HEADER TRANSPORT DE L'OXYGENE 13-JUL-93 2HHB COMPND GLOBINE ALPHA DE L'HEMOGLOBINE HUMAINE (DEOXY) ATOM 1 N VAL A 1 5.428 17.060 5.060 1.00 41.29 ATOM 2 CA VAL A 1 6.168 18.288 4.856 1.00 41.33 ATOM 3 C VAL A 1 7.676 18.052 5.068 1.00 31.64 ATOM 4 O VAL A 1 8.120 17.484 6.076 1.00 38.31 ATOM 5 CB VAL A 1 5.644 19.264 5.884 1.00 52.26 ATOM 6 CG1 VAL A 1 6.044 20.692 5.512 1.00 52.75 ATOM 7 CG2 VAL A 1 4.124 19.116 6.000 1.00 58.75 ATOM 8 N LEU A 2 8.444 18.508 4.116 1.00 27.63 ATOM 9 CA LEU A 2 9.896 18.416 4.308 1.00 33.62 ATOM 10 C LEU A 2 10.360 19.588 5.216 1.00 32.51 ATOM 11 O LEU A 2 10.128 20.756 4.900 1.00 31.03 ATOM 12 CB LEU A 2 10.568 18.580 2.932 1.00 34.38 ATOM 13 CG LEU A 2 10.284 17.484 1.924 1.00 32.23 ATOM 14 CD1 LEU A 2 11.032 17.672 0.580 1.00 36.30 ATOM 15 CD2 LEU A 2 10.576 16.132 2.560 1.00 38.42 ATOM 16 N SER A 3 10.972 19.268 6.312 1.00 26.50 ATOM 17 CA SER A 3 11.584 20.276 7.188 1.00 27.60 ATOM 18 C SER A 3 12.828 20.824 6.488 1.00 30.36 ATOM 19 O SER A 3 13.292 20.256 5.500 1.00 27.40 ATOM 20 CB SER A 3 12.016 19.564 8.480 1.00 23.83 ATOM 21 OG SER A 3 13.144 18.748 8.260 1.00 29.07 ATOM 22 N PRO A 4 13.372 21.956 6.940 1.00 37.36 ATOM 23 CA PRO A 4 14.584 22.544 6.320 1.00 39.58 ATOM 24 C PRO A 4 15.764 21.604 6.444 1.00 21.30 ATOM 25 O PRO A 4 16.588 21.520 5.524 1.00 32.82 ATOM 26 CB PRO A 4 14.936 23.816 7.096 1.00 45.84 ATOM 27 CG PRO A 4 13.696 24.104 7.920 1.00 43.31 ATOM 28 CD PRO A 4 12.812 22.848 7.952 1.00 38.50 ATOM 29 N ALA A 5 15.784 20.892 7.592 1.00 22.62 ATOM 30 CA ALA A 5 16.832 19.916 7.804 1.00 26.71 ATOM 31 C ALA A 5 16.672 18.792 6.752 1.00 24.99 ATOM 32 O ALA A 5 17.684 18.356 6.188 1.00 21.71 ATOM 33 CB ALA A 5 16.792 19.384 9.268 1.00 32.50 ATOM 34 N ASP A 6 15.400 18.352 6.480 1.00 20.58 ATOM 35 CA ASP A 6 15.248 17.376 5.384 1.00 22.32 ATOM 36 C ASP A 6 15.824 17.908 4.080 1.00 19.78 ATOM 37 O ASP A 6 16.500 17.120 3.384 1.00 18.76 ATOM 38 CB ASP A 6 13.824 16.972 5.120 1.00 17.78 ATOM 39 CG ASP A 6 13.224 16.168 6.256 1.00 22.06 ATOM 40 OD1 ASP A 6 13.916 15.324 6.836 1.00 19.41 ATOM 41 OD2 ASP A 6 12.056 16.436 6.528 1.00 22.31 ATOM 42 N LYS A 7 15.544 19.188 3.808 1.00 20.93 ATOM 43 CA LYS A 7 16.048 19.724 2.508 1.00 31.09 ATOM 44 C LYS A 7 17.568 19.768 2.416 1.00 26.90 ATOM 45 O LYS A 7 18.148 19.456 1.356 1.00 20.98 ATOM 46 CB LYS A 7 15.440 21.084 2.264 1.00 32.60 ATOM 47 CG LYS A 7 13.928 21.008 2.348 1.00 36.22 ATOM 48 CD LYS A 7 13.336 22.400 2.216 1.00 43.74 ATOM 49 CE LYS A 7 11.948 22.432 2.812 1.00 38.82 ATOM 50 NZ LYS A 7 11.492 23.816 2.728 1.00 45.01 ATOM 51 N THR A 8 18.180 20.080 3.576 1.00 22.82 ATOM 52 CA THR A 8 19.652 20.080 3.632 1.00 24.55 ATOM 53 C THR A 8 20.216 18.688 3.372 1.00 20.07 ATOM 54 O THR A 8 21.188 18.544 2.624 1.00 20.49 ATOM 55 CB THR A 8 20.068 20.608 5.020 1.00 27.25 ATOM 56 OG1 THR A 8 19.688 21.960 5.100 1.00 29.04 ATOM 57 CG2 THR A 8 21.556 20.528 5.204 1.00 38.97 ATOM 58 N ASN A 9 19.572 17.676 3.992 1.00 17.67 ATOM 59 CA ASN A 9 19.956 16.280 3.844 1.00 21.47 ATOM 60 C ASN A 9 19.828 15.748 2.388 1.00 14.31 ATOM 61 O ASN A 9 20.676 15.020 1.896 1.00 21.97 ATOM 62 CB ASN A 9 19.144 15.400 4.816 1.00 22.36 ATOM 63 CG ASN A 9 19.544 15.640 6.284 1.00 29.08 ATOM 64 OD1 ASN A 9 20.584 16.224 6.604 1.00 26.41 ATOM 65 ND2 ASN A 9 18.700 15.192 7.180 1.00 23.93 ATOM 66 N VAL A 10 18.732 16.068 1.744 1.00 23.07 ATOM 67 CA VAL A 10 18.508 15.636 0.372 1.00 17.62 ATOM 68 C VAL A 10 19.536 16.324 -0.556 1.00 19.10 ATOM 69 O VAL A 10 20.116 15.684 -1.444 1.00 21.61 ATOM 70 CB VAL A 10 17.068 15.968 0.012 1.00 18.24 ATOM 71 CG1 VAL A 10 16.808 15.664 -1.448 1.00 24.49 ATOM 72 CG2 VAL A 10 16.060 15.252 0.856 1.00 19.15 ATOM 73 N LYS A 11 19.724 17.624 -0.336 1.00 21.06 ATOM 74 CA LYS A 11 20.728 18.376 -1.172 1.00 29.00 ATOM 75 C LYS A 11 22.140 17.816 -0.996 1.00 20.34 ATOM 76 O LYS A 11 22.916 17.704 -1.964 1.00 21.57 ATOM 77 CB LYS A 11 20.720 19.836 -0.840 1.00 35.19 ATOM 78 CG LYS A 11 19.468 20.384 -1.400 1.00 32.06 ATOM 79 CD LYS A 11 19.244 21.832 -1.028 1.00 45.07 ATOM 80 CE LYS A 11 17.972 22.320 -1.736 1.00 49.94 ATOM 81 NZ LYS A 11 17.692 23.720 -1.384 1.00 54.50 ATOM 82 N ALA A 12 22.404 17.384 0.204 1.00 21.65 ATOM 83 CA ALA A 12 23.752 16.956 0.388 1.00 27.22 ATOM 84 C ALA A 12 23.936 15.572 -0.208 1.00 37.74 ATOM 85 O ALA A 12 24.948 15.252 -0.840 1.00 35.95 ATOM 86 CB ALA A 12 24.000 16.876 1.892 1.00 35.97 ATOM 87 N ALA A 13 22.940 14.744 -0.040 1.00 22.44 ATOM 88 CA ALA A 13 23.132 13.404 -0.580 1.00 21.57 ATOM 89 C ALA A 13 23.120 13.388 -2.140 1.00 23.91 ATOM 90 O ALA A 13 23.816 12.612 -2.820 1.00 23.65 ATOM 91 CB ALA A 13 21.960 12.576 -0.036 1.00 24.67 ATOM 92 N TRP A 14 22.236 14.236 -2.672 1.00 24.02 ATOM 93 CA TRP A 14 22.044 14.144 -4.116 1.00 22.05 ATOM 94 C TRP A 14 23.252 14.836 -4.772 1.00 34.63 ATOM 95 O TRP A 14 23.700 14.496 -5.880 1.00 31.41 ATOM 96 CB TRP A 14 20.688 14.800 -4.432 1.00 27.59 ATOM 97 CG TRP A 14 20.264 14.488 -5.848 1.00 23.72 ATOM 98 CD1 TRP A 14 20.380 15.308 -6.992 1.00 27.02 ATOM 99 CD2 TRP A 14 19.684 13.284 -6.276 1.00 22.06 ATOM 100 NE1 TRP A 14 19.864 14.604 -8.108 1.00 33.70 ATOM 101 CE2 TRP A 14 19.460 13.388 -7.684 1.00 34.36 ATOM 102 CE3 TRP A 14 19.356 12.132 -5.596 1.00 32.89 ATOM 103 CZ2 TRP A 14 18.936 12.380 -8.456 1.00 37.27 ATOM 104 CZ3 TRP A 14 18.816 11.104 -6.380 1.00 36.23 ATOM 105 CH2 TRP A 14 18.624 11.224 -7.768 1.00 37.57 ATOM 106 N GLY A 15 23.776 15.776 -4.004 1.00 40.19 ATOM 107 CA GLY A 15 25.012 16.460 -4.408 1.00 36.71 ATOM 108 C GLY A 15 26.092 15.408 -4.660 1.00 35.30 ATOM 109 O GLY A 15 26.744 15.460 -5.712 1.00 40.18 ATOM 110 N LYS A 16 26.240 14.484 -3.724 1.00 36.93 ATOM 111 CA LYS A 16 27.200 13.372 -3.840 1.00 28.32 ATOM 112 C LYS A 16 26.892 12.504 -5.060 1.00 30.41 ATOM 113 O LYS A 16 27.816 11.920 -5.636 1.00 36.47 ATOM 114 CB LYS A 16 27.244 12.460 -2.588 1.00 27.04 ATOM 115 CG LYS A 16 28.416 11.464 -2.684 1.00 44.22 ATOM 116 CD LYS A 16 29.816 12.112 -2.568 1.00 54.36 ATOM 117 CE LYS A 16 30.940 11.136 -2.952 1.00 52.60 ATOM 118 NZ LYS A 16 30.740 9.848 -2.284 1.00 50.80 ATOM 119 N VAL A 17 25.596 12.428 -5.416 1.00 41.05 ATOM 120 CA VAL A 17 25.172 11.488 -6.428 1.00 32.09 ATOM 121 C VAL A 17 25.772 12.064 -7.700 1.00 43.28 ATOM 122 O VAL A 17 26.412 11.324 -8.444 1.00 37.34 ATOM 123 CB VAL A 17 23.660 11.304 -6.492 1.00 22.22 ATOM 124 CG1 VAL A 17 23.228 10.888 -7.876 1.00 24.93 ATOM 125 CG2 VAL A 17 23.068 10.424 -5.360 1.00 19.54 ATOM 126 N GLY A 18 25.624 13.384 -7.796 1.00 39.21 ATOM 127 CA GLY A 18 26.228 14.176 -8.868 1.00 40.23 ATOM 128 C GLY A 18 25.924 13.564 -10.232 1.00 32.26 ATOM 129 O GLY A 18 24.768 13.548 -10.684 1.00 39.85 ATOM 130 N ALA A 19 26.996 13.036 -10.788 1.00 31.71 ATOM 131 CA ALA A 19 27.048 12.776 -12.228 1.00 38.51 ATOM 132 C ALA A 19 26.648 11.340 -12.520 1.00 37.26 ATOM 133 O ALA A 19 26.436 10.944 -13.676 1.00 42.56 ATOM 134 CB ALA A 19 28.468 13.088 -12.756 1.00 42.24 ATOM 135 N HIS A 20 26.484 10.576 -11.468 1.00 21.67 ATOM 136 CA HIS A 20 26.064 9.188 -11.588 1.00 18.49 ATOM 137 C HIS A 20 24.540 9.108 -11.580 1.00 17.46 ATOM 138 O HIS A 20 24.008 8.000 -11.504 1.00 19.61 ATOM 139 CB HIS A 20 26.516 8.436 -10.364 1.00 35.15 ATOM 140 CG HIS A 20 28.036 8.320 -10.316 1.00 41.14 ATOM 141 ND1 HIS A 20 28.780 7.584 -11.264 1.00 48.40 ATOM 142 CD2 HIS A 20 28.884 8.884 -9.416 1.00 44.00 ATOM 143 CE1 HIS A 20 30.128 7.708 -10.916 1.00 52.97 ATOM 144 NE2 HIS A 20 30.196 8.504 -9.780 1.00 47.77 ATOM 145 N ALA A 21 23.904 10.264 -11.652 1.00 32.73 ATOM 146 CA ALA A 21 22.464 10.252 -11.368 1.00 39.31 ATOM 147 C ALA A 21 21.764 9.312 -12.372 1.00 44.57 ATOM 148 O ALA A 21 20.916 8.500 -12.000 1.00 29.52 ATOM 149 CB ALA A 21 21.876 11.672 -11.284 1.00 27.88 ATOM 150 N GLY A 22 22.168 9.380 -13.604 1.00 27.73 ATOM 151 CA GLY A 22 21.516 8.564 -14.596 1.00 26.45 ATOM 152 C GLY A 22 21.824 7.084 -14.480 1.00 37.45 ATOM 153 O GLY A 22 20.988 6.260 -14.824 1.00 38.53 ATOM 154 N GLU A 23 23.012 6.748 -14.060 1.00 25.00 ATOM 155 CA GLU A 23 23.404 5.336 -13.928 1.00 14.74 ATOM 156 C GLU A 23 22.620 4.772 -12.712 1.00 12.32 ATOM 157 O GLU A 23 22.208 3.608 -12.692 1.00 16.33 ATOM 158 CB GLU A 23 24.916 5.448 -13.708 1.00 27.54 ATOM 159 CG GLU A 23 25.760 4.196 -13.656 1.00 44.47 ATOM 160 CD GLU A 23 27.140 4.684 -13.160 1.00 62.57 ATOM 161 OE1 GLU A 23 27.476 4.344 -12.004 1.00 49.41 ATOM 162 OE2 GLU A 23 27.804 5.464 -13.880 1.00 48.38 ATOM 163 N TYR A 24 22.464 5.596 -11.708 1.00 19.32 ATOM 164 CA TYR A 24 21.748 5.196 -10.508 1.00 23.55 ATOM 165 C TYR A 24 20.272 5.040 -10.848 1.00 18.89 ATOM 166 O TYR A 24 19.640 4.120 -10.316 1.00 17.43 ATOM 167 CB TYR A 24 21.856 6.180 -9.324 1.00 24.45 ATOM 168 CG TYR A 24 23.276 6.192 -8.704 1.00 17.32 ATOM 169 CD1 TYR A 24 23.596 7.004 -7.640 1.00 27.48 ATOM 170 CD2 TYR A 24 24.236 5.356 -9.228 1.00 16.55 ATOM 171 CE1 TYR A 24 24.896 7.008 -7.128 1.00 23.56 ATOM 172 CE2 TYR A 24 25.528 5.352 -8.732 1.00 29.26 ATOM 173 CZ TYR A 24 25.852 6.200 -7.684 1.00 28.03 ATOM 174 OH TYR A 24 27.172 6.364 -7.340 1.00 31.65 ATOM 175 N GLY A 25 19.732 5.992 -11.632 1.00 18.67 ATOM 176 CA GLY A 25 18.336 5.884 -12.136 1.00 20.96 ATOM 177 C GLY A 25 18.100 4.556 -12.868 1.00 14.73 ATOM 178 O GLY A 25 17.072 3.900 -12.684 1.00 16.21 ATOM 179 N ALA A 26 18.988 4.140 -13.760 1.00 14.20 ATOM 180 CA ALA A 26 18.784 2.876 -14.416 1.00 14.23 ATOM 181 C ALA A 26 18.868 1.636 -13.512 1.00 13.21 ATOM 182 O ALA A 26 18.152 0.640 -13.656 1.00 14.01 ATOM 183 CB ALA A 26 19.852 2.692 -15.444 1.00 20.07 ATOM 184 N GLU A 27 19.804 1.704 -12.580 1.00 13.40 ATOM 185 CA GLU A 27 19.948 0.596 -11.652 1.00 16.51 ATOM 186 C GLU A 27 18.680 0.472 -10.796 1.00 10.39 ATOM 187 O GLU A 27 18.224 -0.644 -10.576 1.00 14.16 ATOM 188 CB GLU A 27 21.208 0.880 -10.796 1.00 19.44 ATOM 189 CG GLU A 27 21.368 -0.196 -9.744 1.00 20.79 ATOM 190 CD GLU A 27 22.584 0.016 -8.816 1.00 28.85 ATOM 191 OE1 GLU A 27 22.476 -0.372 -7.656 1.00 21.53 ATOM 192 OE2 GLU A 27 23.628 0.504 -9.268 1.00 22.95 ATOM 193 N ALA A 28 18.108 1.580 -10.324 1.00 11.39 ATOM 194 CA ALA A 28 16.884 1.488 -9.512 1.00 15.88 ATOM 195 C ALA A 28 15.752 0.880 -10.344 1.00 18.19 ATOM 196 O ALA A 28 14.916 0.124 -9.844 1.00 12.00 ATOM 197 CB ALA A 28 16.456 2.880 -9.068 1.00 18.23 ATOM 198 N LEU A 29 15.688 1.284 -11.644 1.00 13.33 ATOM 199 CA LEU A 29 14.644 0.632 -12.512 1.00 19.05 ATOM 200 C LEU A 29 14.840 -0.876 -12.604 1.00 11.53 ATOM 201 O LEU A 29 13.876 -1.640 -12.472 1.00 11.40 ATOM 202 CB LEU A 29 14.648 1.232 -13.960 1.00 14.56 ATOM 203 CG LEU A 29 14.268 2.700 -13.976 1.00 14.23 ATOM 204 CD1 LEU A 29 14.592 3.260 -15.348 1.00 17.95 ATOM 205 CD2 LEU A 29 12.768 2.760 -13.712 1.00 18.08 ATOM 206 N GLU A 30 16.080 -1.300 -12.884 1.00 12.89 ATOM 207 CA GLU A 30 16.328 -2.740 -12.984 1.00 15.05 ATOM 208 C GLU A 30 16.040 -3.468 -11.660 1.00 14.83 ATOM 209 O GLU A 30 15.540 -4.592 -11.688 1.00 18.74 ATOM 210 CB GLU A 30 17.752 -2.944 -13.420 1.00 21.84 ATOM 211 CG GLU A 30 18.128 -4.392 -13.388 1.00 29.11 ATOM 212 CD GLU A 30 19.504 -4.564 -14.060 1.00 43.98 ATOM 213 OE1 GLU A 30 20.280 -3.592 -14.128 1.00 43.05 ATOM 214 OE2 GLU A 30 19.784 -5.700 -14.460 1.00 41.94 ATOM 215 N ARG A 31 16.340 -2.808 -10.528 1.00 14.14 ATOM 216 CA ARG A 31 15.992 -3.400 -9.228 1.00 14.35 ATOM 217 C ARG A 31 14.480 -3.588 -9.088 1.00 17.92 ATOM 218 O ARG A 31 14.056 -4.668 -8.616 1.00 18.72 ATOM 219 CB ARG A 31 16.532 -2.616 -8.064 1.00 9.24 ATOM 220 CG ARG A 31 18.060 -2.708 -7.968 1.00 11.77 ATOM 221 CD ARG A 31 18.572 -1.804 -6.856 1.00 19.69 ATOM 222 NE ARG A 31 20.072 -1.856 -6.640 1.00 15.98 ATOM 223 CZ ARG A 31 20.708 -2.856 -6.060 1.00 13.75 ATOM 224 NH1 ARG A 31 20.072 -3.908 -5.540 1.00 13.93 ATOM 225 NH2 ARG A 31 22.040 -2.812 -6.088 1.00 19.73 ATOM 226 N MET A 32 13.764 -2.552 -9.524 1.00 12.12 ATOM 227 CA MET A 32 12.312 -2.604 -9.476 1.00 9.87 ATOM 228 C MET A 32 11.744 -3.732 -10.360 1.00 11.20 ATOM 229 O MET A 32 10.880 -4.512 -9.928 1.00 15.20 ATOM 230 CB MET A 32 11.736 -1.252 -9.880 1.00 12.29 ATOM 231 CG MET A 32 10.212 -1.176 -9.804 1.00 16.45 ATOM 232 SD MET A 32 9.564 0.404 -10.376 1.00 15.55 ATOM 233 CE MET A 32 9.956 0.204 -12.104 1.00 14.11 ATOM 234 N PHE A 33 12.176 -3.832 -11.588 1.00 15.44 ATOM 235 CA PHE A 33 11.624 -4.888 -12.500 1.00 16.70 ATOM 236 C PHE A 33 11.916 -6.276 -12.012 1.00 12.86 ATOM 237 O PHE A 33 11.112 -7.164 -12.244 1.00 17.73 ATOM 238 CB PHE A 33 12.220 -4.808 -13.872 1.00 11.73 ATOM 239 CG PHE A 33 11.888 -3.492 -14.584 1.00 12.31 ATOM 240 CD1 PHE A 33 10.644 -2.928 -14.512 1.00 16.95 ATOM 241 CD2 PHE A 33 12.880 -2.856 -15.320 1.00 21.33 ATOM 242 CE1 PHE A 33 10.364 -1.732 -15.164 1.00 20.60 ATOM 243 CE2 PHE A 33 12.600 -1.640 -15.980 1.00 19.17 ATOM 244 CZ PHE A 33 11.348 -1.084 -15.900 1.00 12.88 ATOM 245 N LEU A 34 13.060 -6.464 -11.288 1.00 18.30 ATOM 246 CA LEU A 34 13.364 -7.820 -10.804 1.00 15.04 ATOM 247 C LEU A 34 12.648 -8.096 -9.472 1.00 19.44 ATOM 248 O LEU A 34 12.252 -9.232 -9.232 1.00 22.21 ATOM 249 CB LEU A 34 14.832 -7.960 -10.524 1.00 18.71 ATOM 250 CG LEU A 34 15.664 -7.952 -11.780 1.00 28.30 ATOM 251 CD1 LEU A 34 17.184 -8.060 -11.524 1.00 29.56 ATOM 252 CD2 LEU A 34 15.176 -9.056 -12.668 1.00 35.62 ATOM 253 N SER A 35 12.504 -7.088 -8.596 1.00 16.86 ATOM 254 CA SER A 35 12.008 -7.388 -7.264 1.00 14.29 ATOM 255 C SER A 35 10.492 -7.376 -7.236 1.00 15.54 ATOM 256 O SER A 35 9.852 -8.044 -6.412 1.00 15.86 ATOM 257 CB SER A 35 12.432 -6.296 -6.276 1.00 12.15 ATOM 258 OG SER A 35 13.792 -6.480 -5.980 1.00 16.89 ATOM 259 N PHE A 36 9.964 -6.536 -8.140 1.00 14.57 ATOM 260 CA PHE A 36 8.508 -6.284 -8.260 1.00 12.66 ATOM 261 C PHE A 36 8.068 -6.412 -9.712 1.00 10.29 ATOM 262 O PHE A 36 7.776 -5.384 -10.388 1.00 14.22 ATOM 263 CB PHE A 36 8.112 -4.900 -7.696 1.00 17.63 ATOM 264 CG PHE A 36 8.700 -4.648 -6.300 1.00 16.41 ATOM 265 CD1 PHE A 36 9.772 -3.796 -6.144 1.00 14.73 ATOM 266 CD2 PHE A 36 8.148 -5.312 -5.204 1.00 20.03 ATOM 267 CE1 PHE A 36 10.328 -3.616 -4.884 1.00 18.21 ATOM 268 CE2 PHE A 36 8.700 -5.132 -3.928 1.00 14.33 ATOM 269 CZ PHE A 36 9.788 -4.300 -3.776 1.00 15.43 ATOM 270 N PRO A 37 7.952 -7.616 -10.148 1.00 16.42 ATOM 271 CA PRO A 37 7.660 -7.892 -11.580 1.00 20.72 ATOM 272 C PRO A 37 6.368 -7.292 -12.088 1.00 17.19 ATOM 273 O PRO A 37 6.232 -7.044 -13.300 1.00 19.40 ATOM 274 CB PRO A 37 7.728 -9.384 -11.776 1.00 20.44 ATOM 275 CG PRO A 37 7.780 -9.972 -10.388 1.00 25.07 ATOM 276 CD PRO A 37 8.204 -8.836 -9.440 1.00 25.57 ATOM 277 N THR A 38 5.452 -6.992 -11.188 1.00 19.05 ATOM 278 CA THR A 38 4.196 -6.396 -11.704 1.00 15.81 ATOM 279 C THR A 38 4.452 -5.040 -12.356 1.00 12.98 ATOM 280 O THR A 38 3.664 -4.588 -13.188 1.00 16.95 ATOM 281 CB THR A 38 3.176 -6.260 -10.536 1.00 21.76 ATOM 282 OG1 THR A 38 3.696 -5.544 -9.464 1.00 25.53 ATOM 283 CG2 THR A 38 2.840 -7.696 -10.112 1.00 23.22 ATOM 284 N THR A 39 5.528 -4.388 -11.972 1.00 19.04 ATOM 285 CA THR A 39 5.804 -3.060 -12.556 1.00 14.59 ATOM 286 C THR A 39 6.160 -3.152 -14.056 1.00 10.29 ATOM 287 O THR A 39 6.072 -2.164 -14.768 1.00 15.11 ATOM 288 CB THR A 39 6.940 -2.396 -11.784 1.00 15.75 ATOM 289 OG1 THR A 39 8.180 -3.124 -11.824 1.00 15.48 ATOM 290 CG2 THR A 39 6.580 -2.176 -10.316 1.00 21.07 ATOM 291 N LYS A 40 6.488 -4.312 -14.504 1.00 13.99 ATOM 292 CA LYS A 40 6.864 -4.476 -15.896 1.00 21.14 ATOM 293 C LYS A 40 5.624 -4.320 -16.804 1.00 20.39 ATOM 294 O LYS A 40 5.760 -4.156 -18.004 1.00 16.61 ATOM 295 CB LYS A 40 7.436 -5.896 -16.140 1.00 14.72 ATOM 296 CG LYS A 40 8.832 -6.224 -15.632 1.00 14.49 ATOM 297 CD LYS A 40 8.980 -7.636 -16.120 1.00 29.55 ATOM 298 CE LYS A 40 9.496 -8.580 -15.152 1.00 34.73 ATOM 299 NZ LYS A 40 9.604 -9.888 -15.792 1.00 22.96 ATOM 300 N THR A 41 4.428 -4.392 -16.240 1.00 15.51 ATOM 301 CA THR A 41 3.216 -4.224 -17.028 1.00 16.55 ATOM 302 C THR A 41 3.128 -2.808 -17.608 1.00 17.54 ATOM 303 O THR A 41 2.316 -2.548 -18.516 1.00 16.61 ATOM 304 CB THR A 41 1.968 -4.512 -16.180 1.00 17.58 ATOM 305 OG1 THR A 41 1.884 -3.576 -15.120 1.00 17.58 ATOM 306 CG2 THR A 41 1.896 -5.936 -15.656 1.00 16.29 ATOM 307 N TYR A 42 3.904 -1.848 -17.096 1.00 12.28 ATOM 308 CA TYR A 42 3.828 -0.500 -17.692 1.00 16.17 ATOM 309 C TYR A 42 4.876 -0.300 -18.820 1.00 10.21 ATOM 310 O TYR A 42 4.840 0.740 -19.480 1.00 14.27 ATOM 311 CB TYR A 42 4.080 0.504 -16.616 1.00 16.00 ATOM 312 CG TYR A 42 2.896 0.508 -15.636 1.00 12.77 ATOM 313 CD1 TYR A 42 1.752 1.224 -15.900 1.00 18.68 ATOM 314 CD2 TYR A 42 2.984 -0.240 -14.472 1.00 15.04 ATOM 315 CE1 TYR A 42 0.696 1.196 -15.020 1.00 21.15 ATOM 316 CE2 TYR A 42 1.912 -0.252 -13.584 1.00 13.32 ATOM 317 CZ TYR A 42 0.768 0.464 -13.860 1.00 19.66 ATOM 318 OH TYR A 42 -0.272 0.444 -12.976 1.00 19.74 ATOM 319 N PHE A 43 5.796 -1.284 -18.972 1.00 15.03 ATOM 320 CA PHE A 43 6.852 -1.184 -19.980 1.00 17.69 ATOM 321 C PHE A 43 6.832 -2.352 -20.956 1.00 23.70 ATOM 322 O PHE A 43 7.888 -2.892 -21.296 1.00 23.16 ATOM 323 CB PHE A 43 8.180 -1.120 -19.252 1.00 16.20 ATOM 324 CG PHE A 43 8.348 0.112 -18.328 1.00 15.83 ATOM 325 CD1 PHE A 43 7.904 0.048 -17.016 1.00 14.57 ATOM 326 CD2 PHE A 43 8.912 1.268 -18.776 1.00 17.90 ATOM 327 CE1 PHE A 43 8.048 1.136 -16.180 1.00 17.83 ATOM 328 CE2 PHE A 43 9.068 2.388 -17.944 1.00 16.81 ATOM 329 CZ PHE A 43 8.624 2.304 -16.620 1.00 18.57 ATOM 330 N PRO A 44 5.692 -2.732 -21.488 1.00 18.90 ATOM 331 CA PRO A 44 5.660 -3.864 -22.440 1.00 20.70 ATOM 332 C PRO A 44 6.348 -3.476 -23.796 1.00 22.04 ATOM 333 O PRO A 44 6.756 -4.296 -24.600 1.00 23.83 ATOM 334 CB PRO A 44 4.200 -4.108 -22.660 1.00 25.56 ATOM 335 CG PRO A 44 3.596 -2.704 -22.536 1.00 24.80 ATOM 336 CD PRO A 44 4.376 -2.080 -21.396 1.00 21.03 ATOM 337 N HIS A 45 6.552 -2.240 -24.032 1.00 21.73 ATOM 338 CA HIS A 45 7.184 -1.768 -25.280 1.00 27.16 ATOM 339 C HIS A 45 8.696 -1.564 -25.176 1.00 23.29 ATOM 340 O HIS A 45 9.280 -1.060 -26.132 1.00 21.87 ATOM 341 CB HIS A 45 6.564 -0.404 -25.636 1.00 30.28 ATOM 342 CG HIS A 45 6.632 0.696 -24.560 1.00 22.01 ATOM 343 ND1 HIS A 45 6.172 0.492 -23.244 1.00 28.14 ATOM 344 CD2 HIS A 45 7.140 1.984 -24.656 1.00 22.62 ATOM 345 CE1 HIS A 45 6.372 1.672 -22.524 1.00 26.71 ATOM 346 NE2 HIS A 45 6.980 2.608 -23.408 1.00 30.86 ATOM 347 N PHE A 46 9.304 -1.916 -23.992 1.00 22.28 ATOM 348 CA PHE A 46 10.732 -1.756 -23.768 1.00 16.91 ATOM 349 C PHE A 46 11.440 -3.096 -23.856 1.00 20.97 ATOM 350 O PHE A 46 10.908 -4.156 -23.480 1.00 19.92 ATOM 351 CB PHE A 46 11.012 -1.240 -22.348 1.00 21.58 ATOM 352 CG PHE A 46 11.068 0.276 -22.240 1.00 22.18 ATOM 353 CD1 PHE A 46 11.760 0.856 -21.204 1.00 21.61 ATOM 354 CD2 PHE A 46 10.440 1.076 -23.148 1.00 34.00 ATOM 355 CE1 PHE A 46 11.816 2.224 -21.064 1.00 19.87 ATOM 356 CE2 PHE A 46 10.492 2.472 -23.024 1.00 34.72 ATOM 357 CZ PHE A 46 11.176 3.060 -21.976 1.00 26.89 ATOM 358 N ASP A 47 12.672 -2.988 -24.336 1.00 20.17 ATOM 359 CA ASP A 47 13.576 -4.128 -24.100 1.00 22.87 ATOM 360 C ASP A 47 14.048 -3.980 -22.644 1.00 20.13 ATOM 361 O ASP A 47 14.784 -3.040 -22.340 1.00 20.10 ATOM 362 CB ASP A 47 14.776 -3.944 -25.024 1.00 19.32 ATOM 363 CG ASP A 47 15.780 -5.064 -24.856 1.00 23.82 ATOM 364 OD1 ASP A 47 15.508 -6.120 -24.276 1.00 30.34 ATOM 365 OD2 ASP A 47 16.876 -4.852 -25.372 1.00 40.61 ATOM 366 N LEU A 48 13.592 -4.852 -21.824 1.00 24.24 ATOM 367 CA LEU A 48 13.976 -4.768 -20.452 1.00 18.31 ATOM 368 C LEU A 48 15.168 -5.656 -20.124 1.00 39.06 ATOM 369 O LEU A 48 15.332 -6.012 -18.948 1.00 43.79 ATOM 370 CB LEU A 48 12.808 -5.116 -19.500 1.00 18.99 ATOM 371 CG LEU A 48 11.620 -4.156 -19.616 1.00 23.58 ATOM 372 CD1 LEU A 48 10.448 -4.664 -18.748 1.00 38.48 ATOM 373 CD2 LEU A 48 11.936 -2.728 -19.352 1.00 20.12 ATOM 374 N SER A 49 16.000 -5.976 -21.112 1.00 36.09 ATOM 375 CA SER A 49 17.156 -6.772 -20.716 1.00 36.08 ATOM 376 C SER A 49 18.216 -5.856 -20.104 1.00 31.80 ATOM 377 O SER A 49 18.208 -4.620 -20.268 1.00 23.02 ATOM 378 CB SER A 49 17.636 -7.672 -21.844 1.00 30.87 ATOM 379 OG SER A 49 17.872 -6.896 -22.972 1.00 37.54 ATOM 380 N HIS A 50 19.096 -6.492 -19.324 1.00 31.65 ATOM 381 CA HIS A 50 20.064 -5.708 -18.572 1.00 39.87 ATOM 382 C HIS A 50 20.904 -4.848 -19.500 1.00 22.24 ATOM 383 O HIS A 50 21.464 -5.376 -20.476 1.00 30.69 ATOM 384 CB HIS A 50 21.004 -6.704 -17.872 1.00 48.17 ATOM 385 CG HIS A 50 22.144 -5.992 -17.140 1.00 41.25 ATOM 386 ND1 HIS A 50 21.912 -5.048 -16.148 1.00 38.71 ATOM 387 CD2 HIS A 50 23.500 -6.124 -17.296 1.00 43.94 ATOM 388 CE1 HIS A 50 23.116 -4.568 -15.688 1.00 42.82 ATOM 389 NE2 HIS A 50 24.104 -5.236 -16.400 1.00 43.64 ATOM 390 N GLY A 51 20.956 -3.596 -19.228 1.00 22.98 ATOM 391 CA GLY A 51 21.840 -2.676 -19.928 1.00 41.58 ATOM 392 C GLY A 51 21.228 -2.116 -21.216 1.00 38.25 ATOM 393 O GLY A 51 21.908 -1.432 -21.984 1.00 34.89 ATOM 394 N SER A 52 19.964 -2.416 -21.436 1.00 35.43 ATOM 395 CA SER A 52 19.356 -1.888 -22.672 1.00 28.06 ATOM 396 C SER A 52 19.372 -0.372 -22.708 1.00 17.25 ATOM 397 O SER A 52 19.240 0.344 -21.708 1.00 23.38 ATOM 398 CB SER A 52 17.932 -2.372 -22.836 1.00 23.92 ATOM 399 OG SER A 52 17.044 -1.524 -22.168 1.00 26.81 ATOM 400 N ALA A 53 19.544 0.132 -23.916 1.00 20.16 ATOM 401 CA ALA A 53 19.532 1.580 -24.112 1.00 26.98 ATOM 402 C ALA A 53 18.216 2.236 -23.640 1.00 16.04 ATOM 403 O ALA A 53 18.256 3.368 -23.148 1.00 17.26 ATOM 404 CB ALA A 53 19.668 1.844 -25.632 1.00 30.75 ATOM 405 N GLN A 54 17.088 1.492 -23.768 1.00 18.00 ATOM 406 CA GLN A 54 15.804 2.104 -23.408 1.00 16.57 ATOM 407 C GLN A 54 15.776 2.332 -21.892 1.00 21.30 ATOM 408 O GLN A 54 15.244 3.376 -21.492 1.00 19.43 ATOM 409 CB GLN A 54 14.656 1.136 -23.740 1.00 17.75 ATOM 410 CG GLN A 54 14.168 1.352 -25.172 1.00 21.22 ATOM 411 CD GLN A 54 13.460 0.140 -25.772 1.00 19.40 ATOM 412 OE1 GLN A 54 13.916 -0.996 -25.624 1.00 25.94 ATOM 413 NE2 GLN A 54 12.476 0.420 -26.616 1.00 24.26 ATOM 414 N VAL A 55 16.268 1.320 -21.148 1.00 16.55 ATOM 415 CA VAL A 55 16.296 1.460 -19.660 1.00 17.85 ATOM 416 C VAL A 55 17.300 2.516 -19.196 1.00 15.77 ATOM 417 O VAL A 55 17.004 3.360 -18.344 1.00 17.89 ATOM 418 CB VAL A 55 16.576 0.084 -19.040 1.00 16.80 ATOM 419 CG1 VAL A 55 16.864 0.180 -17.540 1.00 22.32 ATOM 420 CG2 VAL A 55 15.388 -0.796 -19.308 1.00 22.23 ATOM 421 N LYS A 56 18.488 2.488 -19.772 1.00 16.83 ATOM 422 CA LYS A 56 19.456 3.528 -19.452 1.00 17.56 ATOM 423 C LYS A 56 18.916 4.908 -19.752 1.00 20.31 ATOM 424 O LYS A 56 19.096 5.832 -18.948 1.00 19.07 ATOM 425 CB LYS A 56 20.792 3.296 -20.144 1.00 21.03 ATOM 426 CG LYS A 56 21.496 2.028 -19.676 1.00 33.20 ATOM 427 CD LYS A 56 22.908 2.044 -20.332 1.00 54.34 ATOM 428 CE LYS A 56 23.884 0.912 -19.936 1.00 53.54 ATOM 429 NZ LYS A 56 25.164 1.108 -20.668 1.00 46.61 ATOM 430 N GLY A 57 18.280 5.024 -20.924 1.00 19.80 ATOM 431 CA GLY A 57 17.700 6.308 -21.328 1.00 24.27 ATOM 432 C GLY A 57 16.612 6.764 -20.344 1.00 21.80 ATOM 433 O GLY A 57 16.620 7.924 -19.892 1.00 21.79 ATOM 434 N HIS A 58 15.744 5.820 -19.996 1.00 19.52 ATOM 435 CA HIS A 58 14.668 6.200 -19.064 1.00 17.21 ATOM 436 C HIS A 58 15.212 6.528 -17.636 1.00 14.02 ATOM 437 O HIS A 58 14.748 7.484 -16.996 1.00 17.42 ATOM 438 CB HIS A 58 13.656 5.076 -19.080 1.00 17.72 ATOM 439 CG HIS A 58 12.392 5.480 -18.300 1.00 16.50 ATOM 440 ND1 HIS A 58 11.672 6.624 -18.568 1.00 21.16 ATOM 441 CD2 HIS A 58 11.800 4.832 -17.268 1.00 20.11 ATOM 442 CE1 HIS A 58 10.636 6.660 -17.656 1.00 20.38 ATOM 443 NE2 HIS A 58 10.720 5.560 -16.872 1.00 22.93 ATOM 444 N GLY A 59 16.196 5.776 -17.224 1.00 14.90 ATOM 445 CA GLY A 59 16.916 6.032 -15.916 1.00 16.19 ATOM 446 C GLY A 59 17.424 7.460 -15.812 1.00 19.47 ATOM 447 O GLY A 59 17.256 8.168 -14.792 1.00 16.48 ATOM 448 N LYS A 60 18.016 7.932 -16.920 1.00 20.96 ATOM 449 CA LYS A 60 18.544 9.324 -16.984 1.00 21.79 ATOM 450 C LYS A 60 17.420 10.324 -16.904 1.00 16.95 ATOM 451 O LYS A 60 17.568 11.352 -16.256 1.00 19.24 ATOM 452 CB LYS A 60 19.280 9.544 -18.312 1.00 31.97 ATOM 453 CG LYS A 60 20.072 10.832 -18.420 1.00 35.24 ATOM 454 CD LYS A 60 20.768 10.812 -19.800 1.00 53.28 ATOM 455 CE LYS A 60 21.800 11.928 -20.096 1.00 57.30 ATOM 456 NZ LYS A 60 22.568 11.568 -21.368 1.00 50.17 ATOM 457 N LYS A 61 16.312 9.996 -17.556 1.00 15.27 ATOM 458 CA LYS A 61 15.172 10.924 -17.508 1.00 17.77 ATOM 459 C LYS A 61 14.588 10.992 -16.112 1.00 17.98 ATOM 460 O LYS A 61 14.244 12.104 -15.696 1.00 22.99 ATOM 461 CB LYS A 61 14.024 10.508 -18.420 1.00 25.35 ATOM 462 CG LYS A 61 14.280 10.848 -19.892 1.00 40.78 ATOM 463 CD LYS A 61 13.164 10.204 -20.688 1.00 43.42 ATOM 464 CE LYS A 61 13.280 10.448 -22.180 1.00 57.26 ATOM 465 NZ LYS A 61 12.376 9.504 -22.868 1.00 41.24 ATOM 466 N VAL A 62 14.556 9.836 -15.476 1.00 16.67 ATOM 467 CA VAL A 62 14.016 9.816 -14.084 1.00 17.07 ATOM 468 C VAL A 62 14.900 10.664 -13.128 1.00 23.98 ATOM 469 O VAL A 62 14.440 11.548 -12.392 1.00 15.79 ATOM 470 CB VAL A 62 13.856 8.364 -13.660 1.00 11.41 ATOM 471 CG1 VAL A 62 13.556 8.232 -12.160 1.00 19.43 ATOM 472 CG2 VAL A 62 12.640 7.844 -14.416 1.00 16.39 ATOM 473 N ALA A 63 16.164 10.392 -13.276 1.00 17.53 ATOM 474 CA ALA A 63 17.204 11.080 -12.500 1.00 17.46 ATOM 475 C ALA A 63 17.220 12.580 -12.756 1.00 15.20 ATOM 476 O ALA A 63 17.324 13.360 -11.812 1.00 18.52 ATOM 477 CB ALA A 63 18.532 10.388 -12.856 1.00 38.14 ATOM 478 N ASP A 64 17.056 13.044 -14.000 1.00 19.17 ATOM 479 CA ASP A 64 17.012 14.496 -14.188 1.00 25.07 ATOM 480 C ASP A 64 15.808 15.160 -13.548 1.00 19.48 ATOM 481 O ASP A 64 15.932 16.244 -12.984 1.00 19.61 ATOM 482 CB ASP A 64 17.004 14.848 -15.672 1.00 40.22 ATOM 483 CG ASP A 64 18.408 14.612 -16.260 1.00 39.91 ATOM 484 OD1 ASP A 64 19.352 14.328 -15.492 1.00 38.45 ATOM 485 OD2 ASP A 64 18.516 14.668 -17.492 1.00 41.01 ATOM 486 N ALA A 65 14.656 14.492 -13.624 1.00 15.57 ATOM 487 CA ALA A 65 13.484 14.984 -12.940 1.00 21.17 ATOM 488 C ALA A 65 13.724 15.044 -11.420 1.00 17.60 ATOM 489 O ALA A 65 13.296 16.008 -10.776 1.00 18.11 ATOM 490 CB ALA A 65 12.300 14.056 -13.276 1.00 25.68 ATOM 491 N LEU A 66 14.400 14.056 -10.876 1.00 14.59 ATOM 492 CA LEU A 66 14.672 14.136 -9.436 1.00 12.33 ATOM 493 C LEU A 66 15.628 15.284 -9.152 1.00 18.87 ATOM 494 O LEU A 66 15.464 16.064 -8.192 1.00 19.56 ATOM 495 CB LEU A 66 15.224 12.840 -8.900 1.00 16.92 ATOM 496 CG LEU A 66 14.156 11.728 -8.852 1.00 20.17 ATOM 497 CD1 LEU A 66 14.716 10.344 -8.596 1.00 16.55 ATOM 498 CD2 LEU A 66 12.904 12.024 -8.028 1.00 22.60 ATOM 499 N THR A 67 16.596 15.400 -10.004 1.00 15.67 ATOM 500 CA THR A 67 17.504 16.544 -9.832 1.00 16.81 ATOM 501 C THR A 67 16.772 17.896 -9.904 1.00 22.27 ATOM 502 O THR A 67 16.996 18.816 -9.084 1.00 27.16 ATOM 503 CB THR A 67 18.576 16.480 -10.912 1.00 24.50 ATOM 504 OG1 THR A 67 19.364 15.332 -10.760 1.00 26.91 ATOM 505 CG2 THR A 67 19.436 17.736 -10.928 1.00 29.72 ATOM 506 N ASN A 68 15.860 18.016 -10.856 1.00 23.87 ATOM 507 CA ASN A 68 15.008 19.220 -10.916 1.00 20.70 ATOM 508 C ASN A 68 14.224 19.412 -9.608 1.00 31.40 ATOM 509 O ASN A 68 14.100 20.544 -9.144 1.00 27.43 ATOM 510 CB ASN A 68 14.024 19.084 -12.080 1.00 29.82 ATOM 511 CG ASN A 68 13.100 20.304 -12.256 1.00 35.85 ATOM 512 OD1 ASN A 68 13.460 21.424 -11.960 1.00 37.85 ATOM 513 ND2 ASN A 68 11.940 20.104 -12.856 1.00 40.17 ATOM 514 N ALA A 69 13.720 18.312 -8.992 1.00 17.95 ATOM 515 CA ALA A 69 12.908 18.528 -7.808 1.00 13.22 ATOM 516 C ALA A 69 13.796 18.908 -6.624 1.00 12.93 ATOM 517 O ALA A 69 13.324 19.680 -5.796 1.00 18.68 ATOM 518 CB ALA A 69 12.236 17.220 -7.492 1.00 22.21 ATOM 519 N VAL A 70 15.012 18.336 -6.520 1.00 19.14 ATOM 520 CA VAL A 70 15.924 18.764 -5.420 1.00 18.10 ATOM 521 C VAL A 70 16.284 20.244 -5.572 1.00 20.25 ATOM 522 O VAL A 70 16.328 20.948 -4.572 1.00 20.68 ATOM 523 CB VAL A 70 17.140 17.880 -5.436 1.00 16.98 ATOM 524 CG1 VAL A 70 18.296 18.340 -4.552 1.00 23.81 ATOM 525 CG2 VAL A 70 16.772 16.432 -5.068 1.00 27.28 ATOM 526 N ALA A 71 16.476 20.704 -6.824 1.00 24.22 ATOM 527 CA ALA A 71 16.772 22.104 -7.096 1.00 25.08 ATOM 528 C ALA A 71 15.632 22.996 -6.660 1.00 27.78 ATOM 529 O ALA A 71 15.896 24.132 -6.264 1.00 34.63 ATOM 530 CB ALA A 71 17.016 22.348 -8.572 1.00 32.86 ATOM 531 N HIS A 72 14.412 22.508 -6.756 1.00 22.13 ATOM 532 CA HIS A 72 13.268 23.348 -6.476 1.00 20.63 ATOM 533 C HIS A 72 12.432 22.748 -5.372 1.00 19.25 ATOM 534 O HIS A 72 11.208 22.712 -5.520 1.00 25.88 ATOM 535 CB HIS A 72 12.360 23.432 -7.712 1.00 36.78 ATOM 536 CG HIS A 72 13.172 24.056 -8.844 1.00 31.79 ATOM 537 ND1 HIS A 72 13.232 25.440 -9.036 1.00 39.87 ATOM 538 CD2 HIS A 72 13.940 23.460 -9.816 1.00 37.41 ATOM 539 CE1 HIS A 72 14.060 25.680 -10.132 1.00 39.39 ATOM 540 NE2 HIS A 72 14.512 24.472 -10.636 1.00 38.18 ATOM 541 N VAL A 73 13.084 22.316 -4.320 1.00 22.31 ATOM 542 CA VAL A 73 12.420 21.540 -3.304 1.00 24.16 ATOM 543 C VAL A 73 11.336 22.368 -2.644 1.00 32.69 ATOM 544 O VAL A 73 10.340 21.800 -2.204 1.00 41.59 ATOM 545 CB VAL A 73 13.520 20.960 -2.404 1.00 40.48 ATOM 546 CG1 VAL A 73 14.184 21.952 -1.460 1.00 46.24 ATOM 547 CG2 VAL A 73 13.140 19.664 -1.708 1.00 46.50 ATOM 548 N ASP A 74 11.476 23.684 -2.676 1.00 32.98 ATOM 549 CA ASP A 74 10.500 24.572 -2.036 1.00 35.65 ATOM 550 C ASP A 74 9.272 24.816 -2.916 1.00 40.51 ATOM 551 O ASP A 74 8.300 25.432 -2.460 1.00 43.77 ATOM 552 CB ASP A 74 11.188 25.920 -1.724 1.00 45.38 ATOM 553 CG ASP A 74 12.204 25.720 -0.580 1.00 49.18 ATOM 554 OD1 ASP A 74 11.764 25.216 0.448 1.00 48.95 ATOM 555 OD2 ASP A 74 13.408 26.016 -0.720 1.00 45.58 ATOM 556 N ASP A 75 9.296 24.340 -4.120 1.00 35.75 ATOM 557 CA ASP A 75 8.276 24.604 -5.152 1.00 36.56 ATOM 558 C ASP A 75 8.048 23.408 -6.096 1.00 21.14 ATOM 559 O ASP A 75 7.928 23.524 -7.328 1.00 25.18 ATOM 560 CB ASP A 75 8.916 25.700 -5.996 1.00 56.94 ATOM 561 CG ASP A 75 7.828 26.392 -6.784 1.00 62.67 ATOM 562 OD1 ASP A 75 6.792 26.724 -6.180 1.00 49.83 ATOM 563 OD2 ASP A 75 8.028 26.552 -7.996 1.00 49.43 ATOM 564 N MET A 76 8.008 22.260 -5.536 1.00 28.92 ATOM 565 CA MET A 76 7.944 21.032 -6.364 1.00 25.39 ATOM 566 C MET A 76 6.668 20.932 -7.212 1.00 29.68 ATOM 567 O MET A 76 6.764 20.544 -8.376 1.00 26.26 ATOM 568 CB MET A 76 7.976 19.828 -5.432 1.00 30.33 ATOM 569 CG MET A 76 9.392 19.476 -5.076 1.00 42.71 ATOM 570 SD MET A 76 9.448 17.740 -4.564 1.00 39.99 ATOM 571 CE MET A 76 9.392 17.960 -2.808 1.00 42.87 ATOM 572 N PRO A 77 5.496 21.220 -6.676 1.00 26.25 ATOM 573 CA PRO A 77 4.300 21.332 -7.508 1.00 31.86 ATOM 574 C PRO A 77 4.544 22.080 -8.824 1.00 38.25 ATOM 575 O PRO A 77 4.200 21.504 -9.868 1.00 33.74 ATOM 576 CB PRO A 77 3.188 21.928 -6.640 1.00 36.61 ATOM 577 CG PRO A 77 3.864 22.344 -5.344 1.00 50.53 ATOM 578 CD PRO A 77 5.132 21.524 -5.272 1.00 32.17 ATOM 579 N ASN A 78 5.148 23.268 -8.796 1.00 34.40 ATOM 580 CA ASN A 78 5.304 24.032 -10.040 1.00 36.22 ATOM 581 C ASN A 78 6.400 23.388 -10.848 1.00 29.15 ATOM 582 O ASN A 78 6.296 23.264 -12.072 1.00 34.62 ATOM 583 CB ASN A 78 5.680 25.492 -9.856 1.00 44.21 ATOM 584 CG ASN A 78 4.444 26.260 -9.448 1.00 53.27 ATOM 585 OD1 ASN A 78 4.144 26.380 -8.248 1.00 54.64 ATOM 586 ND2 ASN A 78 3.692 26.672 -10.456 1.00 53.17 ATOM 587 N ALA A 79 7.384 22.912 -10.136 1.00 20.99 ATOM 588 CA ALA A 79 8.532 22.412 -10.876 1.00 26.92 ATOM 589 C ALA A 79 8.240 21.128 -11.700 1.00 27.25 ATOM 590 O ALA A 79 8.760 20.972 -12.800 1.00 24.65 ATOM 591 CB ALA A 79 9.656 22.192 -9.876 1.00 33.74 ATOM 592 N LEU A 80 7.428 20.240 -11.168 1.00 26.68 ATOM 593 CA LEU A 80 7.084 18.932 -11.780 1.00 29.40 ATOM 594 C LEU A 80 5.712 18.984 -12.516 1.00 27.01 ATOM 595 O LEU A 80 5.144 17.932 -12.828 1.00 22.37 ATOM 596 CB LEU A 80 7.020 17.852 -10.676 1.00 17.12 ATOM 597 CG LEU A 80 8.368 17.580 -10.012 1.00 26.76 ATOM 598 CD1 LEU A 80 8.248 16.576 -8.860 1.00 29.81 ATOM 599 CD2 LEU A 80 9.368 17.104 -11.072 1.00 37.93 ATOM 600 N SER A 81 5.180 20.180 -12.784 1.00 23.08 ATOM 601 CA SER A 81 3.796 20.288 -13.252 1.00 19.25 ATOM 602 C SER A 81 3.592 19.472 -14.540 1.00 21.86 ATOM 603 O SER A 81 2.588 18.748 -14.728 1.00 25.93 ATOM 604 CB SER A 81 3.572 21.800 -13.484 1.00 37.32 ATOM 605 OG SER A 81 2.188 21.976 -13.680 1.00 40.64 ATOM 606 N ALA A 82 4.608 19.536 -15.408 1.00 24.23 ATOM 607 CA ALA A 82 4.516 18.876 -16.692 1.00 18.94 ATOM 608 C ALA A 82 4.464 17.372 -16.456 1.00 25.65 ATOM 609 O ALA A 82 3.684 16.676 -17.116 1.00 22.93 ATOM 610 CB ALA A 82 5.680 19.264 -17.600 1.00 20.32 ATOM 611 N LEU A 83 5.288 16.912 -15.528 1.00 22.93 ATOM 612 CA LEU A 83 5.360 15.448 -15.296 1.00 21.01 ATOM 613 C LEU A 83 4.124 14.944 -14.564 1.00 20.98 ATOM 614 O LEU A 83 3.672 13.832 -14.864 1.00 19.16 ATOM 615 CB LEU A 83 6.552 15.172 -14.392 1.00 24.83 ATOM 616 CG LEU A 83 7.596 14.248 -14.956 1.00 40.33 ATOM 617 CD1 LEU A 83 7.616 14.308 -16.472 1.00 30.38 ATOM 618 CD2 LEU A 83 8.976 14.544 -14.328 1.00 40.98 ATOM 619 N SER A 84 3.564 15.732 -13.652 1.00 14.23 ATOM 620 CA SER A 84 2.312 15.292 -13.056 1.00 17.45 ATOM 621 C SER A 84 1.192 15.220 -14.092 1.00 15.33 ATOM 622 O SER A 84 0.372 14.332 -13.880 1.00 21.52 ATOM 623 CB SER A 84 1.752 16.128 -11.868 1.00 18.24 ATOM 624 OG SER A 84 2.336 17.384 -11.936 1.00 33.14 ATOM 625 N ASP A 85 1.160 16.140 -15.084 1.00 18.91 ATOM 626 CA ASP A 85 0.064 16.032 -16.096 1.00 20.02 ATOM 627 C ASP A 85 0.272 14.752 -16.904 1.00 20.22 ATOM 628 O ASP A 85 -0.688 14.040 -17.136 1.00 21.23 ATOM 629 CB ASP A 85 0.036 17.216 -17.072 1.00 37.87 ATOM 630 CG ASP A 85 -0.492 18.508 -16.436 1.00 47.79 ATOM 631 OD1 ASP A 85 -1.388 18.388 -15.612 1.00 45.14 ATOM 632 OD2 ASP A 85 -0.068 19.612 -16.824 1.00 44.92 ATOM 633 N LEU A 86 1.524 14.452 -17.260 1.00 22.24 ATOM 634 CA LEU A 86 1.848 13.300 -18.088 1.00 15.47 ATOM 635 C LEU A 86 1.476 11.992 -17.392 1.00 16.48 ATOM 636 O LEU A 86 0.904 11.068 -17.992 1.00 17.11 ATOM 637 CB LEU A 86 3.344 13.372 -18.408 1.00 16.85 ATOM 638 CG LEU A 86 3.816 12.176 -19.172 1.00 24.81 ATOM 639 CD1 LEU A 86 3.184 12.124 -20.544 1.00 44.42 ATOM 640 CD2 LEU A 86 5.336 12.084 -19.316 1.00 36.03 ATOM 641 N HIS A 87 1.804 11.920 -16.084 1.00 15.37 ATOM 642 CA HIS A 87 1.448 10.664 -15.428 1.00 17.57 ATOM 643 C HIS A 87 -0.076 10.580 -15.188 1.00 15.83 ATOM 644 O HIS A 87 -0.636 9.480 -15.236 1.00 15.41 ATOM 645 CB HIS A 87 2.220 10.532 -14.096 1.00 17.54 ATOM 646 CG HIS A 87 3.688 10.140 -14.360 1.00 18.32 ATOM 647 ND1 HIS A 87 4.612 11.108 -14.720 1.00 15.66 ATOM 648 CD2 HIS A 87 4.356 8.904 -14.316 1.00 15.15 ATOM 649 CE1 HIS A 87 5.800 10.468 -14.896 1.00 13.35 ATOM 650 NE2 HIS A 87 5.680 9.112 -14.652 1.00 14.28 ATOM 651 N ALA A 88 -0.700 11.736 -14.892 1.00 22.64 ATOM 652 CA ALA A 88 -2.148 11.668 -14.604 1.00 22.80 ATOM 653 C ALA A 88 -2.984 11.420 -15.876 1.00 30.92 ATOM 654 O ALA A 88 -3.968 10.696 -15.804 1.00 24.84 ATOM 655 CB ALA A 88 -2.676 12.900 -13.864 1.00 16.92 ATOM 656 N HIS A 89 -2.584 12.012 -16.992 1.00 20.87 ATOM 657 CA HIS A 89 -3.472 11.960 -18.164 1.00 25.73 ATOM 658 C HIS A 89 -3.096 10.980 -19.264 1.00 23.27 ATOM 659 O HIS A 89 -3.948 10.528 -20.044 1.00 25.19 ATOM 660 CB HIS A 89 -3.596 13.364 -18.716 1.00 28.76 ATOM 661 CG HIS A 89 -4.180 14.276 -17.628 1.00 41.30 ATOM 662 ND1 HIS A 89 -5.240 13.876 -16.776 1.00 41.23 ATOM 663 CD2 HIS A 89 -3.808 15.560 -17.288 1.00 41.53 ATOM 664 CE1 HIS A 89 -5.520 14.940 -15.908 1.00 37.43 ATOM 665 NE2 HIS A 89 -4.632 15.956 -16.240 1.00 40.90 ATOM 666 N LYS A 90 -1.860 10.620 -19.320 1.00 16.71 ATOM 667 CA LYS A 90 -1.392 9.724 -20.368 1.00 25.11 ATOM 668 C LYS A 90 -0.920 8.376 -19.804 1.00 25.19 ATOM 669 O LYS A 90 -1.524 7.344 -20.112 1.00 25.93 ATOM 670 CB LYS A 90 -0.272 10.436 -21.152 1.00 28.52 ATOM 671 CG LYS A 90 -0.784 11.728 -21.828 1.00 43.69 ATOM 672 CD LYS A 90 -1.992 11.456 -22.736 1.00 55.18 ATOM 673 CE LYS A 90 -2.464 12.684 -23.520 1.00 63.00 ATOM 674 NZ LYS A 90 -3.632 12.296 -24.348 1.00 57.65 ATOM 675 N LEU A 91 0.052 8.380 -18.904 1.00 15.85 ATOM 676 CA LEU A 91 0.696 7.132 -18.540 1.00 17.18 ATOM 677 C LEU A 91 -0.216 6.348 -17.592 1.00 18.54 ATOM 678 O LEU A 91 -0.364 5.136 -17.752 1.00 17.73 ATOM 679 CB LEU A 91 2.048 7.404 -17.812 1.00 13.88 ATOM 680 CG LEU A 91 3.000 8.120 -18.748 1.00 14.86 ATOM 681 CD1 LEU A 91 4.276 8.452 -18.032 1.00 20.68 ATOM 682 CD2 LEU A 91 3.256 7.284 -19.996 1.00 19.69 ATOM 683 N ARG A 92 -0.748 7.064 -16.640 1.00 17.19 ATOM 684 CA ARG A 92 -1.776 6.540 -15.684 1.00 15.48 ATOM 685 C ARG A 92 -1.308 5.332 -14.900 1.00 15.14 ATOM 686 O ARG A 92 -1.972 4.284 -14.836 1.00 17.56 ATOM 687 CB ARG A 92 -3.072 6.196 -16.448 1.00 22.45 ATOM 688 CG ARG A 92 -3.792 7.412 -16.964 1.00 22.19 ATOM 689 CD ARG A 92 -4.144 6.968 -18.376 1.00 46.53 ATOM 690 NE ARG A 92 -5.424 7.312 -18.716 1.00 43.48 ATOM 691 CZ ARG A 92 -5.756 7.096 -20.000 1.00 35.23 ATOM 692 NH1 ARG A 92 -4.904 6.664 -20.940 1.00 25.90 ATOM 693 NH2 ARG A 92 -6.996 7.232 -20.252 1.00 34.04 ATOM 694 N VAL A 93 -0.156 5.472 -14.296 1.00 15.02 ATOM 695 CA VAL A 93 0.436 4.412 -13.508 1.00 15.73 ATOM 696 C VAL A 93 -0.272 4.356 -12.172 1.00 13.15 ATOM 697 O VAL A 93 -0.492 5.396 -11.536 1.00 16.72 ATOM 698 CB VAL A 93 1.892 4.748 -13.304 1.00 11.15 ATOM 699 CG1 VAL A 93 2.484 3.796 -12.284 1.00 15.98 ATOM 700 CG2 VAL A 93 2.648 4.756 -14.652 1.00 14.35 ATOM 701 N ASP A 94 -0.680 3.168 -11.740 1.00 14.27 ATOM 702 CA ASP A 94 -1.400 3.148 -10.452 1.00 13.16 ATOM 703 C ASP A 94 -0.440 3.664 -9.340 1.00 9.53 ATOM 704 O ASP A 94 0.732 3.340 -9.348 1.00 14.52 ATOM 705 CB ASP A 94 -1.788 1.724 -10.136 1.00 12.83 ATOM 706 CG ASP A 94 -2.688 1.716 -8.900 1.00 21.75 ATOM 707 OD1 ASP A 94 -3.900 1.696 -9.076 1.00 19.96 ATOM 708 OD2 ASP A 94 -2.180 1.768 -7.780 1.00 20.06 ATOM 709 N PRO A 95 -0.920 4.452 -8.436 1.00 13.86 ATOM 710 CA PRO A 95 -0.124 5.104 -7.404 1.00 13.24 ATOM 711 C PRO A 95 0.712 4.140 -6.584 1.00 15.52 ATOM 712 O PRO A 95 1.736 4.540 -6.032 1.00 24.32 ATOM 713 CB PRO A 95 -1.108 5.776 -6.488 1.00 20.67 ATOM 714 CG PRO A 95 -2.156 6.216 -7.484 1.00 21.89 ATOM 715 CD PRO A 95 -2.288 5.000 -8.400 1.00 17.63 ATOM 716 N VAL A 96 0.264 2.900 -6.488 1.00 13.50 ATOM 717 CA VAL A 96 0.972 1.992 -5.608 1.00 14.64 ATOM 718 C VAL A 96 2.412 1.796 -6.088 1.00 22.04 ATOM 719 O VAL A 96 3.336 1.548 -5.304 1.00 16.91 ATOM 720 CB VAL A 96 0.156 0.676 -5.600 1.00 21.72 ATOM 721 CG1 VAL A 96 0.252 -0.104 -6.888 1.00 41.97 ATOM 722 CG2 VAL A 96 0.616 -0.212 -4.524 1.00 44.74 ATOM 723 N ASN A 97 2.616 1.928 -7.384 1.00 15.35 ATOM 724 CA ASN A 97 3.940 1.608 -7.972 1.00 12.80 ATOM 725 C ASN A 97 4.972 2.696 -7.660 1.00 7.68 ATOM 726 O ASN A 97 6.144 2.332 -7.712 1.00 11.43 ATOM 727 CB ASN A 97 3.872 1.436 -9.512 1.00 16.75 ATOM 728 CG ASN A 97 2.936 0.272 -9.816 1.00 20.24 ATOM 729 OD1 ASN A 97 3.376 -0.876 -9.748 1.00 12.99 ATOM 730 ND2 ASN A 97 1.648 0.572 -10.132 1.00 22.39 ATOM 731 N PHE A 98 4.568 3.896 -7.284 1.00 8.80 ATOM 732 CA PHE A 98 5.508 4.952 -6.900 1.00 14.61 ATOM 733 C PHE A 98 6.296 4.540 -5.632 1.00 12.81 ATOM 734 O PHE A 98 7.496 4.824 -5.516 1.00 13.49 ATOM 735 CB PHE A 98 4.804 6.296 -6.696 1.00 17.92 ATOM 736 CG PHE A 98 4.360 6.848 -8.036 1.00 14.58 ATOM 737 CD1 PHE A 98 5.180 7.764 -8.640 1.00 15.15 ATOM 738 CD2 PHE A 98 3.180 6.428 -8.628 1.00 14.32 ATOM 739 CE1 PHE A 98 4.836 8.276 -9.848 1.00 23.40 ATOM 740 CE2 PHE A 98 2.832 6.952 -9.872 1.00 17.18 ATOM 741 CZ PHE A 98 3.668 7.868 -10.468 1.00 18.23 ATOM 742 N LYS A 99 5.624 3.852 -4.744 1.00 14.65 ATOM 743 CA LYS A 99 6.228 3.320 -3.488 1.00 14.36 ATOM 744 C LYS A 99 7.276 2.304 -3.804 1.00 14.77 ATOM 745 O LYS A 99 8.320 2.348 -3.164 1.00 14.23 ATOM 746 CB LYS A 99 5.156 2.820 -2.496 1.00 22.38 ATOM 747 CG LYS A 99 4.260 4.036 -2.312 1.00 46.07 ATOM 748 CD LYS A 99 3.128 3.940 -1.312 1.00 61.09 ATOM 749 CE LYS A 99 2.176 2.768 -1.576 1.00 57.41 ATOM 750 NZ LYS A 99 1.116 2.812 -0.540 1.00 63.51 ATOM 751 N LEU A 100 7.044 1.484 -4.832 1.00 11.06 ATOM 752 CA LEU A 100 7.992 0.440 -5.184 1.00 8.76 ATOM 753 C LEU A 100 9.232 1.036 -5.836 1.00 10.93 ATOM 754 O LEU A 100 10.328 0.656 -5.476 1.00 13.73 ATOM 755 CB LEU A 100 7.328 -0.568 -6.092 1.00 13.23 ATOM 756 CG LEU A 100 6.024 -1.124 -5.548 1.00 20.94 ATOM 757 CD1 LEU A 100 5.312 -2.056 -6.572 1.00 22.91 ATOM 758 CD2 LEU A 100 6.316 -1.944 -4.320 1.00 21.12 ATOM 759 N LEU A 101 9.104 1.988 -6.732 1.00 12.81 ATOM 760 CA LEU A 101 10.276 2.620 -7.328 1.00 14.07 ATOM 761 C LEU A 101 11.036 3.440 -6.260 1.00 17.69 ATOM 762 O LEU A 101 12.272 3.464 -6.244 1.00 18.62 ATOM 763 CB LEU A 101 9.788 3.484 -8.484 1.00 15.24 ATOM 764 CG LEU A 101 10.948 4.272 -9.116 1.00 17.96 ATOM 765 CD1 LEU A 101 12.104 3.416 -9.588 1.00 18.54 ATOM 766 CD2 LEU A 101 10.436 5.200 -10.224 1.00 20.38 ATOM 767 N SER A 102 10.320 4.104 -5.348 1.00 15.41 ATOM 768 CA SER A 102 10.976 4.860 -4.272 1.00 9.50 ATOM 769 C SER A 102 11.880 3.952 -3.408 1.00 10.02 ATOM 770 O SER A 102 13.036 4.360 -3.100 1.00 12.63 ATOM 771 CB SER A 102 9.876 5.556 -3.420 1.00 13.59 ATOM 772 OG SER A 102 9.220 6.620 -4.116 1.00 16.06 ATOM 773 N HIS A 103 11.344 2.776 -3.008 1.00 12.82 ATOM 774 CA HIS A 103 12.084 1.776 -2.244 1.00 11.52 ATOM 775 C HIS A 103 13.372 1.400 -3.000 1.00 15.67 ATOM 776 O HIS A 103 14.488 1.364 -2.448 1.00 13.62 ATOM 777 CB HIS A 103 11.188 0.600 -1.844 1.00 19.23 ATOM 778 CG HIS A 103 12.020 -0.468 -1.152 1.00 17.69 ATOM 779 ND1 HIS A 103 12.228 -1.672 -1.756 1.00 10.57 ATOM 780 CD2 HIS A 103 12.668 -0.496 0.060 1.00 12.72 ATOM 781 CE1 HIS A 103 13.024 -2.384 -0.944 1.00 21.57 ATOM 782 NE2 HIS A 103 13.316 -1.708 0.192 1.00 14.05 ATOM 783 N CYS A 104 13.232 1.188 -4.316 1.00 13.99 ATOM 784 CA CYS A 104 14.424 0.712 -5.088 1.00 12.63 ATOM 785 C CYS A 104 15.408 1.836 -5.304 1.00 6.21 ATOM 786 O CYS A 104 16.600 1.560 -5.416 1.00 12.64 ATOM 787 CB CYS A 104 14.004 0.084 -6.408 1.00 16.42 ATOM 788 SG CYS A 104 13.104 -1.456 -6.236 1.00 15.32 ATOM 789 N LEU A 105 14.956 3.076 -5.332 1.00 9.01 ATOM 790 CA LEU A 105 15.908 4.180 -5.484 1.00 11.84 ATOM 791 C LEU A 105 16.656 4.336 -4.148 1.00 13.96 ATOM 792 O LEU A 105 17.868 4.568 -4.132 1.00 15.69 ATOM 793 CB LEU A 105 15.012 5.388 -5.820 1.00 19.46 ATOM 794 CG LEU A 105 15.516 6.516 -6.728 1.00 34.09 ATOM 795 CD1 LEU A 105 15.880 6.012 -8.088 1.00 27.94 ATOM 796 CD2 LEU A 105 14.384 7.536 -6.904 1.00 45.39 ATOM 797 N LEU A 106 15.944 4.144 -3.044 1.00 11.71 ATOM 798 CA LEU A 106 16.584 4.228 -1.708 1.00 12.80 ATOM 799 C LEU A 106 17.636 3.132 -1.536 1.00 13.36 ATOM 800 O LEU A 106 18.776 3.396 -1.056 1.00 13.19 ATOM 801 CB LEU A 106 15.392 4.100 -0.780 1.00 15.25 ATOM 802 CG LEU A 106 15.328 4.900 0.428 1.00 20.18 ATOM 803 CD1 LEU A 106 15.560 6.396 0.236 1.00 17.34 ATOM 804 CD2 LEU A 106 14.020 4.540 1.100 1.00 23.62 ATOM 805 N VAL A 107 17.308 1.908 -1.984 1.00 8.67 ATOM 806 CA VAL A 107 18.244 0.812 -1.992 1.00 7.92 ATOM 807 C VAL A 107 19.448 1.132 -2.856 1.00 13.66 ATOM 808 O VAL A 107 20.580 0.824 -2.476 1.00 13.67 ATOM 809 CB VAL A 107 17.564 -0.464 -2.472 1.00 12.77 ATOM 810 CG1 VAL A 107 18.588 -1.512 -2.836 1.00 17.92 ATOM 811 CG2 VAL A 107 16.564 -1.008 -1.424 1.00 12.57 ATOM 812 N THR A 108 19.240 1.772 -3.984 1.00 12.78 ATOM 813 CA THR A 108 20.360 2.028 -4.900 1.00 11.76 ATOM 814 C THR A 108 21.284 3.044 -4.224 1.00 11.93 ATOM 815 O THR A 108 22.516 2.908 -4.252 1.00 14.17 ATOM 816 CB THR A 108 19.764 2.548 -6.268 1.00 9.99 ATOM 817 OG1 THR A 108 19.020 1.524 -6.944 1.00 11.00 ATOM 818 CG2 THR A 108 20.892 2.876 -7.208 1.00 17.50 ATOM 819 N LEU A 109 20.668 4.092 -3.608 1.00 12.79 ATOM 820 CA LEU A 109 21.476 5.124 -2.964 1.00 12.56 ATOM 821 C LEU A 109 22.280 4.484 -1.804 1.00 18.55 ATOM 822 O LEU A 109 23.472 4.772 -1.612 1.00 15.51 ATOM 823 CB LEU A 109 20.560 6.208 -2.464 1.00 14.26 ATOM 824 CG LEU A 109 20.224 7.356 -3.416 1.00 18.74 ATOM 825 CD1 LEU A 109 20.600 7.232 -4.848 1.00 26.58 ATOM 826 CD2 LEU A 109 18.904 7.984 -3.144 1.00 17.95 ATOM 827 N ALA A 110 21.600 3.632 -1.052 1.00 14.27 ATOM 828 CA ALA A 110 22.300 3.016 0.092 1.00 16.57 ATOM 829 C ALA A 110 23.540 2.224 -0.340 1.00 17.57 ATOM 830 O ALA A 110 24.604 2.220 0.288 1.00 15.09 ATOM 831 CB ALA A 110 21.316 2.080 0.772 1.00 16.34 ATOM 832 N ALA A 111 23.408 1.516 -1.456 1.00 17.35 ATOM 833 CA ALA A 111 24.460 0.688 -2.016 1.00 13.99 ATOM 834 C ALA A 111 25.636 1.496 -2.576 1.00 14.64 ATOM 835 O ALA A 111 26.672 0.884 -2.760 1.00 21.73 ATOM 836 CB ALA A 111 23.964 -0.240 -3.128 1.00 17.06 ATOM 837 N HIS A 112 25.436 2.776 -2.852 1.00 18.32 ATOM 838 CA HIS A 112 26.448 3.580 -3.532 1.00 27.46 ATOM 839 C HIS A 112 26.996 4.680 -2.640 1.00 21.95 ATOM 840 O HIS A 112 28.048 5.228 -3.004 1.00 24.48 ATOM 841 CB HIS A 112 25.916 4.268 -4.832 1.00 16.32 ATOM 842 CG HIS A 112 25.816 3.288 -5.972 1.00 16.40 ATOM 843 ND1 HIS A 112 26.948 3.044 -6.764 1.00 19.18 ATOM 844 CD2 HIS A 112 24.712 2.540 -6.420 1.00 15.70 ATOM 845 CE1 HIS A 112 26.488 2.052 -7.712 1.00 20.39 ATOM 846 NE2 HIS A 112 25.124 1.752 -7.500 1.00 16.44 ATOM 847 N LEU A 113 26.288 4.996 -1.568 1.00 17.46 ATOM 848 CA LEU A 113 26.720 6.144 -0.724 1.00 18.06 ATOM 849 C LEU A 113 26.944 5.652 0.700 1.00 13.82 ATOM 850 O LEU A 113 26.240 6.116 1.584 1.00 20.57 ATOM 851 CB LEU A 113 25.652 7.212 -0.640 1.00 29.38 ATOM 852 CG LEU A 113 25.328 7.944 -1.960 1.00 30.22 ATOM 853 CD1 LEU A 113 24.464 9.188 -1.720 1.00 39.10 ATOM 854 CD2 LEU A 113 26.572 8.332 -2.748 1.00 36.88 ATOM 855 N PRO A 114 27.864 4.744 0.932 1.00 19.32 ATOM 856 CA PRO A 114 28.156 4.140 2.260 1.00 30.73 ATOM 857 C PRO A 114 28.352 5.268 3.300 1.00 29.86 ATOM 858 O PRO A 114 27.736 5.216 4.360 1.00 26.41 ATOM 859 CB PRO A 114 29.428 3.332 2.028 1.00 29.21 ATOM 860 CG PRO A 114 30.060 3.896 0.772 1.00 18.64 ATOM 861 CD PRO A 114 28.828 4.268 -0.036 1.00 16.65 ATOM 862 N ALA A 115 29.112 6.332 3.004 1.00 22.49 ATOM 863 CA ALA A 115 29.356 7.316 4.100 1.00 26.78 ATOM 864 C ALA A 115 28.176 8.256 4.396 1.00 24.82 ATOM 865 O ALA A 115 28.004 8.748 5.516 1.00 24.01 ATOM 866 CB ALA A 115 30.560 8.148 3.736 1.00 40.21 ATOM 867 N GLU A 116 27.388 8.560 3.404 1.00 18.48 ATOM 868 CA GLU A 116 26.340 9.608 3.532 1.00 22.45 ATOM 869 C GLU A 116 24.952 9.068 3.936 1.00 19.48 ATOM 870 O GLU A 116 24.100 9.856 4.332 1.00 23.56 ATOM 871 CB GLU A 116 26.164 10.260 2.144 1.00 23.33 ATOM 872 CG GLU A 116 27.312 11.156 1.704 1.00 29.47 ATOM 873 CD GLU A 116 28.408 10.332 1.040 1.00 28.62 ATOM 874 OE1 GLU A 116 28.248 9.132 0.820 1.00 35.77 ATOM 875 OE2 GLU A 116 29.452 10.908 0.708 1.00 41.74 ATOM 876 N PHE A 117 24.716 7.788 3.784 1.00 15.67 ATOM 877 CA PHE A 117 23.428 7.164 4.084 1.00 18.56 ATOM 878 C PHE A 117 23.204 6.868 5.592 1.00 17.61 ATOM 879 O PHE A 117 23.000 5.732 6.028 1.00 20.37 ATOM 880 CB PHE A 117 23.260 5.912 3.212 1.00 13.41 ATOM 881 CG PHE A 117 21.792 5.456 3.044 1.00 11.14 ATOM 882 CD1 PHE A 117 20.944 6.140 2.192 1.00 18.45 ATOM 883 CD2 PHE A 117 21.324 4.372 3.768 1.00 17.00 ATOM 884 CE1 PHE A 117 19.628 5.728 2.044 1.00 17.57 ATOM 885 CE2 PHE A 117 20.000 3.952 3.640 1.00 22.23 ATOM 886 CZ PHE A 117 19.160 4.640 2.772 1.00 15.24 ATOM 887 N THR A 118 23.176 7.928 6.360 1.00 13.10 ATOM 888 CA THR A 118 22.964 7.792 7.788 1.00 11.24 ATOM 889 C THR A 118 21.472 7.640 8.016 1.00 14.00 ATOM 890 O THR A 118 20.696 7.924 7.108 1.00 14.85 ATOM 891 CB THR A 118 23.416 9.068 8.468 1.00 26.47 ATOM 892 OG1 THR A 118 22.652 10.260 8.012 1.00 25.00 ATOM 893 CG2 THR A 118 24.816 9.332 8.312 1.00 25.00 ATOM 894 N PRO A 119 21.080 7.260 9.216 1.00 17.81 ATOM 895 CA PRO A 119 19.676 7.172 9.608 1.00 10.53 ATOM 896 C PRO A 119 18.912 8.440 9.304 1.00 9.46 ATOM 897 O PRO A 119 17.804 8.408 8.784 1.00 13.68 ATOM 898 CB PRO A 119 19.684 6.852 11.116 1.00 13.69 ATOM 899 CG PRO A 119 20.980 6.068 11.260 1.00 18.69 ATOM 900 CD PRO A 119 21.948 6.788 10.320 1.00 20.10 ATOM 901 N ALA A 120 19.500 9.572 9.632 1.00 16.67 ATOM 902 CA ALA A 120 18.772 10.796 9.424 1.00 16.91 ATOM 903 C ALA A 120 18.652 11.084 7.912 1.00 11.29 ATOM 904 O ALA A 120 17.632 11.580 7.440 1.00 16.53 ATOM 905 CB ALA A 120 19.368 11.988 10.196 1.00 18.86 ATOM 906 N VAL A 121 19.624 10.748 7.168 1.00 15.17 ATOM 907 CA VAL A 121 19.532 11.040 5.736 1.00 13.62 ATOM 908 C VAL A 121 18.564 10.056 5.076 1.00 14.87 ATOM 909 O VAL A 121 17.756 10.464 4.244 1.00 16.55 ATOM 910 CB VAL A 121 20.908 11.008 5.060 1.00 15.10 ATOM 911 CG1 VAL A 121 20.860 10.968 3.528 1.00 18.69 ATOM 912 CG2 VAL A 121 21.824 12.156 5.496 1.00 18.02 ATOM 913 N HIS A 122 18.624 8.812 5.468 1.00 17.61 ATOM 914 CA HIS A 122 17.644 7.788 5.016 1.00 15.33 ATOM 915 C HIS A 122 16.220 8.308 5.244 1.00 13.57 ATOM 916 O HIS A 122 15.376 8.192 4.356 1.00 14.62 ATOM 917 CB HIS A 122 17.992 6.512 5.792 1.00 16.17 ATOM 918 CG HIS A 122 17.160 5.264 5.560 1.00 17.18 ATOM 919 ND1 HIS A 122 17.512 4.040 6.124 1.00 16.96 ATOM 920 CD2 HIS A 122 16.024 5.112 4.800 1.00 18.01 ATOM 921 CE1 HIS A 122 16.556 3.084 5.716 1.00 21.17 ATOM 922 NE2 HIS A 122 15.612 3.744 4.884 1.00 18.68 ATOM 923 N ALA A 123 15.968 8.816 6.424 1.00 12.13 ATOM 924 CA ALA A 123 14.660 9.312 6.756 1.00 12.36 ATOM 925 C ALA A 123 14.268 10.472 5.820 1.00 16.87 ATOM 926 O ALA A 123 13.140 10.492 5.292 1.00 17.58 ATOM 927 CB ALA A 123 14.588 9.732 8.216 1.00 19.23 ATOM 928 N SER A 124 15.232 11.376 5.604 1.00 12.91 ATOM 929 CA SER A 124 14.968 12.548 4.796 1.00 17.15 ATOM 930 C SER A 124 14.740 12.108 3.344 1.00 13.37 ATOM 931 O SER A 124 13.820 12.652 2.704 1.00 15.71 ATOM 932 CB SER A 124 16.096 13.560 4.872 1.00 16.13 ATOM 933 OG SER A 124 16.136 14.096 6.204 1.00 17.43 ATOM 934 N LEU A 125 15.528 11.164 2.900 1.00 10.20 ATOM 935 CA LEU A 125 15.336 10.784 1.496 1.00 9.31 ATOM 936 C LEU A 125 14.020 10.064 1.288 1.00 12.65 ATOM 937 O LEU A 125 13.432 10.200 0.208 1.00 13.26 ATOM 938 CB LEU A 125 16.440 9.860 1.048 1.00 15.24 ATOM 939 CG LEU A 125 17.780 10.508 0.760 1.00 14.66 ATOM 940 CD1 LEU A 125 18.880 9.472 0.704 1.00 22.82 ATOM 941 CD2 LEU A 125 17.700 11.280 -0.520 1.00 22.47 ATOM 942 N ASP A 126 13.588 9.256 2.272 1.00 14.27 ATOM 943 CA ASP A 126 12.324 8.500 2.112 1.00 14.29 ATOM 944 C ASP A 126 11.180 9.520 2.052 1.00 15.55 ATOM 945 O ASP A 126 10.208 9.444 1.300 1.00 13.23 ATOM 946 CB ASP A 126 12.156 7.544 3.296 1.00 12.80 ATOM 947 CG ASP A 126 10.980 6.576 3.112 1.00 16.72 ATOM 948 OD1 ASP A 126 10.928 5.916 2.092 1.00 22.06 ATOM 949 OD2 ASP A 126 10.084 6.500 3.932 1.00 19.66 ATOM 950 N LYS A 127 11.308 10.536 2.884 1.00 14.27 ATOM 951 CA LYS A 127 10.272 11.512 2.932 1.00 12.63 ATOM 952 C LYS A 127 10.280 12.356 1.636 1.00 19.17 ATOM 953 O LYS A 127 9.228 12.696 1.064 1.00 16.65 ATOM 954 CB LYS A 127 10.588 12.164 4.280 1.00 26.76 ATOM 955 CG LYS A 127 9.692 13.176 4.744 1.00 33.50 ATOM 956 CD LYS A 127 10.124 13.404 6.216 1.00 20.55 ATOM 957 CE LYS A 127 9.388 14.704 6.500 1.00 27.79 ATOM 958 NZ LYS A 127 9.864 15.340 7.692 1.00 35.06 ATOM 959 N PHE A 128 11.428 12.644 1.140 1.00 10.74 ATOM 960 CA PHE A 128 11.516 13.348 -0.136 1.00 12.21 ATOM 961 C PHE A 128 10.880 12.540 -1.276 1.00 14.74 ATOM 962 O PHE A 128 10.116 13.128 -2.060 1.00 15.18 ATOM 963 CB PHE A 128 12.980 13.660 -0.424 1.00 12.00 ATOM 964 CG PHE A 128 13.216 14.204 -1.828 1.00 11.64 ATOM 965 CD1 PHE A 128 12.784 15.456 -2.216 1.00 23.83 ATOM 966 CD2 PHE A 128 13.864 13.412 -2.716 1.00 16.37 ATOM 967 CE1 PHE A 128 13.052 15.880 -3.504 1.00 21.28 ATOM 968 CE2 PHE A 128 14.144 13.824 -3.996 1.00 21.63 ATOM 969 CZ PHE A 128 13.748 15.052 -4.384 1.00 17.71 ATOM 970 N LEU A 129 11.152 11.248 -1.332 1.00 10.79 ATOM 971 CA LEU A 129 10.636 10.448 -2.448 1.00 9.38 ATOM 972 C LEU A 129 9.128 10.312 -2.296 1.00 15.56 ATOM 973 O LEU A 129 8.416 10.280 -3.304 1.00 14.84 ATOM 974 CB LEU A 129 11.312 9.080 -2.500 1.00 13.39 ATOM 975 CG LEU A 129 12.772 9.148 -2.956 1.00 16.32 ATOM 976 CD1 LEU A 129 13.496 7.844 -2.764 1.00 18.89 ATOM 977 CD2 LEU A 129 12.784 9.576 -4.428 1.00 22.34 ATOM 978 N ALA A 130 8.652 10.276 -1.064 1.00 15.95 ATOM 979 CA ALA A 130 7.188 10.284 -0.840 1.00 16.39 ATOM 980 C ALA A 130 6.548 11.580 -1.352 1.00 16.92 ATOM 981 O ALA A 130 5.464 11.572 -1.948 1.00 17.45 ATOM 982 CB ALA A 130 6.864 10.032 0.640 1.00 15.21 ATOM 983 N SER A 131 7.196 12.716 -1.164 1.00 13.86 ATOM 984 CA SER A 131 6.628 13.988 -1.624 1.00 17.43 ATOM 985 C SER A 131 6.652 14.056 -3.144 1.00 16.77 ATOM 986 O SER A 131 5.660 14.560 -3.724 1.00 20.25 ATOM 987 CB SER A 131 7.444 15.176 -1.148 1.00 17.32 ATOM 988 OG SER A 131 7.220 15.216 0.220 1.00 30.17 ATOM 989 N VAL A 132 7.752 13.592 -3.720 1.00 12.59 ATOM 990 CA VAL A 132 7.752 13.596 -5.200 1.00 13.15 ATOM 991 C VAL A 132 6.572 12.744 -5.672 1.00 14.91 ATOM 992 O VAL A 132 5.856 13.204 -6.580 1.00 14.29 ATOM 993 CB VAL A 132 9.116 13.120 -5.712 1.00 16.68 ATOM 994 CG1 VAL A 132 9.180 12.788 -7.200 1.00 21.58 ATOM 995 CG2 VAL A 132 10.180 14.168 -5.412 1.00 18.92 ATOM 996 N SER A 133 6.400 11.552 -5.064 1.00 11.55 ATOM 997 CA SER A 133 5.332 10.620 -5.472 1.00 16.38 ATOM 998 C SER A 133 3.948 11.276 -5.300 1.00 23.84 ATOM 999 O SER A 133 3.072 11.112 -6.156 1.00 21.16 ATOM 1000 CB SER A 133 5.432 9.364 -4.632 1.00 17.02 ATOM 1001 OG SER A 133 6.580 8.656 -5.000 1.00 17.17 ATOM 1002 N THR A 134 3.768 12.048 -4.244 1.00 16.08 ATOM 1003 CA THR A 134 2.532 12.720 -4.024 1.00 12.59 ATOM 1004 C THR A 134 2.296 13.780 -5.064 1.00 13.20 ATOM 1005 O THR A 134 1.176 13.944 -5.528 1.00 17.74 ATOM 1006 CB THR A 134 2.592 13.344 -2.620 1.00 25.21 ATOM 1007 OG1 THR A 134 2.480 12.320 -1.696 1.00 26.41 ATOM 1008 CG2 THR A 134 1.436 14.284 -2.332 1.00 37.82 ATOM 1009 N VAL A 135 3.300 14.516 -5.464 1.00 20.67 ATOM 1010 CA VAL A 135 3.084 15.572 -6.448 1.00 18.67 ATOM 1011 C VAL A 135 2.832 14.888 -7.800 1.00 18.62 ATOM 1012 O VAL A 135 1.964 15.344 -8.548 1.00 19.71 ATOM 1013 CB VAL A 135 4.340 16.468 -6.484 1.00 28.82 ATOM 1014 CG1 VAL A 135 4.456 17.352 -7.716 1.00 28.25 ATOM 1015 CG2 VAL A 135 4.532 17.272 -5.188 1.00 19.42 ATOM 1016 N LEU A 136 3.520 13.792 -8.108 1.00 14.66 ATOM 1017 CA LEU A 136 3.276 13.196 -9.432 1.00 18.56 ATOM 1018 C LEU A 136 1.896 12.528 -9.572 1.00 20.18 ATOM 1019 O LEU A 136 1.416 12.232 -10.684 1.00 18.93 ATOM 1020 CB LEU A 136 4.360 12.184 -9.804 1.00 22.86 ATOM 1021 CG LEU A 136 5.760 12.716 -10.096 1.00 20.67 ATOM 1022 CD1 LEU A 136 6.688 11.556 -10.328 1.00 21.85 ATOM 1023 CD2 LEU A 136 5.844 13.792 -11.176 1.00 23.41 ATOM 1024 N THR A 137 1.260 12.280 -8.440 1.00 15.89 ATOM 1025 CA THR A 137 -0.064 11.600 -8.424 1.00 20.64 ATOM 1026 C THR A 137 -1.184 12.588 -8.144 1.00 16.77 ATOM 1027 O THR A 137 -2.348 12.200 -8.096 1.00 18.08 ATOM 1028 CB THR A 137 0.100 10.560 -7.304 1.00 17.88 ATOM 1029 OG1 THR A 137 0.536 9.340 -7.804 1.00 26.88 ATOM 1030 CG2 THR A 137 -0.512 10.596 -5.960 1.00 39.05 ATOM 1031 N SER A 138 -0.840 13.852 -8.000 1.00 19.73 ATOM 1032 CA SER A 138 -1.708 14.948 -7.588 1.00 25.39 ATOM 1033 C SER A 138 -2.960 15.168 -8.428 1.00 22.77 ATOM 1034 O SER A 138 -4.008 15.520 -7.876 1.00 26.13 ATOM 1035 CB SER A 138 -0.932 16.268 -7.716 1.00 24.31 ATOM 1036 OG SER A 138 -0.664 16.448 -6.440 1.00 45.43 ATOM 1037 N LYS A 139 -2.772 14.988 -9.704 1.00 21.11 ATOM 1038 CA LYS A 139 -3.804 15.396 -10.656 1.00 18.75 ATOM 1039 C LYS A 139 -4.516 14.180 -11.200 1.00 15.10 ATOM 1040 O LYS A 139 -5.172 14.320 -12.220 1.00 22.51 ATOM 1041 CB LYS A 139 -3.176 16.192 -11.788 1.00 21.75 ATOM 1042 CG LYS A 139 -2.592 17.484 -11.272 1.00 28.06 ATOM 1043 CD LYS A 139 -1.628 17.984 -12.316 1.00 32.43 ATOM 1044 CE LYS A 139 -1.140 19.384 -12.020 1.00 46.66 ATOM 1045 NZ LYS A 139 -0.212 19.728 -13.116 1.00 47.47 ATOM 1046 N TYR A 140 -4.376 13.040 -10.564 1.00 15.89 ATOM 1047 CA TYR A 140 -4.972 11.816 -11.112 1.00 22.92 ATOM 1048 C TYR A 140 -6.500 11.832 -11.104 1.00 18.71 ATOM 1049 O TYR A 140 -7.116 11.200 -11.972 1.00 23.97 ATOM 1050 CB TYR A 140 -4.560 10.564 -10.384 1.00 19.85 ATOM 1051 CG TYR A 140 -3.268 9.896 -10.860 1.00 13.32 ATOM 1052 CD1 TYR A 140 -3.208 8.516 -10.912 1.00 17.40 ATOM 1053 CD2 TYR A 140 -2.152 10.624 -11.220 1.00 17.41 ATOM 1054 CE1 TYR A 140 -2.068 7.852 -11.328 1.00 20.25 ATOM 1055 CE2 TYR A 140 -0.972 9.952 -11.640 1.00 16.99 ATOM 1056 CZ TYR A 140 -0.948 8.564 -11.696 1.00 18.73 ATOM 1057 OH TYR A 140 0.132 7.924 -12.176 1.00 16.96 ATOM 1058 N ARG A 141 -7.080 12.536 -10.168 1.00 19.32 ATOM 1059 CA ARG A 141 -8.560 12.608 -10.140 1.00 24.84 ATOM 1060 C ARG A 141 -9.024 13.884 -9.448 1.00 39.71 ATOM 1061 O ARG A 141 -8.208 14.504 -8.760 1.00 24.88 ATOM 1062 CB ARG A 141 -9.184 11.356 -9.568 1.00 30.40 ATOM 1063 CG ARG A 141 -8.792 11.084 -8.116 1.00 19.78 ATOM 1064 CD ARG A 141 -9.656 9.928 -7.636 1.00 13.37 ATOM 1065 NE ARG A 141 -9.208 9.676 -6.284 1.00 19.44 ATOM 1066 CZ ARG A 141 -9.848 8.816 -5.484 1.00 27.71 ATOM 1067 NH1 ARG A 141 -10.832 8.008 -5.916 1.00 22.33 ATOM 1068 NH2 ARG A 141 -9.424 8.712 -4.240 1.00 30.51 ATOM 1069 OXT ARG A 141 -10.196 14.224 -9.604 1.00 35.76 HETATM 1070 FE HEM A 1 7.436 7.896 -14.880 1.00 18.06 HETATM 1071 CHA HEM A 1 7.932 8.400 -18.176 1.00 17.24 HETATM 1072 CHB HEM A 1 9.684 10.468 -14.120 1.00 23.17 HETATM 1073 CHC HEM A 1 7.636 6.904 -11.452 1.00 11.04 HETATM 1074 CHD HEM A 1 6.284 4.620 -15.560 1.00 12.91 HETATM 1075 N A HEM A 1 8.596 9.172 -15.948 1.00 18.65 HETATM 1076 C1A HEM A 1 8.576 9.280 -17.320 1.00 21.02 HETATM 1077 C2A HEM A 1 9.400 10.432 -17.728 1.00 23.19 HETATM 1078 C3A HEM A 1 9.892 11.008 -16.592 1.00 25.30 HETATM 1079 C4A HEM A 1 9.412 10.212 -15.468 1.00 22.35 HETATM 1080 CMA HEM A 1 10.908 12.120 -16.532 1.00 23.27 HETATM 1081 CAA HEM A 1 9.740 10.852 -19.136 1.00 25.00 HETATM 1082 CBA HEM A 1 8.708 11.816 -19.688 1.00 37.36 HETATM 1083 CGA HEM A 1 9.096 12.472 -21.032 1.00 42.76 HETATM 1084 O1A HEM A 1 9.508 11.788 -21.964 1.00 34.05 HETATM 1085 O2A HEM A 1 8.872 13.668 -21.172 1.00 46.62 HETATM 1086 N B HEM A 1 8.556 8.504 -13.140 1.00 11.55 HETATM 1087 C1B HEM A 1 9.276 9.664 -13.044 1.00 18.62 HETATM 1088 C2B HEM A 1 9.620 9.912 -11.668 1.00 13.26 HETATM 1089 C3B HEM A 1 9.036 8.912 -10.900 1.00 17.26 HETATM 1090 C4B HEM A 1 8.348 8.044 -11.832 1.00 12.59 HETATM 1091 CMB HEM A 1 10.364 11.136 -11.200 1.00 14.31 HETATM 1092 CAB HEM A 1 8.840 8.904 -9.412 1.00 24.37 HETATM 1093 CBB HEM A 1 9.920 8.924 -8.548 1.00 26.82 HETATM 1094 N C HEM A 1 6.972 6.120 -13.764 1.00 17.38 HETATM 1095 C1C HEM A 1 7.072 5.968 -12.364 1.00 12.89 HETATM 1096 C2C HEM A 1 6.556 4.680 -11.992 1.00 13.29 HETATM 1097 C3C HEM A 1 6.204 4.032 -13.148 1.00 10.65 HETATM 1098 C4C HEM A 1 6.504 4.932 -14.240 1.00 11.26 HETATM 1099 CMC HEM A 1 6.356 4.184 -10.596 1.00 15.06 HETATM 1100 CAC HEM A 1 5.672 2.664 -13.344 1.00 12.54 HETATM 1101 CBC HEM A 1 6.024 1.580 -12.588 1.00 12.87 HETATM 1102 N D HEM A 1 7.080 6.724 -16.536 1.00 17.96 HETATM 1103 C1D HEM A 1 6.580 5.476 -16.644 1.00 13.36 HETATM 1104 C2D HEM A 1 6.380 5.144 -18.048 1.00 19.02 HETATM 1105 C3D HEM A 1 6.832 6.200 -18.764 1.00 21.48 HETATM 1106 C4D HEM A 1 7.292 7.188 -17.824 1.00 17.64 HETATM 1107 CMD HEM A 1 5.648 3.956 -18.628 1.00 18.11 HETATM 1108 CAD HEM A 1 6.908 6.264 -20.268 1.00 23.12 HETATM 1109 CBD HEM A 1 8.268 5.804 -20.788 1.00 36.99 HETATM 1110 CGD HEM A 1 8.312 5.744 -22.324 1.00 34.74 HETATM 1111 O1D HEM A 1 9.420 5.872 -22.780 1.00 42.24 HETATM 1112 O2D HEM A 1 7.312 5.544 -23.024 1.00 41.57 TER 1113 HEM A 1 END