3654 3634 -15 -2 7 C ATOM 486 N ALA A 60 7.591 50.075 -1.021 1.00 29.37 N ANISOU 486 N ALA A 60 3729 3716 3715 1 -5 -7 N ATOM 487 CA ALA A 60 6.664 50.887 -1.807 1.00 29.71 C ANISOU 487 CA ALA A 60 3761 3763 3764 0 -1 -7 C ATOM 488 C ALA A 60 7.173 52.122 -2.535 1.00 29.87 C ANISOU 488 C ALA A 60 3777 3781 3788 2 2 -5 C ATOM 489 O ALA A 60 8.373 52.270 -2.770 1.00 30.32 O ANISOU 489 O ALA A 60 3825 3842 3851 0 1 -10 O ATOM 490 CB ALA A 60 5.512 51.280 -0.910 1.00 29.76 C ANISOU 490 CB ALA A 60 3767 3767 3772 1 5 -13 C ATOM 491 N ASP A 61 6.244 53.013 -2.899 1.00 29.87 N ANISOU 491 N ASP A 61 3773 3789 3787 0 -2 -1 N ATOM 492 CA ASP A 61 4.808 52.889 -2.545 1.00 29.78 C ANISOU 492 CA ASP A 61 3770 3774 3771 0 -2 -5 C ATOM 493 C ASP A 61 3.989 52.323 -3.694 1.00 29.20 C ANISOU 493 C ASP A 61 3698 3690 3706 2 4 -2 C ATOM 494 O ASP A 61 3.329 53.059 -4.429 1.00 29.21 O ANISOU 494 O ASP A 61 3700 3690 3706 11 2 2 O ATOM 495 CB ASP A 61 4.255 54.231 -2.071 1.00 29.99 C ANISOU 495 CB ASP A 61 3797 3790 3808 2 2 -4 C ATOM 496 CG ASP A 61 4.681 54.557 -0.656 1.00 30.87 C ANISOU 496 CG ASP A 61 3919 3924 3885 9 -4 -4 C ATOM 497 OD1 ASP A 61 5.654 55.328 -0.491 1.00 31.90 O ANISOU 497 OD1 ASP A 61 4037 4009 4072 -47 -2 -2 O ATOM 498 OD2 ASP A 61 4.061 54.018 0.290 1.00 32.06 O1- ANISOU 498 OD2 ASP A 61 4050 4057 4073 -26 38 39 O1- ATOM 499 N LYS A 62 4.009 50.999 -3.813 1.00 28.42 N ANISOU 499 N LYS A 62 3598 3600 3597 0 -1 2 N ATOM 500 CA LYS A 62 3.640 50.351 -5.058 1.00 27.72 C ANISOU 500 CA LYS A 62 3507 3507 3517 -1 0 5 C ATOM 501 C LYS A 62 2.165 49.984 -5.141 1.00 27.07 C ANISOU 501 C LYS A 62 3435 3421 3428 2 -4 5 C ATOM 502 O LYS A 62 1.623 49.318 -4.256 1.00 26.99 O ANISOU 502 O LYS A 62 3411 3420 3424 7 2 0 O ATOM 503 CB LYS A 62 4.504 49.114 -5.279 1.00 27.69 C ANISOU 503 CB LYS A 62 3510 3506 3504 0 -2 2 C ATOM 504 CG LYS A 62 4.391 48.554 -6.678 1.00 27.63 C ANISOU 504 CG LYS A 62 3503 3499 3495 0 0 1 C ATOM 505 CD LYS A 62 5.604 47.729 -7.035 1.00 27.50 C ATOM 506 CE LYS A 62 5.355 46.898 -8.282 1.00 27.39 C ANISOU 506 CE LYS A 62 3461 3474 3471 1 -1 4 C ATOM 507 NZ LYS A 62 5.359 47.731 -9.514 1.00 27.52 N1+ ANISOU 507 NZ LYS A 62 3478 3502 3474 0 0 15 N1+ ATOM 508 N LYS A 63 1.537 50.432 -6.227 1.00 26.29 N ANISOU 508 N LYS A 63 3327 3315 3346 0 -2 2 N ATOM 509 CA LYS A 63 0.169 50.066 -6.576 1.00 25.65 C ANISOU 509 CA LYS A 63 3257 3232 3255 1 -2 1 C ATOM 510 C LYS A 63 0.189 49.085 -7.742 1.00 24.71 C ANISOU 510 C LYS A 63 3116 3108 3162 1 -4 11 C ATOM 511 O LYS A 63 0.967 49.245 -8.684 1.00 24.48 O ANISOU 511 O LYS A 63 3109 3063 3130 0 -18 8 O ATOM 512 CB LYS A 63 -0.622 51.313 -6.982 1.00 25.92 C ANISOU 512 CB LYS A 63 3284 3269 3295 8 -2 5 C ATOM 513 CG LYS A 63 -0.833 52.334 -5.866 1.00 26.70 C ANISOU 513 CG LYS A 63 3396 3370 3376 8 -1 -16 C ATOM 514 CD LYS A 63 -1.683 51.795 -4.716 1.00 27.71 C ANISOU 514 CD LYS A 63 3514 3503 3509 -4 11 13 C ATOM 515 CE LYS A 63 -3.091 51.414 -5.162 1.00 28.25 C ANISOU 515 CE LYS A 63 3569 3575 3589 -11 -5 8 C ATOM 516 NZ LYS A 63 -3.966 51.088 -4.002 1.00 28.80 N1+ ANISOU 516 NZ LYS A 63 3644 3660 3637 -7 23 0 N1+ ATOM 517 N VAL A 64 -0.670 48.070 -7.670 1.00 23.64 N ANISOU 517 N VAL A 64 2988 2979 3016 15 -8 5 N ATOM 518 CA VAL A 64 -0.796 47.070 -8.729 1.00 22.90 C ANISOU 518 CA VAL A 64 2876 2884 2940 7 -8 16 C ATOM 519 C VAL A 64 -2.264 46.696 -8.921 1.00 22.35 C ANISOU 519 C VAL A 64 2816 2804 2869 11 -10 11 C ATOM 520 O VAL A 64 -3.085 46.918 -8.031 1.00 22.16 O ANISOU 520 O VAL A 64 2778 2758 2882 15 -5 18 O ATOM 521 CB VAL A 64 0.008 45.789 -8.399 1.00 22.82 C ANISOU 521 CB VAL A 64 2866 2876 2925 10 -4 7 C ATOM 522 CG1 VAL A 64 1.494 46.100 -8.293 1.00 22.55 C ANISOU 522 CG1 VAL A 64 2848 2844 2874 -2 -5 16 C ATOM 523 CG2 VAL A 64 -0.500 45.149 -7.112 1.00 22.85 C ANISOU 523 CG2 VAL A 64 2867 2883 2930 14 -23 20 C ATOM 524 N SER A 65 -2.589 46.133 -10.081 1.00 21.80 N ANISOU 524 N SER A 65 2732 2728 2819 11 -11 19 N ATOM 525 CA SER A 65 -3.948 45.659 -10.343 1.00 21.52 C ANISOU 525 CA SER A 65 2701 2701 2772 8 -7 13 C ATOM 526 C SER A 65 -4.226 44.410 -9.514 1.00 21.25 C ANISOU 526 C SER A 65 2653 2664 2754 4 -11 13 C ATOM 527 O SER A 65 -3.296 43.751 -9.042 1.00 21.18 O ANISOU 527 O SER A 65 2624 2645 2777 8 -23 28 O ATOM 528 CB SER A 65 -4.151 45.367 -11.834 1.00 21.52 C ANISOU 528 CB SER A 65 2693 2703 2779 8 -15 7 C ATOM 529 OG SER A 65 -3.376 44.263 -12.269 1.00 21.31 O ANISOU 529 OG SER A 65 2662 2686 2747 17 -36 10 O ATOM 530 N ALA A 66 -5.506 44.091 -9.336 1.00 20.90 N ANISOU 530 N ALA A 66 2612 2614 2713 14 -13 20 N ATOM 531 CA ALA A 66 -5.910 42.897 -8.588 1.00 20.62 C ANISOU 531 CA ALA A 66 2572 2590 2673 0 -9 7 C ATOM 532 C ALA A 66 -5.306 41.625 -9.184 1.00 20.22 C ANISOU 532 C ALA A 66 2528 2543 2612 2 -17 11 C ATOM 533 O ALA A 66 -4.876 40.735 -8.449 1.00 20.08 O ANISOU 533 O ALA A 66 2505 2500 2622 0 -23 13 O ATOM 534 CB ALA A 66 -7.430 42.788 -8.537 1.00 20.64 C ANISOU 534 CB ALA A 66 2564 2597 2680 13 -9 2 C ATOM 535 N GLU A 67 -5.268 41.552 -10.513 1.00 19.91 N ANISOU 535 N GLU A 67 2491 2498 2577 5 -25 9 N ATOM 536 CA GLU A 67 -4.709 40.398 -11.215 1.00 19.78 C ANISOU 536 CA GLU A 67 2476 2496 2541 1 -20 13 C ATOM 537 C GLU A 67 -3.183 40.366 -11.150 1.00 19.13 C ANISOU 537 C GLU A 67 2395 2403 2470 0 -27 17 C ATOM 538 O GLU A 67 -2.594 39.289 -11.058 1.00 18.94 O ANISOU 538 O GLU A 67 2357 2367 2469 19 -47 34 O ATOM 539 CB GLU A 67 -5.182 40.371 -12.673 1.00 20.14 C ANISOU 539 CB GLU A 67 2540 2539 2572 2 -28 11 C ATOM 540 CG GLU A 67 -6.678 40.112 -12.829 1.00 21.55 C ANISOU 540 CG GLU A 67 2669 2762 2758 2 -22 -16 C ATOM 541 CD GLU A 67 -7.122 38.811 -12.176 1.00 22.04 C ANISOU 541 CD GLU A 67 2718 2802 2853 28 144 28 C ATOM 542 OE1 GLU A 67 -8.106 38.837 -11.405 1.00 25.62 O ANISOU 542 OE1 GLU A 67 3263 3206 3266 -27 -95 31 O ATOM 543 OE2 GLU A 67 -6.473 37.768 -12.421 1.00 25.07 O1- ANISOU 543 OE2 GLU A 67 3255 3160 3110 -65 -38 39 O1- ATOM 544 N GLU A 68 -2.545 41.535 -11.202 1.00 18.43 N ANISOU 544 N GLU A 68 2295 2332 2374 18 -36 28 N ATOM 545 CA GLU A 68 -1.094 41.621 -11.003 1.00 17.97 C ANISOU 545 CA GLU A 68 2248 2279 2297 13 -23 26 C ATOM 546 C GLU A 68 -0.720 41.140 -9.597 1.00 17.31 C ANISOU 546 C GLU A 68 2165 2191 2221 19 -13 25 C ATOM 547 O GLU A 68 0.255 40.405 -9.428 1.00 16.71 O ANISOU 547 O GLU A 68 2081 2119 2148 46 -8 56 O ATOM 548 CB GLU A 68 -0.582 43.048 -11.244 1.00 18.16 C ANISOU 548 CB GLU A 68 2270 2298 2329 11 -28 16 C ATOM 549 CG GLU A 68 -0.382 43.387 -12.726 1.00 18.85 C ANISOU 549 CG GLU A 68 2356 2421 2384 10 -28 8 C ATOM 550 CD GLU A 68 -0.083 44.861 -12.989 1.00 19.11 C ANISOU 550 CD GLU A 68 2428 2469 2363 -9 8 7 C ATOM 551 OE1 GLU A 68 0.309 45.187 -14.132 1.00 20.65 O ANISOU 551 OE1 GLU A 68 2492 2683 2671 -13 -47 45 O ATOM 552 OE2 GLU A 68 -0.242 45.694 -12.070 1.00 20.49 O1- ANISOU 552 OE2 GLU A 68 2572 2587 2625 8 -88 20 O1- ATOM 553 N PHE A 69 -1.510 41.543 -8.603 1.00 16.84 N ANISOU 553 N PHE A 69 2100 2125 2172 17 -22 33 N ATOM 554 CA PHE A 69 -1.324 41.110 -7.214 1.00 16.61 C ANISOU 554 CA PHE A 69 2070 2100 2140 14 -5 11 C ATOM 555 C PHE A 69 -1.361 39.583 -7.097 1.00 16.42 C ANISOU 555 C PHE A 69 2044 2074 2120 11 -17 16 C ATOM 556 O PHE A 69 -0.499 38.980 -6.451 1.00 15.96 O ANISOU 556 O PHE A 69 1965 2010 2088 35 -14 40 O ATOM 557 CB PHE A 69 -2.406 41.730 -6.320 1.00 16.70 C ANISOU 557 CB PHE A 69 2090 2103 2151 19 -13 4 C ATOM 558 CG PHE A 69 -2.219 41.460 -4.855 1.00 16.81 C ANISOU 558 CG PHE A 69 2096 2114 2176 39 22 10 C ATOM 559 CD1 PHE A 69 -1.522 42.354 -4.054 1.00 16.82 C ANISOU 559 CD1 PHE A 69 2076 2112 2202 47 10 17 C ATOM 560 CD2 PHE A 69 -2.752 40.315 -4.272 1.00 17.20 C ANISOU 560 CD2 PHE A 69 2140 2161 2232 16 7 11 C ATOM 561 CE1 PHE A 69 -1.351 42.112 -2.701 1.00 17.28 C ANISOU 561 CE1 PHE A 69 2137 2183 2244 26 31 -2 C ATOM 562 CE2 PHE A 69 -2.585 40.067 -2.920 1.00 17.71 C ANISOU 562 CE2 PHE A 69 2209 2227 2290 36 14 1 C ATOM 563 CZ PHE A 69 -1.884 40.965 -2.133 1.00 17.02 C ANISOU 563 CZ PHE A 69 2131 2137 2197 18 16 18 C ATOM 564 N LYS A 70 -2.358 38.965 -7.726 1.00 16.30 N ANISOU 564 N LYS A 70 2011 2068 2114 17 -18 18 N ATOM 565 CA LYS A 70 -2.507 37.507 -7.694 1.00 16.30 C ANISOU 565 CA LYS A 70 2037 2069 2086 11 -10 18 C ATOM 566 C LYS A 70 -1.346 36.801 -8.388 1.00 15.77 C ANISOU 566 C LYS A 70 1971 2006 2014 8 -10 28 C ATOM 567 O LYS A 70 -0.878 35.762 -7.920 1.00 15.42 O ANISOU 567 O LYS A 70 1905 1971 1981 30 -36 57 O ATOM 568 CB LYS A 70 -3.831 37.071 -8.330 1.00 16.76 C ANISOU 568 CB LYS A 70 2099 2124 2144 2 -25 13 C ATOM 569 CG LYS A 70 -5.059 37.404 -7.496 1.00 18.65 C ANISOU 569 CG LYS A 70 2346 2379 2359 20 19 -2 C ATOM 570 CD LYS A 70 -6.241 36.485 -7.809 1.00 20.86 C ANISOU 570 CD LYS A 70 2606 2641 2679 -38 5 -10 C ATOM 571 CE LYS A 70 -6.655 36.539 -9.274 1.00 22.27 C ANISOU 571 CE LYS A 70 2832 2833 2795 9 -11 15 C ATOM 572 NZ LYS A 70 -5.835 35.645 -10.149 1.00 23.29 N1+ ANISOU 572 NZ LYS A 70 2965 2934 2949 31 21 -19 N1+ ATOM 573 N GLU A 71 -0.883 37.367 -9.498 1.00 15.20 N ANISOU 573 N GLU A 71 1911 1927 1937 25 -16 31 N ATOM 574 CA GLU A 71 0.241 36.801 -10.238 1.00 14.88 C ANISOU 574 CA GLU A 71 1865 1897 1889 9 -19 17 C ATOM 575 C GLU A 71 1.536 36.853 -9.423 1.00 13.92 C ANISOU 575 C GLU A 71 1755 1768 1763 21 -7 20 C ATOM 576 O GLU A 71 2.307 35.898 -9.429 1.00 13.70 O ANISOU 576 O GLU A 71 1715 1760 1729 39 -36 50 O ATOM 577 CB GLU A 71 0.421 37.528 -11.576 1.00 15.29 C ANISOU 577 CB GLU A 71 1927 1947 1936 2 -13 21 C ATOM 578 CG GLU A 71 1.502 36.939 -12.490 1.00 17.34 C ANISOU 578 CG GLU A 71 2157 2291 2138 35 26 20 C ATOM 579 CD GLU A 71 1.234 35.496 -12.909 1.00 18.89 C ANISOU 579 CD GLU A 71 2256 2415 2504 8 20 -32 C ATOM 580 OE1 GLU A 71 0.057 35.067 -12.924 1.00 21.94 O ANISOU 580 OE1 GLU A 71 2785 2805 2747 -30 23 2 O ATOM 581 OE2 GLU A 71 2.209 34.786 -13.239 1.00 22.25 O1- ANISOU 581 OE2 GLU A 71 2824 2862 2768 31 -23 40 O1- ATOM 582 N LEU A 72 1.766 37.963 -8.727 1.00 12.95 N ANISOU 582 N LEU A 72 1607 1668 1643 0 -16 50 N ATOM 583 CA LEU A 72 2.953 38.118 -7.886 1.00 12.25 C ANISOU 583 CA LEU A 72 1535 1574 1545 13 4 43 C ATOM 584 C LEU A 72 2.963 37.093 -6.751 1.00 11.85 C ANISOU 584 C LEU A 72 1471 1523 1508 20 0 50 C ATOM 585 O LEU A 72 3.987 36.459 -6.491 1.00 11.09 O ANISOU 585 O LEU A 72 1384 1437 1390 51 -11 73 O ATOM 586 CB LEU A 72 3.029 39.538 -7.317 1.00 12.29 C ANISOU 586 CB LEU A 72 1529 1582 1555 -2 0 42 C ATOM 587 CG LEU A 72 3.360 40.648 -8.321 1.00 12.32 C ANISOU 587 CG LEU A 72 1566 1581 1532 14 4 38 C ATOM 588 CD1 LEU A 72 3.226 42.011 -7.663 1.00 12.69 C ANISOU 588 CD1 LEU A 72 1610 1606 1603 2 16 30 C ATOM 589 CD2 LEU A 72 4.755 40.462 -8.909 1.00 12.63 C ANISOU 589 CD2 LEU A 72 1575 1654 1569 5 -2 19 C ATOM 590 N ALA A 73 1.824 36.931 -6.084 1.00 11.75 N ANISOU 590 N ALA A 73 1469 1504 1491 33 -1 49 N ATOM 591 CA ALA A 73 1.691 35.928 -5.026 1.00 11.77 C ANISOU 591 CA ALA A 73 1474 1510 1485 22 -1 49 C ATOM 592 C ALA A 73 1.938 34.516 -5.562 1.00 11.98 C ANISOU 592 C ALA A 73 1502 1535 1513 18 1 46 C ATOM 593 O ALA A 73 2.612 33.718 -4.912 1.00 11.73 O ANISOU 593 O ALA A 73 1453 1540 1462 41 -7 78 O ATOM 594 CB ALA A 73 0.321 36.018 -4.374 1.00 11.96 C ANISOU 594 CB ALA A 73 1494 1538 1511 16 5 45 C ATOM 595 N LYS A 74 1.402 34.221 -6.745 1.00 12.24 N ANISOU 595 N LYS A 74 1532 1570 1545 10 -9 44 N ATOM 596 CA LYS A 74 1.600 32.924 -7.396 1.00 12.72 C ANISOU 596 CA LYS A 74 1610 1634 1589 5 -15 30 C ATOM 597 C LYS A 74 3.076 32.675 -7.715 1.00 12.63 C ANISOU 597 C LYS A 74 1602 1613 1584 20 -9 23 C ATOM 598 O LYS A 74 3.585 31.571 -7.496 1.00 12.29 O ANISOU 598 O LYS A 74 1548 1612 1507 55 -43 31 O ATOM 599 CB LYS A 74 0.761 32.830 -8.679 1.00 13.14 C ANISOU 599 CB LYS A 74 1654 1680 1656 -2 -39 30 C ATOM 600 CG LYS A 74 0.875 31.493 -9.413 1.00 14.62 C ANISOU 600 CG LYS A 74 1870 1839 1843 10 -1 -5 C ATOM 601 CD LYS A 74 0.192 31.545 -10.776 1.00 16.64 C ANISOU 601 CD LYS A 74 2096 2163 2063 14 -47 7 C ATOM 602 CE LYS A 74 0.494 30.306 -11.609 1.00 17.97 C ANISOU 602 CE LYS A 74 2270 2270 2286 5 -18 -28 C ATOM 603 NZ LYS A 74 1.938 30.186 -11.970 1.00 19.38 N1+ ANISOU 603 NZ LYS A 74 2396 2531 2434 22 1 -10 N1+ ATOM 604 N ARG A 75 3.753 33.698 -8.236 1.00 12.80 N ANISOU 604 N ARG A 75 1617 1633 1613 25 -5 34 N ATOM 605 CA ARG A 75 5.184 33.608 -8.551 1.00 12.88 C ANISOU 605 CA ARG A 75 1625 1647 1622 22 0 22 C ATOM 606 C ARG A 75 5.994 33.227 -7.315 1.00 12.10 C ANISOU 606 C ARG A 75 1540 1526 1531 27 9 28 C ATOM 607 O ARG A 75 6.796 32.288 -7.347 1.00 12.18 O ANISOU 607 O ARG A 75 1555 1533 1535 73 42 57 O ATOM 608 CB ARG A 75 5.711 34.943 -9.088 1.00 13.50 C ANISOU 608 CB ARG A 75 1700 1709 1721 10 11 8 C ATOM 609 CG ARG A 75 5.339 35.251 -10.526 1.00 15.64 C ANISOU 609 CG ARG A 75 1986 2023 1933 19 -14 31 C ATOM 610 CD ARG A 75 5.836 36.635 -10.924 1.00 18.23 C ANISOU 610 CD ARG A 75 2360 2261 2302 -13 25 18 C ATOM 611 NE ARG A 75 5.118 37.179 -12.074 1.00 21.33 N ANISOU 611 NE ARG A 75 2635 2876 2592 56 -7 -71 N ATOM 612 CZ ARG A 75 5.314 38.396 -12.579 1.00 17.80 C ANISOU 612 CZ ARG A 75 2275 2308 2178 -176 -367 115 C ATOM 613 NH1 ARG A 75 6.220 39.214 -12.049 1.00 25.01 N1+ ANISOU 613 NH1 ARG A 75 3231 3138 3133 238 309 -15 N1+ ATOM 614 NH2 ARG A 75 4.604 38.796 -13.629 1.00 24.87 N ANISOU 614 NH2 ARG A 75 3145 3106 3195 77 260 -66 N ATOM 615 N LYS A 76 5.792 33.966 -6.230 1.00 11.31 N ANISOU 615 N LYS A 76 1429 1434 1431 22 7 42 N ATOM 616 CA LYS A 76 6.506 33.689 -4.987 1.00 10.75 C ANISOU 616 CA LYS A 76 1363 1366 1356 2 2 21 C ATOM 617 C LYS A 76 6.192 32.290 -4.470 1.00 10.55 C ANISOU 617 C LYS A 76 1326 1348 1334 10 7 18 C ATOM 618 O LYS A 76 7.095 31.563 -4.060 1.00 10.14 O ANISOU 618 O LYS A 76 1253 1341 1258 28 2 32 O ATOM 619 CB LYS A 76 6.175 34.727 -3.915 1.00 10.69 C ANISOU 619 CB LYS A 76 1358 1350 1351 4 -11 27 C ATOM 620 CG LYS A 76 6.842 34.454 -2.560 1.00 10.40 C ANISOU 620 CG LYS A 76 1355 1303 1290 -34 -5 5 C ATOM 621 CD LYS A 76 5.920 33.702 -1.602 1.00 10.42 C ANISOU 621 CD LYS A 76 1316 1339 1302 10 21 9 C ATOM 622 CE LYS A 76 6.663 33.266 -0.352 1.00 9.94 C ANISOU 622 CE LYS A 76 1269 1283 1221 -62 25 11 C ATOM 623 NZ LYS A 76 5.743 32.615 0.616 1.00 9.93 N1+ ANISOU 623 NZ LYS A 76 1290 1317 1164 -91 46 36 N1+ ATOM 624 N ASN A 77 4.918 31.907 -4.474 1.00 10.12 N ANISOU 624 N ASN A 77 1272 1296 1276 30 -2 15 N ATOM 625 CA ASN A 77 4.555 30.581 -3.986 1.00 10.01 C ANISOU 625 CA ASN A 77 1257 1300 1246 18 0 22 C ATOM 626 C ASN A 77 5.183 29.467 -4.816 1.00 10.09 C ANISOU 626 C ASN A 77 1295 1285 1251 14 -2 23 C ATOM 627 O ASN A 77 5.639 28.462 -4.267 1.00 9.58 O ANISOU 627 O ASN A 77 1220 1240 1179 51 0 39 O ATOM 628 CB ASN A 77 3.044 30.388 -3.939 1.00 9.95 C ANISOU 628 CB ASN A 77 1249 1276 1255 0 0 7 C ATOM 629 CG ASN A 77 2.664 29.062 -3.320 1.00 9.75 C ANISOU 629 CG ASN A 77 1198 1283 1221 33 19 34 C ATOM 630 ND2 ASN A 77 1.990 28.219 -4.088 1.00 9.32 N ANISOU 630 ND2 ASN A 77 1265 1107 1167 74 46 20 N ATOM 631 OD1 ASN A 77 3.003 28.789 -2.169 1.00 10.32 O ANISOU 631 OD1 ASN A 77 1302 1364 1255 33 123 88 O ATOM 632 N ASP A 78 5.212 29.642 -6.135 1.00 10.32 N ANISOU 632 N ASP A 78 1330 1326 1264 1 10 9 N ATOM 633 CA ASP A 78 5.816 28.643 -7.018 1.00 10.90 C ANISOU 633 CA ASP A 78 1404 1380 1356 8 15 8 C ATOM 634 C ASP A 78 7.290 28.435 -6.675 1.00 10.62 C ANISOU 634 C ASP A 78 1377 1355 1302 5 19 11 C ATOM 635 O ASP A 78 7.773 27.302 -6.658 1.00 10.74 O ANISOU 635 O ASP A 78 1387 1346 1344 -13 47 7 O ATOM 636 CB ASP A 78 5.650 29.039 -8.495 1.00 11.39 C ANISOU 636 CB ASP A 78 1490 1446 1392 11 16 8 C ATOM 637 CG ASP A 78 4.232 28.807 -9.017 1.00 13.02 C ANISOU 637 CG ASP A 78 1668 1668 1608 20 -31 1 C ATOM 638 OD1 ASP A 78 3.465 28.044 -8.394 1.00 14.79 O ANISOU 638 OD1 ASP A 78 1777 2022 1819 -68 -49 13 O ATOM 639 OD2 ASP A 78 3.886 29.385 -10.069 1.00 15.57 O1- ANISOU 639 OD2 ASP A 78 2049 2049 1817 89 -92 61 O1- ATOM 640 N ASN A 79 7.994 29.524 -6.377 1.00 10.55 N ANISOU 640 N ASN A 79 1365 1341 1301 14 20 18 N ATOM 641 CA ASN A 79 9.394 29.442 -5.962 1.00 10.82 C ANISOU 641 CA ASN A 79 1386 1382 1342 14 18 11 C ATOM 642 C ASN A 79 9.519 28.769 -4.594 1.00 10.19 C ANISOU 642 C ASN A 79 1283 1298 1288 21 16 18 C ATOM 643 O ASN A 79 10.365 27.898 -4.404 1.00 9.93 O ANISOU 643 O ASN A 79 1256 1258 1259 38 41 14 O ATOM 644 CB ASN A 79 10.027 30.839 -5.945 1.00 11.30 C ANISOU 644 CB ASN A 79 1468 1414 1408 5 28 16 C ATOM 645 CG ASN A 79 11.523 30.817 -5.639 1.00 13.46 C ANISOU 645 CG ASN A 79 1684 1714 1714 -2 11 8 C ATOM 646 ND2 ASN A 79 12.058 31.967 -5.241 1.00 15.92 N ANISOU 646 ND2 ASN A 79 2063 1908 2077 -41 -28 -31 N ATOM 647 OD1 ASN A 79 12.190 29.790 -5.774 1.00 17.59 O ANISOU 647 OD1 ASN A 79 2152 2133 2396 99 40 30 O ATOM 648 N TYR A 80 8.667 29.171 -3.654 1.00 9.46 N ANISOU 648 N TYR A 80 1198 1207 1190 30 11 28 N ATOM 649 CA TYR A 80 8.647 28.592 -2.307 1.00 9.15 C ANISOU 649 CA TYR A 80 1146 1176 1154 20 -4 10 C ATOM 650 C TYR A 80 8.447 27.077 -2.361 1.00 9.28 C ANISOU 650 C TYR A 80 1165 1193 1165 28 -10 17 C ATOM 651 O TYR A 80 9.162 26.322 -1.696 1.00 8.97 O ANISOU 651 O TYR A 80 1139 1112 1154 39 -54 15 O ATOM 652 CB TYR A 80 7.550 29.256 -1.458 1.00 9.22 C ANISOU 652 CB TYR A 80 1148 1181 1171 13 5 19 C ATOM 653 CG TYR A 80 7.335 28.607 -0.109 1.00 8.81 C ANISOU 653 CG TYR A 80 1100 1117 1129 26 -7 0 C ATOM 654 CD1 TYR A 80 8.210 28.839 0.946 1.00 8.74 C ANISOU 654 CD1 TYR A 80 1105 1132 1083 9 8 -18 C ATOM 655 CD2 TYR A 80 6.262 27.749 0.108 1.00 8.79 C ANISOU 655 CD2 TYR A 80 1092 1142 1104 -11 -21 10 C ATOM 656 CE1 TYR A 80 8.022 28.235 2.176 1.00 8.72 C ANISOU 656 CE1 TYR A 80 1073 1158 1082 19 21 -11 C ATOM 657 CE2 TYR A 80 6.064 27.144 1.338 1.00 8.75 C ANISOU 657 CE2 TYR A 80 1053 1176 1095 -23 -11 18 C ATOM 658 CZ TYR A 80 6.945 27.390 2.365 1.00 8.90 C ANISOU 658 CZ TYR A 80 1148 1142 1092 -28 14 -5 C ATOM 659 OH TYR A 80 6.731 26.779 3.574 1.00 10.57 O ANISOU 659 OH TYR A 80 1327 1477 1212 -62 57 44 O ATOM 660 N VAL A 81 7.488 26.639 -3.173 1.00 9.13 N ANISOU 660 N VAL A 81 1123 1185 1161 17 0 5 N ATOM 661 CA VAL A 81 7.172 25.215 -3.309 1.00 9.50 C ANISOU 661 CA VAL A 81 1184 1224 1200 25 23 5 C ATOM 662 C VAL A 81 8.354 24.411 -3.872 1.00 9.82 C ANISOU 662 C VAL A 81 1218 1259 1251 31 43 15 C ATOM 663 O VAL A 81 8.625 23.302 -3.416 1.00 9.71 O ANISOU 663 O VAL A 81 1211 1220 1257 45 95 0 O ATOM 664 CB VAL A 81 5.899 24.997 -4.161 1.00 9.49 C ANISOU 664 CB VAL A 81 1167 1234 1204 19 19 23 C ATOM 665 CG1 VAL A 81 5.705 23.517 -4.486 1.00 9.77 C ANISOU 665 CG1 VAL A 81 1224 1272 1214 26 31 -21 C ATOM 666 CG2 VAL A 81 4.678 25.537 -3.417 1.00 10.03 C ANISOU 666 CG2 VAL A 81 1266 1308 1236 41 50 22 C ATOM 667 N LYS A 82 9.081 24.975 -4.833 1.00 10.25 N ANISOU 667 N LYS A 82 1278 1301 1314 28 36 31 N ATOM 668 CA LYS A 82 10.293 24.313 -5.323 1.00 10.77 C ANISOU 668 CA LYS A 82 1333 1374 1385 22 38 8 C ATOM 669 C LYS A 82 11.301 24.103 -4.192 1.00 11.09 C ANISOU 669 C LYS A 82 1385 1409 1418 32 39 32 C ATOM 670 O LYS A 82 11.936 23.046 -4.100 1.00 11.53 O ANISOU 670 O LYS A 82 1431 1419 1527 73 53 53 O ATOM 671 CB LYS A 82 10.960 25.126 -6.436 1.00 10.90 C ANISOU 671 CB LYS A 82 1359 1390 1390 34 50 11 C ATOM 672 CG LYS A 82 10.248 25.090 -7.771 1.00 11.88 C ANISOU 672 CG LYS A 82 1496 1501 1516 18 5 5 C ATOM 673 CD LYS A 82 11.039 25.884 -8.801 1.00 13.50 C ANISOU 673 CD LYS A 82 1719 1722 1688 -11 47 28 C ATOM 674 CE LYS A 82 10.261 26.094 -10.079 1.00 14.72 C ANISOU 674 CE LYS A 82 1867 1889 1836 -7 -1 28 C ATOM 675 NZ LYS A 82 10.994 27.009 -11.000 1.00 15.23 N1+ ANISOU 675 NZ LYS A 82 1918 1974 1893 -25 62 83 N1+ ATOM 676 N MET A 83 11.434 25.104 -3.327 1.00 11.23 N ANISOU 676 N MET A 83 1397 1427 1440 35 23 30 N ATOM 677 CA AMET A 83 12.448 25.045 -2.285 0.50 11.42 C ANISOU 677 CA AMET A 83 1422 1463 1452 21 15 21 C ATOM 678 CA BMET A 83 12.419 25.100 -2.238 0.50 11.31 C ANISOU 678 CA BMET A 83 1405 1448 1444 21 20 21 C ATOM 679 C MET A 83 12.094 24.080 -1.150 1.00 11.22 C ANISOU 679 C MET A 83 1391 1444 1428 30 18 25 C ATOM 680 O MET A 83 12.988 23.450 -0.585 1.00 12.01 O ANISOU 680 O MET A 83 1448 1576 1538 77 35 81 O ATOM 681 CB AMET A 83 12.772 26.449 -1.775 0.50 11.70 C ANISOU 681 CB AMET A 83 1467 1494 1482 17 -2 7 C ATOM 682 CB BMET A 83 12.506 26.484 -1.583 0.50 11.50 C ANISOU 682 CB BMET A 83 1432 1469 1468 17 5 13 C ATOM 683 CG AMET A 83 13.664 27.199 -2.750 0.50 12.55 C ANISOU 683 CG AMET A 83 1559 1628 1581 2 -4 21 C ATOM 684 CG BMET A 83 13.027 27.594 -2.474 0.50 11.96 C ANISOU 684 CG BMET A 83 1467 1538 1537 -2 22 26 C ATOM 685 SD AMET A 83 13.918 28.934 -2.367 0.50 13.86 S ANISOU 685 SD AMET A 83 1641 1779 1844 -55 -86 -42 S ATOM 686 SD BMET A 83 12.847 29.212 -1.691 0.50 13.20 S ANISOU 686 SD BMET A 83 1586 1708 1719 -31 105 -23 S ATOM 687 CE AMET A 83 13.872 28.912 -0.582 0.50 14.80 C ANISOU 687 CE AMET A 83 1863 1891 1868 -23 -4 -13 C ATOM 688 CE BMET A 83 13.942 29.042 -0.302 0.50 14.14 C ANISOU 688 CE BMET A 83 1765 1802 1802 -16 25 -15 C ATOM 689 N ILE A 84 10.811 23.927 -0.836 1.00 10.56 N ANISOU 689 N ILE A 84 1334 1340 1336 39 17 15 N ATOM 690 CA ILE A 84 10.415 23.014 0.246 1.00 10.03 C ANISOU 690 CA ILE A 84 1273 1279 1256 18 31 0 C ATOM 691 C ILE A 84 10.343 21.538 -0.161 1.00 9.74 C ANISOU 691 C ILE A 84 1249 1252 1198 25 38 -2 C ATOM 692 O ILE A 84 9.984 20.692 0.656 1.00 9.31 O ANISOU 692 O ILE A 84 1153 1196 1186 -4 22 -7 O ATOM 693 CB ILE A 84 9.091 23.446 0.933 1.00 9.83 C ANISOU 693 CB ILE A 84 1250 1250 1236 2 47 -1 C ATOM 694 CG1 ILE A 84 7.913 23.450 -0.045 1.00 10.34 C ANISOU 694 CG1 ILE A 84 1298 1340 1288 23 60 2 C ATOM 695 CG2 ILE A 84 9.268 24.819 1.578 1.00 10.54 C ANISOU 695 CG2 ILE A 84 1401 1283 1318 10 70 -16 C ATOM 696 CD1 ILE A 84 6.554 23.558 0.646 1.00 10.42 C ANISOU 696 CD1 ILE A 84 1253 1394 1310 2 56 15 C ATOM 697 N GLN A 85 10.718 21.214 -1.399 1.00 9.55 N ANISOU 697 N GLN A 85 1224 1243 1161 32 40 11 N ATOM 698 CA GLN A 85 10.750 19.815 -1.835 1.00 9.54 C ANISOU 698 CA GLN A 85 1208 1252 1163 20 28 11 C ATOM 699 C GLN A 85 11.713 18.954 -1.016 1.00 9.56 C ANISOU 699 C GLN A 85 1194 1285 1152 22 39 9 C ATOM 700 O GLN A 85 11.529 17.741 -0.938 1.00 9.59 O ANISOU 700 O GLN A 85 1164 1296 1183 62 62 -2 O ATOM 701 CB GLN A 85 11.130 19.702 -3.317 1.00 9.37 C ANISOU 701 CB GLN A 85 1174 1246 1140 27 26 -11 C ATOM 702 CG GLN A 85 10.142 20.344 -4.282 1.00 9.75 C ANISOU 702 CG GLN A 85 1225 1272 1206 50 5 5 C ATOM 703 CD GLN A 85 8.758 19.726 -4.203 1.00 10.16 C ANISOU 703 CD GLN A 85 1271 1287 1300 11 -10 18 C ATOM 704 NE2 GLN A 85 7.758 20.551 -3.902 1.00 9.90 N ANISOU 704 NE2 GLN A 85 1280 1258 1223 36 -52 19 N ATOM 705 OE1 GLN A 85 8.589 18.524 -4.402 1.00 11.38 O ANISOU 705 OE1 GLN A 85 1409 1408 1503 44 0 -71 O ATOM 706 N ASP A 86 12.736 19.567 -0.421 1.00 10.04 N ANISOU 706 N ASP A 86 1264 1344 1207 14 45 23 N ATOM 707 CA ASP A 86 13.707 18.806 0.368 1.00 10.66 C ANISOU 707 CA ASP A 86 1317 1434 1298 2 15 16 C ATOM 708 C ASP A 86 13.473 18.869 1.887 1.00 10.56 C ANISOU 708 C ASP A 86 1295 1448 1267 21 17 26 C ATOM 709 O ASP A 86 14.308 18.401 2.659 1.00 10.96 O ANISOU 709 O ASP A 86 1308 1598 1256 57 15 56 O ATOM 710 CB ASP A 86 15.139 19.205 0.000 1.00 11.30 C ANISOU 710 CB ASP A 86 1381 1528 1383 4 30 40 C ATOM 711 CG ASP A 86 15.582 20.483 0.654 1.00 13.59 C ANISOU 711 CG ASP A 86 1719 1744 1699 -23 14 -2 C ATOM 712 OD1 ASP A 86 16.782 20.557 0.997 1.00 16.85 O ANISOU 712 OD1 ASP A 86 1886 2271 2243 -23 -32 32 O ATOM 713 OD2 ASP A 86 14.749 21.400 0.836 1.00 16.53 O1- ANISOU 713 OD2 ASP A 86 2001 2065 2211 55 -27 16 O1- ATOM 714 N VAL A 87 12.339 19.424 2.311 1.00 10.01 N ANISOU 714 N VAL A 87 1240 1376 1186 2 2 17 N ATOM 715 CA VAL A 87 11.916 19.299 3.705 1.00 9.67 C ANISOU 715 CA VAL A 87 1195 1318 1162 8 5 4 C ATOM 716 C VAL A 87 11.783 17.807 4.030 1.00 9.48 C ANISOU 716 C VAL A 87 1156 1298 1146 0 11 -4 C ATOM 717 O VAL A 87 11.337 17.025 3.191 1.00 9.55 O ANISOU 717 O VAL A 87 1198 1320 1109 -11 22 -22 O ATOM 718 CB VAL A 87 10.586 20.040 3.968 1.00 9.66 C ANISOU 718 CB VAL A 87 1195 1311 1163 2 15 5 C ATOM 719 CG1 VAL A 87 10.029 19.685 5.341 1.00 9.53 C ANISOU 719 CG1 VAL A 87 1188 1307 1124 26 9 34 C ATOM 720 CG2 VAL A 87 10.789 21.538 3.845 1.00 9.76 C ANISOU 720 CG2 VAL A 87 1205 1322 1179 0 5 10 C ATOM 721 N GLY A 88 12.194 17.414 5.233 1.00 0.00 N ATOM 722 CA GLY A 88 12.269 16.007 5.616 1.00 0.00 C ATOM 723 C GLY A 88 11.886 15.819 7.064 1.00 0.00 C ATOM 724 O GLY A 88 11.700 16.802 7.782 1.00 0.00 O ATOM 725 N GLY A 89 11.785 14.572 7.552 1.00 0.00 N ATOM 726 CA GLY A 89 11.463 14.310 8.952 1.00 0.00 C ATOM 727 C GLY A 89 12.508 14.901 9.867 1.00 0.00 C ATOM 728 O GLY A 89 12.186 15.174 11.058 1.00 0.00 O ATOM 729 N GLY A 90 13.741 15.152 9.442 1.00 0.00 N ATOM 730 CA GLY A 90 14.780 15.752 10.273 1.00 0.00 C ATOM 731 C GLY A 90 14.440 17.182 10.616 1.00 0.00 C ATOM 732 O GLY A 90 15.068 17.770 11.529 1.00 0.00 O ATOM 733 N GLY A 91 13.473 17.805 9.936 1.00 0.00 N ATOM 734 CA GLY A 91 13.113 19.202 10.159 1.00 0.00 C ATOM 735 C GLY A 91 12.012 19.320 11.185 1.00 0.00 C ATOM 736 O GLY A 91 11.650 20.459 11.559 1.00 0.00 O ATOM 737 N VAL A 92 11.458 18.232 11.686 1.00 6.98 N ANISOU 737 N VAL A 92 850 932 869 -11 16 -41 N ATOM 738 CA VAL A 92 10.489 18.290 12.775 1.00 6.50 C ANISOU 738 CA VAL A 92 772 882 814 11 9 -44 C ATOM 739 C VAL A 92 11.176 18.826 14.037 1.00 6.24 C ANISOU 739 C VAL A 92 737 824 809 31 -2 -46 C ATOM 740 O VAL A 92 12.260 18.374 14.412 1.00 6.51 O ANISOU 740 O VAL A 92 704 906 861 -42 8 -57 O ATOM 741 CB VAL A 92 9.834 16.915 13.038 1.00 6.42 C ANISOU 741 CB VAL A 92 759 879 799 22 13 -56 C ATOM 742 CG1 VAL A 92 8.854 16.992 14.211 1.00 6.56 C ANISOU 742 CG1 VAL A 92 762 947 782 7 66 -55 C ATOM 743 CG2 VAL A 92 9.121 16.429 11.792 1.00 7.20 C ANISOU 743 CG2 VAL A 92 869 1035 829 7 -47 -34 C ATOM 744 N TYR A 93 10.538 19.804 14.677 1.00 5.77 N ANISOU 744 N TYR A 93 654 780 755 16 -8 -54 N ATOM 745 CA TYR A 93 11.109 20.473 15.841 1.00 5.71 C ANISOU 745 CA TYR A 93 675 746 743 15 4 -28 C ATOM 746 C TYR A 93 11.281 19.517 17.026 1.00 5.87 C ANISOU 746 C TYR A 93 690 787 751 19 -4 -36 C ATOM 747 O TYR A 93 10.584 18.506 17.124 1.00 5.41 O ANISOU 747 O TYR A 93 646 733 677 80 -25 16 O ATOM 748 CB TYR A 93 10.232 21.676 16.239 1.00 5.95 C ANISOU 748 CB TYR A 93 704 775 782 14 16 -39 C ATOM 749 CG TYR A 93 10.667 23.022 15.684 1.00 6.48 C ANISOU 749 CG TYR A 93 801 854 804 -21 -22 -41 C ATOM 750 CD1 TYR A 93 11.555 23.128 14.608 1.00 7.17 C ANISOU 750 CD1 TYR A 93 932 896 893 -44 23 -7 C ATOM 751 CD2 TYR A 93 10.171 24.198 16.233 1.00 6.86 C ANISOU 751 CD2 TYR A 93 874 897 830 2 11 -52 C ATOM 752 CE1 TYR A 93 11.945 24.362 14.124 1.00 7.87 C ANISOU 752 CE1 TYR A 93 1028 960 1001 -28 47 28 C ATOM 753 CE2 TYR A 93 10.551 25.434 15.752 1.00 8.07 C ANISOU 753 CE2 TYR A 93 1062 998 1006 5 -31 11 C ATOM 754 CZ TYR A 93 11.436 25.511 14.697 1.00 8.36 C ANISOU 754 CZ TYR A 93 1109 975 1091 -66 42 0 C ATOM 755 OH TYR A 93 11.822 26.740 14.220 1.00 10.60 O ANISOU 755 OH TYR A 93 1532 1218 1275 -171 50 148 O ATOM 756 N PRO A 94 12.223 19.839 17.929 1.00 6.18 N ANISOU 756 N PRO A 94 756 840 748 5 -4 -21 N ATOM 757 CA PRO A 94 12.490 18.989 19.085 1.00 6.59 C ANISOU 757 CA PRO A 94 819 851 832 7 -16 -14 C ATOM 758 C PRO A 94 11.232 18.716 19.910 1.00 6.49 C ANISOU 758 C PRO A 94 815 827 823 16 -5 -1 C ATOM 759 O PRO A 94 10.460 19.639 20.188 1.00 6.62 O ANISOU 759 O PRO A 94 930 730 856 30 8 11 O ATOM 760 CB PRO A 94 13.492 19.808 19.908 1.00 6.82 C ANISOU 760 CB PRO A 94 833 922 835 -2 -25 -36 C ATOM 761 CG PRO A 94 14.035 20.811 18.994 1.00 7.37 C ANISOU 761 CG PRO A 94 955 959 884 -9 -28 -16 C ATOM 762 CD PRO A 94 13.040 21.065 17.933 1.00 6.68 C ANISOU 762 CD PRO A 94 830 879 825 5 19 -5 C ATOM 763 N GLY A 95 11.024 17.453 20.276 1.00 6.78 N ANISOU 763 N GLY A 95 873 824 876 15 -42 -17 N ATOM 764 CA GLY A 95 9.904 17.042 21.118 1.00 6.77 C ANISOU 764 CA GLY A 95 887 823 861 10 -39 5 C ATOM 765 C GLY A 95 8.575 16.811 20.408 1.00 6.53 C ANISOU 765 C GLY A 95 848 795 837 -4 -11 2 C ATOM 766 O GLY A 95 7.683 16.167 20.958 1.00 7.19 O ANISOU 766 O GLY A 95 993 819 920 -37 -11 34 O ATOM 767 N ILE A 96 8.430 17.327 19.190 1.00 6.33 N ANISOU 767 N ILE A 96 803 763 838 14 -21 -11 N ATOM 768 CA ILE A 96 7.127 17.351 18.529 1.00 6.20 C ANISOU 768 CA ILE A 96 784 760 811 2 -18 -15 C ATOM 769 C ILE A 96 6.671 15.955 18.088 1.00 6.51 C ANISOU 769 C ILE A 96 821 788 864 2 -9 -8 C ATOM 770 O ILE A 96 5.504 15.597 18.269 1.00 6.76 O ANISOU 770 O ILE A 96 849 803 914 -30 -52 -9 O ATOM 771 CB ILE A 96 7.134 18.336 17.337 1.00 6.13 C ANISOU 771 CB ILE A 96 792 738 798 -5 -7 -20 C ATOM 772 CG1 ILE A 96 7.262 19.779 17.847 1.00 5.93 C ANISOU 772 CG1 ILE A 96 724 724 806 -15 13 -27 C ATOM 773 CG2 ILE A 96 5.893 18.173 16.473 1.00 6.01 C ANISOU 773 CG2 ILE A 96 740 771 770 -26 -10 0 C ATOM 774 CD1 ILE A 96 6.098 20.262 18.701 1.00 6.90 C ANISOU 774 CD1 ILE A 96 775 921 924 44 26 -28 C ATOM 775 N LEU A 97 7.580 15.157 17.535 1.00 6.67 N ANISOU 775 N LEU A 97 815 817 901 15 -11 2 N ATOM 776 CA LEU A 97 7.209 13.813 17.107 1.00 6.78 C ANISOU 776 CA LEU A 97 856 830 889 15 -21 -14 C ATOM 777 C LEU A 97 6.729 12.965 18.285 1.00 6.78 C ANISOU 777 C LEU A 97 857 825 895 1 -15 -8 C ATOM 778 O LEU A 97 5.707 12.289 18.183 1.00 6.78 O ANISOU 778 O LEU A 97 866 814 893 -5 -9 -25 O ATOM 779 CB LEU A 97 8.365 13.113 16.389 1.00 6.85 C ANISOU 779 CB LEU A 97 863 828 912 15 -2 -20 C ATOM 780 CG LEU A 97 8.076 11.681 15.904 1.00 7.31 C ANISOU 780 CG LEU A 97 977 847 953 23 2 -45 C ATOM 781 CD1 LEU A 97 6.888 11.645 14.952 1.00 8.39 C ANISOU 781 CD1 LEU A 97 1049 1100 1038 47 22 -27 C ATOM 782 CD2 LEU A 97 9.302 11.091 15.232 1.00 8.20 C ANISOU 782 CD2 LEU A 97 1001 990 1125 102 47 -8 C ATOM 783 N GLN A 98 7.443 13.003 19.408 1.00 7.04 N ANISOU 783 N GLN A 98 900 872 903 -11 -10 10 N ATOM 784 CA GLN A 98 7.016 12.213 20.563 1.00 7.57 C ANISOU 784 CA GLN A 98 959 947 969 -19 -10 10 C ATOM 785 C GLN A 98 5.702 12.725 21.137 1.00 7.18 C ANISOU 785 C GLN A 98 941 893 893 -15 -1 4 C ATOM 786 O GLN A 98 4.869 11.932 21.575 1.00 7.46 O ANISOU 786 O GLN A 98 924 909 999 -51 38 -5 O ATOM 787 CB GLN A 98 8.086 12.167 21.652 1.00 8.06 C ANISOU 787 CB GLN A 98 1019 1017 1023 10 -23 11 C ATOM 788 CG GLN A 98 7.789 11.131 22.732 1.00 9.33 C ANISOU 788 CG GLN A 98 1198 1224 1120 26 4 71 C ATOM 789 CD GLN A 98 7.727 9.722 22.173 1.00 10.49 C ANISOU 789 CD GLN A 98 1375 1335 1275 36 -8 79 C ATOM 790 NE2 GLN A 98 6.615 9.025 22.409 1.00 11.50 N ANISOU 790 NE2 GLN A 98 1465 1439 1465 61 -37 45 N ATOM 791 OE1 GLN A 98 8.679 9.262 21.538 1.00 12.92 O ANISOU 791 OE1 GLN A 98 1679 1670 1558 157 70 2 O ATOM 792 N LEU A 99 5.499 14.041 21.118 1.00 6.79 N ANISOU 792 N LEU A 99 853 856 869 -19 -2 0 N ATOM 793 CA LEU A 99 4.229 14.607 21.564 1.00 6.63 C ANISOU 793 CA LEU A 99 864 819 833 -2 14 -4 C ATOM 794 C LEU A 99 3.082 14.074 20.716 1.00 6.66 C ANISOU 794 C LEU A 99 851 824 854 -2 32 5 C ATOM 795 O LEU A 99 2.069 13.632 21.251 1.00 6.87 O ANISOU 795 O LEU A 99 846 805 958 -23 72 4 O ATOM 796 CB LEU A 99 4.254 16.136 21.502 1.00 6.69 C ANISOU 796 CB LEU A 99 876 819 846 -21 -8 2 C ATOM 797 CG LEU A 99 2.925 16.819 21.836 1.00 6.57 C ANISOU 797 CG LEU A 99 898 847 750 5 -25 -14 C ATOM 798 CD1 LEU A 99 2.471 16.482 23.253 1.00 7.72 C ANISOU 798 CD1 LEU A 99 1066 1034 833 42 68 -8 C ATOM 799 CD2 LEU A 99 3.043 18.319 21.652 1.00 7.25 C ANISOU 799 CD2 LEU A 99 1087 839 826 -23 -37 19 C ATOM 800 N LEU A 100 3.247 14.111 19.396 1.00 6.51 N ANISOU 800 N LEU A 100 838 795 839 -5 40 23 N ATOM 801 CA LEU A 100 2.231 13.592 18.481 1.00 6.50 C ANISOU 801 CA LEU A 100 839 783 845 -11 36 14 C ATOM 802 C LEU A 100 1.934 12.114 18.740 1.00 6.75 C ANISOU 802 C LEU A 100 863 805 897 -4 23 20 C ATOM 803 O LEU A 100 0.773 11.706 18.764 1.00 6.87 O ANISOU 803 O LEU A 100 879 808 922 -20 83 34 O ATOM 804 CB LEU A 100 2.661 13.801 17.025 1.00 6.32 C ANISOU 804 CB LEU A 100 806 796 799 5 9 17 C ATOM 805 CG LEU A 100 2.663 15.256 16.539 1.00 5.86 C ANISOU 805 CG LEU A 100 711 777 734 7 37 17 C ATOM 806 CD1 LEU A 100 3.392 15.378 15.201 1.00 5.84 C ANISOU 806 CD1 LEU A 100 712 784 723 -57 60 47 C ATOM 807 CD2 LEU A 100 1.245 15.823 16.434 1.00 5.88 C ANISOU 807 CD2 LEU A 100 709 784 738 13 62 46 C ATOM 808 N LYS A 101 2.984 11.325 18.946 1.00 7.09 N ANISOU 808 N LYS A 101 922 837 935 -9 28 17 N ATOM 809 CA LYS A 101 2.823 9.908 19.256 1.00 7.45 C ANISOU 809 CA LYS A 101 966 875 989 -19 7 9 C ATOM 810 C LYS A 101 2.035 9.709 20.549 1.00 7.75 C ANISOU 810 C LYS A 101 1008 914 1022 -13 13 4 C ATOM 811 O LYS A 101 1.139 8.864 20.608 1.00 7.85 O ANISOU 811 O LYS A 101 1036 846 1098 -52 63 34 O ATOM 812 CB LYS A 101 4.184 9.226 19.378 1.00 7.59 C ANISOU 812 CB LYS A 101 990 881 1011 -1 7 11 C ATOM 813 CG LYS A 101 4.872 8.959 18.061 1.00 8.20 C ANISOU 813 CG LYS A 101 1067 985 1061 1 -1 -13 C ATOM 814 CD LYS A 101 6.252 8.372 18.284 1.00 9.15 C ANISOU 814 CD LYS A 101 1161 1134 1181 9 -30 -7 C ATOM 815 CE LYS A 101 6.948 8.054 16.978 1.00 10.44 C ANISOU 815 CE LYS A 101 1306 1329 1329 11 27 -16 C ATOM 816 NZ LYS A 101 8.361 7.655 17.213 1.00 11.52 N1+ ANISOU 816 NZ LYS A 101 1400 1492 1482 73 11 -65 N1+ ATOM 817 N ASP A 102 2.374 10.481 21.580 1.00 7.90 N ANISOU 817 N ASP A 102 1037 918 1044 -14 20 4 N ATOM 818 CA ASP A 102 1.722 10.357 22.884 1.00 8.32 C ANISOU 818 CA ASP A 102 1074 993 1090 -5 23 22 C ATOM 819 C ASP A 102 0.264 10.818 22.854 1.00 8.24 C ANISOU 819 C ASP A 102 1067 980 1084 -5 37 28 C ATOM 820 O ASP A 102 -0.600 10.187 23.464 1.00 8.48 O ANISOU 820 O ASP A 102 1050 1012 1159 -15 80 63 O ATOM 821 CB ASP A 102 2.518 11.111 23.954 1.00 8.58 C ANISOU 821 CB ASP A 102 1112 1053 1094 -16 30 8 C ATOM 822 CG ASP A 102 3.851 10.439 24.286 1.00 9.64 C ANISOU 822 CG ASP A 102 1235 1205 1221 2 0 13 C ATOM 823 OD1 ASP A 102 4.112 9.317 23.806 1.00 11.12 O ANISOU 823 OD1 ASP A 102 1498 1321 1403 22 7 19 O ATOM 824 OD2 ASP A 102 4.648 11.040 25.035 1.00 11.65 O1- ANISOU 824 OD2 ASP A 102 1386 1531 1508 -61 -77 -47 O1- ATOM 825 N LEU A 103 -0.020 11.905 22.142 1.00 7.98 N ANISOU 825 N LEU A 103 1015 958 1059 -11 35 33 N ATOM 826 CA LEU A 103 -1.403 12.343 21.952 1.00 7.81 C ANISOU 826 CA LEU A 103 1007 932 1027 8 18 32 C ATOM 827 C LEU A 103 -2.227 11.256 21.255 1.00 7.91 C ANISOU 827 C LEU A 103 998 939 1067 14 27 17 C ATOM 828 O LEU A 103 -3.328 10.918 21.697 1.00 8.09 O ANISOU 828 O LEU A 103 1052 856 1165 11 57 18 O ATOM 829 CB LEU A 103 -1.453 13.650 21.151 1.00 7.55 C ANISOU 829 CB LEU A 103 966 898 1003 5 15 30 C ATOM 830 CG LEU A 103 -0.938 14.887 21.893 1.00 7.04 C ANISOU 830 CG LEU A 103 893 924 856 -5 9 25 C ATOM 831 CD1 LEU A 103 -0.747 16.052 20.941 1.00 7.03 C ANISOU 831 CD1 LEU A 103 950 859 859 35 91 13 C ATOM 832 CD2 LEU A 103 -1.869 15.279 23.032 1.00 7.80 C ANISOU 832 CD2 LEU A 103 1088 1014 859 17 73 2 C ATOM 833 N ARG A 104 -1.679 10.696 20.180 1.00 8.13 N ANISOU 833 N ARG A 104 1022 981 1084 1 26 1 N ATOM 834 CA ARG A 104 -2.375 9.663 19.418 1.00 8.58 C ANISOU 834 CA ARG A 104 1095 1041 1121 -8 21 -5 C ATOM 835 C ARG A 104 -2.638 8.433 20.279 1.00 8.95 C ANISOU 835 C ARG A 104 1144 1090 1166 -17 35 -5 C ATOM 836 O ARG A 104 -3.749 7.901 20.283 1.00 9.09 O ANISOU 836 O ARG A 104 1163 1090 1201 -50 46 -33 O ATOM 837 CB ARG A 104 -1.576 9.275 18.171 1.00 8.54 C ANISOU 837 CB ARG A 104 1087 1043 1115 4 21 -15 C ATOM 838 CG ARG A 104 -2.253 8.232 17.296 1.00 9.07 C ANISOU 838 CG ARG A 104 1175 1074 1196 -15 5 14 C ATOM 839 CD ARG A 104 -1.527 8.069 15.975 1.00 9.75 C ANISOU 839 CD ARG A 104 1270 1212 1223 -22 8 2 C ATOM 840 NE ARG A 104 -2.108 6.997 15.171 1.00 10.69 N ANISOU 840 NE ARG A 104 1451 1265 1343 -52 19 -18 N ATOM 841 CZ ARG A 104 -3.236 7.094 14.470 1.00 11.31 C ANISOU 841 CZ ARG A 104 1475 1395 1427 -15 5 2 C ATOM 842 NH1 ARG A 104 -3.947 8.224 14.459 1.00 11.25 N1+ ANISOU 842 NH1 ARG A 104 1460 1414 1399 -1 -7 1 N1+ ATOM 843 NH2 ARG A 104 -3.666 6.045 13.775 1.00 11.91 N ANISOU 843 NH2 ARG A 104 1565 1454 1505 -18 5 -42 N ATOM 844 N SER A 105 -1.622 8.002 21.021 1.00 9.41 N ANISOU 844 N SER A 105 1225 1133 1215 -11 33 21 N ATOM 845 CA SER A 105 -1.744 6.818 21.876 1.00 9.93 C ANISOU 845 CA SER A 105 1301 1185 1286 -8 56 20 C ATOM 846 C SER A 105 -2.842 6.986 22.920 1.00 10.19 C ANISOU 846 C SER A 105 1324 1237 1308 -10 49 10 C ATOM 847 O SER A 105 -3.508 6.019 23.276 1.00 10.68 O ANISOU 847 O SER A 105 1378 1255 1424 -26 92 -2 O ATOM 848 CB SER A 105 -0.419 6.509 22.570 1.00 10.14 C ANISOU 848 CB SER A 105 1335 1218 1297 0 44 27 C ATOM 849 OG SER A 105 0.591 6.175 21.633 1.00 11.39 O ANISOU 849 OG SER A 105 1499 1345 1481 77 111 23 O ATOM 850 N ASN A 106 -3.023 8.215 23.396 1.00 10.11 N ANISOU 850 N ASN A 106 1303 1224 1313 -16 46 2 N ATOM 851 CA ASN A 106 -4.045 8.530 24.398 1.00 10.39 C ANISOU 851 CA ASN A 106 1328 1278 1342 -13 36 2 C ATOM 852 C ASN A 106 -5.380 8.992 23.797 1.00 10.16 C ANISOU 852 C ASN A 106 1298 1231 1329 -19 38 -1 C ATOM 853 O ASN A 106 -6.257 9.473 24.520 1.00 10.34 O ANISOU 853 O ASN A 106 1314 1255 1359 -20 80 10 O ATOM 854 CB ASN A 106 -3.498 9.579 25.368 1.00 10.74 C ANISOU 854 CB ASN A 106 1381 1326 1372 -14 57 -17 C ATOM 855 CG ASN A 106 -2.437 9.014 26.294 1.00 11.90 C ANISOU 855 CG ASN A 106 1515 1495 1508 -26 14 7 C ATOM 856 ND2 ASN A 106 -2.875 8.439 27.405 1.00 13.80 N ANISOU 856 ND2 ASN A 106 1845 1818 1580 -7 43 103 N ATOM 857 OD1 ASN A 106 -1.241 9.074 26.007 1.00 13.51 O ANISOU 857 OD1 ASN A 106 1661 1715 1755 -23 41 14 O ATOM 858 N LYS A 107 -5.528 8.829 22.482 1.00 10.00 N ANISOU 858 N LYS A 107 1259 1209 1332 -20 34 2 N ATOM 859 CA LYS A 107 -6.758 9.151 21.750 1.00 9.95 C ANISOU 859 CA LYS A 107 1248 1210 1322 -16 23 -1 C ATOM 860 C LYS A 107 -7.188 10.616 21.888 1.00 9.33 C ANISOU 860 C LYS A 107 1145 1143 1254 -11 15 -7 C ATOM 861 O LYS A 107 -8.380 10.936 21.926 1.00 9.88 O ANISOU 861 O LYS A 107 1191 1164 1396 -23 18 -23 O ATOM 862 CB LYS A 107 -7.885 8.183 22.128 1.00 10.31 C ANISOU 862 CB LYS A 107 1290 1256 1370 -18 15 -1 C ATOM 863 CG LYS A 107 -7.539 6.731 21.815 1.00 11.19 C ANISOU 863 CG LYS A 107 1411 1348 1491 23 13 0 C ATOM 864 CD LYS A 107 -8.740 5.806 21.941 1.00 12.54 C ANISOU 864 CD LYS A 107 1588 1510 1666 -33 -2 -17 C ATOM 865 CE LYS A 107 -9.141 5.608 23.388 1.00 13.47 C ANISOU 865 CE LYS A 107 1701 1632 1784 -33 36 9 C ATOM 866 NZ LYS A 107 -10.266 4.639 23.513 1.00 14.99 N1+ ANISOU 866 NZ LYS A 107 1821 1775 2097 -107 75 -8 N1+ ATOM 867 N ILE A 108 -6.192 11.496 21.953 1.00 8.45 N ANISOU 867 N ILE A 108 1051 1035 1125 0 21 -8 N ATOM 868 CA AILE A 108 -6.418 12.937 21.930 0.50 8.27 C ANISOU 868 CA AILE A 108 1038 1021 1083 -7 10 -2 C ATOM 869 CA BILE A 108 -6.424 12.934 21.932 0.50 8.12 C ANISOU 869 CA BILE A 108 1014 1004 1066 -8 10 -2 C ATOM 870 C ILE A 108 -6.314 13.401 20.481 1.00 7.98 C ANISOU 870 C ILE A 108 990 980 1062 -10 23 -5 C ATOM 871 O ILE A 108 -5.360 13.053 19.781 1.00 7.98 O ANISOU 871 O ILE A 108 965 977 1089 -7 65 -19 O ATOM 872 CB AILE A 108 -5.389 13.687 22.798 0.50 8.25 C ANISOU 872 CB AILE A 108 1052 1015 1067 -7 8 -1 C ATOM 873 CB BILE A 108 -5.418 13.679 22.834 0.50 7.96 C ANISOU 873 CB BILE A 108 1014 980 1027 -10 10 2 C ATOM 874 CG1AILE A 108 -5.454 13.190 24.244 0.50 8.86 C ANISOU 874 CG1AILE A 108 1149 1099 1117 -8 -20 8 C ATOM 875 CG1BILE A 108 -5.636 13.286 24.300 0.50 7.93 C ANISOU 875 CG1BILE A 108 984 1003 1024 -13 -11 5 C ATOM 876 CG2AILE A 108 -5.636 15.193 22.745 0.50 8.12 C ANISOU 876 CG2AILE A 108 1056 999 1030 2 -7 -17 C ATOM 877 CG2BILE A 108 -5.561 15.190 22.672 0.50 7.81 C ANISOU 877 CG2BILE A 108 1007 961 995 1 -5 -15 C ATOM 878 CD1AILE A 108 -6.842 13.211 24.828 0.50 9.50 C ANISOU 878 CD1AILE A 108 1245 1227 1134 0 -5 11 C ATOM 879 CD1BILE A 108 -4.446 13.569 25.192 0.50 7.48 C ANISOU 879 CD1BILE A 108 993 950 896 -43 -23 38 C ATOM 880 N LYS A 109 -7.301 14.170 20.026 1.00 7.67 N ANISOU 880 N LYS A 109 929 978 1007 -21 5 -5 N ATOM 881 CA LYS A 109 -7.358 14.609 18.637 1.00 7.56 C ANISOU 881 CA LYS A 109 940 941 990 -20 27 -31 C ATOM 882 C LYS A 109 -6.236 15.595 18.335 1.00 7.04 C ANISOU 882 C LYS A 109 878 876 919 -16 31 -21 C ATOM 883 O LYS A 109 -5.807 16.354 19.209 1.00 6.70 O ANISOU 883 O LYS A 109 832 872 839 -4 76 -54 O ATOM 884 CB LYS A 109 -8.708 15.251 18.320 1.00 7.88 C ANISOU 884 CB LYS A 109 972 995 1023 -20 20 -11 C ATOM 885 CG LYS A 109 -9.911 14.315 18.441 1.00 9.49 C ANISOU 885 CG LYS A 109 1121 1225 1256 -44 42 -5 C ATOM 886 CD LYS A 109 -9.901 13.216 17.391 1.00 11.80 C ANISOU 886 CD LYS A 109 1484 1490 1506 -32 23 -44 C ATOM 887 CE LYS A 109 -11.246 12.506 17.332 1.00 13.73 C ANISOU 887 CE LYS A 109 1653 1785 1778 -51 -23 -23 C ATOM 888 NZ LYS A 109 -11.279 11.447 16.293 1.00 15.73 N1+ ANISOU 888 NZ LYS A 109 2014 1910 2053 -44 -9 -97 N1+ ATOM 889 N ILE A 110 -5.768 15.550 17.091 1.00 6.62 N ANISOU 889 N ILE A 110 843 809 861 -36 28 -18 N ATOM 890 CA ILE A 110 -4.661 16.362 16.603 1.00 6.40 C ANISOU 890 CA ILE A 110 822 777 830 -34 10 -27 C ATOM 891 C ILE A 110 -5.130 17.067 15.344 1.00 6.26 C ANISOU 891 C ILE A 110 796 763 816 -20 21 -22 C ATOM 892 O ILE A 110 -5.521 16.417 14.381 1.00 6.31 O ANISOU 892 O ILE A 110 830 748 817 -63 0 -47 O ATOM 893 CB ILE A 110 -3.439 15.478 16.273 1.00 6.35 C ANISOU 893 CB ILE A 110 817 760 835 -34 32 -13 C ATOM 894 CG1 ILE A 110 -2.921 14.791 17.545 1.00 6.71 C ANISOU 894 CG1 ILE A 110 858 786 905 -1 -1 -23 C ATOM 895 CG2 ILE A 110 -2.330 16.295 15.617 1.00 6.33 C ANISOU 895 CG2 ILE A 110 800 785 817 -61 50 -18 C ATOM 896 CD1 ILE A 110 -1.888 13.707 17.283 1.00 7.45 C ANISOU 896 CD1 ILE A 110 915 858 1056 31 -17 -52 C ATOM 897 N ALA A 111 -5.109 18.397 15.356 1.00 6.14 N ANISOU 897 N ALA A 111 796 758 775 -13 -11 -28 N ATOM 898 CA ALA A 111 -5.547 19.184 14.205 1.00 6.15 C ANISOU 898 CA ALA A 111 775 781 781 19 7 -23 C ATOM 899 C ALA A 111 -4.519 20.248 13.873 1.00 6.20 C ANISOU 899 C ALA A 111 790 790 775 13 -4 -16 C ATOM 900 O ALA A 111 -3.829 20.746 14.771 1.00 6.48 O ANISOU 900 O ALA A 111 884 805 774 -37 16 -70 O ATOM 901 CB ALA A 111 -6.900 19.831 14.494 1.00 6.43 C ANISOU 901 CB ALA A 111 772 837 832 31 23 -11 C ATOM 902 N LEU A 112 -4.400 20.579 12.587 1.00 5.90 N ANISOU 902 N LEU A 112 748 763 728 -5 -5 -21 N ATOM 903 CA LEU A 112 -3.528 21.673 12.154 1.00 5.98 C ANISOU 903 CA LEU A 112 748 771 753 -17 -17 -11 C ATOM 904 C LEU A 112 -4.337 22.962 11.996 1.00 6.13 C ANISOU 904 C LEU A 112 752 809 765 2 5 -28 C ATOM 905 O LEU A 112 -5.397 22.968 11.366 1.00 6.33 O ANISOU 905 O LEU A 112 782 811 812 -14 -39 -63 O ATOM 906 CB LEU A 112 -2.809 21.331 10.842 1.00 6.07 C ANISOU 906 CB LEU A 112 729 776 801 -11 -5 -1 C ATOM 907 CG LEU A 112 -1.599 22.227 10.528 1.00 6.14 C ANISOU 907 CG LEU A 112 717 781 835 1 5 7 C ATOM 908 CD1 LEU A 112 -0.425 21.880 11.438 1.00 7.28 C ANISOU 908 CD1 LEU A 112 862 1007 895 -23 -71 -77 C ATOM 909 CD2 LEU A 112 -1.195 22.130 9.060 1.00 6.83 C ANISOU 909 CD2 LEU A 112 759 920 914 8 11 -39 C ATOM 910 N ALA A 113 -3.826 24.046 12.578 1.00 6.32 N ANISOU 910 N ALA A 113 756 806 835 -17 0 -19 N ATOM 911 CA ALA A 113 -4.435 25.375 12.485 1.00 6.65 C ANISOU 911 CA ALA A 113 825 850 850 4 4 -25 C ATOM 912 C ALA A 113 -3.373 26.367 12.016 1.00 7.06 C ANISOU 912 C ALA A 113 876 898 909 -8 0 -36 C ATOM 913 O ALA A 113 -3.057 27.345 12.695 1.00 7.73 O ANISOU 913 O ALA A 113 977 963 995 -52 28 -104 O ATOM 914 CB ALA A 113 -5.018 25.795 13.832 1.00 6.96 C ANISOU 914 CB ALA A 113 861 898 882 -17 7 -47 C ATOM 915 N SER A 114 -2.823 26.095 10.838 1.00 7.40 N ANISOU 915 N SER A 114 948 945 918 -4 -1 -37 N ATOM 916 CA SER A 114 -1.773 26.913 10.239 1.00 7.60 C ANISOU 916 CA SER A 114 943 981 963 -2 -10 -5 C ATOM 917 C SER A 114 -2.344 27.856 9.192 1.00 7.92 C ANISOU 917 C SER A 114 992 1041 975 -4 -14 -1 C ATOM 918 O SER A 114 -3.311 27.521 8.517 1.00 8.06 O ANISOU 918 O SER A 114 960 1092 1007 52 -66 34 O ATOM 919 CB SER A 114 -0.735 26.005 9.573 1.00 7.67 C ANISOU 919 CB SER A 114 965 990 956 5 2 -11 C ATOM 920 OG SER A 114 0.202 26.746 8.806 1.00 7.94 O ANISOU 920 OG SER A 114 943 999 1073 26 0 33 O ATOM 921 N ALA A 115 -1.721 29.023 9.050 1.00 8.22 N ANISOU 921 N ALA A 115 1039 1076 1007 11 -19 11 N ATOM 922 CA ALA A 115 -2.040 29.961 7.975 1.00 8.54 C ANISOU 922 CA ALA A 115 1077 1113 1053 18 -5 26 C ATOM 923 C ALA A 115 -1.536 29.480 6.607 1.00 8.63 C ANISOU 923 C ALA A 115 1075 1141 1061 21 -14 26 C ATOM 924 O ALA A 115 -1.949 30.009 5.572 1.00 8.88 O ANISOU 924 O ALA A 115 1122 1189 1062 -15 -14 56 O ATOM 925 CB ALA A 115 -1.451 31.328 8.290 1.00 8.76 C ANISOU 925 CB ALA A 115 1115 1131 1081 28 8 0 C ATOM 926 N SER A 116 -0.631 28.499 6.605 1.00 8.78 N ANISOU 926 N SER A 116 1092 1164 1077 20 2 -5 N ATOM 927 CA SER A 116 -0.011 28.016 5.374 1.00 8.98 C ANISOU 927 CA SER A 116 1119 1202 1088 14 19 0 C ATOM 928 C SER A 116 -0.932 27.125 4.553 1.00 8.98 C ANISOU 928 C SER A 116 1114 1190 1108 4 19 13 C ATOM 929 O SER A 116 -1.402 26.091 5.027 1.00 9.09 O ANISOU 929 O SER A 116 1130 1193 1127 -5 23 46 O ATOM 930 CB SER A 116 1.269 27.240 5.685 1.00 9.08 C ANISOU 930 CB SER A 116 1114 1239 1097 16 19 -25 C ATOM 931 OG SER A 116 1.851 26.741 4.486 1.00 10.60 O ANISOU 931 OG SER A 116 1286 1539 1202 45 53 -104 O ATOM 932 N LYS A 117 -1.161 27.517 3.304 1.00 9.18 N ANISOU 932 N LYS A 117 1130 1226 1132 11 7 11 N ATOM 933 CA LYS A 117 -1.882 26.673 2.359 1.00 9.58 C ANISOU 933 CA LYS A 117 1199 1249 1190 2 2 -7 C ATOM 934 C LYS A 117 -1.007 25.504 1.878 1.00 9.19 C ANISOU 934 C LYS A 117 1162 1210 1119 -5 5 -14 C ATOM 935 O LYS A 117 -1.497 24.588 1.221 1.00 9.76 O ANISOU 935 O LYS A 117 1230 1312 1164 -23 -8 -47 O ATOM 936 CB LYS A 117 -2.380 27.510 1.175 1.00 10.02 C ANISOU 936 CB LYS A 117 1278 1302 1226 -7 -8 13 C ATOM 937 CG LYS A 117 -3.431 28.559 1.557 1.00 11.97 C ANISOU 937 CG LYS A 117 1500 1550 1497 28 -2 -11 C ATOM 938 CD LYS A 117 -3.854 29.411 0.361 1.00 14.51 C ANISOU 938 CD LYS A 117 1867 1854 1791 46 -45 52 C ATOM 939 CE LYS A 117 -2.998 30.663 0.216 1.00 16.55 C ANISOU 939 CE LYS A 117 2113 2082 2093 -11 -11 25 C ATOM 940 NZ LYS A 117 -3.444 31.758 1.127 1.00 18.19 N1+ ANISOU 940 NZ LYS A 117 2336 2245 2329 36 -11 -22 N1+ ATOM 941 N ASN A 118 0.280 25.537 2.221 1.00 8.53 N ANISOU 941 N ASN A 118 1083 1118 1039 5 27 -25 N ATOM 942 CA ASN A 118 1.203 24.437 1.936 1.00 8.08 C ANISOU 942 CA ASN A 118 1031 1043 995 5 18 -5 C ATOM 943 C ASN A 118 1.336 23.442 3.097 1.00 7.52 C ANISOU 943 C ASN A 118 939 995 921 0 37 -5 C ATOM 944 O ASN A 118 2.194 22.561 3.074 1.00 7.19 O ANISOU 944 O ASN A 118 935 946 851 -11 63 -18 O ATOM 945 CB ASN A 118 2.576 25.005 1.569 1.00 8.26 C ANISOU 945 CB ASN A 118 1061 1071 1005 20 33 -8 C ATOM 946 CG ASN A 118 2.567 25.717 0.233 1.00 8.66 C ANISOU 946 CG ASN A 118 1116 1088 1085 -10 47 41 C ATOM 947 ND2 ASN A 118 2.355 24.955 -0.829 1.00 8.91 N ANISOU 947 ND2 ASN A 118 1152 1171 1061 -92 88 69 N ATOM 948 OD1 ASN A 118 2.732 26.941 0.155 1.00 10.81 O ANISOU 948 OD1 ASN A 118 1323 1310 1472 -36 71 16 O ATOM 949 N GLY A 119 0.474 23.574 4.105 1.00 6.98 N ANISOU 949 N GLY A 119 868 935 847 7 49 2 N ATOM 950 CA GLY A 119 0.519 22.719 5.294 1.00 6.77 C ANISOU 950 CA GLY A 119 827 907 839 -17 16 15 C ATOM 951 C GLY A 119 0.453 21.225 5.033 1.00 6.86 C ANISOU 951 C GLY A 119 832 939 835 -16 31 5 C ATOM 952 O GLY A 119 1.283 20.475 5.543 1.00 6.57 O ANISOU 952 O GLY A 119 789 901 806 -36 73 23 O ATOM 953 N PRO A 120 -0.540 20.772 4.246 1.00 6.96 N ANISOU 953 N PRO A 120 842 932 869 -25 16 -2 N ATOM 954 CA PRO A 120 -0.624 19.336 3.970 1.00 7.26 C ANISOU 954 CA PRO A 120 893 960 903 -13 10 -18 C ATOM 955 C PRO A 120 0.646 18.746 3.350 1.00 7.14 C ANISOU 955 C PRO A 120 869 938 903 -26 9 -19 C ATOM 956 O PRO A 120 1.103 17.691 3.788 1.00 7.25 O ANISOU 956 O PRO A 120 868 963 921 -18 16 -47 O ATOM 957 CB PRO A 120 -1.817 19.237 3.013 1.00 7.63 C ANISOU 957 CB PRO A 120 911 998 989 -18 5 -11 C ATOM 958 CG PRO A 120 -2.690 20.380 3.420 1.00 7.44 C ANISOU 958 CG PRO A 120 909 977 938 -13 18 1 C ATOM 959 CD PRO A 120 -1.728 21.490 3.745 1.00 7.24 C ANISOU 959 CD PRO A 120 929 937 883 -10 -14 0 C ATOM 960 N PHE A 121 1.225 19.431 2.367 1.00 7.15 N ANISOU 960 N PHE A 121 875 950 889 13 2 -23 N ATOM 961 CA PHE A 121 2.454 18.946 1.739 1.00 7.19 C ANISOU 961 CA PHE A 121 888 956 888 18 9 -26 C ATOM 962 C PHE A 121 3.617 18.924 2.733 1.00 6.96 C ANISOU 962 C PHE A 121 852 926 863 22 11 -39 C ATOM 963 O PHE A 121 4.402 17.980 2.751 1.00 6.76 O ANISOU 963 O PHE A 121 814 941 813 54 55 9 O ATOM 964 CB PHE A 121 2.823 19.793 0.524 1.00 7.69 C ANISOU 964 CB PHE A 121 956 1039 925 13 10 -23 C ATOM 965 CG PHE A 121 4.067 19.325 -0.177 1.00 8.84 C ANISOU 965 CG PHE A 121 1105 1200 1051 56 28 10 C ATOM 966 CD1 PHE A 121 4.089 18.096 -0.817 1.00 10.07 C ANISOU 966 CD1 PHE A 121 1270 1306 1250 0 42 -14 C ATOM 967 CD2 PHE A 121 5.212 20.103 -0.189 1.00 10.29 C ANISOU 967 CD2 PHE A 121 1305 1325 1281 26 51 37 C ATOM 968 CE1 PHE A 121 5.237 17.650 -1.459 1.00 11.15 C ANISOU 968 CE1 PHE A 121 1417 1434 1383 55 64 -33 C ATOM 969 CE2 PHE A 121 6.364 19.664 -0.837 1.00 10.91 C ANISOU 969 CE2 PHE A 121 1328 1419 1398 53 43 17 C ATOM 970 CZ PHE A 121 6.368 18.437 -1.471 1.00 10.71 C ANISOU 970 CZ PHE A 121 1361 1443 1264 49 28 10 C ATOM 971 N LEU A 122 3.721 19.956 3.566 1.00 6.64 N ANISOU 971 N LEU A 122 794 896 830 36 16 -26 N ATOM 972 CA LEU A 122 4.790 20.008 4.558 1.00 6.61 C ANISOU 972 CA LEU A 122 780 889 842 18 2 -16 C ATOM 973 C LEU A 122 4.680 18.867 5.566 1.00 6.52 C ANISOU 973 C LEU A 122 776 867 832 1 -1 -23 C ATOM 974 O LEU A 122 5.685 18.249 5.921 1.00 6.21 O ANISOU 974 O LEU A 122 700 842 817 39 11 -10 O ATOM 975 CB LEU A 122 4.818 21.367 5.260 1.00 6.62 C ANISOU 975 CB LEU A 122 788 890 837 -5 0 -14 C ATOM 976 CG LEU A 122 5.428 22.477 4.398 1.00 7.71 C ANISOU 976 CG LEU A 122 954 979 994 -9 2 18 C ATOM 977 CD1 LEU A 122 5.050 23.839 4.937 1.00 8.95 C ANISOU 977 CD1 LEU A 122 1189 976 1233 -36 32 -23 C ATOM 978 CD2 LEU A 122 6.948 22.330 4.295 1.00 8.60 C ANISOU 978 CD2 LEU A 122 1022 1129 1116 -45 8 8 C ATOM 979 N LEU A 123 3.465 18.567 6.016 1.00 6.63 N ANISOU 979 N LEU A 123 785 881 851 5 -17 -21 N ATOM 980 CA LEU A 123 3.255 17.432 6.909 1.00 7.03 C ANISOU 980 CA LEU A 123 867 913 888 9 0 -20 C ATOM 981 C LEU A 123 3.649 16.112 6.243 1.00 7.34 C ANISOU 981 C LEU A 123 906 956 925 11 20 -18 C ATOM 982 O LEU A 123 4.199 15.228 6.895 1.00 7.05 O ANISOU 982 O LEU A 123 848 943 887 27 26 -62 O ATOM 983 CB LEU A 123 1.800 17.372 7.373 1.00 7.03 C ANISOU 983 CB LEU A 123 863 888 918 -14 -2 -2 C ATOM 984 CG LEU A 123 1.333 18.492 8.302 1.00 7.38 C ANISOU 984 CG LEU A 123 929 960 915 8 49 -2 C ATOM 985 CD1 LEU A 123 -0.115 18.229 8.659 1.00 7.68 C ANISOU 985 CD1 LEU A 123 903 1027 985 -5 74 -63 C ATOM 986 CD2 LEU A 123 2.180 18.584 9.564 1.00 7.37 C ANISOU 986 CD2 LEU A 123 869 971 959 -74 52 -42 C ATOM 987 N GLU A 124 3.377 15.988 4.947 1.00 7.97 N ANISOU 987 N GLU A 124 987 1038 1002 28 -11 -14 N ATOM 988 CA GLU A 124 3.784 14.801 4.204 1.00 8.73 C ANISOU 988 CA GLU A 124 1093 1119 1102 18 2 -30 C ATOM 989 C GLU A 124 5.308 14.693 4.101 1.00 8.55 C ANISOU 989 C GLU A 124 1078 1106 1065 22 -4 -35 C ATOM 990 O GLU A 124 5.869 13.613 4.297 1.00 8.79 O ANISOU 990 O GLU A 124 1123 1113 1104 39 -37 -57 O ATOM 991 CB GLU A 124 3.160 14.785 2.813 1.00 9.41 C ANISOU 991 CB GLU A 124 1169 1221 1185 5 2 -20 C ATOM 992 CG GLU A 124 3.428 13.497 2.077 1.00 11.57 C ANISOU 992 CG GLU A 124 1457 1450 1486 54 15 -71 C ATOM 993 CD GLU A 124 2.880 13.513 0.689 1.00 14.36 C ANISOU 993 CD GLU A 124 1827 1883 1743 10 -47 -39 C ATOM 994 OE1 GLU A 124 1.644 13.626 0.539 1.00 16.82 O ANISOU 994 OE1 GLU A 124 2041 2189 2158 104 -14 -31 O ATOM 995 OE2 GLU A 124 3.692 13.414 -0.249 1.00 17.18 O1- ANISOU 995 OE2 GLU A 124 2126 2248 2153 44 84 -66 O1- ATOM 996 N ARG A 125 5.969 15.809 3.803 1.00 8.26 N ANISOU 996 N ARG A 125 1027 1077 1033 32 17 -31 N ATOM 997 CA ARG A 125 7.440 15.851 3.740 1.00 8.36 C ANISOU 997 CA ARG A 125 1013 1101 1063 22 22 -27 C ATOM 998 C ARG A 125 8.069 15.390 5.055 1.00 7.96 C ANISOU 998 C ARG A 125 964 1055 1005 35 39 -25 C ATOM 999 O ARG A 125 9.095 14.710 5.067 1.00 8.28 O ANISOU 999 O ARG A 125 952 1131 1060 45 8 -14 O ATOM 1000 CB ARG A 125 7.934 17.267 3.432 1.00 8.83 C ANISOU 1000 CB ARG A 125 1097 1139 1119 30 22 -9 C ATOM 1001 CG ARG A 125 7.613 17.792 2.043 1.00 10.52 C ANISOU 1001 CG ARG A 125 1303 1390 1302 -19 -20 23 C ATOM 1002 CD ARG A 125 8.517 17.219 0.980 1.00 12.27 C ANISOU 1002 CD ARG A 125 1554 1603 1502 20 2 4 C ATOM 1003 NE ARG A 125 7.983 15.988 0.405 1.00 13.99 N ANISOU 1003 NE ARG A 125 1789 1764 1763 -23 30 -36 N ATOM 1004 CZ ARG A 125 8.418 15.429 -0.722 1.00 15.31 C ANISOU 1004 CZ ARG A 125 1965 1968 1881 16 28 -47 C ATOM 1005 NH1 ARG A 125 7.857 14.309 -1.158 1.00 16.26 N1+ ANISOU 1005 NH1 ARG A 125 2044 2084 2050 -64 28 -64 N1+ ATOM 1006 NH2 ARG A 125 9.414 15.975 -1.413 1.00 15.39 N ANISOU 1006 NH2 ARG A 125 1962 1961 1923 -5 2 -46 N ATOM 1007 N MET A 126 7.437 15.754 6.166 1.00 7.28 N ANISOU 1007 N MET A 126 872 998 893 40 23 -38 N ATOM 1008 CA MET A 126 7.953 15.421 7.493 1.00 7.08 C ANISOU 1008 CA MET A 126 862 945 882 43 22 -25 C ATOM 1009 C MET A 126 7.459 14.071 8.022 1.00 7.19 C ANISOU 1009 C MET A 126 876 956 900 35 30 -28 C ATOM 1010 O MET A 126 7.775 13.700 9.156 1.00 7.15 O ANISOU 1010 O MET A 126 852 949 914 63 64 -38 O ATOM 1011 CB MET A 126 7.582 16.546 8.462 1.00 6.95 C ANISOU 1011 CB MET A 126 862 906 872 56 20 -23 C ATOM 1012 CG MET A 126 8.310 17.846 8.158 1.00 7.07 C ANISOU 1012 CG MET A 126 835 939 911 45 -9 -26 C ATOM 1013 SD MET A 126 8.004 19.151 9.352 1.00 7.25 S ANISOU 1013 SD MET A 126 882 1025 845 70 -90 -55 S ATOM 1014 CE MET A 126 6.347 19.679 8.899 1.00 8.77 C ANISOU 1014 CE MET A 126 1004 1242 1083 154 1 -83 C ATOM 1015 N ASN A 127 6.707 13.345 7.188 1.00 7.38 N ANISOU 1015 N ASN A 127 911 969 924 16 17 -19 N ATOM 1016 CA AASN A 127 6.115 12.054 7.552 0.50 7.73 C ANISOU 1016 CA AASN A 127 968 1002 966 2 28 -15 C ATOM 1017 CA BASN A 127 6.125 12.054 7.556 0.50 7.71 C ANISOU 1017 CA BASN A 127 970 995 964 5 28 -14 C ATOM 1018 C ASN A 127 5.202 12.145 8.778 1.00 7.55 C ANISOU 1018 C ASN A 127 935 974 959 5 31 -2 C ATOM 1019 O ASN A 127 5.211 11.265 9.641 1.00 7.79 O ANISOU 1019 O ASN A 127 1002 1000 959 17 108 15 O ATOM 1020 CB AASN A 127 7.199 10.986 7.760 0.50 8.06 C ANISOU 1020 CB AASN A 127 1003 1039 1019 -5 4 -2 C ATOM 1021 CB BASN A 127 7.230 11.013 7.782 0.50 8.03 C ANISOU 1021 CB BASN A 127 1004 1040 1008 2 9 -4 C ATOM 1022 CG AASN A 127 7.980 10.691 6.492 0.50 8.95 C ANISOU 1022 CG AASN A 127 1121 1170 1109 -1 16 -23 C ATOM 1023 CG BASN A 127 6.735 9.589 7.609 0.50 8.87 C ANISOU 1023 CG BASN A 127 1153 1094 1123 15 18 -14 C ATOM 1024 ND2AASN A 127 9.073 9.952 6.633 0.50 9.92 N ANISOU 1024 ND2AASN A 127 1265 1240 1261 47 -13 -31 N ATOM 1025 ND2BASN A 127 7.354 8.655 8.321 0.50 9.96 N ANISOU 1025 ND2BASN A 127 1278 1279 1226 42 -33 42 N ATOM 1026 OD1AASN A 127 7.602 11.114 5.400 0.50 10.79 O ANISOU 1026 OD1AASN A 127 1342 1437 1318 33 4 34 O ATOM 1027 OD1BASN A 127 5.805 9.334 6.844 0.50 10.43 O ANISOU 1027 OD1BASN A 127 1318 1287 1358 19 -41 -27 O ATOM 1028 N LEU A 128 4.406 13.212 8.840 1.00 7.26 N ANISOU 1028 N LEU A 128 893 927 936 -9 50 0 N ATOM 1029 CA LEU A 128 3.491 13.438 9.964 1.00 7.29 C ANISOU 1029 CA LEU A 128 924 918 927 -16 39 -14 C ATOM 1030 C LEU A 128 2.015 13.297 9.589 1.00 7.71 C ANISOU 1030 C LEU A 128 956 995 977 -5 28 -8 C ATOM 1031 O LEU A 128 1.157 13.384 10.463 1.00 7.64 O ANISOU 1031 O LEU A 128 889 985 1028 1 84 -32 O ATOM 1032 CB LEU A 128 3.727 14.828 10.568 1.00 7.20 C ANISOU 1032 CB LEU A 128 918 907 910 -19 30 -5 C ATOM 1033 CG LEU A 128 5.108 15.095 11.170 1.00 6.85 C ANISOU 1033 CG LEU A 128 869 845 887 23 41 -14 C ATOM 1034 CD1 LEU A 128 5.149 16.514 11.723 1.00 6.93 C ANISOU 1034 CD1 LEU A 128 801 871 959 5 78 -81 C ATOM 1035 CD2 LEU A 128 5.457 14.074 12.251 1.00 7.23 C ANISOU 1035 CD2 LEU A 128 910 916 920 10 2 2 C ATOM 1036 N THR A 129 1.721 13.067 8.310 1.00 7.96 N ANISOU 1036 N THR A 129 984 1040 998 9 37 -13 N ATOM 1037 CA THR A 129 0.342 13.041 7.805 1.00 8.62 C ANISOU 1037 CA THR A 129 1073 1123 1078 -19 17 -8 C ATOM 1038 C THR A 129 -0.599 12.167 8.636 1.00 8.50 C ANISOU 1038 C THR A 129 1060 1103 1067 -18 18 -19 C ATOM 1039 O THR A 129 -1.724 12.573 8.948 1.00 8.92 O ANISOU 1039 O THR A 129 1086 1177 1123 -75 15 -49 O ATOM 1040 CB THR A 129 0.313 12.542 6.340 1.00 8.74 C ANISOU 1040 CB THR A 129 1098 1172 1050 -28 25 -4 C ATOM 1041 CG2 THR A 129 -1.107 12.477 5.799 1.00 9.69 C ANISOU 1041 CG2 THR A 129 1186 1311 1184 1 22 21 C ATOM 1042 OG1 THR A 129 1.091 13.427 5.522 1.00 10.61 O ANISOU 1042 OG1 THR A 129 1291 1403 1335 -139 11 76 O ATOM 1043 N GLY A 130 -0.130 10.976 8.998 1.00 8.55 N ANISOU 1043 N GLY A 130 1074 1090 1083 -13 39 -21 N ATOM 1044 CA GLY A 130 -0.949 10.002 9.720 1.00 8.52 C ANISOU 1044 CA GLY A 130 1064 1069 1101 -10 32 -11 C ATOM 1045 C GLY A 130 -1.377 10.428 11.115 1.00 8.51 C ANISOU 1045 C GLY A 130 1066 1065 1101 -19 38 -23 C ATOM 1046 O GLY A 130 -2.377 9.933 11.640 1.00 9.01 O ANISOU 1046 O GLY A 130 1081 1133 1207 -53 67 -50 O ATOM 1047 N TYR A 131 -0.626 11.336 11.733 1.00 8.19 N ANISOU 1047 N TYR A 131 997 1038 1075 -37 47 -26 N ATOM 1048 CA TYR A 131 -0.956 11.806 13.083 1.00 7.92 C ANISOU 1048 CA TYR A 131 992 985 1030 -19 34 -17 C ATOM 1049 C TYR A 131 -2.116 12.786 13.102 1.00 7.74 C ANISOU 1049 C TYR A 131 973 961 1005 -22 28 -11 C ATOM 1050 O TYR A 131 -2.801 12.906 14.117 1.00 8.20 O ANISOU 1050 O TYR A 131 1041 1016 1057 -2 51 -28 O ATOM 1051 CB TYR A 131 0.258 12.456 13.749 1.00 7.85 C ANISOU 1051 CB TYR A 131 985 970 1027 -37 40 -31 C ATOM 1052 CG TYR A 131 1.368 11.476 14.017 1.00 7.86 C ANISOU 1052 CG TYR A 131 974 988 1024 -30 9 -36 C ATOM 1053 CD1 TYR A 131 1.223 10.480 14.977 1.00 8.93 C ANISOU 1053 CD1 TYR A 131 1093 1106 1194 16 37 22 C ATOM 1054 CD2 TYR A 131 2.556 11.527 13.299 1.00 8.52 C ANISOU 1054 CD2 TYR A 131 1066 1047 1120 -66 45 -59 C ATOM 1055 CE1 TYR A 131 2.232 9.562 15.213 1.00 9.39 C ANISOU 1055 CE1 TYR A 131 1197 1161 1208 26 -4 2 C ATOM 1056 CE2 TYR A 131 3.574 10.619 13.537 1.00 8.87 C ANISOU 1056 CE2 TYR A 131 1095 1138 1134 -14 -15 -68 C ATOM 1057 CZ TYR A 131 3.405 9.642 14.494 1.00 9.71 C ANISOU 1057 CZ TYR A 131 1188 1209 1290 27 -28 -30 C ATOM 1058 OH TYR A 131 4.407 8.735 14.726 1.00 11.34 O ANISOU 1058 OH TYR A 131 1407 1342 1558 189 -77 -22 O ATOM 1059 N PHE A 132 -2.345 13.480 11.990 1.00 7.72 N ANISOU 1059 N PHE A 132 949 968 1014 8 54 -25 N ATOM 1060 CA PHE A 132 -3.326 14.559 11.975 1.00 7.61 C ANISOU 1060 CA PHE A 132 952 959 980 -2 28 -17 C ATOM 1061 C PHE A 132 -4.726 14.073 11.627 1.00 7.87 C ANISOU 1061 C PHE A 132 972 1015 1002 -5 26 -33 C ATOM 1062 O PHE A 132 -4.971 13.548 10.543 1.00 8.63 O ANISOU 1062 O PHE A 132 1092 1127 1058 -14 30 -37 O ATOM 1063 CB PHE A 132 -2.850 15.697 11.072 1.00 7.35 C ANISOU 1063 CB PHE A 132 908 935 946 13 33 -20 C ATOM 1064 CG PHE A 132 -1.829 16.559 11.736 1.00 7.17 C ANISOU 1064 CG PHE A 132 893 918 912 0 39 -2 C ATOM 1065 CD1 PHE A 132 -2.190 17.770 12.306 1.00 7.30 C ANISOU 1065 CD1 PHE A 132 926 905 941 20 53 25 C ATOM 1066 CD2 PHE A 132 -0.516 16.119 11.870 1.00 7.77 C ANISOU 1066 CD2 PHE A 132 977 1002 972 0 30 -4 C ATOM 1067 CE1 PHE A 132 -1.257 18.549 12.960 1.00 7.62 C ANISOU 1067 CE1 PHE A 132 922 936 1036 28 60 -42 C ATOM 1068 CE2 PHE A 132 0.426 16.894 12.527 1.00 7.66 C ANISOU 1068 CE2 PHE A 132 943 951 1013 -47 40 31 C ATOM 1069 CZ PHE A 132 0.051 18.111 13.076 1.00 7.32 C ANISOU 1069 CZ PHE A 132 889 980 909 7 7 28 C ATOM 1070 N ASP A 133 -5.636 14.241 12.582 1.00 8.12 N ANISOU 1070 N ASP A 133 1028 1050 1007 -44 27 -26 N ATOM 1071 CA ASP A 133 -7.034 13.885 12.390 1.00 8.42 C ANISOU 1071 CA ASP A 133 1050 1100 1046 -49 11 -36 C ATOM 1072 C ASP A 133 -7.718 14.824 11.402 1.00 8.28 C ANISOU 1072 C ASP A 133 1019 1101 1025 -50 15 -36 C ATOM 1073 O ASP A 133 -8.655 14.427 10.710 1.00 9.18 O ANISOU 1073 O ASP A 133 1100 1265 1123 -97 -18 -69 O ATOM 1074 CB ASP A 133 -7.769 13.895 13.728 1.00 8.73 C ANISOU 1074 CB ASP A 133 1102 1120 1091 -70 11 -39 C ATOM 1075 CG ASP A 133 -7.287 12.806 14.652 1.00 9.69 C ANISOU 1075 CG ASP A 133 1282 1213 1185 -59 41 -2 C ATOM 1076 OD1 ASP A 133 -7.549 11.620 14.351 1.00 13.05 O ANISOU 1076 OD1 ASP A 133 1902 1401 1652 -174 -2 -2 O ATOM 1077 OD2 ASP A 133 -6.637 13.127 15.666 1.00 10.12 O1- ANISOU 1077 OD2 ASP A 133 1303 1276 1266 -123 28 -16 O1- ATOM 1078 N ALA A 134 -7.245 16.065 11.332 1.00 7.85 N ANISOU 1078 N ALA A 134 966 1037 979 -23 19 -57 N ATOM 1079 CA ALA A 134 -7.767 17.025 10.369 1.00 7.83 C ANISOU 1079 CA ALA A 134 956 1030 985 -9 30 -49 C ATOM 1080 C ALA A 134 -6.821 18.201 10.191 1.00 7.92 C ANISOU 1080 C ALA A 134 959 1043 1006 -5 -2 -51 C ATOM 1081 O ALA A 134 -5.967 18.467 11.043 1.00 8.05 O ANISOU 1081 O ALA A 134 960 1099 995 -2 -8 -66 O ATOM 1082 CB ALA A 134 -9.158 17.516 10.796 1.00 8.19 C ANISOU 1082 CB ALA A 134 966 1103 1039 4 11 -42 C ATOM 1083 N ILE A 135 -6.988 18.895 9.069 1.00 8.14 N ANISOU 1083 N ILE A 135 1016 1062 1014 -5 -17 -40 N ATOM 1084 CA ILE A 135 -6.241 20.113 8.762 1.00 8.64 C ANISOU 1084 CA ILE A 135 1096 1109 1077 -8 -36 -28 C ATOM 1085 C ILE A 135 -7.251 21.203 8.427 1.00 9.01 C ANISOU 1085 C ILE A 135 1145 1160 1116 8 -62 -25 C ATOM 1086 O ILE A 135 -8.023 21.063 7.479 1.00 9.93 O ANISOU 1086 O ILE A 135 1301 1258 1211 61 -142 -46 O ATOM 1087 CB ILE A 135 -5.288 19.906 7.567 1.00 8.72 C ANISOU 1087 CB ILE A 135 1111 1130 1072 -11 -45 -11 C ATOM 1088 CG1 ILE A 135 -4.250 18.827 7.893 1.00 8.96 C ANISOU 1088 CG1 ILE A 135 1109 1155 1139 -17 11 -32 C ATOM 1089 CG2 ILE A 135 -4.611 21.220 7.185 1.00 9.05 C ANISOU 1089 CG2 ILE A 135 1179 1139 1119 -11 -20 -33 C ATOM 1090 CD1 ILE A 135 -3.371 18.441 6.719 1.00 10.28 C ANISOU 1090 CD1 ILE A 135 1297 1355 1250 18 59 -13 C ATOM 1091 N ALA A 136 -7.271 22.274 9.216 1.00 9.51 N ANISOU 1091 N ALA A 136 1212 1210 1188 4 -60 -17 N ATOM 1092 CA ALA A 136 -8.142 23.407 8.928 1.00 9.95 C ANISOU 1092 CA ALA A 136 1236 1290 1254 -1 -45 -14 C ATOM 1093 C ALA A 136 -7.603 24.123 7.695 1.00 10.59 C ANISOU 1093 C ALA A 136 1307 1386 1329 -4 -31 10 C ATOM 1094 O ALA A 136 -6.410 24.401 7.609 1.00 10.66 O ANISOU 1094 O ALA A 136 1278 1424 1346 -36 -70 35 O ATOM 1095 CB ALA A 136 -8.205 24.353 10.116 1.00 9.98 C ANISOU 1095 CB ALA A 136 1265 1283 1242 11 -25 -15 C ATOM 1096 N ASP A 137 -8.481 24.409 6.738 1.00 11.33 N ANISOU 1096 N ASP A 137 1382 1495 1426 -5 -41 13 N ATOM 1097 CA ASP A 137 -8.082 25.007 5.467 1.00 12.31 C ANISOU 1097 CA ASP A 137 1522 1618 1535 4 -21 1 C ATOM 1098 C ASP A 137 -8.058 26.538 5.554 1.00 13.21 C ANISOU 1098 C ASP A 137 1642 1700 1676 15 -11 8 C ATOM 1099 O ASP A 137 -9.115 27.158 5.671 1.00 12.98 O ANISOU 1099 O ASP A 137 1568 1688 1671 30 -17 11 O ATOM 1100 CB ASP A 137 -9.057 24.553 4.374 1.00 12.43 C ANISOU 1100 CB ASP A 137 1532 1621 1569 -4 -42 0 C ATOM 1101 CG ASP A 137 -8.641 24.996 2.980 1.00 12.96 C ANISOU 1101 CG ASP A 137 1624 1719 1579 -7 -31 -28 C ATOM 1102 OD1 ASP A 137 -7.666 25.763 2.834 1.00 12.88 O ANISOU 1102 OD1 ASP A 137 1680 1729 1484 -33 -55 -75 O ATOM 1103 OD2 ASP A 137 -9.311 24.573 2.012 1.00 14.90 O1- ANISOU 1103 OD2 ASP A 137 1961 1981 1715 -5 -107 -109 O1- ATOM 1104 N PRO A 138 -6.856 27.155 5.486 1.00 14.47 N ANISOU 1104 N PRO A 138 1770 1860 1865 13 -11 4 N ATOM 1105 CA PRO A 138 -6.699 28.608 5.408 1.00 15.84 C ANISOU 1105 CA PRO A 138 1976 2009 2034 4 -1 -2 C ATOM 1106 C PRO A 138 -7.553 29.292 4.355 1.00 17.32 C ANISOU 1106 C PRO A 138 2163 2198 2220 25 -2 26 C ATOM 1107 O PRO A 138 -8.029 30.401 4.584 1.00 17.66 O ANISOU 1107 O PRO A 138 2269 2205 2235 25 -7 2 O ATOM 1108 CB PRO A 138 -5.233 28.770 5.003 1.00 15.96 C ANISOU 1108 CB PRO A 138 1976 2025 2059 -14 5 11 C ATOM 1109 CG PRO A 138 -4.566 27.638 5.565 1.00 14.96 C ANISOU 1109 CG PRO A 138 1839 1915 1927 -5 0 -10 C ATOM 1110 CD PRO A 138 -5.541 26.499 5.621 1.00 14.50 C ANISOU 1110 CD PRO A 138 1785 1854 1870 18 -13 -5 C ATOM 1111 N ALA A 139 -7.705 28.646 3.202 1.00 19.04 N ANISOU 1111 N ALA A 139 2412 2409 2412 7 -8 -5 N ATOM 1112 CA ALA A 139 -8.475 29.198 2.091 1.00 20.51 C ANISOU 1112 CA ALA A 139 2605 2597 2587 18 -23 18 C ATOM 1113 C ALA A 139 -9.981 29.246 2.367 1.00 21.83 C ANISOU 1113 C ALA A 139 2748 2776 2770 16 -20 4 C ATOM 1114 O ALA A 139 -10.712 29.934 1.650 1.00 22.21 O ANISOU 1114 O ALA A 139 2819 2801 2816 42 -28 36 O ATOM 1115 CB ALA A 139 -8.197 28.406 0.816 1.00 20.55 C ANISOU 1115 CB ALA A 139 2599 2602 2604 17 -5 5 C ATOM 1116 N GLU A 140 -10.444 28.513 3.384 1.00 23.16 N ANISOU 1116 N GLU A 140 2932 2938 2929 5 -11 21 N ATOM 1117 CA GLU A 140 -11.856 28.553 3.810 1.00 24.24 C ANISOU 1117 CA GLU A 140 3054 3080 3074 4 -4 11 C ATOM 1118 C GLU A 140 -12.079 29.201 5.153 1.00 24.74 C ANISOU 1118 C GLU A 140 3120 3140 3137 1 1 9 C ATOM 1119 O GLU A 140 -13.089 28.954 5.811 1.00 25.09 O ANISOU 1119 O GLU A 140 3155 3187 3187 -1 11 17 O ATOM 1120 CB GLU A 140 -12.430 27.162 3.964 1.00 24.64 C ANISOU 1120 CB GLU A 140 3095 3118 3148 -1 -14 18 C ATOM 1121 CG GLU A 140 -12.226 26.256 2.826 1.00 25.89 C ANISOU 1121 CG GLU A 140 3255 3326 3255 43 -9 -15 C ATOM 1122 CD GLU A 140 -12.952 24.951 3.040 1.00 22.95 C ANISOU 1122 CD GLU A 140 3352 3100 2268 -129 244 -164 C ATOM 1123 OE1 GLU A 140 -13.041 24.181 2.077 1.00 29.61 O ANISOU 1123 OE1 GLU A 140 3444 3870 3936 22 -28 244 O ATOM 1124 OE2 GLU A 140 -13.442 24.693 4.164 1.00 29.69 O1- ANISOU 1124 OE2 GLU A 140 3773 3444 4063 57 -244 -99 O1- ATOM 1125 N VAL A 141 -11.123 29.976 5.605 1.00 25.04 N ANISOU 1125 N VAL A 141 3148 3187 3178 1 -5 7 N ATOM 1126 CA VAL A 141 -11.377 30.839 6.713 1.00 25.18 C ANISOU 1126 CA VAL A 141 3176 3197 3191 0 -11 2 C ATOM 1127 C VAL A 141 -10.777 32.116 6.245 1.00 25.00 C ANISOU 1127 C VAL A 141 3159 3171 3167 8 -5 -4 C ATOM 1128 O VAL A 141 -9.743 32.119 5.578 1.00 25.24 O ANISOU 1128 O VAL A 141 3178 3222 3187 13 -1 5 O ATOM 1129 CB VAL A 141 -10.672 30.379 8.008 1.00 25.32 C ANISOU 1129 CB VAL A 141 3194 3217 3205 0 -10 9 C ATOM 1130 CG1 VAL A 141 -11.209 29.027 8.455 1.00 25.35 C ANISOU 1130 CG1 VAL A 141 3196 3219 3214 1 -16 20 C ATOM 1131 CG2 VAL A 141 -9.162 30.319 7.815 1.00 25.57 C ANISOU 1131 CG2 VAL A 141 3214 3257 3242 -5 -11 -4 C ATOM 1132 N ALA A 142 -11.445 33.208 6.540 1.00 24.52 N ANISOU 1132 N ALA A 142 3096 3101 3120 0 -11 -7 N ATOM 1133 CA ALA A 142 -10.676 34.396 6.786 1.00 23.92 C ANISOU 1133 CA ALA A 142 3016 3029 3043 5 -5 -10 C ATOM 1134 C ALA A 142 -11.508 35.630 6.816 1.00 23.07 C ANISOU 1134 C ALA A 142 2908 2925 2929 -4 -18 -16 C ATOM 1135 O ALA A 142 -12.535 35.723 6.129 1.00 23.58 O ANISOU 1135 O ALA A 142 2942 3032 2984 25 -17 7 O ATOM 1136 CB ALA A 142 -9.530 34.558 5.765 1.00 24.07 C ANISOU 1136 CB ALA A 142 3042 3053 3049 -1 -2 -11 C ATOM 1137 N ALA A 143 -11.111 36.566 7.668 1.00 21.71 N ANISOU 1137 N ALA A 143 2733 2770 2746 9 -13 -7 N ATOM 1138 CA ALA A 143 -10.333 36.339 8.919 1.00 20.13 C ANISOU 1138 CA ALA A 143 2519 2551 2577 14 -13 5 C ATOM 1139 C ALA A 143 -9.046 35.465 9.057 1.00 18.63 C ANISOU 1139 C ALA A 143 2342 2353 2383 -5 -10 9 C ATOM 1140 O ALA A 143 -9.117 34.272 9.381 1.00 19.01 O ANISOU 1140 O ALA A 143 2384 2388 2449 -13 -18 9 O ATOM 1141 CB ALA A 143 -11.308 35.907 9.995 1.00 20.44 C ANISOU 1141 CB ALA A 143 2562 2609 2592 4 -5 10 C ATOM 1142 N ASER A 144 -7.884 36.074 8.851 0.50 17.67 N ANISOU 1142 N ASER A 144 2223 2232 2258 13 -16 10 N ATOM 1143 N BSER A 144 -7.892 36.095 8.845 0.50 17.61 N ANISOU 1143 N BSER A 144 2215 2225 2251 14 -16 10 N ATOM 1144 CA ASER A 144 -6.625 35.484 9.296 0.50 16.78 C ANISOU 1144 CA ASER A 144 2119 2118 2136 -2 -8 7 C ATOM 1145 CA BSER A 144 -6.604 35.571 9.302 0.50 16.67 C ANISOU 1145 CA BSER A 144 2104 2106 2123 0 -5 7 C ATOM 1146 C ASER A 144 -6.461 35.775 10.787 0.50 15.86 C ANISOU 1146 C ASER A 144 1986 1996 2043 2 -8 13 C ATOM 1147 C BSER A 144 -6.473 35.778 10.806 0.50 15.80 C ANISOU 1147 C BSER A 144 1978 1988 2036 2 -7 11 C ATOM 1148 O ASER A 144 -7.206 36.577 11.351 0.50 15.54 O ANISOU 1148 O ASER A 144 1941 1967 1994 -4 -13 17 O ATOM 1149 O BSER A 144 -7.247 36.529 11.401 0.50 15.50 O ANISOU 1149 O BSER A 144 1937 1962 1988 -2 -13 17 O ATOM 1150 CB ASER A 144 -5.455 36.083 8.522 0.50 16.85 C ANISOU 1150 CB ASER A 144 2121 2134 2146 5 -7 7 C ATOM 1151 CB BSER A 144 -5.460 36.313 8.609 0.50 16.71 C ANISOU 1151 CB BSER A 144 2103 2114 2131 5 -2 8 C ATOM 1152 OG ASER A 144 -5.339 37.468 8.793 0.50 17.10 O ANISOU 1152 OG ASER A 144 2172 2149 2177 -17 -2 0 O ATOM 1153 OG BSER A 144 -5.258 35.829 7.294 0.50 16.68 O ANISOU 1153 OG BSER A 144 2097 2119 2120 14 7 5 O ATOM 1154 N LYS A 145 -5.485 35.126 11.418 1.00 14.97 N ANISOU 1154 N LYS A 145 1881 1882 1925 -11 1 7 N ATOM 1155 CA LYS A 145 -5.138 35.406 12.816 1.00 13.88 C ANISOU 1155 CA LYS A 145 1739 1726 1807 2 0 16 C ATOM 1156 C LYS A 145 -4.817 36.914 12.917 1.00 13.24 C ANISOU 1156 C LYS A 145 1666 1643 1718 2 -8 21 C ATOM 1157 O LYS A 145 -4.169 37.457 12.018 1.00 13.66 O ANISOU 1157 O LYS A 145 1710 1699 1780 1 0 40 O ATOM 1158 CB LYS A 145 -3.933 34.562 13.252 1.00 13.49 C ANISOU 1158 CB LYS A 145 1703 1681 1739 -2 -4 5 C ATOM 1159 CG LYS A 145 -4.173 33.041 13.214 1.00 12.46 C ANISOU 1159 CG LYS A 145 1531 1589 1611 14 2 -1 C ATOM 1160 CD LYS A 145 -2.855 32.257 13.198 1.00 11.43 C ANISOU 1160 CD LYS A 145 1427 1461 1453 11 -11 11 C ATOM 1161 CE LYS A 145 -3.070 30.789 12.840 1.00 10.10 C ANISOU 1161 CE LYS A 145 1190 1359 1287 56 -27 44 C ATOM 1162 NZ LYS A 145 -1.824 29.956 12.942 1.00 9.69 N1+ ANISOU 1162 NZ LYS A 145 1201 1268 1213 99 18 0 N1+ ATOM 1163 N PRO A 146 -5.243 37.591 14.004 1.00 12.39 N ANISOU 1163 N PRO A 146 1560 1510 1634 2 -20 30 N ATOM 1164 CA PRO A 146 -5.752 37.099 15.282 1.00 11.77 C ANISOU 1164 CA PRO A 146 1472 1443 1554 11 -20 13 C ATOM 1165 C PRO A 146 -7.228 36.704 15.348 1.00 11.28 C ANISOU 1165 C PRO A 146 1419 1373 1492 31 -13 22 C ATOM 1166 O PRO A 146 -7.706 36.371 16.429 1.00 11.21 O ANISOU 1166 O PRO A 146 1385 1360 1512 50 -34 56 O ATOM 1167 CB PRO A 146 -5.489 38.282 16.222 1.00 11.89 C ANISOU 1167 CB PRO A 146 1504 1446 1564 15 -31 28 C ATOM 1168 CG PRO A 146 -5.674 39.463 15.353 1.00 12.12 C ANISOU 1168 CG PRO A 146 1514 1469 1618 9 -36 39 C ATOM 1169 CD PRO A 146 -5.121 39.063 14.013 1.00 12.19 C ANISOU 1169 CD PRO A 146 1533 1477 1621 13 -31 30 C ATOM 1170 N ALA A 147 -7.949 36.727 14.230 1.00 10.86 N ANISOU 1170 N ALA A 147 1354 1321 1449 28 -7 31 N ATOM 1171 CA ALA A 147 -9.316 36.203 14.237 1.00 10.84 C ANISOU 1171 CA ALA A 147 1361 1324 1429 21 -26 13 C ATOM 1172 C ALA A 147 -9.263 34.729 14.651 1.00 10.79 C ANISOU 1172 C ALA A 147 1346 1327 1424 28 -8 19 C ATOM 1173 O ALA A 147 -8.349 34.008 14.240 1.00 10.58 O ANISOU 1173 O ALA A 147 1317 1287 1412 56 11 8 O ATOM 1174 CB ALA A 147 -9.968 36.360 12.879 1.00 10.97 C ANISOU 1174 CB ALA A 147 1383 1354 1429 28 -41 28 C ATOM 1175 N PRO A 148 -10.222 34.281 15.483 1.00 10.53 N ANISOU 1175 N PRO A 148 1308 1298 1392 36 4 5 N ATOM 1176 CA PRO A 148 -10.188 32.911 16.009 1.00 10.47 C ANISOU 1176 CA PRO A 148 1290 1297 1388 20 -7 14 C ATOM 1177 C PRO A 148 -10.610 31.819 15.019 1.00 10.30 C ANISOU 1177 C PRO A 148 1262 1283 1366 25 2 8 C ATOM 1178 O PRO A 148 -10.462 30.629 15.322 1.00 10.07 O ANISOU 1178 O PRO A 148 1210 1234 1382 18 7 15 O ATOM 1179 CB PRO A 148 -11.175 32.968 17.176 1.00 10.45 C ANISOU 1179 CB PRO A 148 1283 1298 1387 25 -27 -5 C ATOM 1180 CG PRO A 148 -12.143 34.012 16.787 1.00 10.53 C ANISOU 1180 CG PRO A 148 1305 1291 1402 33 -16 2 C ATOM 1181 CD PRO A 148 -11.348 35.049 16.045 1.00 10.66 C ANISOU 1181 CD PRO A 148 1301 1324 1424 28 5 9 C ATOM 1182 N ASP A 149 -11.097 32.225 13.848 1.00 10.43 N ANISOU 1182 N ASP A 149 1256 1298 1407 22 -10 7 N ATOM 1183 CA ASP A 149 -11.750 31.329 12.891 1.00 10.75 C ANISOU 1183 CA ASP A 149 1319 1355 1409 28 -17 5 C ATOM 1184 C ASP A 149 -10.990 30.034 12.580 1.00 10.07 C ANISOU 1184 C ASP A 149 1225 1278 1322 13 -30 21 C ATOM 1185 O ASP A 149 -11.584 28.956 12.561 1.00 10.28 O ANISOU 1185 O ASP A 149 1261 1267 1377 50 -79 36 O ATOM 1186 CB ASP A 149 -12.028 32.073 11.581 1.00 11.20 C ANISOU 1186 CB ASP A 149 1369 1406 1479 10 -35 35 C ATOM 1187 CG ASP A 149 -12.915 33.295 11.769 1.00 13.10 C ANISOU 1187 CG ASP A 149 1634 1607 1734 63 -13 2 C ATOM 1188 OD1 ASP A 149 -12.765 34.009 12.784 1.00 14.61 O ANISOU 1188 OD1 ASP A 149 1876 1800 1872 120 -141 15 O ATOM 1189 OD2 ASP A 149 -13.757 33.550 10.887 1.00 16.10 O1- ANISOU 1189 OD2 ASP A 149 1999 2062 2054 94 -154 44 O1- ATOM 1190 N ILE A 150 -9.685 30.137 12.340 1.00 9.38 N ANISOU 1190 N ILE A 150 1155 1195 1213 2 -30 15 N ATOM 1191 CA ILE A 150 -8.895 28.964 11.954 1.00 8.88 C ANISOU 1191 CA ILE A 150 1085 1151 1135 -1 -31 7 C ATOM 1192 C ILE A 150 -8.803 27.944 13.097 1.00 8.50 C ANISOU 1192 C ILE A 150 1033 1114 1080 0 -23 -5 C ATOM 1193 O ILE A 150 -8.824 26.735 12.857 1.00 8.27 O ANISOU 1193 O ILE A 150 980 1126 1035 8 -41 -43 O ATOM 1194 CB ILE A 150 -7.483 29.359 11.443 1.00 8.92 C ANISOU 1194 CB ILE A 150 1099 1174 1116 -7 -35 18 C ATOM 1195 CG1 ILE A 150 -6.809 28.184 10.718 1.00 9.21 C ANISOU 1195 CG1 ILE A 150 1156 1198 1144 -20 -38 17 C ATOM 1196 CG2 ILE A 150 -6.617 29.881 12.584 1.00 8.59 C ANISOU 1196 CG2 ILE A 150 1036 1113 1114 -51 -38 -2 C ATOM 1197 CD1 ILE A 150 -7.455 27.822 9.388 1.00 10.55 C ANISOU 1197 CD1 ILE A 150 1382 1374 1253 7 -80 -27 C ATOM 1198 N PHE A 151 -8.730 28.427 14.335 1.00 8.14 N ANISOU 1198 N PHE A 151 990 1059 1043 -18 -25 -19 N ATOM 1199 CA PHE A 151 -8.709 27.531 15.496 1.00 7.86 C ANISOU 1199 CA PHE A 151 966 1003 1017 5 -19 -14 C ATOM 1200 C PHE A 151 -10.082 26.923 15.775 1.00 7.69 C ANISOU 1200 C PHE A 151 941 995 985 15 -8 -16 C ATOM 1201 O PHE A 151 -10.181 25.754 16.140 1.00 7.74 O ANISOU 1201 O PHE A 151 913 1013 1015 -7 -18 -26 O ATOM 1202 CB PHE A 151 -8.125 28.229 16.732 1.00 7.80 C ANISOU 1202 CB PHE A 151 938 1008 1016 -11 -26 16 C ATOM 1203 CG PHE A 151 -6.632 28.369 16.672 1.00 7.35 C ANISOU 1203 CG PHE A 151 905 968 920 28 -11 -23 C ATOM 1204 CD1 PHE A 151 -5.817 27.288 16.973 1.00 6.99 C ANISOU 1204 CD1 PHE A 151 889 909 856 14 -39 -17 C ATOM 1205 CD2 PHE A 151 -6.042 29.558 16.273 1.00 7.85 C ANISOU 1205 CD2 PHE A 151 949 1056 975 9 -90 -14 C ATOM 1206 CE1 PHE A 151 -4.440 27.390 16.890 1.00 7.58 C ANISOU 1206 CE1 PHE A 151 926 987 963 19 -22 -42 C ATOM 1207 CE2 PHE A 151 -4.662 29.666 16.193 1.00 8.14 C ANISOU 1207 CE2 PHE A 151 990 1061 1041 -40 -7 0 C ATOM 1208 CZ PHE A 151 -3.865 28.583 16.503 1.00 7.79 C ANISOU 1208 CZ PHE A 151 912 1061 988 -23 1 -2 C ATOM 1209 N ILE A 152 -11.140 27.705 15.579 1.00 7.76 N ANISOU 1209 N ILE A 152 915 1015 1015 -1 -28 -4 N ATOM 1210 CA ILE A 152 -12.497 27.182 15.708 1.00 7.91 C ANISOU 1210 CA ILE A 152 937 1039 1028 2 4 5 C ATOM 1211 C ILE A 152 -12.714 26.077 14.670 1.00 7.66 C ANISOU 1211 C ILE A 152 893 1011 1004 11 15 9 C ATOM 1212 O ILE A 152 -13.237 25.005 14.984 1.00 7.78 O ANISOU 1212 O ILE A 152 846 1043 1065 2 17 14 O ATOM 1213 CB ILE A 152 -13.556 28.285 15.529 1.00 7.89 C ANISOU 1213 CB ILE A 152 936 1036 1024 7 -17 5 C ATOM 1214 CG1 ILE A 152 -13.419 29.351 16.621 1.00 8.14 C ANISOU 1214 CG1 ILE A 152 973 1043 1076 4 2 9 C ATOM 1215 CG2 ILE A 152 -14.957 27.685 15.561 1.00 8.73 C ANISOU 1215 CG2 ILE A 152 978 1156 1184 0 -60 26 C ATOM 1216 CD1 ILE A 152 -14.244 30.597 16.369 1.00 9.62 C ANISOU 1216 CD1 ILE A 152 1106 1228 1320 83 34 25 C ATOM 1217 N ALA A 153 -12.288 26.336 13.435 1.00 7.74 N ANISOU 1217 N ALA A 153 908 1040 992 18 -23 23 N ATOM 1218 CA ALA A 153 -12.405 25.353 12.360 1.00 7.70 C ANISOU 1218 CA ALA A 153 903 1027 990 2 -11 7 C ATOM 1219 C ALA A 153 -11.619 24.072 12.665 1.00 7.68 C ANISOU 1219 C ALA A 153 901 1019 995 -7 -15 -13 C ATOM 1220 O ALA A 153 -12.107 22.967 12.438 1.00 8.14 O ANISOU 1220 O ALA A 153 927 1072 1093 -35 -16 10 O ATOM 1221 CB ALA A 153 -11.947 25.963 11.029 1.00 7.97 C ANISOU 1221 CB ALA A 153 946 1077 1004 -4 -16 22 C ATOM 1222 N ALA A 154 -10.407 24.230 13.188 1.00 7.46 N ANISOU 1222 N ALA A 154 856 1014 964 11 -11 -19 N ATOM 1223 CA ALA A 154 -9.555 23.090 13.512 1.00 7.24 C ANISOU 1223 CA ALA A 154 830 966 952 -4 -11 -25 C ATOM 1224 C ALA A 154 -10.198 22.216 14.584 1.00 7.05 C ANISOU 1224 C ALA A 154 796 964 916 5 -5 -33 C ATOM 1225 O ALA A 154 -10.219 20.991 14.459 1.00 7.25 O ANISOU 1225 O ALA A 154 790 1011 951 22 -17 -65 O ATOM 1226 CB ALA A 154 -8.180 23.561 13.967 1.00 7.28 C ANISOU 1226 CB ALA A 154 800 989 976 0 -15 -52 C ATOM 1227 N ALA A 155 -10.737 22.851 15.625 1.00 6.97 N ANISOU 1227 N ALA A 155 794 954 897 10 -14 -45 N ATOM 1228 CA ALA A 155 -11.429 22.131 16.690 1.00 6.84 C ANISOU 1228 CA ALA A 155 803 920 872 -5 -18 -32 C ATOM 1229 C ALA A 155 -12.643 21.386 16.146 1.00 7.04 C ANISOU 1229 C ALA A 155 821 938 913 -17 5 -25 C ATOM 1230 O ALA A 155 -12.800 20.186 16.365 1.00 7.19 O ANISOU 1230 O ALA A 155 792 1012 926 -63 5 -22 O ATOM 1231 CB ALA A 155 -11.849 23.090 17.797 1.00 6.82 C ANISOU 1231 CB ALA A 155 805 915 869 1 18 -56 C ATOM 1232 N HIS A 156 -13.485 22.100 15.408 1.00 7.32 N ANISOU 1232 N HIS A 156 849 970 961 -28 -2 -26 N ATOM 1233 CA HIS A 156 -14.686 21.495 14.831 1.00 7.66 C ANISOU 1233 CA HIS A 156 895 1009 1005 -44 -10 -26 C ATOM 1234 C HIS A 156 -14.375 20.394 13.817 1.00 8.02 C ANISOU 1234 C HIS A 156 936 1049 1059 -38 4 -37 C ATOM 1235 O HIS A 156 -15.148 19.440 13.676 1.00 8.54 O ANISOU 1235 O HIS A 156 956 1129 1159 -95 -21 -82 O ATOM 1236 CB HIS A 156 -15.582 22.559 14.201 1.00 7.64 C ANISOU 1236 CB HIS A 156 885 1026 992 -34 5 -21 C ATOM 1237 CG HIS A 156 -16.213 23.476 15.200 1.00 7.94 C ANISOU 1237 CG HIS A 156 913 1023 1079 -32 0 -27 C ATOM 1238 CD2 HIS A 156 -16.303 23.398 16.549 1.00 7.72 C ANISOU 1238 CD2 HIS A 156 871 997 1066 -28 -42 -25 C ATOM 1239 ND1 HIS A 156 -16.831 24.653 14.841 1.00 8.59 N ANISOU 1239 ND1 HIS A 156 960 1127 1176 75 14 -59 N ATOM 1240 CE1 HIS A 156 -17.292 25.251 15.926 1.00 9.17 C ANISOU 1240 CE1 HIS A 156 1144 1197 1142 57 -11 -38 C ATOM 1241 NE2 HIS A 156 -16.985 24.510 16.975 1.00 7.98 N ANISOU 1241 NE2 HIS A 156 931 993 1107 -41 11 -55 N ATOM 1242 N ALA A 157 -13.247 20.520 13.123 1.00 8.23 N ANISOU 1242 N ALA A 157 970 1090 1067 -28 9 -50 N ATOM 1243 CA ALA A 157 -12.810 19.507 12.160 1.00 8.65 C ANISOU 1243 CA ALA A 157 1043 1138 1105 -11 9 -52 C ATOM 1244 C ALA A 157 -12.548 18.139 12.806 1.00 8.94 C ANISOU 1244 C ALA A 157 1083 1167 1145 -14 21 -54 C ATOM 1245 O ALA A 157 -12.609 17.115 12.128 1.00 9.99 O ANISOU 1245 O ALA A 157 1188 1333 1272 -2 17 -119 O ATOM 1246 CB ALA A 157 -11.571 19.989 11.424 1.00 8.74 C ANISOU 1246 CB ALA A 157 1045 1144 1130 8 28 -49 C ATOM 1247 N VAL A 158 -12.251 18.127 14.108 1.00 8.83 N ANISOU 1247 N VAL A 158 1080 1164 1111 0 2 -76 N ATOM 1248 CA VAL A 158 -12.033 16.883 14.852 1.00 8.82 C ANISOU 1248 CA VAL A 158 1082 1159 1110 -8 4 -57 C ATOM 1249 C VAL A 158 -13.132 16.621 15.899 1.00 8.90 C ANISOU 1249 C VAL A 158 1104 1167 1109 2 5 -36 C ATOM 1250 O VAL A 158 -12.970 15.780 16.791 1.00 9.15 O ANISOU 1250 O VAL A 158 1141 1164 1171 -16 36 -36 O ATOM 1251 CB VAL A 158 -10.624 16.849 15.509 1.00 8.88 C ANISOU 1251 CB VAL A 158 1092 1143 1139 -5 -7 -65 C ATOM 1252 CG1 VAL A 158 -9.544 16.898 14.437 1.00 9.34 C ANISOU 1252 CG1 VAL A 158 1173 1211 1163 2 -2 -91 C ATOM 1253 CG2 VAL A 158 -10.446 17.992 16.510 1.00 8.74 C ANISOU 1253 CG2 VAL A 158 1090 1142 1089 -27 -14 -72 C ATOM 1254 N GLY A 159 -14.248 17.341 15.778 1.00 8.92 N ANISOU 1254 N GLY A 159 1114 1165 1109 4 0 -43 N ATOM 1255 CA GLY A 159 -15.449 17.059 16.572 1.00 8.93 C ANISOU 1255 CA GLY A 159 1113 1165 1115 -28 -2 -23 C ATOM 1256 C GLY A 159 -15.429 17.543 18.015 1.00 8.85 C ANISOU 1256 C GLY A 159 1105 1158 1099 -20 -14 -11 C ATOM 1257 O GLY A 159 -16.187 17.044 18.856 1.00 9.32 O ANISOU 1257 O GLY A 159 1122 1257 1160 -64 -39 -15 O ATOM 1258 N VAL A 160 -14.580 18.530 18.294 1.00 8.67 N ANISOU 1258 N VAL A 160 1082 1114 1097 -15 -2 -8 N ATOM 1259 CA AVAL A 160 -14.469 19.064 19.653 0.50 8.48 C ANISOU 1259 CA AVAL A 160 1058 1092 1071 -2 2 -9 C ATOM 1260 CA BVAL A 160 -14.375 19.063 19.639 0.50 8.70 C ANISOU 1260 CA BVAL A 160 1089 1117 1098 -2 5 -9 C ATOM 1261 C VAL A 160 -14.675 20.569 19.675 1.00 8.50 C ANISOU 1261 C VAL A 160 1060 1096 1072 0 13 -5 C ATOM 1262 O VAL A 160 -14.504 21.259 18.671 1.00 8.97 O ANISOU 1262 O VAL A 160 1138 1143 1125 9 61 -2 O ATOM 1263 CB AVAL A 160 -13.117 18.719 20.328 0.50 8.42 C ANISOU 1263 CB AVAL A 160 1068 1067 1062 0 -11 -13 C ATOM 1264 CB BVAL A 160 -12.906 18.811 20.089 0.50 8.79 C ANISOU 1264 CB BVAL A 160 1106 1114 1119 2 -9 -7 C ATOM 1265 CG1AVAL A 160 -12.835 17.223 20.244 0.50 7.95 C ANISOU 1265 CG1AVAL A 160 976 997 1047 -4 -40 5 C ATOM 1266 CG1BVAL A 160 -11.921 19.509 19.160 0.50 9.48 C ANISOU 1266 CG1BVAL A 160 1161 1234 1205 -11 -11 2 C ATOM 1267 CG2AVAL A 160 -11.983 19.528 19.722 0.50 8.65 C ANISOU 1267 CG2AVAL A 160 1064 1129 1094 -8 2 -2 C ATOM 1268 CG2BVAL A 160 -12.681 19.255 21.516 0.50 9.02 C ANISOU 1268 CG2BVAL A 160 1142 1136 1146 -18 1 -7 C ATOM 1269 N ALA A 161 -15.102 21.071 20.831 1.00 8.17 N ANISOU 1269 N ALA A 161 1001 1082 1019 -8 19 -5 N ATOM 1270 CA ALA A 161 -15.259 22.505 21.023 1.00 8.02 C ANISOU 1270 CA ALA A 161 951 1075 1022 5 15 -15 C ATOM 1271 C ALA A 161 -13.879 23.074 21.331 1.00 7.87 C ANISOU 1271 C ALA A 161 938 1057 995 14 8 -9 C ATOM 1272 O ALA A 161 -13.066 22.398 21.966 1.00 7.50 O ANISOU 1272 O ALA A 161 869 998 979 62 35 -52 O ATOM 1273 CB ALA A 161 -16.223 22.792 22.170 1.00 8.57 C ANISOU 1273 CB ALA A 161 1046 1154 1055 11 28 -23 C ATOM 1274 N PRO A 162 -13.603 24.309 20.881 1.00 7.50 N ANISOU 1274 N PRO A 162 897 995 956 21 -2 -28 N ATOM 1275 CA PRO A 162 -12.353 24.947 21.285 1.00 7.84 C ANISOU 1275 CA PRO A 162 951 1016 1009 16 1 -23 C ATOM 1276 C PRO A 162 -12.125 24.943 22.803 1.00 7.76 C ANISOU 1276 C PRO A 162 939 1019 988 18 15 -26 C ATOM 1277 O PRO A 162 -10.988 24.776 23.234 1.00 7.74 O ANISOU 1277 O PRO A 162 896 1040 1005 75 14 -49 O ATOM 1278 CB PRO A 162 -12.503 26.370 20.751 1.00 7.87 C ANISOU 1278 CB PRO A 162 961 1026 1002 5 4 -8 C ATOM 1279 CG PRO A 162 -13.384 26.235 19.575 1.00 8.16 C ANISOU 1279 CG PRO A 162 992 1050 1058 5 -17 -8 C ATOM 1280 CD PRO A 162 -14.348 25.135 19.911 1.00 7.86 C ANISOU 1280 CD PRO A 162 952 1025 1006 9 -1 -15 C ATOM 1281 N SER A 163 -13.191 25.081 23.597 1.00 8.24 N ANISOU 1281 N SER A 163 987 1087 1054 41 -1 -40 N ATOM 1282 CA SER A 163 -13.097 25.028 25.064 1.00 8.56 C ANISOU 1282 CA SER A 163 1030 1122 1097 32 21 -37 C ATOM 1283 C SER A 163 -12.493 23.730 25.600 1.00 8.52 C ANISOU 1283 C SER A 163 1036 1129 1073 36 15 -32 C ATOM 1284 O SER A 163 -12.007 23.696 26.734 1.00 9.42 O ANISOU 1284 O SER A 163 1139 1274 1164 84 34 -60 O ATOM 1285 CB SER A 163 -14.483 25.216 25.694 1.00 8.51 C ANISOU 1285 CB SER A 163 1040 1111 1082 38 56 -70 C ATOM 1286 OG SER A 163 -15.339 24.124 25.385 1.00 10.35 O ANISOU 1286 OG SER A 163 1208 1372 1353 -22 -9 -89 O ATOM 1287 N GLU A 164 -12.547 22.673 24.788 1.00 8.38 N ANISOU 1287 N GLU A 164 1013 1097 1071 35 27 -14 N ATOM 1288 CA GLU A 164 -12.015 21.362 25.135 1.00 8.50 C ANISOU 1288 CA GLU A 164 1039 1100 1089 7 23 -9 C ATOM 1289 C GLU A 164 -10.625 21.138 24.535 1.00 7.70 C ANISOU 1289 C GLU A 164 930 978 1016 2 14 -7 C ATOM 1290 O GLU A 164 -10.132 20.007 24.518 1.00 7.30 O ANISOU 1290 O GLU A 164 823 934 1016 -14 22 9 O ATOM 1291 CB GLU A 164 -12.960 20.273 24.606 1.00 9.10 C ANISOU 1291 CB GLU A 164 1131 1131 1193 -21 26 -9 C ATOM 1292 CG GLU A 164 -14.437 20.444 24.975 1.00 10.97 C ANISOU 1292 CG GLU A 164 1313 1452 1401 4 36 34 C ATOM 1293 CD GLU A 164 -15.342 19.398 24.329 1.00 12.82 C ANISOU 1293 CD GLU A 164 1651 1608 1608 -28 18 18 C ATOM 1294 OE1 GLU A 164 -15.503 19.406 23.087 1.00 12.79 O ANISOU 1294 OE1 GLU A 164 1592 1705 1561 57 94 33 O ATOM 1295 OE2 GLU A 164 -15.909 18.568 25.074 1.00 14.81 O1- ANISOU 1295 OE2 GLU A 164 1887 1867 1873 -86 115 127 O1- ATOM 1296 N SER A 165 -9.999 22.210 24.045 1.00 6.71 N ANISOU 1296 N SER A 165 798 869 881 -4 17 -40 N ATOM 1297 CA SER A 165 -8.753 22.108 23.280 1.00 6.39 C ANISOU 1297 CA SER A 165 753 839 833 -23 11 -27 C ATOM 1298 C SER A 165 -7.625 22.973 23.829 1.00 6.07 C ANISOU 1298 C SER A 165 719 796 789 -2 -10 -34 C ATOM 1299 O SER A 165 -7.864 24.020 24.442 1.00 6.49 O ANISOU 1299 O SER A 165 723 909 833 -25 -5 -61 O ATOM 1300 CB SER A 165 -8.985 22.534 21.826 1.00 6.28 C ANISOU 1300 CB SER A 165 728 854 801 -27 2 -56 C ATOM 1301 OG SER A 165 -10.059 21.828 21.232 1.00 7.05 O ANISOU 1301 OG SER A 165 776 992 908 -126 -37 -104 O ATOM 1302 N ILE A 166 -6.396 22.523 23.575 1.00 5.63 N ANISOU 1302 N ILE A 166 666 729 741 -23 10 -28 N ATOM 1303 CA ILE A 166 -5.190 23.336 23.756 1.00 5.75 C ANISOU 1303 CA ILE A 166 716 713 754 -22 9 -27 C ATOM 1304 C ILE A 166 -4.699 23.776 22.380 1.00 5.67 C ANISOU 1304 C ILE A 166 709 719 723 -18 -1 -39 C ATOM 1305 O ILE A 166 -4.727 22.996 21.431 1.00 6.15 O ANISOU 1305 O ILE A 166 840 733 763 -20 40 -54 O ATOM 1306 CB ILE A 166 -4.069 22.535 24.454 1.00 5.96 C ANISOU 1306 CB ILE A 166 735 767 762 -28 -14 -41 C ATOM 1307 CG1 ILE A 166 -4.414 22.300 25.922 1.00 6.21 C ANISOU 1307 CG1 ILE A 166 775 772 812 -2 19 35 C ATOM 1308 CG2 ILE A 166 -2.714 23.249 24.338 1.00 6.03 C ANISOU 1308 CG2 ILE A 166 709 733 847 1 -47 -42 C ATOM 1309 CD1 ILE A 166 -3.441 21.376 26.616 1.00 6.31 C ANISOU 1309 CD1 ILE A 166 786 864 747 59 32 85 C ATOM 1310 N GLY A 167 -4.260 25.026 22.277 1.00 5.31 N ANISOU 1310 N GLY A 167 675 659 684 -8 0 -28 N ATOM 1311 CA GLY A 167 -3.633 25.538 21.059 1.00 5.34 C ANISOU 1311 CA GLY A 167 636 673 718 -28 -4 -23 C ATOM 1312 C GLY A 167 -2.163 25.847 21.294 1.00 5.35 C ANISOU 1312 C GLY A 167 646 678 709 -17 -20 -18 C ATOM 1313 O GLY A 167 -1.805 26.428 22.318 1.00 5.56 O ANISOU 1313 O GLY A 167 679 670 764 -5 -10 -35 O ATOM 1314 N LEU A 168 -1.319 25.457 20.341 1.00 5.13 N ANISOU 1314 N LEU A 168 632 640 675 0 -30 -23 N ATOM 1315 CA LEU A 168 0.121 25.713 20.408 1.00 5.01 C ANISOU 1315 CA LEU A 168 623 628 653 -5 -30 -4 C ATOM 1316 C LEU A 168 0.539 26.703 19.317 1.00 4.84 C ANISOU 1316 C LEU A 168 613 611 613 0 -23 7 C ATOM 1317 O LEU A 168 0.263 26.481 18.133 1.00 5.29 O ANISOU 1317 O LEU A 168 734 625 649 -13 -64 90 O ATOM 1318 CB LEU A 168 0.904 24.401 20.272 1.00 5.02 C ANISOU 1318 CB LEU A 168 623 645 637 10 -44 -9 C ATOM 1319 CG LEU A 168 0.511 23.272 21.230 1.00 5.33 C ANISOU 1319 CG LEU A 168 645 660 718 28 -20 -22 C ATOM 1320 CD1 LEU A 168 1.387 22.039 21.000 1.00 6.23 C ANISOU 1320 CD1 LEU A 168 766 724 873 78 -13 -76 C ATOM 1321 CD2 LEU A 168 0.594 23.730 22.677 1.00 5.13 C ANISOU 1321 CD2 LEU A 168 598 663 689 16 -53 2 C ATOM 1322 N GLU A 169 1.211 27.784 19.722 1.00 4.92 N ANISOU 1322 N GLU A 169 656 608 602 8 -39 16 N ATOM 1323 CA GLU A 169 1.527 28.912 18.831 1.00 5.21 C ANISOU 1323 CA GLU A 169 684 638 655 18 -22 1 C ATOM 1324 C GLU A 169 2.836 29.597 19.205 1.00 5.33 C ANISOU 1324 C GLU A 169 688 658 678 30 -52 4 C ATOM 1325 O GLU A 169 3.253 29.564 20.365 1.00 5.42 O ANISOU 1325 O GLU A 169 721 673 662 39 -57 13 O ATOM 1326 CB GLU A 169 0.394 29.944 18.866 1.00 5.41 C ANISOU 1326 CB GLU A 169 696 669 687 4 -17 18 C ATOM 1327 CG GLU A 169 -0.567 29.835 17.706 1.00 6.32 C ANISOU 1327 CG GLU A 169 792 804 803 54 -45 -55 C ATOM 1328 CD GLU A 169 -0.021 30.432 16.427 1.00 7.48 C ANISOU 1328 CD GLU A 169 945 966 929 45 -47 -9 C ATOM 1329 OE1 GLU A 169 -0.689 30.267 15.387 1.00 8.62 O ANISOU 1329 OE1 GLU A 169 1189 1180 903 162 -92 -95 O ATOM 1330 OE2 GLU A 169 1.053 31.082 16.449 1.00 8.71 O1- ANISOU 1330 OE2 GLU A 169 1053 1233 1021 4 -28 -32 O1- ATOM 1331 N ASP A 170 3.458 30.227 18.209 1.00 5.92 N ANISOU 1331 N ASP A 170 741 734 772 2 -42 -5 N ATOM 1332 CA ASP A 170 4.706 30.983 18.379 1.00 6.44 C ANISOU 1332 CA ASP A 170 790 806 850 -26 -10 -2 C ATOM 1333 C ASP A 170 4.557 32.480 18.102 1.00 7.03 C ANISOU 1333 C ASP A 170 874 859 936 -9 -15 15 C ATOM 1334 O ASP A 170 5.558 33.197 18.133 1.00 7.53 O ANISOU 1334 O ASP A 170 911 880 1068 -36 8 9 O ATOM 1335 CB ASP A 170 5.798 30.435 17.448 1.00 6.79 C ANISOU 1335 CB ASP A 170 833 855 892 -32 2 -16 C ATOM 1336 CG ASP A 170 5.530 30.753 15.987 1.00 7.02 C ANISOU 1336 CG ASP A 170 842 927 895 -52 32 -14 C ATOM 1337 OD1 ASP A 170 4.367 30.601 15.558 1.00 7.85 O ANISOU 1337 OD1 ASP A 170 956 1113 912 -51 -45 -32 O ATOM 1338 OD2 ASP A 170 6.469 31.162 15.263 1.00 7.97 O1- ANISOU 1338 OD2 ASP A 170 1027 999 999 -138 89 -25 O1- ATOM 1339 N SER A 171 3.333 32.948 17.841 1.00 7.56 N ANISOU 1339 N SER A 171 940 922 1010 5 -7 19 N ATOM 1340 CA SER A 171 3.099 34.347 17.435 1.00 8.05 C ANISOU 1340 CA SER A 171 1014 966 1075 5 -9 11 C ATOM 1341 C SER A 171 2.023 35.040 18.274 1.00 7.92 C ANISOU 1341 C SER A 171 995 956 1055 9 -1 14 C ATOM 1342 O SER A 171 1.103 34.394 18.775 1.00 7.32 O ANISOU 1342 O SER A 171 924 821 1036 10 -16 17 O ATOM 1343 CB SER A 171 2.692 34.407 15.960 1.00 8.48 C ANISOU 1343 CB SER A 171 1088 1022 1111 32 18 7 C ATOM 1344 OG SER A 171 1.374 33.928 15.773 1.00 10.70 O ANISOU 1344 OG SER A 171 1366 1318 1381 1 -9 5 O ATOM 1345 N GLN A 172 2.130 36.364 18.387 1.00 7.92 N ANISOU 1345 N GLN A 172 995 942 1070 -2 -21 -4 N ATOM 1346 CA GLN A 172 1.137 37.189 19.089 1.00 8.26 C ANISOU 1346 CA GLN A 172 1037 995 1106 2 -11 4 C ATOM 1347 C GLN A 172 -0.269 36.986 18.527 1.00 8.07 C ANISOU 1347 C GLN A 172 1026 956 1082 11 -8 1 C ATOM 1348 O GLN A 172 -1.217 36.746 19.278 1.00 7.95 O ANISOU 1348 O GLN A 172 1021 875 1125 16 -19 -16 O ATOM 1349 CB GLN A 172 1.495 38.681 18.984 1.00 8.43 C ANISOU 1349 CB GLN A 172 1062 1004 1134 14 -28 -23 C ATOM 1350 CG GLN A 172 2.689 39.141 19.826 1.00 9.48 C ANISOU 1350 CG GLN A 172 1146 1143 1313 -15 -61 -5 C ATOM 1351 CD GLN A 172 2.347 39.538 21.261 1.00 10.17 C ANISOU 1351 CD GLN A 172 1252 1210 1401 9 -47 -2 C ATOM 1352 NE2 GLN A 172 1.063 39.658 21.565 1.00 10.14 N ANISOU 1352 NE2 GLN A 172 1253 1242 1355 -30 38 -49 N ATOM 1353 OE1 GLN A 172 3.247 39.749 22.087 1.00 12.59 O ANISOU 1353 OE1 GLN A 172 1466 1568 1749 8 -145 -61 O ATOM 1354 N ALA A 173 -0.397 37.092 17.204 1.00 7.87 N ANISOU 1354 N ALA A 173 1001 934 1055 0 -1 11 N ATOM 1355 CA ALA A 173 -1.702 36.980 16.549 1.00 7.88 C ANISOU 1355 CA ALA A 173 1009 970 1013 2 -18 26 C ATOM 1356 C ALA A 173 -2.300 35.597 16.766 1.00 7.88 C ANISOU 1356 C ALA A 173 984 955 1055 15 -11 23 C ATOM 1357 O ALA A 173 -3.500 35.462 17.009 1.00 8.13 O ANISOU 1357 O ALA A 173 1001 1006 1081 1 -66 46 O ATOM 1358 CB ALA A 173 -1.597 37.282 15.062 1.00 8.10 C ANISOU 1358 CB ALA A 173 1068 981 1029 -5 -10 59 C ATOM 1359 N GLY A 174 -1.456 34.569 16.690 1.00 7.65 N ANISOU 1359 N GLY A 174 938 927 1037 23 -16 8 N ATOM 1360 CA GLY A 174 -1.896 33.202 16.925 1.00 7.58 C ANISOU 1360 CA GLY A 174 935 916 1026 23 -15 -2 C ATOM 1361 C GLY A 174 -2.366 32.956 18.346 1.00 7.35 C ANISOU 1361 C GLY A 174 919 864 1008 35 -30 0 C ATOM 1362 O GLY A 174 -3.393 32.319 18.561 1.00 7.30 O ANISOU 1362 O GLY A 174 883 846 1044 87 -52 20 O ATOM 1363 N ILE A 175 -1.618 33.469 19.320 1.00 7.41 N ANISOU 1363 N ILE A 175 925 881 1010 31 -22 -14 N ATOM 1364 CA ILE A 175 -2.014 33.361 20.721 1.00 7.35 C ANISOU 1364 CA ILE A 175 914 868 1010 32 -25 -5 C ATOM 1365 C ILE A 175 -3.373 34.033 20.948 1.00 7.46 C ANISOU 1365 C ILE A 175 922 891 1019 31 0 -10 C ATOM 1366 O ILE A 175 -4.240 33.470 21.603 1.00 7.27 O ANISOU 1366 O ILE A 175 853 819 1089 60 2 10 O ATOM 1367 CB ILE A 175 -0.940 33.964 21.663 1.00 7.40 C ANISOU 1367 CB ILE A 175 924 864 1021 20 -35 -4 C ATOM 1368 CG1 ILE A 175 0.325 33.096 21.664 1.00 7.62 C ANISOU 1368 CG1 ILE A 175 937 905 1053 27 -28 -15 C ATOM 1369 CG2 ILE A 175 -1.474 34.105 23.081 1.00 7.52 C ANISOU 1369 CG2 ILE A 175 960 861 1034 16 -15 -2 C ATOM 1370 CD1 ILE A 175 0.166 31.715 22.284 1.00 8.33 C ANISOU 1370 CD1 ILE A 175 1090 997 1075 -53 -17 19 C ATOM 1371 N GLN A 176 -3.564 35.222 20.385 1.00 7.70 N ANISOU 1371 N GLN A 176 927 927 1068 28 7 -7 N ATOM 1372 CA GLN A 176 -4.840 35.927 20.520 1.00 8.19 C ANISOU 1372 CA GLN A 176 990 995 1122 35 5 -5 C ATOM 1373 C GLN A 176 -5.979 35.155 19.840 1.00 8.02 C ANISOU 1373 C GLN A 176 973 961 1111 40 2 -5 C ATOM 1374 O GLN A 176 -7.095 35.091 20.368 1.00 7.99 O ANISOU 1374 O GLN A 176 969 901 1162 75 27 -2 O ATOM 1375 CB GLN A 176 -4.740 37.345 19.956 1.00 8.45 C ANISOU 1375 CB GLN A 176 1041 1013 1153 45 -1 -20 C ATOM 1376 CG GLN A 176 -5.970 38.216 20.224 1.00 9.75 C ANISOU 1376 CG GLN A 176 1155 1148 1399 61 18 11 C ATOM 1377 CD GLN A 176 -6.267 38.383 21.705 1.00 11.04 C ANISOU 1377 CD GLN A 176 1383 1291 1518 66 -5 -56 C ATOM 1378 NE2 GLN A 176 -7.544 38.303 22.064 1.00 12.75 N ANISOU 1378 NE2 GLN A 176 1528 1524 1789 -30 85 -74 N ATOM 1379 OE1 GLN A 176 -5.362 38.584 22.515 1.00 12.92 O ANISOU 1379 OE1 GLN A 176 1555 1598 1754 94 -45 -115 O ATOM 1380 N ALA A 177 -5.692 34.562 18.683 1.00 7.72 N ANISOU 1380 N ALA A 177 922 950 1061 35 -16 9 N ATOM 1381 CA ALA A 177 -6.674 33.731 17.979 1.00 7.63 C ANISOU 1381 CA ALA A 177 908 961 1027 33 -38 9 C ATOM 1382 C ALA A 177 -7.111 32.540 18.836 1.00 7.51 C ANISOU 1382 C ALA A 177 875 956 1022 13 -31 13 C ATOM 1383 O ALA A 177 -8.298 32.224 18.917 1.00 7.76 O ANISOU 1383 O ALA A 177 856 974 1116 41 -26 71 O ATOM 1384 CB ALA A 177 -6.120 33.257 16.636 1.00 7.66 C ANISOU 1384 CB ALA A 177 901 979 1030 5 -27 8 C ATOM 1385 N ILE A 178 -6.155 31.887 19.496 1.00 7.38 N ANISOU 1385 N ILE A 178 890 932 979 31 -16 11 N ATOM 1386 CA ILE A 178 -6.484 30.773 20.389 1.00 7.33 C ANISOU 1386 CA ILE A 178 887 947 951 16 -11 0 C ATOM 1387 C ILE A 178 -7.391 31.248 21.533 1.00 7.88 C ANISOU 1387 C ILE A 178 948 1016 1028 14 1 -5 C ATOM 1388 O ILE A 178 -8.439 30.653 21.782 1.00 7.58 O ANISOU 1388 O ILE A 178 840 1006 1032 14 -16 -67 O ATOM 1389 CB ILE A 178 -5.219 30.093 20.964 1.00 7.07 C ANISOU 1389 CB ILE A 178 864 910 912 23 9 7 C ATOM 1390 CG1 ILE A 178 -4.404 29.434 19.848 1.00 6.80 C ANISOU 1390 CG1 ILE A 178 833 864 884 -1 -32 -36 C ATOM 1391 CG2 ILE A 178 -5.608 29.044 21.997 1.00 6.98 C ANISOU 1391 CG2 ILE A 178 830 922 898 5 46 20 C ATOM 1392 CD1 ILE A 178 -2.960 29.142 20.234 1.00 6.26 C ANISOU 1392 CD1 ILE A 178 736 771 872 11 52 -28 C ATOM 1393 N LYS A 179 -6.994 32.326 22.208 1.00 8.53 N ANISOU 1393 N LYS A 179 1047 1077 1115 14 18 -21 N ATOM 1394 CA LYS A 179 -7.795 32.906 23.299 1.00 9.11 C ANISOU 1394 CA LYS A 179 1134 1140 1188 21 21 -22 C ATOM 1395 C LYS A 179 -9.233 33.175 22.873 1.00 9.53 C ANISOU 1395 C LYS A 179 1178 1169 1273 31 23 -23 C ATOM 1396 O LYS A 179 -10.184 32.780 23.554 1.00 9.37 O ANISOU 1396 O LYS A 179 1104 1123 1330 66 17 -42 O ATOM 1397 CB LYS A 179 -7.181 34.224 23.776 1.00 9.41 C ANISOU 1397 CB LYS A 179 1179 1154 1239 5 37 -23 C ATOM 1398 CG LYS A 179 -5.918 34.081 24.591 1.00 10.10 C ANISOU 1398 CG LYS A 179 1247 1281 1308 26 23 -5 C ATOM 1399 CD LYS A 179 -5.429 35.436 25.096 1.00 11.36 C ANISOU 1399 CD LYS A 179 1447 1401 1469 -2 18 -39 C ATOM 1400 CE LYS A 179 -4.152 35.315 25.920 1.00 11.93 C ANISOU 1400 CE LYS A 179 1466 1480 1583 10 10 -35 C ATOM 1401 NZ LYS A 179 -3.578 36.647 26.268 1.00 13.77 N1+ ANISOU 1401 NZ LYS A 179 1782 1661 1786 -23 -55 -86 N1+ ATOM 1402 N ASP A 180 -9.387 33.844 21.738 1.00 10.03 N ANISOU 1402 N ASP A 180 1205 1247 1356 44 8 -16 N ATOM 1403 CA ASP A 180 -10.712 34.269 21.288 1.00 10.49 C ANISOU 1403 CA ASP A 180 1244 1322 1419 34 -17 -19 C ATOM 1404 C ASP A 180 -11.557 33.113 20.742 1.00 10.41 C ANISOU 1404 C ASP A 180 1221 1298 1436 36 -17 -28 C ATOM 1405 O ASP A 180 -12.771 33.251 20.590 1.00 11.51 O ANISOU 1405 O ASP A 180 1268 1436 1666 41 -42 -25 O ATOM 1406 CB ASP A 180 -10.592 35.418 20.279 1.00 10.89 C ANISOU 1406 CB ASP A 180 1288 1382 1466 33 -4 -4 C ATOM 1407 CG ASP A 180 -10.233 36.746 20.946 1.00 12.13 C ANISOU 1407 CG ASP A 180 1459 1519 1631 16 2 -17 C ATOM 1408 OD1 ASP A 180 -10.467 36.895 22.163 1.00 14.82 O ANISOU 1408 OD1 ASP A 180 1933 1828 1867 28 35 -44 O ATOM 1409 OD2 ASP A 180 -9.727 37.651 20.254 1.00 13.80 O1- ANISOU 1409 OD2 ASP A 180 1659 1661 1920 -5 47 40 O1- ATOM 1410 N SER A 181 -10.931 31.970 20.475 1.00 9.89 N ANISOU 1410 N SER A 181 1161 1238 1359 11 -15 -32 N ATOM 1411 CA SER A 181 -11.678 30.759 20.139 1.00 9.46 C ANISOU 1411 CA SER A 181 1132 1188 1274 13 -2 -23 C ATOM 1412 C SER A 181 -12.256 30.079 21.387 1.00 9.40 C ANISOU 1412 C SER A 181 1116 1180 1272 8 -5 -26 C ATOM 1413 O SER A 181 -13.232 29.334 21.286 1.00 9.96 O ANISOU 1413 O SER A 181 1133 1236 1413 2 21 -19 O ATOM 1414 CB SER A 181 -10.790 29.774 19.373 1.00 9.09 C ANISOU 1414 CB SER A 181 1112 1140 1202 -5 -7 -36 C ATOM 1415 OG SER A 181 -9.896 29.091 20.239 1.00 8.83 O ANISOU 1415 OG SER A 181 1085 1118 1149 63 51 -30 O ATOM 1416 N GLY A 182 -11.652 30.324 22.550 1.00 9.24 N ANISOU 1416 N GLY A 182 1136 1144 1228 11 28 -14 N ATOM 1417 CA GLY A 182 -12.028 29.639 23.783 1.00 9.02 C ANISOU 1417 CA GLY A 182 1104 1142 1181 9 9 -20 C ATOM 1418 C GLY A 182 -11.072 28.526 24.187 1.00 8.78 C ANISOU 1418 C GLY A 182 1100 1096 1138 2 22 -7 C ATOM 1419 O GLY A 182 -11.174 27.990 25.291 1.00 9.43 O ANISOU 1419 O GLY A 182 1222 1115 1245 26 14 11 O ATOM 1420 N ALA A 183 -10.141 28.175 23.300 1.00 8.38 N ANISOU 1420 N ALA A 183 1039 1058 1086 0 5 2 N ATOM 1421 CA ALA A 183 -9.125 27.170 23.612 1.00 7.84 C ANISOU 1421 CA ALA A 183 972 988 1019 -28 2 -18 C ATOM 1422 C ALA A 183 -8.053 27.750 24.529 1.00 7.51 C ANISOU 1422 C ALA A 183 930 951 969 -26 8 -20 C ATOM 1423 O ALA A 183 -7.978 28.966 24.723 1.00 7.80 O ANISOU 1423 O ALA A 183 919 993 1051 -36 4 -21 O ATOM 1424 CB ALA A 183 -8.504 26.634 22.338 1.00 8.03 C ANISOU 1424 CB ALA A 183 1001 1022 1028 -25 23 -16 C ATOM 1425 N LEU A 184 -7.241 26.863 25.098 1.00 7.03 N ANISOU 1425 N LEU A 184 877 884 910 -9 31 -50 N ATOM 1426 CA LEU A 184 -6.179 27.254 26.024 1.00 6.83 C ANISOU 1426 CA LEU A 184 863 859 871 16 20 -43 C ATOM 1427 C LEU A 184 -4.858 27.371 25.271 1.00 6.71 C ANISOU 1427 C LEU A 184 834 824 889 0 20 -37 C ATOM 1428 O LEU A 184 -4.373 26.377 24.739 1.00 6.21 O ANISOU 1428 O LEU A 184 777 723 858 -1 32 -75 O ATOM 1429 CB LEU A 184 -6.039 26.224 27.151 1.00 6.93 C ANISOU 1429 CB LEU A 184 873 867 893 16 31 -39 C ATOM 1430 CG LEU A 184 -5.007 26.535 28.236 1.00 7.23 C ANISOU 1430 CG LEU A 184 934 931 881 33 42 -39 C ATOM 1431 CD1 LEU A 184 -5.412 27.786 28.999 1.00 7.92 C ANISOU 1431 CD1 LEU A 184 1063 954 990 44 37 -90 C ATOM 1432 CD2 LEU A 184 -4.852 25.354 29.180 1.00 7.74 C ANISOU 1432 CD2 LEU A 184 1073 906 958 47 10 -33 C ATOM 1433 N PRO A 185 -4.257 28.573 25.231 1.00 6.74 N ANISOU 1433 N PRO A 185 863 813 885 23 20 -50 N ATOM 1434 CA PRO A 185 -2.977 28.683 24.536 1.00 6.86 C ANISOU 1434 CA PRO A 185 874 858 874 17 -2 -46 C ATOM 1435 C PRO A 185 -1.795 28.283 25.408 1.00 6.88 C ANISOU 1435 C PRO A 185 873 890 850 10 -2 -57 C ATOM 1436 O PRO A 185 -1.780 28.571 26.604 1.00 7.26 O ANISOU 1436 O PRO A 185 938 1006 813 -17 -5 -105 O ATOM 1437 CB PRO A 185 -2.883 30.175 24.180 1.00 6.93 C ANISOU 1437 CB PRO A 185 893 859 878 8 8 -36 C ATOM 1438 CG PRO A 185 -4.062 30.850 24.822 1.00 7.46 C ANISOU 1438 CG PRO A 185 947 907 978 27 -2 -38 C ATOM 1439 CD PRO A 185 -4.719 29.876 25.739 1.00 6.89 C ANISOU 1439 CD PRO A 185 884 840 893 33 26 -73 C ATOM 1440 N ILE A 186 -0.818 27.617 24.807 1.00 6.51 N ANISOU 1440 N ILE A 186 806 840 825 23 -23 -70 N ATOM 1441 CA ILE A 186 0.503 27.471 25.415 1.00 6.38 C ANISOU 1441 CA ILE A 186 798 818 806 23 -1 -38 C ATOM 1442 C ILE A 186 1.495 27.926 24.356 1.00 6.07 C ANISOU 1442 C ILE A 186 763 766 776 27 1 -43 C ATOM 1443 O ILE A 186 1.608 27.308 23.297 1.00 6.16 O ANISOU 1443 O ILE A 186 786 782 772 51 11 -42 O ATOM 1444 CB ILE A 186 0.813 26.029 25.869 1.00 6.58 C ANISOU 1444 CB ILE A 186 826 821 853 27 8 -45 C ATOM 1445 CG1 ILE A 186 -0.307 25.476 26.758 1.00 7.17 C ANISOU 1445 CG1 ILE A 186 943 878 900 28 13 -27 C ATOM 1446 CG2 ILE A 186 2.142 25.992 26.618 1.00 7.04 C ANISOU 1446 CG2 ILE A 186 915 905 854 7 -15 -41 C ATOM 1447 CD1 ILE A 186 -0.099 24.024 27.180 1.00 7.95 C ANISOU 1447 CD1 ILE A 186 1094 927 999 0 1 1 C ATOM 1448 N GLY A 187 2.188 29.024 24.634 1.00 5.76 N ANISOU 1448 N GLY A 187 714 723 750 38 -2 -37 N ATOM 1449 CA GLY A 187 3.078 29.637 23.658 1.00 5.83 C ANISOU 1449 CA GLY A 187 725 720 767 17 -11 -28 C ATOM 1450 C GLY A 187 4.482 29.074 23.731 1.00 5.87 C ANISOU 1450 C GLY A 187 731 733 764 25 -5 -28 C ATOM 1451 O GLY A 187 4.909 28.601 24.786 1.00 6.53 O ANISOU 1451 O GLY A 187 787 852 840 23 -11 -31 O ATOM 1452 N VAL A 188 5.194 29.132 22.608 1.00 5.81 N ANISOU 1452 N VAL A 188 713 724 769 18 2 -44 N ATOM 1453 CA VAL A 188 6.610 28.779 22.561 1.00 6.25 C ANISOU 1453 CA VAL A 188 755 788 832 27 5 -31 C ATOM 1454 C VAL A 188 7.425 29.980 22.081 1.00 6.70 C ANISOU 1454 C VAL A 188 803 859 881 17 21 -19 C ATOM 1455 O VAL A 188 7.140 30.561 21.034 1.00 7.06 O ANISOU 1455 O VAL A 188 798 903 978 40 26 11 O ATOM 1456 CB VAL A 188 6.890 27.534 21.671 1.00 5.98 C ANISOU 1456 CB VAL A 188 714 737 819 -5 -10 -47 C ATOM 1457 CG1 VAL A 188 6.353 27.710 20.243 1.00 6.21 C ANISOU 1457 CG1 VAL A 188 780 767 810 31 26 -54 C ATOM 1458 CG2 VAL A 188 8.393 27.204 21.669 1.00 6.65 C ANISOU 1458 CG2 VAL A 188 759 845 921 69 -35 -11 C ATOM 1459 N GLY A 189 8.433 30.345 22.868 1.00 7.37 N ANISOU 1459 N GLY A 189 864 956 976 15 4 8 N ATOM 1460 CA GLY A 189 9.305 31.478 22.567 1.00 8.08 C ANISOU 1460 CA GLY A 189 977 1027 1063 -7 7 0 C ATOM 1461 C GLY A 189 9.406 32.427 23.742 1.00 8.78 C ANISOU 1461 C GLY A 189 1073 1128 1135 -28 -19 -9 C ATOM 1462 O GLY A 189 9.240 32.021 24.895 1.00 8.89 O ANISOU 1462 O GLY A 189 1109 1128 1138 -123 13 -52 O ATOM 1463 N ARG A 190 9.685 33.693 23.445 1.00 9.85 N ANISOU 1463 N ARG A 190 1214 1247 1281 -9 -23 13 N ATOM 1464 CA ARG A 190 9.802 34.731 24.465 1.00 10.61 C ANISOU 1464 CA ARG A 190 1330 1331 1369 -1 -34 -11 C ATOM 1465 C ARG A 190 8.438 35.368 24.719 1.00 10.72 C ANISOU 1465 C ARG A 190 1335 1338 1397 -19 -28 -1 C ATOM 1466 O ARG A 190 7.678 35.581 23.773 1.00 10.43 O ANISOU 1466 O ARG A 190 1279 1272 1411 -36 -83 -23 O ATOM 1467 CB ARG A 190 10.795 35.803 24.018 1.00 11.29 C ANISOU 1467 CB ARG A 190 1427 1406 1456 -5 -33 -19 C ATOM 1468 CG ARG A 190 12.206 35.283 23.805 1.00 13.40 C ANISOU 1468 CG ARG A 190 1651 1714 1724 25 -26 -41 C ATOM 1469 CD ARG A 190 13.102 36.348 23.205 1.00 16.75 C ANISOU 1469 CD ARG A 190 2119 2103 2140 -57 28 11 C ATOM 1470 NE ARG A 190 14.464 35.863 22.994 1.00 19.75 N ANISOU 1470 NE ARG A 190 2437 2546 2518 20 32 -23 N ATOM 1471 CZ ARG A 190 15.385 35.727 23.949 1.00 21.76 C ANISOU 1471 CZ ARG A 190 2668 2852 2747 40 -31 0 C ATOM 1472 NH1 ARG A 190 15.114 36.035 25.219 1.00 22.09 N1+ ANISOU 1472 NH1 ARG A 190 2655 2980 2757 53 2 -40 N1+ ATOM 1473 NH2 ARG A 190 16.596 35.277 23.632 1.00 24.25 N ANISOU 1473 NH2 ARG A 190 3013 2968 3231 -20 35 34 N ATOM 1474 N PRO A 191 8.121 35.689 25.988 1.00 11.01 N ANISOU 1474 N PRO A 191 1384 1383 1416 -21 -53 2 N ATOM 1475 CA PRO A 191 6.813 36.283 26.287 1.00 11.41 C ANISOU 1475 CA PRO A 191 1448 1434 1454 -10 -11 -15 C ATOM 1476 C PRO A 191 6.450 37.523 25.461 1.00 11.50 C ANISOU 1476 C PRO A 191 1445 1450 1472 -10 -8 -5 C ATOM 1477 O PRO A 191 5.280 37.698 25.105 1.00 11.67 O ANISOU 1477 O PRO A 191 1464 1464 1504 -8 -30 -7 O ATOM 1478 CB PRO A 191 6.926 36.636 27.772 1.00 11.58 C ANISOU 1478 CB PRO A 191 1465 1469 1465 -15 -20 -11 C ATOM 1479 CG PRO A 191 7.883 35.650 28.312 1.00 11.80 C ANISOU 1479 CG PRO A 191 1495 1492 1496 -20 -13 15 C ATOM 1480 CD PRO A 191 8.882 35.410 27.223 1.00 11.30 C ANISOU 1480 CD PRO A 191 1442 1414 1435 -10 -40 -2 C ATOM 1481 N GLU A 192 7.441 38.352 25.129 1.00 11.73 N ANISOU 1481 N GLU A 192 1463 1481 1514 0 -9 -10 N ATOM 1482 CA AGLU A 192 7.157 39.584 24.388 0.50 11.70 C ANISOU 1482 CA AGLU A 192 1454 1479 1511 -5 0 1 C ATOM 1483 CA BGLU A 192 7.228 39.587 24.360 0.50 11.69 C ANISOU 1483 CA BGLU A 192 1454 1477 1509 -8 0 -1 C ATOM 1484 C GLU A 192 6.725 39.296 22.943 1.00 11.42 C ANISOU 1484 C GLU A 192 1414 1436 1487 -7 5 7 C ATOM 1485 O GLU A 192 6.127 40.157 22.295 1.00 11.23 O ANISOU 1485 O GLU A 192 1358 1432 1474 -13 2 28 O ATOM 1486 CB AGLU A 192 8.296 40.631 24.464 0.50 12.04 C ANISOU 1486 CB AGLU A 192 1519 1505 1549 -13 8 2 C ATOM 1487 CB BGLU A 192 8.520 40.419 24.267 0.50 11.97 C ANISOU 1487 CB BGLU A 192 1501 1498 1548 -13 2 4 C ATOM 1488 CG AGLU A 192 9.714 40.145 24.779 0.50 13.22 C ANISOU 1488 CG AGLU A 192 1642 1643 1738 -17 -30 38 C ATOM 1489 CG BGLU A 192 9.352 40.480 25.541 0.50 12.65 C ANISOU 1489 CG BGLU A 192 1590 1593 1622 23 2 -13 C ATOM 1490 CD AGLU A 192 10.434 39.585 23.583 0.50 12.80 C ANISOU 1490 CD AGLU A 192 1466 1787 1610 69 -46 -34 C ATOM 1491 CD BGLU A 192 10.359 39.343 25.628 0.50 14.37 C ANISOU 1491 CD BGLU A 192 1787 1811 1859 22 -125 -78 C ATOM 1492 OE1AGLU A 192 9.818 39.502 22.504 0.50 15.77 O ANISOU 1492 OE1AGLU A 192 1986 1926 2075 -11 23 -8 O ATOM 1493 OE1BGLU A 192 11.367 39.370 24.888 0.50 13.63 O ANISOU 1493 OE1BGLU A 192 1676 1845 1656 -26 103 -32 O ATOM 1494 OE2AGLU A 192 11.627 39.238 23.718 0.50 15.72 O1- ANISOU 1494 OE2AGLU A 192 2058 1958 1954 -73 55 -15 O1- ATOM 1495 OE2BGLU A 192 10.135 38.422 26.436 0.50 13.02 O1- ANISOU 1495 OE2BGLU A 192 1620 1568 1757 -75 23 68 O1- ATOM 1496 N ASP A 193 6.992 38.079 22.460 1.00 10.96 N ANISOU 1496 N ASP A 193 1348 1379 1436 0 5 10 N ATOM 1497 CA ASP A 193 6.561 37.642 21.130 1.00 10.82 C ANISOU 1497 CA ASP A 193 1342 1343 1424 1 19 -8 C ATOM 1498 C ASP A 193 5.265 36.822 21.153 1.00 10.24 C ANISOU 1498 C ASP A 193 1269 1281 1337 15 17 -19 C ATOM 1499 O ASP A 193 4.824 36.339 20.106 1.00 10.26 O ANISOU 1499 O ASP A 193 1252 1313 1333 32 34 -10 O ATOM 1500 CB ASP A 193 7.659 36.793 20.479 1.00 11.15 C ANISOU 1500 CB ASP A 193 1382 1395 1460 0 21 -13 C ATOM 1501 CG ASP A 193 8.927 37.573 20.220 1.00 12.22 C ANISOU 1501 CG ASP A 193 1471 1519 1654 -26 23 -16 C ATOM 1502 OD1 ASP A 193 8.835 38.782 19.913 1.00 14.28 O ANISOU 1502 OD1 ASP A 193 1717 1693 2015 10 107 66 O ATOM 1503 OD2 ASP A 193 10.016 36.966 20.308 1.00 13.95 O1- ANISOU 1503 OD2 ASP A 193 1560 1705 2036 -7 73 -19 O1- ATOM 1504 N LEU A 194 4.652 36.677 22.327 1.00 9.76 N ANISOU 1504 N LEU A 194 1222 1188 1297 20 0 -26 N ATOM 1505 CA LEU A 194 3.532 35.755 22.499 1.00 9.48 C ANISOU 1505 CA LEU A 194 1190 1172 1237 17 -10 -26 C ATOM 1506 C LEU A 194 2.317 36.437 23.111 1.00 9.68 C ANISOU 1506 C LEU A 194 1218 1194 1263 18 -7 -31 C ATOM 1507 O LEU A 194 1.247 36.465 22.510 1.00 9.59 O ANISOU 1507 O LEU A 194 1211 1135 1297 51 -14 -54 O ATOM 1508 CB LEU A 194 3.972 34.573 23.366 1.00 9.15 C ANISOU 1508 CB LEU A 194 1148 1130 1195 -9 -27 -28 C ATOM 1509 CG LEU A 194 5.024 33.675 22.713 1.00 8.34 C ANISOU 1509 CG LEU A 194 1039 1077 1051 -59 -40 -57 C ATOM 1510 CD1 LEU A 194 5.688 32.776 23.745 1.00 8.11 C ANISOU 1510 CD1 LEU A 194 1037 953 1089 -57 -13 -57 C ATOM 1511 CD2 LEU A 194 4.400 32.847 21.594 1.00 8.41 C ANISOU 1511 CD2 LEU A 194 1083 1063 1049 -4 -67 -108 C ATOM 1512 N GLY A 195 2.483 36.981 24.309 1.00 10.15 N ANISOU 1512 N GLY A 195 1265 1272 1317 35 -10 -38 N ATOM 1513 CA GLY A 195 1.390 37.653 24.994 1.00 10.55 C ANISOU 1513 CA GLY A 195 1342 1314 1354 32 4 -28 C ATOM 1514 C GLY A 195 1.405 37.393 26.482 1.00 11.08 C ANISOU 1514 C GLY A 195 1423 1386 1400 41 5 -35 C ATOM 1515 O GLY A 195 2.383 36.869 27.024 1.00 11.37 O ANISOU 1515 O GLY A 195 1507 1411 1400 57 2 -50 O ATOM 1516 N ASP A 196 0.296 37.747 27.126 1.00 11.56 N ANISOU 1516 N ASP A 196 1484 1431 1477 34 34 -31 N ATOM 1517 CA ASP A 196 0.185 37.731 28.577 1.00 11.91 C ANISOU 1517 CA ASP A 196 1529 1472 1522 26 18 -28 C ATOM 1518 C ASP A 196 -0.884 36.752 29.038 1.00 12.13 C ANISOU 1518 C ASP A 196 1540 1505 1563 26 27 -31 C ATOM 1519 O ASP A 196 -1.733 36.324 28.253 1.00 12.30 O ANISOU 1519 O ASP A 196 1548 1537 1588 64 38 -28 O ATOM 1520 CB ASP A 196 -0.166 39.133 29.074 1.00 12.13 C ANISOU 1520 CB ASP A 196 1554 1496 1555 23 30 -38 C ATOM 1521 CG ASP A 196 0.812 40.178 28.590 1.00 12.76 C ANISOU 1521 CG ASP A 196 1683 1535 1626 0 28 -64 C ATOM 1522 OD1 ASP A 196 2.014 40.054 28.900 1.00 13.57 O ANISOU 1522 OD1 ASP A 196 1782 1547 1827 -5 -19 -72 O ATOM 1523 OD2 ASP A 196 0.380 41.120 27.896 1.00 14.59 O1- ANISOU 1523 OD2 ASP A 196 1975 1755 1810 -16 -28 -15 O1- ATOM 1524 N ASP A 197 -0.829 36.409 30.323 1.00 12.49 N ANISOU 1524 N ASP A 197 1586 1560 1597 11 20 -27 N ATOM 1525 CA ASP A 197 -1.846 35.576 30.969 1.00 13.04 C ANISOU 1525 CA ASP A 197 1658 1626 1670 -5 28 -33 C ATOM 1526 C ASP A 197 -1.882 34.165 30.388 1.00 12.42 C ANISOU 1526 C ASP A 197 1555 1561 1603 -2 35 -39 C ATOM 1527 O ASP A 197 -2.929 33.513 30.400 1.00 12.99 O ANISOU 1527 O ASP A 197 1592 1638 1702 10 97 -70 O ATOM 1528 CB ASP A 197 -3.238 36.220 30.854 1.00 13.79 C ANISOU 1528 CB ASP A 197 1743 1727 1767 1 28 -23 C ATOM 1529 CG ASP A 197 -3.259 37.666 31.312 1.00 16.00 C ANISOU 1529 CG ASP A 197 2066 1942 2070 -7 25 -37 C ATOM 1530 OD1 ASP A 197 -2.988 37.911 32.507 1.00 19.24 O ANISOU 1530 OD1 ASP A 197 2544 2445 2319 -20 -10 -89 O ATOM 1531 OD2 ASP A 197 -3.561 38.555 30.483 1.00 18.83 O1- ANISOU 1531 OD2 ASP A 197 2463 2316 2375 47 -14 47 O1- ATOM 1532 N ILE A 198 -0.738 33.701 29.883 1.00 11.67 N ANISOU 1532 N ILE A 198 1469 1468 1495 2 26 -40 N ATOM 1533 CA ILE A 198 -0.627 32.369 29.287 1.00 11.11 C ANISOU 1533 CA ILE A 198 1396 1418 1406 -8 18 -23 C ATOM 1534 C ILE A 198 0.630 31.650 29.762 1.00 10.33 C ANISOU 1534 C ILE A 198 1303 1318 1303 -17 17 -36 C ATOM 1535 O ILE A 198 1.617 32.279 30.154 1.00 10.27 O ANISOU 1535 O ILE A 198 1252 1333 1314 -30 22 -47 O ATOM 1536 CB ILE A 198 -0.595 32.422 27.736 1.00 11.19 C ANISOU 1536 CB ILE A 198 1413 1434 1403 16 5 -7 C ATOM 1537 CG1 ILE A 198 0.568 33.285 27.236 1.00 11.38 C ANISOU 1537 CG1 ILE A 198 1408 1514 1401 33 15 -11 C ATOM 1538 CG2 ILE A 198 -1.914 32.954 27.184 1.00 11.32 C ANISOU 1538 CG2 ILE A 198 1434 1470 1396 34 -13 -5 C ATOM 1539 CD1 ILE A 198 0.917 33.036 25.783 1.00 12.02 C ANISOU 1539 CD1 ILE A 198 1558 1596 1409 69 37 -19 C ATOM 1540 N VAL A 199 0.591 30.324 29.715 1.00 9.52 N ANISOU 1540 N VAL A 199 1188 1222 1205 -10 10 -26 N ATOM 1541 CA VAL A 199 1.776 29.527 29.964 1.00 9.13 C ANISOU 1541 CA VAL A 199 1148 1164 1157 -10 0 -25 C ATOM 1542 C VAL A 199 2.673 29.609 28.733 1.00 8.89 C ANISOU 1542 C VAL A 199 1109 1144 1124 -5 -9 -15 C ATOM 1543 O VAL A 199 2.193 29.538 27.596 1.00 8.34 O ANISOU 1543 O VAL A 199 1038 1088 1040 20 13 -39 O ATOM 1544 CB VAL A 199 1.431 28.063 30.273 1.00 9.13 C ANISOU 1544 CB VAL A 199 1140 1155 1172 7 5 -22 C ATOM 1545 CG1 VAL A 199 2.704 27.225 30.384 1.00 9.20 C ANISOU 1545 CG1 VAL A 199 1196 1098 1200 39 -22 -5 C ATOM 1546 CG2 VAL A 199 0.609 27.977 31.554 1.00 9.04 C ANISOU 1546 CG2 VAL A 199 1126 1186 1122 17 -14 -17 C ATOM 1547 N ILE A 200 3.973 29.766 28.973 1.00 8.63 N ANISOU 1547 N ILE A 200 1049 1130 1097 4 -7 -26 N ATOM 1548 CA ILE A 200 4.959 29.919 27.909 1.00 8.66 C ANISOU 1548 CA ILE A 200 1075 1136 1080 5 -11 -14 C ATOM 1549 C ILE A 200 6.154 29.006 28.161 1.00 8.51 C ANISOU 1549 C ILE A 200 1058 1125 1049 17 -11 -23 C ATOM 1550 O ILE A 200 6.667 28.950 29.277 1.00 8.94 O ANISOU 1550 O ILE A 200 1130 1224 1042 53 -31 -59 O ATOM 1551 CB ILE A 200 5.456 31.375 27.821 1.00 8.83 C ANISOU 1551 CB ILE A 200 1094 1138 1120 15 18 -15 C ATOM 1552 CG1 ILE A 200 4.318 32.299 27.375 1.00 9.42 C ANISOU 1552 CG1 ILE A 200 1141 1189 1248 26 -4 -2 C ATOM 1553 CG2 ILE A 200 6.633 31.486 26.856 1.00 9.41 C ANISOU 1553 CG2 ILE A 200 1156 1212 1207 -8 83 -2 C ATOM 1554 CD1 ILE A 200 4.644 33.770 27.481 1.00 10.72 C ANISOU 1554 CD1 ILE A 200 1355 1274 1441 2 30 -43 C ATOM 1555 N VAL A 201 6.583 28.293 27.120 1.00 8.10 N ANISOU 1555 N VAL A 201 1003 1063 1010 27 -27 -19 N ATOM 1556 CA VAL A 201 7.787 27.462 27.170 1.00 8.09 C ANISOU 1556 CA VAL A 201 995 1046 1030 -2 -1 -20 C ATOM 1557 C VAL A 201 8.846 28.067 26.243 1.00 7.77 C ANISOU 1557 C VAL A 201 969 993 987 -2 -14 -35 C ATOM 1558 O VAL A 201 8.515 28.672 25.233 1.00 7.53 O ANISOU 1558 O VAL A 201 945 934 979 -37 -8 -33 O ATOM 1559 CB VAL A 201 7.494 25.998 26.777 1.00 8.14 C ANISOU 1559 CB VAL A 201 992 1042 1056 4 5 5 C ATOM 1560 CG1 VAL A 201 6.473 25.382 27.731 1.00 8.59 C ANISOU 1560 CG1 VAL A 201 1114 1069 1078 -31 11 38 C ATOM 1561 CG2 VAL A 201 7.015 25.899 25.331 1.00 8.41 C ANISOU 1561 CG2 VAL A 201 1057 1042 1095 21 -7 -17 C ATOM 1562 N PRO A 202 10.130 27.933 26.599 1.00 7.79 N ANISOU 1562 N PRO A 202 966 999 990 2 -23 -27 N ATOM 1563 CA PRO A 202 11.159 28.588 25.790 1.00 7.65 C ANISOU 1563 CA PRO A 202 950 1000 954 -2 -26 -28 C ATOM 1564 C PRO A 202 11.415 27.912 24.441 1.00 7.23 C ANISOU 1564 C PRO A 202 884 950 913 -1 -11 -21 C ATOM 1565 O PRO A 202 11.848 28.573 23.499 1.00 7.65 O ANISOU 1565 O PRO A 202 950 1009 946 -18 1 -43 O ATOM 1566 CB PRO A 202 12.406 28.518 26.679 1.00 7.81 C ANISOU 1566 CB PRO A 202 938 1026 1001 -15 -44 -38 C ATOM 1567 CG PRO A 202 12.159 27.414 27.615 1.00 8.51 C ANISOU 1567 CG PRO A 202 1038 1137 1058 -2 -41 -15 C ATOM 1568 CD PRO A 202 10.679 27.353 27.835 1.00 7.85 C ANISOU 1568 CD PRO A 202 998 1001 980 1 -28 -18 C ATOM 1569 N ASP A 203 11.157 26.610 24.364 1.00 7.05 N ANISOU 1569 N ASP A 203 859 943 874 7 1 -17 N ATOM 1570 CA ASP A 203 11.291 25.861 23.120 1.00 6.91 C ANISOU 1570 CA ASP A 203 858 890 876 4 -26 -11 C ATOM 1571 C ASP A 203 10.395 24.626 23.161 1.00 6.49 C ANISOU 1571 C ASP A 203 816 846 803 -8 -2 -14 C ATOM 1572 O ASP A 203 9.849 24.274 24.213 1.00 6.21 O ANISOU 1572 O ASP A 203 763 854 740 -4 11 -57 O ATOM 1573 CB ASP A 203 12.759 25.495 22.854 1.00 7.25 C ANISOU 1573 CB ASP A 203 883 932 938 -14 -22 -17 C ATOM 1574 CG ASP A 203 13.344 24.578 23.903 1.00 8.07 C ANISOU 1574 CG ASP A 203 990 1056 1019 9 -33 -33 C ATOM 1575 OD1 ASP A 203 12.855 23.438 24.051 1.00 8.59 O ANISOU 1575 OD1 ASP A 203 946 1123 1193 44 -79 61 O ATOM 1576 OD2 ASP A 203 14.322 24.992 24.562 1.00 10.29 O1- ANISOU 1576 OD2 ASP A 203 1189 1424 1295 27 -166 -75 O1- ATOM 1577 N THR A 204 10.248 23.968 22.014 1.00 5.84 N ANISOU 1577 N THR A 204 727 765 724 -8 4 -27 N ATOM 1578 CA THR A 204 9.275 22.878 21.878 1.00 5.99 C ANISOU 1578 CA THR A 204 753 769 753 -7 9 -9 C ATOM 1579 C THR A 204 9.655 21.586 22.613 1.00 6.35 C ANISOU 1579 C THR A 204 793 819 796 -1 2 -14 C ATOM 1580 O THR A 204 8.807 20.714 22.772 1.00 6.56 O ANISOU 1580 O THR A 204 887 801 804 -33 -5 7 O ATOM 1581 CB THR A 204 8.965 22.563 20.392 1.00 5.43 C ANISOU 1581 CB THR A 204 678 700 685 2 19 -2 C ATOM 1582 CG2 THR A 204 8.250 23.732 19.731 1.00 5.57 C ANISOU 1582 CG2 THR A 204 687 714 714 57 -33 -5 C ATOM 1583 OG1 THR A 204 10.178 22.282 19.682 1.00 5.71 O ANISOU 1583 OG1 THR A 204 683 794 693 -25 41 -35 O ATOM 1584 N SER A 205 10.897 21.459 23.082 1.00 7.20 N ANISOU 1584 N SER A 205 902 922 908 2 -1 -10 N ATOM 1585 CA SER A 205 11.266 20.296 23.899 1.00 7.77 C ANISOU 1585 CA SER A 205 987 983 981 28 -17 -14 C ATOM 1586 C SER A 205 10.455 20.234 25.203 1.00 7.95 C ANISOU 1586 C SER A 205 1014 1004 999 23 -16 -1 C ATOM 1587 O SER A 205 10.328 19.171 25.812 1.00 8.60 O ANISOU 1587 O SER A 205 1145 1036 1086 45 -11 -14 O ATOM 1588 CB SER A 205 12.773 20.266 24.196 1.00 7.84 C ANISOU 1588 CB SER A 205 989 987 999 51 -11 -5 C ATOM 1589 OG SER A 205 13.131 21.158 25.238 1.00 9.55 O ANISOU 1589 OG SER A 205 1181 1205 1239 76 -79 -74 O ATOM 1590 N HIS A 206 9.897 21.375 25.611 1.00 7.76 N ANISOU 1590 N HIS A 206 993 984 972 19 -23 -22 N ATOM 1591 CA HIS A 206 9.034 21.459 26.794 1.00 8.16 C ANISOU 1591 CA HIS A 206 1025 1057 1015 5 -4 -4 C ATOM 1592 C HIS A 206 7.587 21.034 26.537 1.00 7.81 C ANISOU 1592 C HIS A 206 1001 1003 961 -11 5 -15 C ATOM 1593 O HIS A 206 6.808 20.863 27.478 1.00 8.06 O ANISOU 1593 O HIS A 206 1058 1065 937 5 18 -17 O ATOM 1594 CB HIS A 206 9.017 22.890 27.325 1.00 8.49 C ANISOU 1594 CB HIS A 206 1099 1086 1039 -7 -5 -23 C ATOM 1595 CG HIS A 206 10.303 23.329 27.949 1.00 10.27 C ANISOU 1595 CG HIS A 206 1288 1323 1288 -47 -35 -4 C ATOM 1596 CD2 HIS A 206 10.635 23.533 29.246 1.00 12.09 C ANISOU 1596 CD2 HIS A 206 1538 1649 1404 -30 -30 -25 C ATOM 1597 ND1 HIS A 206 11.419 23.656 27.212 1.00 12.02 N ANISOU 1597 ND1 HIS A 206 1458 1624 1482 -44 -66 -61 N ATOM 1598 CE1 HIS A 206 12.391 24.018 28.031 1.00 12.65 C ANISOU 1598 CE1 HIS A 206 1539 1699 1565 -90 -37 -35 C ATOM 1599 NE2 HIS A 206 11.939 23.957 29.269 1.00 13.86 N ANISOU 1599 NE2 HIS A 206 1710 1845 1709 -105 -44 -27 N ATOM 1600 N TYR A 207 7.209 20.914 25.270 1.00 7.59 N ANISOU 1600 N TYR A 207 963 984 937 0 21 0 N ATOM 1601 CA TYR A 207 5.871 20.458 24.925 1.00 7.71 C ANISOU 1601 CA TYR A 207 1003 974 950 5 15 -1 C ATOM 1602 C TYR A 207 5.800 18.937 25.080 1.00 8.14 C ANISOU 1602 C TYR A 207 1075 1014 1001 19 15 -9 C ATOM 1603 O TYR A 207 6.031 18.192 24.129 1.00 8.89 O ANISOU 1603 O TYR A 207 1249 1070 1056 -4 55 -14 O ATOM 1604 CB TYR A 207 5.518 20.836 23.486 1.00 7.49 C ANISOU 1604 CB TYR A 207 978 927 938 13 -5 0 C ATOM 1605 CG TYR A 207 5.079 22.265 23.195 1.00 6.61 C ANISOU 1605 CG TYR A 207 793 861 855 10 -10 -21 C ATOM 1606 CD1 TYR A 207 4.349 23.030 24.109 1.00 6.54 C ANISOU 1606 CD1 TYR A 207 827 843 814 -23 -17 1 C ATOM 1607 CD2 TYR A 207 5.323 22.816 21.941 1.00 6.53 C ANISOU 1607 CD2 TYR A 207 822 825 834 -1 75 -13 C ATOM 1608 CE1 TYR A 207 3.914 24.325 23.778 1.00 6.30 C ANISOU 1608 CE1 TYR A 207 811 793 789 -28 -15 -57 C ATOM 1609 CE2 TYR A 207 4.897 24.088 21.607 1.00 6.09 C ANISOU 1609 CE2 TYR A 207 714 801 796 -46 92 -4 C ATOM 1610 CZ TYR A 207 4.195 24.842 22.518 1.00 5.90 C ANISOU 1610 CZ TYR A 207 752 702 787 -15 -1 -33 C ATOM 1611 OH TYR A 207 3.776 26.095 22.127 1.00 6.00 O ANISOU 1611 OH TYR A 207 690 707 882 -82 28 -84 O ATOM 1612 N THR A 208 5.473 18.482 26.284 1.00 8.37 N ANISOU 1612 N THR A 208 1108 1032 1040 16 28 0 N ATOM 1613 CA THR A 208 5.258 17.058 26.544 1.00 8.53 C ANISOU 1613 CA THR A 208 1142 1047 1050 18 21 -7 C ATOM 1614 C THR A 208 3.808 16.849 26.944 1.00 8.66 C ANISOU 1614 C THR A 208 1141 1073 1074 11 18 -11 C ATOM 1615 O THR A 208 3.147 17.787 27.402 1.00 8.67 O ANISOU 1615 O THR A 208 1149 1059 1086 39 63 -5 O ATOM 1616 CB THR A 208 6.163 16.540 27.671 1.00 8.53 C ANISOU 1616 CB THR A 208 1119 1046 1075 8 11 -5 C ATOM 1617 CG2 THR A 208 7.631 16.847 27.382 1.00 8.73 C ANISOU 1617 CG2 THR A 208 1132 1098 1086 23 -9 -2 C ATOM 1618 OG1 THR A 208 5.777 17.150 28.908 1.00 9.19 O ANISOU 1618 OG1 THR A 208 1227 1194 1070 40 52 0 O ATOM 1619 N LEU A 209 3.305 15.629 26.780 1.00 9.12 N ANISOU 1619 N LEU A 209 1202 1123 1141 20 16 5 N ATOM 1620 CA LEU A 209 1.932 15.333 27.176 1.00 9.48 C ANISOU 1620 CA LEU A 209 1223 1186 1191 -1 16 7 C ATOM 1621 C LEU A 209 1.754 15.600 28.668 1.00 9.82 C ANISOU 1621 C LEU A 209 1268 1222 1240 -20 20 0 C ATOM 1622 O LEU A 209 0.763 16.189 29.081 1.00 9.53 O ANISOU 1622 O LEU A 209 1228 1169 1223 -19 56 -10 O ATOM 1623 CB LEU A 209 1.541 13.888 26.838 1.00 9.79 C ANISOU 1623 CB LEU A 209 1256 1234 1227 -1 14 -5 C ATOM 1624 CG LEU A 209 0.107 13.473 27.213 1.00 10.26 C ANISOU 1624 CG LEU A 209 1300 1275 1321 -5 38 -2 C ATOM 1625 CD1 LEU A 209 -0.932 14.425 26.621 1.00 11.62 C ANISOU 1625 CD1 LEU A 209 1383 1495 1534 16 -10 8 C ATOM 1626 CD2 LEU A 209 -0.175 12.042 26.783 1.00 11.61 C ANISOU 1626 CD2 LEU A 209 1472 1380 1557 -45 41 -33 C ATOM 1627 N GLU A 210 2.731 15.173 29.463 1.00 10.09 N ANISOU 1627 N GLU A 210 1293 1256 1282 -7 16 9 N ATOM 1628 CA GLU A 210 2.722 15.405 30.907 1.00 10.65 C ANISOU 1628 CA GLU A 210 1390 1337 1318 -2 13 1 C ATOM 1629 C GLU A 210 2.552 16.890 31.241 1.00 9.89 C ANISOU 1629 C GLU A 210 1281 1255 1222 1 5 9 C ATOM 1630 O GLU A 210 1.744 17.245 32.098 1.00 9.72 O ANISOU 1630 O GLU A 210 1318 1217 1159 -9 9 2 O ATOM 1631 CB GLU A 210 4.018 14.873 31.531 1.00 11.48 C ANISOU 1631 CB GLU A 210 1469 1455 1436 5 -2 17 C ATOM 1632 CG GLU A 210 4.135 15.063 33.043 1.00 14.18 C ANISOU 1632 CG GLU A 210 1870 1820 1697 -11 14 -2 C ATOM 1633 CD GLU A 210 5.408 14.458 33.624 1.00 17.88 C ANISOU 1633 CD GLU A 210 2208 2323 2263 52 -49 25 C ATOM 1634 OE1 GLU A 210 6.391 14.267 32.873 1.00 19.67 O ANISOU 1634 OE1 GLU A 210 2421 2640 2410 56 61 17 O ATOM 1635 OE2 GLU A 210 5.429 14.179 34.843 1.00 20.81 O1- ANISOU 1635 OE2 GLU A 210 2764 2718 2423 -2 -4 71 O1- ATOM 1636 N PHE A 211 3.313 17.750 30.565 1.00 9.37 N ANISOU 1636 N PHE A 211 1212 1189 1156 7 5 -4 N ATOM 1637 CA PHE A 211 3.255 19.186 30.828 1.00 9.29 C ANISOU 1637 CA PHE A 211 1189 1179 1158 21 10 -2 C ATOM 1638 C PHE A 211 1.911 19.780 30.399 1.00 8.91 C ANISOU 1638 C PHE A 211 1137 1128 1117 21 22 -19 C ATOM 1639 O PHE A 211 1.322 20.573 31.138 1.00 9.01 O ANISOU 1639 O PHE A 211 1133 1131 1159 66 70 -45 O ATOM 1640 CB PHE A 211 4.410 19.922 30.144 1.00 9.27 C ANISOU 1640 CB PHE A 211 1172 1172 1177 25 -11 -9 C ATOM 1641 CG PHE A 211 4.470 21.391 30.474 1.00 9.77 C ANISOU 1641 CG PHE A 211 1230 1220 1260 43 -13 -13 C ATOM 1642 CD1 PHE A 211 4.743 21.814 31.767 1.00 9.89 C ANISOU 1642 CD1 PHE A 211 1245 1237 1275 33 -50 22 C ATOM 1643 CD2 PHE A 211 4.245 22.349 29.495 1.00 9.60 C ANISOU 1643 CD2 PHE A 211 1188 1227 1232 5 45 1 C ATOM 1644 CE1 PHE A 211 4.796 23.170 32.077 1.00 9.92 C ANISOU 1644 CE1 PHE A 211 1254 1275 1238 30 -67 -21 C ATOM 1645 CE2 PHE A 211 4.294 23.707 29.801 1.00 9.80 C ANISOU 1645 CE2 PHE A 211 1208 1231 1283 2 33 13 C ATOM 1646 CZ PHE A 211 4.579 24.113 31.090 1.00 9.60 C ANISOU 1646 CZ PHE A 211 1190 1176 1282 -22 1 1 C ATOM 1647 N LEU A 212 1.424 19.400 29.219 1.00 8.69 N ANISOU 1647 N LEU A 212 1112 1100 1088 20 28 -7 N ATOM 1648 CA LEU A 212 0.113 19.862 28.744 1.00 8.56 C ANISOU 1648 CA LEU A 212 1100 1083 1069 2 13 -15 C ATOM 1649 C LEU A 212 -1.005 19.496 29.727 1.00 8.97 C ANISOU 1649 C LEU A 212 1143 1148 1115 9 16 -14 C ATOM 1650 O LEU A 212 -1.894 20.307 29.992 1.00 8.43 O ANISOU 1650 O LEU A 212 1086 1076 1038 8 13 5 O ATOM 1651 CB LEU A 212 -0.199 19.314 27.342 1.00 8.51 C ANISOU 1651 CB LEU A 212 1090 1069 1072 0 10 -5 C ATOM 1652 CG LEU A 212 0.247 20.182 26.155 1.00 8.44 C ANISOU 1652 CG LEU A 212 1095 1070 1040 10 8 -14 C ATOM 1653 CD1 LEU A 212 1.747 20.435 26.151 1.00 8.91 C ANISOU 1653 CD1 LEU A 212 1121 1116 1146 5 -51 7 C ATOM 1654 CD2 LEU A 212 -0.194 19.550 24.843 1.00 8.89 C ANISOU 1654 CD2 LEU A 212 1210 1148 1019 25 27 -33 C ATOM 1655 N LYS A 213 -0.941 18.283 30.272 1.00 9.56 N ANISOU 1655 N LYS A 213 1209 1218 1206 11 33 -10 N ATOM 1656 CA LYS A 213 -1.911 17.824 31.270 1.00 10.36 C ANISOU 1656 CA LYS A 213 1321 1325 1288 5 28 7 C ATOM 1657 C LYS A 213 -1.859 18.657 32.546 1.00 10.49 C ANISOU 1657 C LYS A 213 1333 1342 1308 17 23 7 C ATOM 1658 O LYS A 213 -2.900 19.024 33.099 1.00 10.48 O ANISOU 1658 O LYS A 213 1340 1365 1276 22 35 -4 O ATOM 1659 CB LYS A 213 -1.670 16.350 31.613 1.00 10.71 C ANISOU 1659 CB LYS A 213 1351 1356 1360 20 42 17 C ATOM 1660 CG LYS A 213 -2.130 15.378 30.552 1.00 12.39 C ANISOU 1660 CG LYS A 213 1552 1617 1537 -16 21 -4 C ATOM 1661 CD LYS A 213 -1.962 13.940 31.024 1.00 15.26 C ANISOU 1661 CD LYS A 213 1954 1870 1971 34 18 36 C ATOM 1662 CE LYS A 213 -2.600 12.946 30.069 1.00 16.86 C ANISOU 1662 CE LYS A 213 2147 2109 2150 -15 5 -5 C ATOM 1663 NZ LYS A 213 -2.845 11.631 30.715 1.00 18.83 N1+ ANISOU 1663 NZ LYS A 213 2469 2253 2429 -31 30 33 N1+ ATOM 1664 N GLU A 214 -0.645 18.950 33.006 1.00 10.73 N ANISOU 1664 N GLU A 214 1373 1370 1333 2 14 -14 N ATOM 1665 CA GLU A 214 -0.449 19.773 34.200 1.00 11.07 C ANISOU 1665 CA GLU A 214 1422 1419 1364 7 11 -21 C ATOM 1666 C GLU A 214 -0.985 21.187 33.984 1.00 10.50 C ANISOU 1666 C GLU A 214 1348 1358 1283 -9 21 -14 C ATOM 1667 O GLU A 214 -1.721 21.714 34.819 1.00 10.46 O ANISOU 1667 O GLU A 214 1379 1337 1258 16 18 -40 O ATOM 1668 CB GLU A 214 1.033 19.806 34.596 1.00 11.70 C ANISOU 1668 CB GLU A 214 1482 1507 1453 -9 4 -26 C ATOM 1669 CG GLU A 214 1.561 18.473 35.126 1.00 14.43 C ANISOU 1669 CG GLU A 214 1906 1777 1799 23 15 0 C ATOM 1670 CD GLU A 214 3.081 18.420 35.248 1.00 16.94 C ANISOU 1670 CD GLU A 214 2117 2089 2229 -2 -55 75 C ATOM 1671 OE1 GLU A 214 3.761 19.411 34.896 1.00 20.60 O ANISOU 1671 OE1 GLU A 214 2611 2617 2597 -41 -46 -14 O ATOM 1672 OE2 GLU A 214 3.600 17.371 35.695 1.00 20.43 O1- ANISOU 1672 OE2 GLU A 214 2591 2569 2601 59 -22 5 O1- ATOM 1673 N VAL A 215 -0.634 21.788 32.850 1.00 9.90 N ANISOU 1673 N VAL A 215 1256 1291 1215 -11 11 -23 N ATOM 1674 CA VAL A 215 -1.121 23.120 32.504 1.00 9.82 C ANISOU 1674 CA VAL A 215 1239 1278 1213 -16 5 -28 C ATOM 1675 C VAL A 215 -2.649 23.141 32.380 1.00 9.88 C ANISOU 1675 C VAL A 215 1246 1281 1227 -4 28 -23 C ATOM 1676 O VAL A 215 -3.305 24.061 32.869 1.00 9.57 O ANISOU 1676 O VAL A 215 1200 1261 1172 5 57 -56 O ATOM 1677 CB VAL A 215 -0.476 23.627 31.192 1.00 9.58 C ANISOU 1677 CB VAL A 215 1187 1245 1205 -30 5 -23 C ATOM 1678 CG1 VAL A 215 -1.185 24.875 30.681 1.00 9.63 C ANISOU 1678 CG1 VAL A 215 1199 1238 1221 -69 -27 -11 C ATOM 1679 CG2 VAL A 215 1.019 23.892 31.404 1.00 10.27 C ANISOU 1679 CG2 VAL A 215 1238 1342 1320 -44 -49 -30 C ATOM 1680 N TRP A 216 -3.218 22.123 31.741 1.00 10.03 N ANISOU 1680 N TRP A 216 1259 1320 1229 2 36 -34 N ATOM 1681 CA TRP A 216 -4.669 22.028 31.621 1.00 10.58 C ANISOU 1681 CA TRP A 216 1331 1368 1319 5 14 -27 C ATOM 1682 C TRP A 216 -5.335 22.112 32.994 1.00 11.39 C ANISOU 1682 C TRP A 216 1439 1480 1406 8 26 -27 C ATOM 1683 O TRP A 216 -6.233 22.927 33.206 1.00 11.61 O ANISOU 1683 O TRP A 216 1458 1519 1432 39 33 -40 O ATOM 1684 CB TRP A 216 -5.081 20.731 30.928 1.00 10.35 C ANISOU 1684 CB TRP A 216 1298 1338 1295 0 5 -26 C ATOM 1685 CG TRP A 216 -6.550 20.671 30.664 1.00 9.98 C ANISOU 1685 CG TRP A 216 1253 1275 1265 26 21 -17 C ATOM 1686 CD1 TRP A 216 -7.486 19.980 31.376 1.00 9.89 C ANISOU 1686 CD1 TRP A 216 1240 1239 1278 46 -4 -10 C ATOM 1687 CD2 TRP A 216 -7.255 21.352 29.624 1.00 9.55 C ANISOU 1687 CD2 TRP A 216 1178 1189 1260 36 23 -64 C ATOM 1688 CE2 TRP A 216 -8.619 21.020 29.757 1.00 9.99 C ANISOU 1688 CE2 TRP A 216 1248 1279 1266 23 8 -55 C ATOM 1689 CE3 TRP A 216 -6.865 22.209 28.587 1.00 9.90 C ANISOU 1689 CE3 TRP A 216 1254 1312 1194 37 -7 -63 C ATOM 1690 NE1 TRP A 216 -8.734 20.180 30.834 1.00 10.64 N ANISOU 1690 NE1 TRP A 216 1285 1388 1368 -5 -15 -32 N ATOM 1691 CZ2 TRP A 216 -9.596 21.510 28.886 1.00 10.01 C ANISOU 1691 CZ2 TRP A 216 1190 1327 1287 50 27 -64 C ATOM 1692 CZ3 TRP A 216 -7.838 22.702 27.727 1.00 9.87 C ANISOU 1692 CZ3 TRP A 216 1222 1308 1220 64 23 -51 C ATOM 1693 CH2 TRP A 216 -9.187 22.350 27.884 1.00 10.33 C ANISOU 1693 CH2 TRP A 216 1285 1315 1322 21 0 -50 C ATOM 1694 N LEU A 217 -4.876 21.283 33.926 1.00 12.20 N ANISOU 1694 N LEU A 217 1547 1584 1503 9 25 -21 N ATOM 1695 CA LEU A 217 -5.453 21.242 35.273 1.00 13.13 C ANISOU 1695 CA LEU A 217 1666 1707 1613 0 36 -19 C ATOM 1696 C LEU A 217 -5.288 22.572 36.012 1.00 13.59 C ANISOU 1696 C LEU A 217 1721 1778 1661 5 28 -33 C ATOM 1697 O LEU A 217 -6.185 22.993 36.741 1.00 13.66 O ANISOU 1697 O LEU A 217 1734 1821 1631 25 45 -63 O ATOM 1698 CB LEU A 217 -4.836 20.097 36.081 1.00 13.50 C ANISOU 1698 CB LEU A 217 1719 1751 1658 2 39 -9 C ATOM 1699 CG LEU A 217 -5.222 18.685 35.636 1.00 14.73 C ANISOU 1699 CG LEU A 217 1870 1884 1841 1 22 -27 C ATOM 1700 CD1 LEU A 217 -4.398 17.639 36.381 1.00 16.04 C ANISOU 1700 CD1 LEU A 217 2072 2051 1969 34 -14 44 C ATOM 1701 CD2 LEU A 217 -6.713 18.433 35.822 1.00 15.49 C ANISOU 1701 CD2 LEU A 217 1955 2009 1921 -11 45 -40 C ATOM 1702 N GLN A 218 -4.152 23.235 35.806 1.00 14.18 N ANISOU 1702 N GLN A 218 1800 1830 1756 -2 37 -37 N ATOM 1703 CA GLN A 218 -3.898 24.558 36.391 1.00 14.78 C ANISOU 1703 CA GLN A 218 1879 1901 1835 -13 18 -44 C ATOM 1704 C GLN A 218 -4.876 25.630 35.914 1.00 15.26 C ANISOU 1704 C GLN A 218 1939 1947 1910 1 28 -47 C ATOM 1705 O GLN A 218 -5.110 26.616 36.620 1.00 15.60 O ANISOU 1705 O GLN A 218 1976 2012 1938 10 23 -92 O ATOM 1706 CB GLN A 218 -2.475 25.019 36.066 1.00 14.98 C ANISOU 1706 CB GLN A 218 1898 1923 1868 -7 26 -51 C ATOM 1707 CG GLN A 218 -1.404 24.281 36.823 1.00 15.83 C ANISOU 1707 CG GLN A 218 1997 2038 1979 5 21 -38 C ATOM 1708 CD GLN A 218 -0.007 24.590 36.316 1.00 16.52 C ANISOU 1708 CD GLN A 218 2026 2099 2149 -42 19 -23 C ATOM 1709 NE2 GLN A 218 0.950 23.746 36.673 1.00 17.21 N ANISOU 1709 NE2 GLN A 218 2095 2151 2291 -27 8 -16 N ATOM 1710 OE1 GLN A 218 0.207 25.576 35.608 1.00 18.45 O ANISOU 1710 OE1 GLN A 218 2268 2287 2454 23 66 57 O ATOM 1711 N LYS A 219 -5.434 25.445 34.718 1.00 15.65 N ANISOU 1711 N LYS A 219 1994 2014 1938 -2 23 -45 N ATOM 1712 CA LYS A 219 -6.321 26.434 34.104 1.00 16.27 C ANISOU 1712 CA LYS A 219 2073 2077 2029 5 23 -26 C ATOM 1713 C LYS A 219 -7.803 26.031 34.143 1.00 17.03 C ANISOU 1713 C LYS A 219 2151 2175 2142 8 9 -37 C ATOM 1714 O LYS A 219 -8.623 26.609 33.421 1.00 17.06 O ANISOU 1714 O LYS A 219 2168 2156 2155 17 43 -41 O ATOM 1715 CB LYS A 219 -5.872 26.708 32.662 1.00 16.24 C ANISOU 1715 CB LYS A 219 2071 2078 2020 2 10 -25 C ATOM 1716 CG LYS A 219 -4.469 27.295 32.553 1.00 16.60 C ANISOU 1716 CG LYS A 219 2097 2117 2090 11 20 -14 C ATOM 1717 CD LYS A 219 -4.383 28.685 33.168 1.00 16.92 C ANISOU 1717 CD LYS A 219 2123 2155 2151 -11 9 -18 C ATOM 1718 CE LYS A 219 -3.065 29.366 32.826 1.00 17.17 C ANISOU 1718 CE LYS A 219 2130 2214 2177 -21 4 -13 C ATOM 1719 NZ LYS A 219 -2.927 30.684 33.505 1.00 18.17 N1+ ANISOU 1719 NZ LYS A 219 2286 2283 2334 -32 4 -22 N1+ ATOM 1720 N GLN A 220 -8.127 25.038 34.975 1.00 17.83 N ANISOU 1720 N GLN A 220 2256 2271 2248 11 19 -23 N ATOM 1721 CA AGLN A 220 -9.518 24.662 35.216 0.50 18.25 C ANISOU 1721 CA AGLN A 220 2303 2327 2305 5 10 -11 C ATOM 1722 CA BGLN A 220 -9.512 24.627 35.239 0.50 18.39 C ANISOU 1722 CA BGLN A 220 2318 2351 2319 5 9 -7 C ATOM 1723 C GLN A 220 -9.963 25.193 36.577 1.00 18.98 C ANISOU 1723 C GLN A 220 2403 2428 2380 9 9 -17 C ATOM 1724 O GLN A 220 -9.179 25.237 37.526 1.00 19.20 O ANISOU 1724 O GLN A 220 2416 2481 2398 20 16 -27 O ATOM 1725 CB AGLN A 220 -9.692 23.143 35.141 0.50 18.11 C ANISOU 1725 CB AGLN A 220 2290 2313 2276 1 13 -10 C ATOM 1726 CB BGLN A 220 -9.638 23.102 35.307 0.50 18.60 C ANISOU 1726 CB BGLN A 220 2378 2352 2334 2 5 -18 C ATOM 1727 CG AGLN A 220 -9.609 22.585 33.724 0.50 17.48 C ANISOU 1727 CG AGLN A 220 2182 2240 2220 5 -7 2 C ATOM 1728 CG BGLN A 220 -9.295 22.370 34.033 0.50 19.46 C ANISOU 1728 CG BGLN A 220 2458 2419 2514 -43 63 -86 C ATOM 1729 CD AGLN A 220 -10.843 22.895 32.894 0.50 17.73 C ANISOU 1729 CD AGLN A 220 2259 2213 2263 38 0 -64 C ATOM 1730 CD BGLN A 220 -9.829 23.061 32.805 0.50 14.53 C ANISOU 1730 CD BGLN A 220 1279 2459 1780 23 376 344 C ATOM 1731 NE2AGLN A 220 -10.653 23.633 31.803 0.50 16.12 N ANISOU 1731 NE2AGLN A 220 2016 2065 2044 -5 30 15 N ATOM 1732 NE2BGLN A 220 -11.138 23.273 32.763 0.50 21.26 N ANISOU 1732 NE2BGLN A 220 3256 2423 2398 -182 4 -49 N ATOM 1733 OE1AGLN A 220 -11.951 22.468 33.223 0.50 16.79 O ANISOU 1733 OE1AGLN A 220 2064 2147 2167 -46 41 0 O ATOM 1734 OE1BGLN A 220 -9.072 23.409 31.904 0.50 22.95 O ANISOU 1734 OE1BGLN A 220 3138 2458 3124 219 -394 -197 O ATOM 1735 N LYS A 221 -11.226 25.607 36.657 1.00 19.91 N ANISOU 1735 N LYS A 221 2506 2541 2515 1 14 -4 N ATOM 1736 CA LYS A 221 -11.812 26.100 37.901 1.00 20.97 C ANISOU 1736 CA LYS A 221 2659 2671 2638 -1 17 -9 C ATOM 1737 C LYS A 221 -13.005 25.225 38.269 1.00 21.33 C ANISOU 1737 C LYS A 221 2700 2723 2680 -11 14 -2 C ATOM 1738 O LYS A 221 -13.667 24.657 37.399 1.00 21.83 O ANISOU 1738 O LYS A 221 2762 2793 2738 -20 7 -2 O ATOM 1739 CB LYS A 221 -12.257 27.556 37.750 1.00 21.18 C ANISOU 1739 CB LYS A 221 2682 2692 2671 14 9 -5 C ATOM 1740 CG LYS A 221 -11.146 28.527 37.356 1.00 22.30 C ANISOU 1740 CG LYS A 221 2814 2817 2838 -1 14 -5 C ATOM 1741 CD LYS A 221 -10.108 28.753 38.456 1.00 23.63 C ANISOU 1741 CD LYS A 221 2980 3014 2980 1 -22 7 C ATOM 1742 CE LYS A 221 -10.662 29.536 39.635 1.00 24.40 C ANISOU 1742 CE LYS A 221 3089 3104 3074 19 4 -16 C ATOM 1743 NZ LYS A 221 -11.360 28.656 40.609 1.00 25.35 N1+ ANISOU 1743 NZ LYS A 221 3187 3196 3246 -20 25 26 N1+ ATOM 1744 OXT LYS A 221 -13.335 25.060 39.442 1.00 21.94 O1- ANISOU 1744 OXT LYS A 221 2787 2813 2735 -23 26 7 O1- TER HETATM 1745 MG MG A1222 3.600 30.193 13.594 1.00 7.70 MG ANISOU 1745 MG MG A1222 792 1022 1110 -159 -31 50 MG HETATM 1746 P AG6P A1223 1.798 29.991 2.520 0.50 12.02 P ANISOU 1746 P AG6P A1223 1722 1494 1348 -56 -2 42 P HETATM 1747 O1PAG6P A1223 2.613 28.669 2.371 0.50 11.94 O ANISOU 1747 O1PAG6P A1223 1637 1555 1342 -5 -51 -2 O HETATM 1748 O2PAG6P A1223 0.181 29.696 2.288 0.50 12.76 O1- ANISOU 1748 O2PAG6P A1223 1729 1649 1468 -63 23 81 O1- HETATM 1749 O3PAG6P A1223 2.278 31.118 1.561 0.50 12.25 O ANISOU 1749 O3PAG6P A1223 1709 1552 1394 -57 4 37 O HETATM 1750 C1 AG6P A1223 2.848 30.848 8.163 0.50 14.95 C ANISOU 1750 C1 AG6P A1223 1892 1913 1874 4 -7 18 C HETATM 1751 O1 AG6P A1223 1.976 31.393 8.984 0.50 14.45 O ANISOU 1751 O1 AG6P A1223 1845 1835 1807 19 -28 11 O HETATM 1752 C2 AG6P A1223 4.254 31.584 8.037 0.50 15.25 C ANISOU 1752 C2 AG6P A1223 1954 1912 1926 -23 2 61 C HETATM 1753 O2 AG6P A1223 4.706 31.885 9.226 0.50 16.28 O ANISOU 1753 O2 AG6P A1223 2014 2082 2087 -47 -50 -2 O HETATM 1754 C3 AG6P A1223 4.123 32.788 7.086 0.50 14.94 C ANISOU 1754 C3 AG6P A1223 1893 1890 1892 -28 -31 55 C HETATM 1755 O3 AG6P A1223 5.406 33.393 6.953 0.50 15.78 O ANISOU 1755 O3 AG6P A1223 1954 2036 2006 -59 -21 47 O HETATM 1756 C4 AG6P A1223 3.489 32.427 5.805 0.50 14.13 C ANISOU 1756 C4 AG6P A1223 1822 1751 1792 -27 -10 61 C HETATM 1757 O4 AG6P A1223 3.355 33.587 4.972 0.50 14.37 O ANISOU 1757 O4 AG6P A1223 1886 1802 1769 -62 -49 125 O HETATM 1758 C5 AG6P A1223 2.100 31.759 5.946 0.50 13.74 C ANISOU 1758 C5 AG6P A1223 1763 1757 1699 15 -4 52 C HETATM 1759 O5 AG6P A1223 2.247 30.578 6.819 0.50 14.24 O ANISOU 1759 O5 AG6P A1223 1850 1777 1782 -13 -8 75 O HETATM 1760 C6 AG6P A1223 1.357 31.429 4.725 0.50 13.21 C ANISOU 1760 C6 AG6P A1223 1678 1661 1678 0 27 -2 C HETATM 1761 O6 AG6P A1223 2.122 30.397 4.028 0.50 12.28 O ANISOU 1761 O6 AG6P A1223 1650 1611 1405 -21 -9 -10 O HETATM 1762 P BBG6 A1224 1.798 29.991 2.520 0.50 12.02 P ANISOU 1762 P BBG6 A1224 1722 1494 1348 -56 -2 42 P HETATM 1763 O1PBBG6 A1224 2.613 28.669 2.371 0.50 11.94 O ANISOU 1763 O1PBBG6 A1224 1637 1555 1342 -5 -51 -2 O HETATM 1764 O2PBBG6 A1224 0.181 29.696 2.288 0.50 12.76 O1- ANISOU 1764 O2PBBG6 A1224 1729 1649 1468 -63 23 81 O1- HETATM 1765 O3PBBG6 A1224 2.278 31.118 1.561 0.50 12.25 O ANISOU 1765 O3PBBG6 A1224 1709 1552 1394 -57 4 37 O HETATM 1766 C1 BBG6 A1224 2.848 30.848 8.163 0.50 14.95 C ANISOU 1766 C1 BBG6 A1224 1892 1913 1874 4 -7 18 C HETATM 1767 O1 BBG6 A1224 2.817 29.678 8.634 0.50 15.03 O ANISOU 1767 O1 BBG6 A1224 1969 1889 1850 -9 15 20 O HETATM 1768 C2 BBG6 A1224 4.254 31.584 8.037 0.50 15.25 C ANISOU 1768 C2 BBG6 A1224 1954 1912 1926 -23 2 61 C HETATM 1769 O2 BBG6 A1224 4.706 31.885 9.226 0.50 16.28 O ANISOU 1769 O2 BBG6 A1224 2014 2082 2087 -47 -50 -2 O HETATM 1770 C3 BBG6 A1224 4.123 32.788 7.086 0.50 14.94 C ANISOU 1770 C3 BBG6 A1224 1893 1890 1892 -28 -31 55 C HETATM 1771 O3 BBG6 A1224 5.406 33.393 6.953 0.50 15.78 O ANISOU 1771 O3 BBG6 A1224 1954 2036 2006 -59 -21 47 O HETATM 1772 C4 BBG6 A1224 3.489 32.427 5.805 0.50 14.13 C ANISOU 1772 C4 BBG6 A1224 1822 1751 1792 -27 -10 61 C HETATM 1773 O4 BBG6 A1224 3.355 33.587 4.972 0.50 14.37 O ANISOU 1773 O4 BBG6 A1224 1886 1802 1769 -62 -49 125 O HETATM 1774 C5 BBG6 A1224 2.100 31.759 5.946 0.50 13.74 C ANISOU 1774 C5 BBG6 A1224 1763 1757 1699 15 -4 52 C HETATM 1775 O5 BBG6 A1224 2.247 30.578 6.819 0.50 14.24 O ANISOU 1775 O5 BBG6 A1224 1850 1777 1782 -13 -8 75 O HETATM 1776 C6 BBG6 A1224 1.357 31.429 4.725 0.50 13.21 C ANISOU 1776 C6 BBG6 A1224 1678 1661 1678 0 27 -2 C HETATM 1777 O6 BBG6 A1224 2.122 30.397 4.028 0.50 12.28 O ANISOU 1777 O6 BBG6 A1224 1650 1611 1405 -21 -9 -10 O HETATM 1778 BE BEF A1225 1.499 28.964 11.484 1.00 8.38 BE ANISOU 1778 BE BEF A1225 1022 1034 1125 57 -68 35 BE HETATM 1779 F1 BEF A1225 0.366 29.822 10.769 1.00 8.83 F ANISOU 1779 F1 BEF A1225 1173 981 1200 101 -121 88 F HETATM 1780 F2 BEF A1225 1.847 27.819 10.588 1.00 7.86 F ANISOU 1780 F2 BEF A1225 935 1190 862 41 -89 27 F HETATM 1781 F3 BEF A1225 2.744 29.862 11.836 1.00 8.63 F ANISOU 1781 F3 BEF A1225 1040 1148 1088 5 -59 -20 F HETATM 1782 NA NA A1226 17.670 18.794 5.333 0.70 17.02 NA ANISOU 1782 NA NA A1226 1923 2266 2278 55 95 -49 NA HETATM 1783 O HOH A2001 -11.148 19.265 31.916 1.00 30.03 O ANISOU 1783 O HOH A2001 3747 3791 3870 -49 34 -11 O HETATM 1784 O HOH A2002 -12.356 18.811 27.546 1.00 24.08 O ANISOU 1784 O HOH A2002 3024 3080 3044 -26 -32 8 O HETATM 1785 O HOH A2003 -9.320 13.418 26.650 1.00 25.88 O ANISOU 1785 O HOH A2003 3325 3153 3356 -57 -1 -5 O HETATM 1786 O HOH A2004 -12.947 13.242 20.893 1.00 28.27 O ANISOU 1786 O HOH A2004 3614 3535 3593 -34 40 13 O HETATM 1787 O HOH A2005 -10.497 13.351 22.030 1.00 16.37 O ANISOU 1787 O HOH A2005 2134 2102 1983 -117 74 -92 O HETATM 1788 O HOH A2006 4.976 31.445 12.788 1.00 12.63 O ANISOU 1788 O HOH A2006 1613 1530 1656 -107 117 -67 O HETATM 1789 O HOH A2007 9.502 28.674 17.550 1.00 10.90 O ANISOU 1789 O HOH A2007 1151 1331 1658 -46 -125 20 O HETATM 1790 O HOH A2008 12.840 9.737 14.810 1.00 26.56 O ANISOU 1790 O HOH A2008 3457 3217 3414 61 10 -21 O HETATM 1791 O HOH A2009 12.702 11.878 16.450 1.00 16.57 O ANISOU 1791 O HOH A2009 2025 2167 2103 72 -25 25 O HETATM 1792 O HOH A2010 11.083 23.127 7.433 1.00 32.45 O ANISOU 1792 O HOH A2010 4138 4157 4031 14 18 -9 O HETATM 1793 O HOH A2011 9.863 29.893 12.630 1.00 26.45 O ANISOU 1793 O HOH A2011 3353 3336 3358 -62 -15 -11 O HETATM 1794 O HOH A2012 13.157 27.618 6.986 1.00 24.53 O ANISOU 1794 O HOH A2012 3160 3076 3081 -39 51 50 O HETATM 1795 O HOH A2013 -6.438 29.295 -2.128 1.00 34.37 O ANISOU 1795 O HOH A2013 4371 4390 4298 5 31 34 O HETATM 1796 O HOH A2014 -0.899 30.177 -6.247 1.00 25.97 O ANISOU 1796 O HOH A2014 3272 3293 3302 -2 -7 0 O HETATM 1797 O HOH A2015 16.362 35.022 -2.594 1.00 26.09 O ANISOU 1797 O HOH A2015 3256 3382 3274 -10 11 57 O HETATM 1798 O HOH A2016 10.034 34.260 -5.504 1.00 15.83 O ANISOU 1798 O HOH A2016 1920 2012 2081 -65 54 -69 O HETATM 1799 O HOH A2017 16.795 43.475 1.079 1.00 38.17 O ANISOU 1799 O HOH A2017 4806 4915 4783 -8 -23 4 O HETATM 1800 O HOH A2018 3.545 42.895 -11.772 1.00 35.84 O ANISOU 1800 O HOH A2018 4595 4529 4490 4 20 35 O HETATM 1801 O HOH A2019 14.681 37.898 -8.321 1.00 27.40 O ANISOU 1801 O HOH A2019 3394 3522 3493 0 30 2 O HETATM 1802 O HOH A2020 16.962 42.648 -1.685 1.00 24.66 O ANISOU 1802 O HOH A2020 3116 3180 3075 -44 -22 72 O HETATM 1803 O HOH A2021 17.201 36.879 -4.474 1.00 31.93 O ANISOU 1803 O HOH A2021 4054 4020 4057 -38 14 2 O HETATM 1804 O HOH A2022 7.947 33.515 -12.643 1.00 32.25 O ANISOU 1804 O HOH A2022 4038 4099 4114 -25 62 30 O HETATM 1805 O HOH A2023 3.177 23.415 -9.846 1.00 29.10 O ANISOU 1805 O HOH A2023 3625 3662 3768 -11 13 -25 O HETATM 1806 O HOH A2024 10.333 35.642 -8.117 1.00 32.95 O ANISOU 1806 O HOH A2024 4206 4196 4116 5 19 -11 O HETATM 1807 O HOH A2025 8.487 48.434 -8.786 1.00 29.06 O ANISOU 1807 O HOH A2025 3653 3651 3736 -11 54 2 O HETATM 1808 O HOH A2026 2.630 21.051 -3.359 1.00 23.23 O ANISOU 1808 O HOH A2026 3006 2967 2853 47 55 -38 O HETATM 1809 O HOH A2027 3.904 17.507 -5.165 1.00 24.30 O ANISOU 1809 O HOH A2027 3099 3064 3066 -25 55 -2 O HETATM 1810 O HOH A2028 5.709 20.867 -6.997 1.00 21.26 O ANISOU 1810 O HOH A2028 2659 2788 2629 -4 66 28 O HETATM 1811 O HOH A2029 18.029 14.430 5.861 1.00 34.66 O ANISOU 1811 O HOH A2029 4437 4396 4337 -27 -4 2 O HETATM 1812 O HOH A2030 15.499 44.919 -4.646 1.00 20.83 O ANISOU 1812 O HOH A2030 2641 2627 2644 0 2 -95 O HETATM 1813 O HOH A2031 14.103 43.889 -1.097 1.00 19.34 O ANISOU 1813 O HOH A2031 2471 2637 2240 -109 2 42 O HETATM 1814 O HOH A2032 12.516 11.248 12.588 1.00 23.19 O ANISOU 1814 O HOH A2032 2948 2864 2996 97 -7 -10 O HETATM 1815 O HOH A2033 11.659 14.155 15.202 1.00 9.16 O ANISOU 1815 O HOH A2033 1138 1319 1021 81 -2 -60 O HETATM 1816 O HOH A2034 16.696 13.613 13.079 1.00 26.11 O ANISOU 1816 O HOH A2034 3176 3358 3383 54 59 -43 O HETATM 1817 O HOH A2035 11.973 50.326 -2.840 1.00 42.32 O ANISOU 1817 O HOH A2035 5381 5315 5383 -2 -8 0 O HETATM 1818 O HOH A2036 17.576 45.110 -2.933 1.00 25.88 O ANISOU 1818 O HOH A2036 3260 3299 3274 -60 78 39 O HETATM 1819 O HOH A2037 7.457 13.892 24.907 1.00 17.58 O ANISOU 1819 O HOH A2037 2246 2112 2321 -1 10 -67 O HETATM 1820 O HOH A2038 11.299 11.581 18.838 1.00 16.44 O ANISOU 1820 O HOH A2038 2080 2028 2138 -43 -8 57 O HETATM 1821 O HOH A2039 11.309 13.832 22.167 1.00 20.22 O ANISOU 1821 O HOH A2039 2544 2643 2493 -109 -157 -13 O HETATM 1822 O HOH A2040 9.792 5.652 23.168 1.00 38.31 O ANISOU 1822 O HOH A2040 4887 4825 4843 -4 -11 -28 O HETATM 1823 O HOH A2041 14.212 46.644 7.370 1.00 41.06 O ANISOU 1823 O HOH A2041 5208 5209 5181 2 -2 -9 O HETATM 1824 O HOH A2042 7.043 9.568 28.792 1.00 47.90 O ANISOU 1824 O HOH A2042 6088 6052 6056 11 -22 -1 O HETATM 1825 O HOH A2043 5.666 5.072 24.103 1.00 18.66 O ANISOU 1825 O HOH A2043 2415 2350 2325 9 64 -8 O HETATM 1826 O HOH A2044 17.709 35.976 14.223 1.00 35.71 O ANISOU 1826 O HOH A2044 4494 4507 4568 40 -49 -36 O HETATM 1827 O HOH A2045 3.035 3.615 24.136 1.00 18.15 O ANISOU 1827 O HOH A2045 2416 2214 2262 -50 -54 16 O HETATM 1828 O HOH A2046 -6.959 7.227 17.295 1.00 25.87 O ANISOU 1828 O HOH A2046 3283 3182 3363 27 -57 -18 O HETATM 1829 O HOH A2047 13.915 34.985 9.273 1.00 37.99 O ANISOU 1829 O HOH A2047 4796 4848 4790 -22 7 5 O HETATM 1830 O HOH A2048 8.372 35.554 5.344 1.00 21.33 O ANISOU 1830 O HOH A2048 2772 2754 2576 -25 -71 -10 O HETATM 1831 O HOH A2049 9.889 34.138 7.147 1.00 26.64 O ANISOU 1831 O HOH A2049 3383 3427 3312 -45 -28 16 O HETATM 1832 O HOH A2050 -4.647 23.456 4.254 1.00 14.77 O ANISOU 1832 O HOH A2050 1805 2048 1755 122 -88 -85 O HETATM 1833 O HOH A2051 1.699 24.501 -5.584 1.00 25.13 O ANISOU 1833 O HOH A2051 3204 3239 3104 -7 4 -23 O HETATM 1834 O HOH A2052 5.439 43.955 14.732 1.00 40.40 O ANISOU 1834 O HOH A2052 5114 5117 5120 5 28 11 O HETATM 1835 O HOH A2053 5.153 15.269 -4.505 1.00 21.04 O ANISOU 1835 O HOH A2053 2674 2805 2514 5 70 -1 O HETATM 1836 O HOH A2054 1.462 36.915 12.757 1.00 28.41 O ANISOU 1836 O HOH A2054 3660 3575 3559 -25 5 -4 O HETATM 1837 O HOH A2055 0.275 32.249 11.842 1.00 15.13 O ANISOU 1837 O HOH A2055 1884 1819 2044 21 26 -53 O HETATM 1838 O HOH A2056 -1.865 34.841 9.630 1.00 24.92 O ANISOU 1838 O HOH A2056 3120 3116 3229 8 53 23 O HETATM 1839 O HOH A2057 -7.284 9.719 18.266 1.00 18.46 O ANISOU 1839 O HOH A2057 2305 2363 2346 -53 -21 55 O HETATM 1840 O HOH A2058 -5.296 36.841 4.121 1.00 34.01 O ANISOU 1840 O HOH A2058 4286 4295 4338 5 5 2 O HETATM 1841 O HOH A2059 -11.214 19.246 7.928 1.00 18.40 O ANISOU 1841 O HOH A2059 2295 2467 2227 68 -54 60 O HETATM 1842 O HOH A2060 -5.430 26.720 -1.390 1.00 23.37 O ANISOU 1842 O HOH A2060 2996 3034 2849 -37 30 44 O HETATM 1843 O HOH A2061 -0.887 27.215 -2.183 1.00 19.75 O ANISOU 1843 O HOH A2061 2507 2516 2481 -63 10 -31 O HETATM 1844 O HOH A2062 -0.667 32.448 -4.726 1.00 21.38 O ANISOU 1844 O HOH A2062 2785 2735 2602 -47 36 56 O HETATM 1845 O HOH A2063 -2.194 28.825 -4.052 1.00 23.42 O ANISOU 1845 O HOH A2063 2888 2955 3053 2 -20 7 O HETATM 1846 O HOH A2064 -2.309 37.507 7.931 1.00 24.20 O ANISOU 1846 O HOH A2064 3043 3094 3056 15 85 -26 O HETATM 1847 O HOH A2065 -14.990 24.734 9.207 1.00 30.95 O ANISOU 1847 O HOH A2065 3847 3915 3997 -4 -32 28 O HETATM 1848 O HOH A2066 -12.562 21.654 8.188 1.00 29.58 O ANISOU 1848 O HOH A2066 3714 3738 3785 -42 -19 5 O HETATM 1849 O HOH A2067 -17.109 27.297 20.598 1.00 12.01 O ANISOU 1849 O HOH A2067 1300 1504 1758 72 -28 -147 O HETATM 1850 O HOH A2068 -12.740 15.027 8.164 1.00 25.32 O ANISOU 1850 O HOH A2068 3210 3201 3210 -43 21 -55 O HETATM 1851 O HOH A2069 5.487 47.433 4.915 1.00 29.99 O ANISOU 1851 O HOH A2069 3892 3814 3686 -20 5 -25 O HETATM 1852 O HOH A2070 1.379 41.341 16.245 1.00 33.27 O ANISOU 1852 O HOH A2070 4229 4217 4195 -40 2 -18 O HETATM 1853 O HOH A2071 -0.242 48.490 -2.495 1.00 27.55 O ANISOU 1853 O HOH A2071 3463 3514 3488 2 10 41 O HETATM 1854 O HOH A2072 -8.261 40.499 17.823 1.00 20.10 O ANISOU 1854 O HOH A2072 2572 2414 2649 62 -47 19 O HETATM 1855 O HOH A2073 3.377 49.559 -9.886 1.00 41.61 O ANISOU 1855 O HOH A2073 5296 5309 5202 9 1 5 O HETATM 1856 O HOH A2074 -6.408 52.765 -5.594 1.00 35.48 O ANISOU 1856 O HOH A2074 4476 4495 4509 -16 4 10 O HETATM 1857 O HOH A2075 -8.695 26.684 29.661 1.00 22.81 O ANISOU 1857 O HOH A2075 2809 3093 2765 52 85 4 O HETATM 1858 O HOH A2076 13.296 32.150 26.040 1.00 29.22 O ANISOU 1858 O HOH A2076 3720 3676 3706 -11 -19 -20 O HETATM 1859 O HOH A2077 -6.002 40.098 -5.823 1.00 35.84 O ANISOU 1859 O HOH A2077 4522 4535 4558 -2 -2 33 O HETATM 1860 O HOH A2078 -1.129 39.247 -14.269 1.00 33.31 O ANISOU 1860 O HOH A2078 4291 4235 4129 0 23 10 O HETATM 1861 O HOH A2079 -3.464 37.057 -12.398 1.00 30.86 O ANISOU 1861 O HOH A2079 3876 3904 3943 5 11 5 O HETATM 1862 O HOH A2080 -6.628 37.552 -15.729 1.00 28.47 O ANISOU 1862 O HOH A2080 3608 3615 3590 -21 23 -35 O HETATM 1863 O HOH A2081 -9.463 41.898 -11.463 1.00 29.77 O ANISOU 1863 O HOH A2081 3777 3768 3766 22 13 11 O HETATM 1864 O HOH A2082 -7.088 43.423 -12.694 1.00 20.88 O ANISOU 1864 O HOH A2082 2544 2554 2833 101 -103 -11 O HETATM 1865 O HOH A2083 12.489 32.993 21.011 1.00 26.62 O ANISOU 1865 O HOH A2083 3267 3435 3410 -5 0 -15 O HETATM 1866 O HOH A2084 2.201 47.201 -11.735 1.00 24.75 O ANISOU 1866 O HOH A2084 3177 3141 3084 -61 -9 -52 O HETATM 1867 O HOH A2085 1.089 47.343 -15.194 1.00 22.94 O ANISOU 1867 O HOH A2085 2906 2947 2862 27 8 -15 O HETATM 1868 O HOH A2086 -1.172 48.208 -12.661 1.00 33.01 O ANISOU 1868 O HOH A2086 4190 4190 4161 -7 7 42 O HETATM 1869 O HOH A2087 2.047 40.657 -12.024 1.00 38.03 O ANISOU 1869 O HOH A2087 4818 4854 4778 13 -25 0 O HETATM 1870 O HOH A2088 -0.310 43.466 -16.013 1.00 36.11 O ANISOU 1870 O HOH A2088 4572 4622 4525 8 -9 -28 O HETATM 1871 O HOH A2089 -6.150 32.075 27.792 1.00 18.68 O ANISOU 1871 O HOH A2089 2496 2289 2312 83 65 -106 O HETATM 1872 O HOH A2090 -2.194 34.232 -6.098 1.00 19.27 O ANISOU 1872 O HOH A2090 2482 2463 2377 -56 46 137 O HETATM 1873 O HOH A2091 11.399 27.213 18.820 1.00 11.88 O ANISOU 1873 O HOH A2091 1480 1434 1598 -4 -140 -23 O HETATM 1874 O HOH A2092 12.110 30.932 19.506 1.00 19.08 O ANISOU 1874 O HOH A2092 2499 2341 2409 2 -62 -5 O HETATM 1875 O HOH A2093 3.042 32.202 -13.545 1.00 37.68 O ANISOU 1875 O HOH A2093 4805 4738 4773 11 23 32 O HETATM 1876 O HOH A2094 -2.184 34.508 -11.521 1.00 33.96 O ANISOU 1876 O HOH A2094 4307 4284 4309 1 -54 11 O HETATM 1877 O HOH A2095 7.939 23.633 30.952 1.00 27.61 O ANISOU 1877 O HOH A2095 3547 3537 3406 -21 -9 -55 O HETATM 1878 O HOH A2096 -1.433 16.500 35.617 1.00 41.17 O ANISOU 1878 O HOH A2096 5213 5230 5197 0 13 8 O HETATM 1879 O HOH A2097 7.109 41.903 -12.887 1.00 23.11 O ANISOU 1879 O HOH A2097 2984 2910 2885 -62 -66 -19 O HETATM 1880 O HOH A2098 6.513 25.028 -7.651 1.00 16.48 O ANISOU 1880 O HOH A2098 2246 1961 2055 37 103 -84 O HETATM 1881 O HOH A2099 1.374 28.997 -6.838 1.00 21.87 O ANISOU 1881 O HOH A2099 2857 2795 2656 81 -57 43 O HETATM 1882 O HOH A2100 6.347 30.613 -11.492 1.00 32.33 O ANISOU 1882 O HOH A2100 4151 4089 4044 23 19 2 O HETATM 1883 O HOH A2101 3.657 25.498 -7.221 1.00 18.27 O ANISOU 1883 O HOH A2101 2398 2403 2138 18 -40 -41 O HETATM 1884 O HOH A2102 13.665 27.847 -6.831 1.00 32.14 O ANISOU 1884 O HOH A2102 4177 4041 3993 0 34 -16 O HETATM 1885 O HOH A2103 13.207 21.166 -5.420 1.00 24.18 O ANISOU 1885 O HOH A2103 3042 3110 3033 20 74 5 O HETATM 1886 O HOH A2104 14.064 21.723 -2.838 1.00 23.61 O ANISOU 1886 O HOH A2104 2965 3046 2958 -34 57 -9 O HETATM 1887 O HOH A2105 12.706 15.297 -0.188 1.00 19.62 O ANISOU 1887 O HOH A2105 2413 2361 2678 -2 -115 36 O HETATM 1888 O HOH A2106 4.887 20.044 -4.472 1.00 15.62 O ANISOU 1888 O HOH A2106 1887 2030 2018 49 -18 -72 O HETATM 1889 O HOH A2107 17.441 17.727 3.204 1.00 25.51 O ANISOU 1889 O HOH A2107 3146 3276 3271 -26 -5 -5 O HETATM 1890 O HOH A2108 18.512 21.736 2.356 1.00 31.96 O ANISOU 1890 O HOH A2108 4016 4104 4021 27 17 -20 O HETATM 1891 O HOH A2109 15.162 12.816 7.426 1.00 30.77 O ANISOU 1891 O HOH A2109 3785 3946 3958 7 -13 1 O HETATM 1892 O HOH A2110 16.971 16.640 5.698 1.00 28.45 O ANISOU 1892 O HOH A2110 3627 3618 3562 31 55 13 O HETATM 1893 O HOH A2111 10.855 13.366 12.634 1.00 8.65 O ANISOU 1893 O HOH A2111 990 1142 1154 -22 71 32 O HETATM 1894 O HOH A2112 15.942 16.157 13.594 1.00 11.33 O ANISOU 1894 O HOH A2112 1346 1581 1377 17 -166 106 O HETATM 1895 O HOH A2113 14.803 12.102 11.036 1.00 34.23 O ANISOU 1895 O HOH A2113 4344 4296 4364 40 27 13 O HETATM 1896 O HOH A2114 17.215 18.495 7.848 1.00 31.38 O ANISOU 1896 O HOH A2114 3955 3960 4008 28 2 -2 O HETATM 1897 O HOH A2115 13.893 22.189 11.895 1.00 16.28 O ANISOU 1897 O HOH A2115 1933 2119 2130 -9 -33 -60 O HETATM 1898 O HOH A2116 15.488 18.733 5.055 1.00 20.37 O ANISOU 1898 O HOH A2116 2373 2841 2525 25 11 -123 O HETATM 1899 O HOH A2117 16.200 20.605 10.880 1.00 13.59 O ANISOU 1899 O HOH A2117 1441 1943 1777 -160 -149 66 O HETATM 1900 O HOH A2118 13.499 16.036 15.113 1.00 16.57 O ANISOU 1900 O HOH A2118 1917 2027 2351 -42 -59 -13 O HETATM 1901 O HOH A2119 13.516 28.025 17.161 1.00 20.78 O ANISOU 1901 O HOH A2119 2602 2663 2629 0 103 -42 O HETATM 1902 O HOH A2120 10.446 15.698 17.225 1.00 7.38 O ANISOU 1902 O HOH A2120 708 908 1188 45 -20 9 O HETATM 1903 O HOH A2121 14.039 28.243 13.716 1.00 38.96 O ANISOU 1903 O HOH A2121 4933 4942 4927 22 -25 -5 O HETATM 1904 O HOH A2122 10.864 29.043 15.103 1.00 16.18 O ANISOU 1904 O HOH A2122 2078 1928 2138 -72 115 -5 O HETATM 1905 O HOH A2123 12.965 15.422 19.678 1.00 17.01 O ANISOU 1905 O HOH A2123 2082 2044 2333 129 -120 -112 O HETATM 1906 O HOH A2124 7.784 16.176 23.619 1.00 14.99 O ANISOU 1906 O HOH A2124 2141 1857 1696 264 0 -32 O HETATM 1907 O HOH A2125 12.772 16.366 23.125 1.00 21.25 O ANISOU 1907 O HOH A2125 2620 2779 2673 31 -52 10 O HETATM 1908 O HOH A2126 10.180 14.072 19.530 1.00 11.70 O ANISOU 1908 O HOH A2126 1455 1487 1503 -106 -102 11 O HETATM 1909 O HOH A2127 9.345 9.675 18.874 1.00 17.55 O ANISOU 1909 O HOH A2127 2283 2231 2154 -15 -28 -33 O HETATM 1910 O HOH A2128 5.796 6.051 21.428 1.00 21.35 O ANISOU 1910 O HOH A2128 2771 2558 2781 -45 7 14 O HETATM 1911 O HOH A2129 8.434 6.489 21.018 1.00 38.71 O ANISOU 1911 O HOH A2129 4963 4850 4894 -9 -9 -44 O HETATM 1912 O HOH A2130 1.291 6.821 18.701 1.00 13.42 O ANISOU 1912 O HOH A2130 1752 1587 1758 -44 38 -78 O HETATM 1913 O HOH A2131 7.967 5.197 18.692 1.00 28.94 O ANISOU 1913 O HOH A2131 3651 3648 3698 47 13 36 O HETATM 1914 O HOH A2132 8.825 7.368 14.264 1.00 18.01 O ANISOU 1914 O HOH A2132 2379 2298 2162 -2 98 -10 O HETATM 1915 O HOH A2133 4.905 13.696 25.438 1.00 15.89 O ANISOU 1915 O HOH A2133 1844 2019 2175 -14 -4 -180 O HETATM 1916 O HOH A2134 2.982 7.085 22.839 1.00 17.19 O ANISOU 1916 O HOH A2134 2142 2034 2353 105 -99 -28 O HETATM 1917 O HOH A2135 6.961 10.239 26.159 1.00 23.97 O ANISOU 1917 O HOH A2135 2960 3132 3015 30 -25 51 O HETATM 1918 O HOH A2136 5.307 7.293 25.581 1.00 24.15 O ANISOU 1918 O HOH A2136 3024 3029 3122 64 -28 2 O HETATM 1919 O HOH A2137 -6.491 4.263 14.817 1.00 26.07 O ANISOU 1919 O HOH A2137 3176 3350 3379 4 -10 25 O HETATM 1920 O HOH A2138 -5.147 5.987 18.926 1.00 12.19 O ANISOU 1920 O HOH A2138 1534 1346 1752 -16 -60 -25 O HETATM 1921 O HOH A2139 -6.856 6.926 14.566 1.00 38.49 O ANISOU 1921 O HOH A2139 4865 4835 4923 -5 21 1 O HETATM 1922 O HOH A2140 1.905 3.764 21.523 1.00 12.59 O ANISOU 1922 O HOH A2140 1618 1333 1830 30 -62 34 O HETATM 1923 O HOH A2141 -5.690 5.400 24.813 1.00 20.87 O ANISOU 1923 O HOH A2141 2619 2701 2609 -62 103 32 O HETATM 1924 O HOH A2142 -9.891 10.359 19.556 1.00 37.04 O ANISOU 1924 O HOH A2142 4658 4739 4675 -18 -9 -2 O HETATM 1925 O HOH A2143 -11.708 13.299 14.132 1.00 24.76 O ANISOU 1925 O HOH A2143 3165 3085 3156 -47 7 32 O HETATM 1926 O HOH A2144 -3.530 32.156 5.137 1.00 19.45 O ANISOU 1926 O HOH A2144 2443 2422 2524 54 -1 143 O HETATM 1927 O HOH A2145 -2.737 24.043 6.152 1.00 8.09 O ANISOU 1927 O HOH A2145 992 1217 862 145 59 -100 O HETATM 1928 O HOH A2146 -3.977 23.631 1.569 1.00 12.95 O ANISOU 1928 O HOH A2146 1631 1759 1530 -141 -1 86 O HETATM 1929 O HOH A2147 -1.395 32.034 2.958 1.00 19.78 O ANISOU 1929 O HOH A2147 2595 2540 2379 -92 -13 -27 O HETATM 1930 O HOH A2148 1.311 22.282 -1.409 1.00 19.93 O ANISOU 1930 O HOH A2148 2738 2484 2348 59 38 -26 O HETATM 1931 O HOH A2149 1.120 25.574 -3.152 1.00 14.27 O ANISOU 1931 O HOH A2149 1741 1895 1784 -5 -13 -46 O HETATM 1932 O HOH A2150 -0.198 21.381 0.686 1.00 10.71 O ANISOU 1932 O HOH A2150 1252 1522 1293 107 -131 -40 O HETATM 1933 O HOH A2151 -0.487 12.905 1.710 1.00 30.75 O ANISOU 1933 O HOH A2151 3804 3968 3908 -40 13 44 O HETATM 1934 O HOH A2152 4.802 11.075 4.129 1.00 24.30 O ANISOU 1934 O HOH A2152 3164 2973 3096 -45 28 2 O HETATM 1935 O HOH A2153 5.047 13.853 -2.398 1.00 23.48 O ANISOU 1935 O HOH A2153 3003 3002 2914 60 7 -64 O HETATM 1936 O HOH A2154 10.264 13.006 3.291 1.00 19.05 O ANISOU 1936 O HOH A2154 2435 2377 2425 85 55 7 O HETATM 1937 O HOH A2155 9.273 14.376 -3.873 1.00 21.97 O ANISOU 1937 O HOH A2155 2627 2801 2917 33 60 -128 O HETATM 1938 O HOH A2156 8.518 12.523 11.524 1.00 11.48 O ANISOU 1938 O HOH A2156 1320 1636 1402 35 7 131 O HETATM 1939 O HOH A2157 9.629 9.518 9.878 1.00 26.35 O ANISOU 1939 O HOH A2157 3275 3306 3429 14 47 25 O HETATM 1940 O HOH A2158 7.126 10.243 11.326 1.00 17.52 O ANISOU 1940 O HOH A2158 2312 2126 2218 -38 -107 -61 O HETATM 1941 O HOH A2159 3.183 10.903 6.228 1.00 22.50 O ANISOU 1941 O HOH A2159 2786 2890 2870 -84 8 8 O HETATM 1942 O HOH A2160 -3.150 14.499 7.770 1.00 25.13 O ANISOU 1942 O HOH A2160 3232 3147 3164 5 74 -36 O HETATM 1943 O HOH A2161 -0.321 15.493 4.654 1.00 15.65 O ANISOU 1943 O HOH A2161 1904 1933 2107 -97 23 141 O HETATM 1944 O HOH A2162 2.384 9.743 8.448 1.00 23.84 O ANISOU 1944 O HOH A2162 2938 2985 3133 55 61 -11 O HETATM 1945 O HOH A2163 6.509 8.293 13.074 1.00 16.19 O ANISOU 1945 O HOH A2163 2121 2033 1996 -28 41 51 O HETATM 1946 O HOH A2164 -3.471 10.776 15.578 1.00 11.51 O ANISOU 1946 O HOH A2164 1629 1315 1428 92 76 18 O HETATM 1947 O HOH A2165 4.024 6.203 15.210 1.00 28.62 O ANISOU 1947 O HOH A2165 3652 3584 3636 11 15 17 O HETATM 1948 O HOH A2166 -5.662 15.085 8.383 1.00 15.02 O ANISOU 1948 O HOH A2166 1942 1832 1931 76 -40 -34 O HETATM 1949 O HOH A2167 -5.389 11.594 17.475 1.00 10.50 O ANISOU 1949 O HOH A2167 1334 1350 1305 18 63 -95 O HETATM 1950 O HOH A2168 -9.476 11.895 10.164 1.00 22.56 O ANISOU 1950 O HOH A2168 2852 2945 2772 -68 -16 -19 O HETATM 1951 O HOH A2169 -5.590 10.237 13.436 1.00 22.91 O ANISOU 1951 O HOH A2169 2934 2902 2866 69 -55 -38 O HETATM 1952 O HOH A2170 -8.096 13.935 7.165 1.00 23.49 O ANISOU 1952 O HOH A2170 2997 2968 2960 -5 82 -32 O HETATM 1953 O HOH A2171 -9.420 10.627 12.614 1.00 30.22 O ANISOU 1953 O HOH A2171 3847 3817 3812 -27 -37 5 O HETATM 1954 O HOH A2172 -8.940 10.003 16.014 1.00 19.23 O ANISOU 1954 O HOH A2172 2565 2337 2404 -92 -31 9 O HETATM 1955 O HOH A2173 -8.892 17.873 7.136 1.00 10.82 O ANISOU 1955 O HOH A2173 1432 1570 1110 -157 -146 -66 O HETATM 1956 O HOH A2174 -3.962 24.758 8.568 1.00 7.79 O ANISOU 1956 O HOH A2174 903 1138 915 0 -52 -19 O HETATM 1957 O HOH A2175 -9.478 25.102 -0.561 1.00 30.03 O ANISOU 1957 O HOH A2175 3839 3830 3741 13 -10 21 O HETATM 1958 O HOH A2176 -11.259 23.549 6.696 1.00 26.92 O ANISOU 1958 O HOH A2176 3256 3492 3477 -27 2 64 O HETATM 1959 O HOH A2177 -6.009 25.281 0.751 1.00 18.18 O ANISOU 1959 O HOH A2177 2273 2467 2167 89 95 110 O HETATM 1960 O HOH A2178 -4.876 33.143 7.396 1.00 28.74 O ANISOU 1960 O HOH A2178 3630 3655 3634 32 17 -46 O HETATM 1961 O HOH A2179 -7.717 38.596 7.341 1.00 29.64 O ANISOU 1961 O HOH A2179 3733 3723 3804 18 -23 30 O HETATM 1962 O HOH A2180 -8.090 39.103 11.028 1.00 23.74 O ANISOU 1962 O HOH A2180 3110 2896 3013 54 1 23 O HETATM 1963 O HOH A2181 -3.916 33.272 9.891 1.00 19.47 O ANISOU 1963 O HOH A2181 2468 2451 2478 157 -4 -51 O HETATM 1964 O HOH A2182 -8.456 32.738 11.885 1.00 12.51 O ANISOU 1964 O HOH A2182 1554 1512 1685 -10 92 61 O HETATM 1965 O HOH A2183 -15.416 33.481 14.611 1.00 34.76 O ANISOU 1965 O HOH A2183 4361 4428 4416 5 -21 53 O HETATM 1966 O HOH A2184 -14.235 28.981 11.779 1.00 20.72 O ANISOU 1966 O HOH A2184 2480 2658 2732 53 -125 -14 O HETATM 1967 O HOH A2185 -14.054 22.581 10.508 1.00 12.87 O ANISOU 1967 O HOH A2185 1520 1898 1470 -55 -152 -119 O HETATM 1968 O HOH A2186 -17.433 19.563 15.307 1.00 13.81 O ANISOU 1968 O HOH A2186 1377 1850 2019 -38 65 -119 O HETATM 1969 O HOH A2187 -17.705 24.741 19.569 1.00 9.39 O ANISOU 1969 O HOH A2187 1244 1101 1220 26 39 -7 O HETATM 1970 O HOH A2188 -16.861 25.614 12.259 1.00 26.39 O ANISOU 1970 O HOH A2188 3340 3407 3279 -21 -14 5 O HETATM 1971 O HOH A2189 -12.905 17.380 9.267 1.00 14.51 O ANISOU 1971 O HOH A2189 1829 1878 1806 -130 101 -63 O HETATM 1972 O HOH A2190 -12.918 14.450 12.114 1.00 27.68 O ANISOU 1972 O HOH A2190 3580 3355 3579 -17 8 19 O HETATM 1973 O HOH A2191 -14.037 14.128 18.686 1.00 20.16 O ANISOU 1973 O HOH A2191 2511 2548 2601 -102 -33 71 O HETATM 1974 O HOH A2192 -13.277 21.459 28.830 1.00 24.70 O ANISOU 1974 O HOH A2192 3032 3184 3168 -11 -2 -47 O HETATM 1975 O HOH A2193 -15.721 22.717 27.828 1.00 26.13 O ANISOU 1975 O HOH A2193 3374 3331 3222 -27 -46 40 O HETATM 1976 O HOH A2194 -17.095 17.451 22.106 1.00 27.29 O ANISOU 1976 O HOH A2194 3468 3430 3468 -66 -50 63 O HETATM 1977 O HOH A2195 2.103 31.595 13.971 1.00 9.97 O ANISOU 1977 O HOH A2195 1270 1182 1335 130 92 1 O HETATM 1978 O HOH A2196 7.177 35.315 17.100 1.00 27.77 O ANISOU 1978 O HOH A2196 3528 3481 3542 -26 14 19 O HETATM 1979 O HOH A2197 7.767 32.775 19.555 1.00 16.41 O ANISOU 1979 O HOH A2197 1984 2016 2234 35 -66 -28 O HETATM 1980 O HOH A2198 0.012 34.771 13.551 1.00 23.34 O ANISOU 1980 O HOH A2198 2900 3028 2937 13 1 35 O HETATM 1981 O HOH A2199 0.319 41.043 24.011 1.00 13.62 O ANISOU 1981 O HOH A2199 1812 1412 1950 106 0 -17 O HETATM 1982 O HOH A2200 4.559 37.618 17.199 1.00 19.28 O ANISOU 1982 O HOH A2200 2327 2455 2544 -120 132 -30 O HETATM 1983 O HOH A2201 3.062 40.930 24.835 1.00 11.78 O ANISOU 1983 O HOH A2201 1533 1322 1618 72 28 -211 O HETATM 1984 O HOH A2202 1.774 37.932 15.314 1.00 14.67 O ANISOU 1984 O HOH A2202 1876 1734 1960 2 62 49 O HETATM 1985 O HOH A2203 -5.475 41.035 24.820 1.00 37.65 O ANISOU 1985 O HOH A2203 4749 4744 4811 10 -7 35 O HETATM 1986 O HOH A2204 -3.491 41.591 22.812 1.00 21.69 O ANISOU 1986 O HOH A2204 2798 2622 2819 22 4 -36 O HETATM 1987 O HOH A2205 -3.127 37.734 23.687 1.00 12.99 O ANISOU 1987 O HOH A2205 1438 1723 1772 -33 73 -105 O HETATM 1988 O HOH A2206 -10.254 32.382 26.227 1.00 16.82 O ANISOU 1988 O HOH A2206 2158 2129 2102 67 53 -129 O HETATM 1989 O HOH A2207 -8.971 37.513 24.827 1.00 39.83 O ANISOU 1989 O HOH A2207 5049 5066 5018 25 -1 -15 O HETATM 1990 O HOH A2208 -9.294 38.040 17.777 1.00 20.60 O ANISOU 1990 O HOH A2208 2523 2530 2771 82 -2 -74 O HETATM 1991 O HOH A2209 -15.483 28.911 24.018 1.00 29.63 O ANISOU 1991 O HOH A2209 3708 3738 3809 -44 -13 -9 O HETATM 1992 O HOH A2210 -15.414 29.233 19.558 1.00 20.26 O ANISOU 1992 O HOH A2210 2389 2728 2577 -65 -2 9 O HETATM 1993 O HOH A2211 -10.046 26.188 27.421 1.00 20.77 O ANISOU 1993 O HOH A2211 2602 2754 2532 -1 57 47 O HETATM 1994 O HOH A2212 -12.990 28.837 27.207 1.00 21.77 O ANISOU 1994 O HOH A2212 2660 2907 2701 2 51 11 O HETATM 1995 O HOH A2213 -8.366 30.562 26.957 1.00 17.04 O ANISOU 1995 O HOH A2213 2134 2251 2088 115 -33 -158 O HETATM 1996 O HOH A2214 -2.109 29.286 29.206 1.00 10.51 O ANISOU 1996 O HOH A2214 1286 1409 1297 -137 9 -158 O HETATM 1997 O HOH A2215 9.523 31.114 18.538 1.00 22.49 O ANISOU 1997 O HOH A2215 2837 2769 2937 18 -95 -102 O HETATM 1998 O HOH A2216 10.292 31.706 27.285 1.00 15.53 O ANISOU 1998 O HOH A2216 1974 2096 1829 120 -154 -39 O HETATM 1999 O HOH A2217 17.836 32.732 23.898 1.00 36.73 O ANISOU 1999 O HOH A2217 4629 4651 4672 47 1 -5 O HETATM 2000 O HOH A2218 4.081 39.466 26.980 1.00 14.60 O ANISOU 2000 O HOH A2218 1994 1710 1840 -2 -34 -109 O HETATM 2001 O HOH A2219 12.155 36.971 27.295 1.00 32.40 O ANISOU 2001 O HOH A2219 4137 4112 4059 13 -41 -19 O HETATM 2002 O HOH A2220 12.106 38.697 20.563 1.00 32.51 O ANISOU 2002 O HOH A2220 4089 4106 4154 -9 5 5 O HETATM 2003 O HOH A2221 9.932 34.274 20.605 1.00 12.24 O ANISOU 2003 O HOH A2221 1562 1489 1600 -8 104 5 O HETATM 2004 O HOH A2222 6.860 39.282 17.873 1.00 20.67 O ANISOU 2004 O HOH A2222 2726 2580 2544 40 2 -20 O HETATM 2005 O HOH A2223 -1.157 37.555 21.879 1.00 10.55 O ANISOU 2005 O HOH A2223 1207 1332 1467 -63 68 -75 O HETATM 2006 O HOH A2224 3.657 36.457 29.500 1.00 25.21 O ANISOU 2006 O HOH A2224 3246 3231 3100 -11 20 14 O HETATM 2007 O HOH A2225 -1.533 42.304 26.458 1.00 24.63 O ANISOU 2007 O HOH A2225 3101 3168 3086 18 37 28 O HETATM 2008 O HOH A2226 3.348 38.775 30.831 1.00 25.97 O ANISOU 2008 O HOH A2226 3327 3280 3258 -5 -60 -23 O HETATM 2009 O HOH A2227 -1.580 39.341 25.443 1.00 13.15 O ANISOU 2009 O HOH A2227 1596 1593 1805 158 -5 -68 O HETATM 2010 O HOH A2228 0.953 37.624 32.280 1.00 26.23 O ANISOU 2010 O HOH A2228 3345 3300 3321 -76 18 -47 O HETATM 2011 O HOH A2229 -3.290 34.999 33.881 1.00 37.57 O ANISOU 2011 O HOH A2229 4718 4751 4805 5 4 -7 O HETATM 2012 O HOH A2230 -4.174 31.066 29.713 1.00 14.93 O ANISOU 2012 O HOH A2230 1880 1879 1913 50 130 -240 O HETATM 2013 O HOH A2231 2.033 34.706 31.136 1.00 21.67 O ANISOU 2013 O HOH A2231 2749 2673 2811 -38 34 -45 O HETATM 2014 O HOH A2232 7.586 26.876 30.883 1.00 17.46 O ANISOU 2014 O HOH A2232 2411 2168 2054 108 30 -47 O HETATM 2015 O HOH A2233 12.716 31.209 23.635 1.00 20.51 O ANISOU 2015 O HOH A2233 2530 2491 2769 -11 -15 16 O HETATM 2016 O HOH A2234 12.488 28.611 20.864 1.00 8.87 O ANISOU 2016 O HOH A2234 1010 1181 1176 -21 -82 -115 O HETATM 2017 O HOH A2235 16.293 26.470 22.946 1.00 13.31 O ANISOU 2017 O HOH A2235 1519 1762 1773 132 -89 -28 O HETATM 2018 O HOH A2236 11.682 24.624 19.533 1.00 8.82 O ANISOU 2018 O HOH A2236 767 1355 1228 -64 -50 13 O HETATM 2019 O HOH A2237 14.554 20.548 27.413 1.00 31.45 O ANISOU 2019 O HOH A2237 3975 4025 3947 2 -23 17 O HETATM 2020 O HOH A2238 10.458 16.728 24.720 1.00 13.75 O ANISOU 2020 O HOH A2238 1876 1766 1579 68 81 -63 O HETATM 2021 O HOH A2239 7.944 20.625 30.066 1.00 18.55 O ANISOU 2021 O HOH A2239 2340 2604 2102 -69 -25 -11 O HETATM 2022 O HOH A2240 7.365 16.685 31.033 1.00 21.71 O ANISOU 2022 O HOH A2240 2652 2949 2646 -23 -23 45 O HETATM 2023 O HOH A2241 0.741 15.304 33.944 1.00 23.08 O ANISOU 2023 O HOH A2241 2996 2990 2780 31 28 -9 O HETATM 2024 O HOH A2242 4.920 13.261 28.661 1.00 15.03 O ANISOU 2024 O HOH A2242 1923 1642 2142 145 92 42 O HETATM 2025 O HOH A2243 -5.153 17.216 32.635 1.00 26.03 O ANISOU 2025 O HOH A2243 3297 3321 3271 4 2 20 O HETATM 2026 O HOH A2244 5.962 18.032 33.324 1.00 37.80 O ANISOU 2026 O HOH A2244 4817 4811 4732 2 0 15 O HETATM 2027 O HOH A2245 -1.680 20.745 37.450 1.00 26.43 O ANISOU 2027 O HOH A2245 3403 3384 3253 5 30 -10 O HETATM 2028 O HOH A2246 -7.596 27.436 37.260 1.00 36.49 O ANISOU 2028 O HOH A2246 4560 4690 4611 30 7 -9 O HETATM 2029 O HOH A2247 -0.328 28.177 35.057 1.00 16.66 O ANISOU 2029 O HOH A2247 2062 2171 2094 -64 -40 -45 O HETATM 2030 O HOH A2248 -5.124 32.386 32.933 1.00 32.85 O ANISOU 2030 O HOH A2248 4151 4144 4184 35 2 1 O HETATM 2031 O HOH A2249 -2.473 29.513 36.135 1.00 23.13 O ANISOU 2031 O HOH A2249 2868 3044 2877 -26 -42 -71 O HETATM 2032 O HOH A2250 -0.353 31.594 32.846 1.00 16.98 O ANISOU 2032 O HOH A2250 2016 2303 2129 50 -36 11 O HETATM 2033 O HOH A2251 -7.543 24.601 30.634 1.00 34.11 O ANISOU 2033 O HOH A2251 4333 4315 4311 41 -23 -33 O HETATM 2034 O HOH A2252 -14.502 22.774 32.022 1.00 29.44 O ANISOU 2034 O HOH A2252 3739 3726 3720 7 9 16 O HETATM 2035 O HOH A2253 -11.878 29.651 43.035 1.00 36.12 O ANISOU 2035 O HOH A2253 4595 4538 4588 9 -18 16 O HETATM 2036 O HOH A2254 3.521 33.408 2.182 1.00 10.63 O ANISOU 2036 O HOH A2254 1413 1413 1213 -92 69 0 O HETATM 2037 O HOH A2255 5.510 35.492 4.809 1.00 16.72 O ANISOU 2037 O HOH A2255 2169 2122 2061 -162 131 91 O HETATM 2038 O HOH A2256 4.044 30.673 -0.385 1.00 10.43 O ANISOU 2038 O HOH A2256 1281 1353 1328 -153 -22 5 O CONECT 71 1778 CONECT 1746 1747 1748 1749 1761 CONECT 1747 1746 CONECT 1748 1746 CONECT 1749 1746 CONECT 1750 1751 1752 1759 CONECT 1751 1750 CONECT 1752 1750 1753 1754 CONECT 1753 1752 CONECT 1754 1752 1755 1756 CONECT 1755 1754 CONECT 1756 1754 1757 1758 CONECT 1757 1756 CONECT 1758 1756 1759 1760 CONECT 1759 1750 1758 CONECT 1760 1758 1761 CONECT 1761 1760 1746 CONECT 1762 1763 1764 1765 1777 CONECT 1763 1762 CONECT 1764 1762 CONECT 1765 1762 CONECT 1766 1767 1768 1775 CONECT 1767 1766 CONECT 1768 1766 1769 1770 CONECT 1769 1768 CONECT 1770 1768 1771 1772 CONECT 1771 1770 CONECT 1772 1770 1773 1774 CONECT 1773 1772 CONECT 1774 1772 1776 1775 CONECT 1775 1766 1774 CONECT 1776 1774 1777 CONECT 1777 1776 1762 CONECT 1778 71 1779 1780 1781 CONECT 1779 1778 CONECT 1780 1778 CONECT 1781 1778 END If you find results from this site helpful for your research, please cite one of our papers:
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