HEADER TRANSPORT(THYROXINE) 02-NOV-92 1TTB 1TTB 2 MODEL 1 ATOM 107 N VAL A 16 26.134 36.570 37.291 1.00 12.40 1TTB 234 ATOM 108 CA VAL A 16 26.799 36.600 38.613 1.00 11.86 1TTB 235 ATOM 109 C VAL A 16 27.741 37.827 38.601 1.00 12.26 1TTB 236 ATOM 110 O VAL A 16 28.441 38.003 37.563 1.00 12.35 1TTB 237 ATOM 111 CB VAL A 16 27.525 35.285 38.884 1.00 12.29 1TTB 238 ATOM 112 CG1 VAL A 16 28.157 35.252 40.299 1.00 11.99 1TTB 239 ATOM 113 CG2 VAL A 16 26.649 34.024 38.735 1.00 11.81 1TTB 240 ATOM 114 N LEU A 17 27.706 38.617 39.639 1.00 11.79 1TTB 241 ATOM 115 CA LEU A 17 28.561 39.794 39.761 1.00 12.01 1TTB 242 ATOM 116 C LEU A 17 29.437 39.698 41.014 1.00 11.54 1TTB 243 ATOM 117 O LEU A 17 29.066 39.105 42.017 1.00 10.64 1TTB 244 ATOM 118 CB LEU A 17 27.649 41.053 39.766 1.00 13.55 1TTB 245 ATOM 119 CG LEU A 17 26.789 41.410 38.576 1.00 14.37 1TTB 246 ATOM 120 CD1ALEU A 17 26.106 42.778 38.781 0.80 14.02 1TTB 247 ATOM 121 CD1BLEU A 17 27.755 41.506 37.360 0.20 16.10 1TTB 248 ATOM 122 CD2ALEU A 17 27.667 41.515 37.318 0.80 15.37 1TTB 249 ATOM 123 CD2BLEU A 17 25.851 40.244 38.205 0.20 16.04 1TTB 250 ATOM 124 N ASP A 18 30.589 40.353 40.927 1.00 11.16 1TTB 251 ATOM 125 CA ASP A 18 31.595 40.441 42.003 1.00 11.25 1TTB 252 ATOM 126 C ASP A 18 31.584 41.844 42.667 1.00 11.27 1TTB 253 ATOM 127 O ASP A 18 31.887 42.876 41.989 1.00 11.30 1TTB 254 ATOM 128 CB ASP A 18 32.921 40.054 41.363 1.00 12.02 1TTB 255 ATOM 129 CG ASP A 18 34.100 40.055 42.308 1.00 13.92 1TTB 256 ATOM 130 OD1 ASP A 18 34.079 40.821 43.282 1.00 12.49 1TTB 257 ATOM 131 OD2 ASP A 18 35.003 39.227 42.011 1.00 15.16 1TTB 258 ATOM 132 N ALA A 19 31.272 41.890 43.957 1.00 10.81 1TTB 259 ATOM 133 CA ALA A 19 31.152 43.160 44.682 1.00 11.36 1TTB 260 ATOM 134 C ALA A 19 32.500 43.665 45.212 1.00 11.43 1TTB 261 ATOM 135 O ALA A 19 32.499 44.786 45.765 1.00 12.10 1TTB 262 ATOM 136 CB ALA A 19 30.202 43.070 45.871 1.00 10.99 1TTB 263 ATOM 137 N VAL A 20 33.493 42.835 45.168 1.00 12.11 1TTB 264 ATOM 138 CA VAL A 20 34.842 43.157 45.630 1.00 12.88 1TTB 265 ATOM 139 C VAL A 20 35.590 43.846 44.474 1.00 13.85 1TTB 266 ATOM 140 O VAL A 20 36.258 44.882 44.742 1.00 14.16 1TTB 267 ATOM 141 CB VAL A 20 35.552 41.920 46.200 1.00 13.93 1TTB 268 ATOM 142 CG1 VAL A 20 37.066 42.184 46.383 1.00 14.83 1TTB 269 ATOM 143 CG2 VAL A 20 34.976 41.414 47.516 1.00 13.45 1TTB 270 ATOM 144 N ARG A 21 35.504 43.363 43.283 1.00 14.68 1TTB 271 ATOM 145 CA ARG A 21 36.189 43.919 42.121 1.00 15.38 1TTB 272 ATOM 146 C ARG A 21 35.374 44.835 41.238 1.00 14.90 1TTB 273 ATOM 147 O ARG A 21 35.965 45.481 40.336 1.00 15.16 1TTB 274 ATOM 148 CB ARG A 21 36.645 42.731 41.229 1.00 17.87 1TTB 275 ATOM 149 CG ARG A 21 37.846 42.017 41.872 1.00 20.64 1TTB 276 ATOM 150 CD ARG A 21 37.904 40.584 41.411 1.00 21.96 1TTB 277 ATOM 151 NE ARG A 21 38.485 40.445 40.090 0.75 23.32 1TTB 278 ATOM 152 CZ ARG A 21 38.773 39.239 39.559 0.50 23.35 1TTB 279 ATOM 153 NH1 ARG A 21 38.524 38.115 40.215 0.00 23.39 1TTB 280 ATOM 154 NH2 ARG A 21 39.337 39.193 38.355 0.00 23.38 1TTB 281 ATOM 155 N GLY A 22 34.078 44.866 41.418 1.00 13.75 1TTB 282 ATOM 156 CA GLY A 22 33.171 45.679 40.605 1.00 13.21 1TTB 283 ATOM 157 C GLY A 22 33.223 45.193 39.136 1.00 12.78 1TTB 284 ATOM 158 O GLY A 22 33.424 45.976 38.190 1.00 12.48 1TTB 285 ATOM 159 N SER A 23 33.048 43.891 38.987 1.00 13.37 1TTB 286 ATOM 160 CA SER A 23 33.042 43.302 37.628 1.00 13.85 1TTB 287 ATOM 161 C SER A 23 32.186 42.053 37.592 1.00 13.74 1TTB 288 ATOM 162 O SER A 23 31.745 41.566 38.650 1.00 14.12 1TTB 289 ATOM 163 CB SER A 23 34.513 42.943 37.322 1.00 16.02 1TTB 290 ATOM 164 OG SER A 23 34.827 41.831 38.131 1.00 17.57 1TTB 291 ATOM 165 N PRO A 24 31.947 41.549 36.395 1.00 13.43 1TTB 292 ATOM 166 CA PRO A 24 31.273 40.266 36.238 1.00 13.54 1TTB 293 ATOM 167 C PRO A 24 32.111 39.205 36.916 1.00 13.29 1TTB 294 ATOM 168 O PRO A 24 33.381 39.336 37.009 1.00 13.64 1TTB 295 ATOM 169 CB PRO A 24 31.175 40.028 34.720 1.00 13.59 1TTB 296 ATOM 170 CG PRO A 24 31.611 41.304 34.089 1.00 14.04 1TTB 297 ATOM 171 CD PRO A 24 32.400 42.097 35.103 1.00 13.52 1TTB 298 ATOM 172 N ALA A 25 31.445 38.134 37.348 1.00 12.58 1TTB 299 ATOM 173 CA ALA A 25 32.147 36.972 37.986 1.00 12.38 1TTB 300 ATOM 174 C ALA A 25 32.275 35.975 36.834 1.00 12.86 1TTB 301 ATOM 175 O ALA A 25 31.252 35.407 36.386 1.00 12.04 1TTB 302 ATOM 176 CB ALA A 25 31.320 36.466 39.144 1.00 12.02 1TTB 303 ATOM 177 N ILE A 26 33.483 35.797 36.372 1.00 12.95 1TTB 304 ATOM 178 CA ILE A 26 33.776 35.003 35.164 1.00 14.15 1TTB 305 ATOM 179 C ILE A 26 34.194 33.590 35.518 1.00 13.94 1TTB 306 ATOM 180 O ILE A 26 34.878 33.478 36.550 1.00 13.70 1TTB 307 ATOM 181 CB ILE A 26 34.927 35.799 34.431 1.00 16.74 1TTB 308 ATOM 182 CG1 ILE A 26 34.283 37.127 33.895 1.00 17.34 1TTB 309 ATOM 183 CG2 ILE A 26 35.699 35.039 33.340 1.00 17.72 1TTB 310 ATOM 184 CD1 ILE A 26 35.370 38.064 33.297 1.00 19.28 1TTB 311 TER ENDMDL END