HEADER VIRAL PROTEIN/IMMUNE SYSTEM 23-JAN-25 9LOY TITLE CRYO-EM STRUCTURE OF SARS-COV-2 JN.1 SPIKE GLYCOPROTEIN IN COMPLEX TITLE 2 WITH F61R2-780 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: F61R2-780 HEAVY CHAIN; COMPND 9 CHAIN: E, H; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: F61R2-780 LIGHT CHAIN; COMPND 13 CHAIN: F, I; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 STRAIN: JN.1; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SARS-COV-2, SPIKE, ANTIBODY, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL KEYWDS 2 PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR X.WANG,X.LI REVDAT 1 28-JAN-26 9LOY 0 JRNL AUTH X.WANG,X.LI JRNL TITL CRYO-EM STRUCTURE OF SARS-COV-2 JN.1 SPIKE GLYCOPROTEIN IN JRNL TITL 2 COMPLEX WITH F61R2-780 FAB JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.66 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.660 REMARK 3 NUMBER OF PARTICLES : 499045 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9LOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 06-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300056137. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : CRYO-EM STRUCTURE OF SARS-COV-2 REMARK 245 JN.1 SPIKE GLYCOPROTEIN IN REMARK 245 COMPLEX WITH F61R2-780 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, H, I REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 4 REMARK 465 PHE A 5 REMARK 465 VAL A 6 REMARK 465 PHE A 7 REMARK 465 LEU A 8 REMARK 465 VAL A 9 REMARK 465 LEU A 10 REMARK 465 LEU A 11 REMARK 465 PRO A 12 REMARK 465 LEU A 13 REMARK 465 VAL A 14 REMARK 465 SER A 15 REMARK 465 SER A 16 REMARK 465 GLN A 17 REMARK 465 CYS A 18 REMARK 465 VAL A 19 REMARK 465 ASN A 20 REMARK 465 LEU A 21 REMARK 465 ILE A 22 REMARK 465 THR A 23 REMARK 465 THR A 24 REMARK 465 THR A 25 REMARK 465 GLN A 26 REMARK 465 SER A 27 REMARK 465 HIS A 68 REMARK 465 ALA A 69 REMARK 465 ILE A 70 REMARK 465 SER A 71 REMARK 465 GLY A 72 REMARK 465 THR A 73 REMARK 465 ASN A 74 REMARK 465 GLY A 75 REMARK 465 THR A 76 REMARK 465 LYS A 77 REMARK 465 ARG A 78 REMARK 465 PHE A 79 REMARK 465 ASP A 80 REMARK 465 ASN A 81 REMARK 465 PRO A 82 REMARK 465 VAL A 83 REMARK 465 GLU A 96 REMARK 465 LYS A 97 REMARK 465 SER A 98 REMARK 465 ASN A 99 REMARK 465 THR A 109 REMARK 465 LEU A 110 REMARK 465 ASP A 111 REMARK 465 SER A 112 REMARK 465 LYS A 113 REMARK 465 THR A 114 REMARK 465 GLN A 115 REMARK 465 SER A 116 REMARK 465 LYS A 147 REMARK 465 ASN A 148 REMARK 465 ASN A 149 REMARK 465 LYS A 150 REMARK 465 SER A 151 REMARK 465 TRP A 152 REMARK 465 MET A 153 REMARK 465 GLU A 154 REMARK 465 SER A 155 REMARK 465 GLU A 156 REMARK 465 SER A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 ASP A 178 REMARK 465 LEU A 179 REMARK 465 GLU A 180 REMARK 465 GLY A 181 REMARK 465 LYS A 182 REMARK 465 GLN A 183 REMARK 465 GLY A 184 REMARK 465 ASN A 185 REMARK 465 ILE A 212 REMARK 465 GLY A 213 REMARK 465 ARG A 214 REMARK 465 ASP A 215 REMARK 465 ALA A 243 REMARK 465 LEU A 244 REMARK 465 ASN A 245 REMARK 465 ARG A 246 REMARK 465 SER A 247 REMARK 465 TYR A 248 REMARK 465 LEU A 249 REMARK 465 THR A 250 REMARK 465 PRO A 251 REMARK 465 GLY A 252 REMARK 465 ASP A 253 REMARK 465 SER A 254 REMARK 465 SER A 255 REMARK 465 SER A 256 REMARK 465 GLY A 257 REMARK 465 TRP A 258 REMARK 465 THR A 259 REMARK 465 ALA A 260 REMARK 465 GLY A 261 REMARK 465 ALA A 262 REMARK 465 ALA A 263 REMARK 465 ASN A 331 REMARK 465 VAL A 332 REMARK 465 LYS A 528 REMARK 465 LYS A 679 REMARK 465 SER A 680 REMARK 465 ARG A 681 REMARK 465 GLY A 682 REMARK 465 SER A 683 REMARK 465 ALA A 684 REMARK 465 SER A 685 REMARK 465 SER A 686 REMARK 465 VAL A 687 REMARK 465 ALA A 829 REMARK 465 ASP A 830 REMARK 465 ALA A 831 REMARK 465 GLY A 832 REMARK 465 PHE A 833 REMARK 465 ILE A 834 REMARK 465 LYS A 835 REMARK 465 GLN A 836 REMARK 465 TYR A 837 REMARK 465 GLY A 838 REMARK 465 ASP A 839 REMARK 465 CYS A 840 REMARK 465 LEU A 841 REMARK 465 GLY A 842 REMARK 465 ASP A 843 REMARK 465 ILE A 844 REMARK 465 ALA A 845 REMARK 465 ALA A 846 REMARK 465 ARG A 847 REMARK 465 ASP A 848 REMARK 465 LEU A 849 REMARK 465 ILE A 850 REMARK 465 CYS A 851 REMARK 465 ALA A 852 REMARK 465 GLN A 853 REMARK 465 ASP A 1146 REMARK 465 SER A 1147 REMARK 465 PHE A 1148 REMARK 465 LYS A 1149 REMARK 465 GLU A 1150 REMARK 465 GLU A 1151 REMARK 465 LEU A 1152 REMARK 465 ASP A 1153 REMARK 465 LYS A 1154 REMARK 465 TYR A 1155 REMARK 465 PHE A 1156 REMARK 465 LYS A 1157 REMARK 465 ASN A 1158 REMARK 465 HIS A 1159 REMARK 465 THR A 1160 REMARK 465 SER A 1161 REMARK 465 PRO A 1162 REMARK 465 ASP A 1163 REMARK 465 VAL A 1164 REMARK 465 ASP A 1165 REMARK 465 LEU A 1166 REMARK 465 GLY A 1167 REMARK 465 ASP A 1168 REMARK 465 ILE A 1169 REMARK 465 SER A 1170 REMARK 465 GLY A 1171 REMARK 465 ILE A 1172 REMARK 465 ASN A 1173 REMARK 465 ALA A 1174 REMARK 465 SER A 1175 REMARK 465 VAL A 1176 REMARK 465 VAL A 1177 REMARK 465 ASN A 1178 REMARK 465 ILE A 1179 REMARK 465 GLN A 1180 REMARK 465 LYS A 1181 REMARK 465 GLU A 1182 REMARK 465 ILE A 1183 REMARK 465 ASP A 1184 REMARK 465 ARG A 1185 REMARK 465 LEU A 1186 REMARK 465 ASN A 1187 REMARK 465 GLU A 1188 REMARK 465 VAL A 1189 REMARK 465 ALA A 1190 REMARK 465 LYS A 1191 REMARK 465 ASN A 1192 REMARK 465 LEU A 1193 REMARK 465 ASN A 1194 REMARK 465 GLU A 1195 REMARK 465 SER A 1196 REMARK 465 LEU A 1197 REMARK 465 ILE A 1198 REMARK 465 ASP A 1199 REMARK 465 LEU A 1200 REMARK 465 GLN A 1201 REMARK 465 GLU A 1202 REMARK 465 LEU A 1203 REMARK 465 GLY A 1204 REMARK 465 LYS A 1205 REMARK 465 TYR A 1206 REMARK 465 GLU A 1207 REMARK 465 GLN A 1208 REMARK 465 MET B 4 REMARK 465 PHE B 5 REMARK 465 VAL B 6 REMARK 465 PHE B 7 REMARK 465 LEU B 8 REMARK 465 VAL B 9 REMARK 465 LEU B 10 REMARK 465 LEU B 11 REMARK 465 PRO B 12 REMARK 465 LEU B 13 REMARK 465 VAL B 14 REMARK 465 SER B 15 REMARK 465 SER B 16 REMARK 465 GLN B 17 REMARK 465 CYS B 18 REMARK 465 VAL B 19 REMARK 465 ASN B 20 REMARK 465 LEU B 21 REMARK 465 ILE B 22 REMARK 465 THR B 23 REMARK 465 THR B 24 REMARK 465 THR B 25 REMARK 465 GLN B 26 REMARK 465 SER B 27 REMARK 465 HIS B 68 REMARK 465 ALA B 69 REMARK 465 ILE B 70 REMARK 465 SER B 71 REMARK 465 GLY B 72 REMARK 465 THR B 73 REMARK 465 ASN B 74 REMARK 465 GLY B 75 REMARK 465 THR B 76 REMARK 465 LYS B 77 REMARK 465 ARG B 78 REMARK 465 PHE B 79 REMARK 465 ASP B 80 REMARK 465 ASN B 81 REMARK 465 PRO B 82 REMARK 465 VAL B 83 REMARK 465 LYS B 97 REMARK 465 SER B 98 REMARK 465 ASN B 99 REMARK 465 ASP B 143 REMARK 465 VAL B 144 REMARK 465 TYR B 145 REMARK 465 HIS B 146 REMARK 465 LYS B 147 REMARK 465 ASN B 148 REMARK 465 ASN B 149 REMARK 465 LYS B 150 REMARK 465 SER B 151 REMARK 465 TRP B 152 REMARK 465 MET B 153 REMARK 465 GLU B 154 REMARK 465 SER B 155 REMARK 465 LEU B 176 REMARK 465 MET B 177 REMARK 465 ASP B 178 REMARK 465 LEU B 179 REMARK 465 GLU B 180 REMARK 465 GLY B 181 REMARK 465 LYS B 182 REMARK 465 GLN B 183 REMARK 465 GLY B 184 REMARK 465 ASN B 185 REMARK 465 PHE B 186 REMARK 465 LEU B 244 REMARK 465 ASN B 245 REMARK 465 ARG B 246 REMARK 465 SER B 247 REMARK 465 TYR B 248 REMARK 465 LEU B 249 REMARK 465 THR B 250 REMARK 465 PRO B 251 REMARK 465 GLY B 252 REMARK 465 ASP B 253 REMARK 465 SER B 254 REMARK 465 SER B 255 REMARK 465 SER B 256 REMARK 465 GLY B 257 REMARK 465 TRP B 258 REMARK 465 THR B 259 REMARK 465 ALA B 260 REMARK 465 GLY B 261 REMARK 465 ALA B 262 REMARK 465 PHE B 330 REMARK 465 PRO B 331 REMARK 465 ASN B 332 REMARK 465 VAL B 333 REMARK 465 THR B 334 REMARK 465 ASN B 335 REMARK 465 LEU B 336 REMARK 465 CYS B 337 REMARK 465 PRO B 338 REMARK 465 PHE B 339 REMARK 465 HIS B 340 REMARK 465 GLU B 341 REMARK 465 VAL B 342 REMARK 465 PHE B 343 REMARK 465 ASN B 344 REMARK 465 ALA B 345 REMARK 465 THR B 346 REMARK 465 ARG B 347 REMARK 465 PHE B 348 REMARK 465 ALA B 349 REMARK 465 SER B 350 REMARK 465 VAL B 351 REMARK 465 TYR B 352 REMARK 465 ALA B 353 REMARK 465 TRP B 354 REMARK 465 ASN B 355 REMARK 465 ARG B 356 REMARK 465 THR B 357 REMARK 465 ARG B 358 REMARK 465 ILE B 359 REMARK 465 SER B 360 REMARK 465 ASN B 361 REMARK 465 CYS B 362 REMARK 465 VAL B 363 REMARK 465 ALA B 364 REMARK 465 ASP B 365 REMARK 465 TYR B 366 REMARK 465 SER B 367 REMARK 465 VAL B 368 REMARK 465 LEU B 369 REMARK 465 TYR B 370 REMARK 465 ASN B 371 REMARK 465 PHE B 372 REMARK 465 ALA B 373 REMARK 465 PRO B 374 REMARK 465 PHE B 375 REMARK 465 PHE B 376 REMARK 465 ALA B 377 REMARK 465 PHE B 378 REMARK 465 LYS B 379 REMARK 465 CYS B 380 REMARK 465 TYR B 381 REMARK 465 GLY B 382 REMARK 465 VAL B 383 REMARK 465 SER B 384 REMARK 465 PRO B 385 REMARK 465 THR B 386 REMARK 465 LYS B 387 REMARK 465 LEU B 388 REMARK 465 ASN B 389 REMARK 465 ASP B 390 REMARK 465 LEU B 391 REMARK 465 CYS B 392 REMARK 465 PHE B 393 REMARK 465 THR B 394 REMARK 465 ASN B 395 REMARK 465 VAL B 396 REMARK 465 TYR B 397 REMARK 465 ALA B 398 REMARK 465 ASP B 399 REMARK 465 SER B 400 REMARK 465 PHE B 401 REMARK 465 VAL B 402 REMARK 465 ILE B 403 REMARK 465 LYS B 404 REMARK 465 GLY B 405 REMARK 465 ASN B 406 REMARK 465 GLU B 407 REMARK 465 VAL B 408 REMARK 465 SER B 409 REMARK 465 GLN B 410 REMARK 465 ILE B 411 REMARK 465 ALA B 412 REMARK 465 PRO B 413 REMARK 465 GLY B 414 REMARK 465 GLN B 415 REMARK 465 THR B 416 REMARK 465 GLY B 417 REMARK 465 ASN B 418 REMARK 465 ILE B 419 REMARK 465 ALA B 420 REMARK 465 ASP B 421 REMARK 465 TYR B 422 REMARK 465 ASN B 423 REMARK 465 TYR B 424 REMARK 465 LYS B 425 REMARK 465 LEU B 426 REMARK 465 PRO B 427 REMARK 465 ASP B 428 REMARK 465 ASP B 429 REMARK 465 PHE B 430 REMARK 465 THR B 431 REMARK 465 GLY B 432 REMARK 465 CYS B 433 REMARK 465 VAL B 434 REMARK 465 ILE B 435 REMARK 465 ALA B 436 REMARK 465 TRP B 437 REMARK 465 ASN B 438 REMARK 465 SER B 439 REMARK 465 ASN B 440 REMARK 465 LYS B 441 REMARK 465 LEU B 442 REMARK 465 ASP B 443 REMARK 465 SER B 444 REMARK 465 LYS B 445 REMARK 465 HIS B 446 REMARK 465 SER B 447 REMARK 465 GLY B 448 REMARK 465 ASN B 449 REMARK 465 TYR B 450 REMARK 465 ASP B 451 REMARK 465 TYR B 452 REMARK 465 TRP B 453 REMARK 465 TYR B 454 REMARK 465 ARG B 455 REMARK 465 SER B 456 REMARK 465 PHE B 457 REMARK 465 ARG B 458 REMARK 465 LYS B 459 REMARK 465 SER B 460 REMARK 465 LYS B 461 REMARK 465 LEU B 462 REMARK 465 LYS B 463 REMARK 465 PRO B 464 REMARK 465 PHE B 465 REMARK 465 GLU B 466 REMARK 465 ARG B 467 REMARK 465 ASP B 468 REMARK 465 ILE B 469 REMARK 465 SER B 470 REMARK 465 THR B 471 REMARK 465 GLU B 472 REMARK 465 ILE B 473 REMARK 465 TYR B 474 REMARK 465 GLN B 475 REMARK 465 ALA B 476 REMARK 465 GLY B 477 REMARK 465 ASN B 478 REMARK 465 LYS B 479 REMARK 465 PRO B 480 REMARK 465 CYS B 481 REMARK 465 LYS B 482 REMARK 465 GLY B 483 REMARK 465 LYS B 484 REMARK 465 GLY B 485 REMARK 465 PRO B 486 REMARK 465 ASN B 487 REMARK 465 CYS B 488 REMARK 465 TYR B 489 REMARK 465 PHE B 490 REMARK 465 PRO B 491 REMARK 465 LEU B 492 REMARK 465 GLN B 493 REMARK 465 SER B 494 REMARK 465 TYR B 495 REMARK 465 GLY B 496 REMARK 465 PHE B 497 REMARK 465 ARG B 498 REMARK 465 PRO B 499 REMARK 465 THR B 500 REMARK 465 TYR B 501 REMARK 465 GLY B 502 REMARK 465 VAL B 503 REMARK 465 GLY B 504 REMARK 465 HIS B 505 REMARK 465 GLN B 506 REMARK 465 PRO B 507 REMARK 465 TYR B 508 REMARK 465 ARG B 509 REMARK 465 VAL B 510 REMARK 465 VAL B 511 REMARK 465 VAL B 512 REMARK 465 LEU B 513 REMARK 465 SER B 514 REMARK 465 PHE B 515 REMARK 465 GLU B 516 REMARK 465 LEU B 517 REMARK 465 LEU B 518 REMARK 465 HIS B 519 REMARK 465 ALA B 520 REMARK 465 PRO B 521 REMARK 465 ALA B 522 REMARK 465 THR B 523 REMARK 465 VAL B 524 REMARK 465 CYS B 525 REMARK 465 GLY B 526 REMARK 465 PRO B 527 REMARK 465 LYS B 528 REMARK 465 LYS B 679 REMARK 465 SER B 680 REMARK 465 ARG B 681 REMARK 465 GLY B 682 REMARK 465 SER B 683 REMARK 465 ALA B 684 REMARK 465 SER B 685 REMARK 465 SER B 686 REMARK 465 VAL B 687 REMARK 465 ALA B 829 REMARK 465 ASP B 830 REMARK 465 ALA B 831 REMARK 465 GLY B 832 REMARK 465 PHE B 833 REMARK 465 ILE B 834 REMARK 465 LYS B 835 REMARK 465 GLN B 836 REMARK 465 TYR B 837 REMARK 465 GLY B 838 REMARK 465 ASP B 839 REMARK 465 CYS B 840 REMARK 465 LEU B 841 REMARK 465 GLY B 842 REMARK 465 ASP B 843 REMARK 465 ILE B 844 REMARK 465 ALA B 845 REMARK 465 ALA B 846 REMARK 465 ARG B 847 REMARK 465 ASP B 848 REMARK 465 LEU B 849 REMARK 465 ILE B 850 REMARK 465 CYS B 851 REMARK 465 ALA B 852 REMARK 465 GLN B 853 REMARK 465 ASP B 1146 REMARK 465 SER B 1147 REMARK 465 PHE B 1148 REMARK 465 LYS B 1149 REMARK 465 GLU B 1150 REMARK 465 GLU B 1151 REMARK 465 LEU B 1152 REMARK 465 ASP B 1153 REMARK 465 LYS B 1154 REMARK 465 TYR B 1155 REMARK 465 PHE B 1156 REMARK 465 LYS B 1157 REMARK 465 ASN B 1158 REMARK 465 HIS B 1159 REMARK 465 THR B 1160 REMARK 465 SER B 1161 REMARK 465 PRO B 1162 REMARK 465 ASP B 1163 REMARK 465 VAL B 1164 REMARK 465 ASP B 1165 REMARK 465 LEU B 1166 REMARK 465 GLY B 1167 REMARK 465 ASP B 1168 REMARK 465 ILE B 1169 REMARK 465 SER B 1170 REMARK 465 GLY B 1171 REMARK 465 ILE B 1172 REMARK 465 ASN B 1173 REMARK 465 ALA B 1174 REMARK 465 SER B 1175 REMARK 465 VAL B 1176 REMARK 465 VAL B 1177 REMARK 465 ASN B 1178 REMARK 465 ILE B 1179 REMARK 465 GLN B 1180 REMARK 465 LYS B 1181 REMARK 465 GLU B 1182 REMARK 465 ILE B 1183 REMARK 465 ASP B 1184 REMARK 465 ARG B 1185 REMARK 465 LEU B 1186 REMARK 465 ASN B 1187 REMARK 465 GLU B 1188 REMARK 465 VAL B 1189 REMARK 465 ALA B 1190 REMARK 465 LYS B 1191 REMARK 465 ASN B 1192 REMARK 465 LEU B 1193 REMARK 465 ASN B 1194 REMARK 465 GLU B 1195 REMARK 465 SER B 1196 REMARK 465 LEU B 1197 REMARK 465 ILE B 1198 REMARK 465 ASP B 1199 REMARK 465 LEU B 1200 REMARK 465 GLN B 1201 REMARK 465 GLU B 1202 REMARK 465 LEU B 1203 REMARK 465 GLY B 1204 REMARK 465 LYS B 1205 REMARK 465 TYR B 1206 REMARK 465 GLU B 1207 REMARK 465 GLN B 1208 REMARK 465 MET C 4 REMARK 465 PHE C 5 REMARK 465 VAL C 6 REMARK 465 PHE C 7 REMARK 465 LEU C 8 REMARK 465 VAL C 9 REMARK 465 LEU C 10 REMARK 465 LEU C 11 REMARK 465 PRO C 12 REMARK 465 LEU C 13 REMARK 465 VAL C 14 REMARK 465 SER C 15 REMARK 465 SER C 16 REMARK 465 GLN C 17 REMARK 465 CYS C 18 REMARK 465 VAL C 19 REMARK 465 ASN C 20 REMARK 465 LEU C 21 REMARK 465 ILE C 22 REMARK 465 THR C 23 REMARK 465 THR C 24 REMARK 465 THR C 25 REMARK 465 GLN C 26 REMARK 465 SER C 27 REMARK 465 ILE C 70 REMARK 465 SER C 71 REMARK 465 GLY C 72 REMARK 465 THR C 73 REMARK 465 ASN C 74 REMARK 465 GLY C 75 REMARK 465 THR C 76 REMARK 465 LYS C 77 REMARK 465 ARG C 78 REMARK 465 PHE C 79 REMARK 465 ASP C 80 REMARK 465 ASN C 81 REMARK 465 PRO C 82 REMARK 465 TYR C 145 REMARK 465 HIS C 146 REMARK 465 LYS C 147 REMARK 465 ASN C 148 REMARK 465 ASN C 149 REMARK 465 LYS C 150 REMARK 465 SER C 151 REMARK 465 TRP C 152 REMARK 465 MET C 153 REMARK 465 GLU C 154 REMARK 465 SER C 155 REMARK 465 GLU C 156 REMARK 465 SER C 157 REMARK 465 GLY C 158 REMARK 465 VAL C 159 REMARK 465 TYR C 160 REMARK 465 SER C 161 REMARK 465 SER C 162 REMARK 465 LEU C 179 REMARK 465 GLU C 180 REMARK 465 GLY C 181 REMARK 465 LYS C 182 REMARK 465 GLN C 183 REMARK 465 GLY C 184 REMARK 465 ASN C 185 REMARK 465 PHE C 186 REMARK 465 ALA C 243 REMARK 465 LEU C 244 REMARK 465 ASN C 245 REMARK 465 ARG C 246 REMARK 465 SER C 247 REMARK 465 TYR C 248 REMARK 465 LEU C 249 REMARK 465 THR C 250 REMARK 465 PRO C 251 REMARK 465 GLY C 252 REMARK 465 ASP C 253 REMARK 465 SER C 254 REMARK 465 SER C 255 REMARK 465 SER C 256 REMARK 465 GLY C 257 REMARK 465 TRP C 258 REMARK 465 ASN C 331 REMARK 465 VAL C 332 REMARK 465 LYS C 528 REMARK 465 LYS C 679 REMARK 465 SER C 680 REMARK 465 ARG C 681 REMARK 465 GLY C 682 REMARK 465 SER C 683 REMARK 465 ALA C 684 REMARK 465 SER C 685 REMARK 465 SER C 686 REMARK 465 VAL C 687 REMARK 465 ALA C 829 REMARK 465 ASP C 830 REMARK 465 ALA C 831 REMARK 465 GLY C 832 REMARK 465 PHE C 833 REMARK 465 ILE C 834 REMARK 465 LYS C 835 REMARK 465 GLN C 836 REMARK 465 TYR C 837 REMARK 465 GLY C 838 REMARK 465 ASP C 839 REMARK 465 CYS C 840 REMARK 465 LEU C 841 REMARK 465 GLY C 842 REMARK 465 ASP C 843 REMARK 465 ILE C 844 REMARK 465 ALA C 845 REMARK 465 ALA C 846 REMARK 465 ARG C 847 REMARK 465 ASP C 848 REMARK 465 LEU C 849 REMARK 465 ILE C 850 REMARK 465 CYS C 851 REMARK 465 ALA C 852 REMARK 465 GLN C 853 REMARK 465 ASP C 1146 REMARK 465 SER C 1147 REMARK 465 PHE C 1148 REMARK 465 LYS C 1149 REMARK 465 GLU C 1150 REMARK 465 GLU C 1151 REMARK 465 LEU C 1152 REMARK 465 ASP C 1153 REMARK 465 LYS C 1154 REMARK 465 TYR C 1155 REMARK 465 PHE C 1156 REMARK 465 LYS C 1157 REMARK 465 ASN C 1158 REMARK 465 HIS C 1159 REMARK 465 THR C 1160 REMARK 465 SER C 1161 REMARK 465 PRO C 1162 REMARK 465 ASP C 1163 REMARK 465 VAL C 1164 REMARK 465 ASP C 1165 REMARK 465 LEU C 1166 REMARK 465 GLY C 1167 REMARK 465 ASP C 1168 REMARK 465 ILE C 1169 REMARK 465 SER C 1170 REMARK 465 GLY C 1171 REMARK 465 ILE C 1172 REMARK 465 ASN C 1173 REMARK 465 ALA C 1174 REMARK 465 SER C 1175 REMARK 465 VAL C 1176 REMARK 465 VAL C 1177 REMARK 465 ASN C 1178 REMARK 465 ILE C 1179 REMARK 465 GLN C 1180 REMARK 465 LYS C 1181 REMARK 465 GLU C 1182 REMARK 465 ILE C 1183 REMARK 465 ASP C 1184 REMARK 465 ARG C 1185 REMARK 465 LEU C 1186 REMARK 465 ASN C 1187 REMARK 465 GLU C 1188 REMARK 465 VAL C 1189 REMARK 465 ALA C 1190 REMARK 465 LYS C 1191 REMARK 465 ASN C 1192 REMARK 465 LEU C 1193 REMARK 465 ASN C 1194 REMARK 465 GLU C 1195 REMARK 465 SER C 1196 REMARK 465 LEU C 1197 REMARK 465 ILE C 1198 REMARK 465 ASP C 1199 REMARK 465 LEU C 1200 REMARK 465 GLN C 1201 REMARK 465 GLU C 1202 REMARK 465 LEU C 1203 REMARK 465 GLY C 1204 REMARK 465 LYS C 1205 REMARK 465 TYR C 1206 REMARK 465 GLU C 1207 REMARK 465 GLN C 1208 REMARK 465 VAL F 1 REMARK 465 LEU F 2 REMARK 465 THR F 3 REMARK 465 GLN F 4 REMARK 465 SER F 5 REMARK 465 PRO F 6 REMARK 465 VAL I 1 REMARK 465 LEU I 2 REMARK 465 THR I 3 REMARK 465 GLN I 4 REMARK 465 SER I 5 REMARK 465 PRO I 6 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG B 237 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR A 91 OE2 GLU A 191 2.06 REMARK 500 O THR A 108 OG1 THR A 236 2.17 REMARK 500 OH TYR C 91 OE1 GLU C 191 2.18 REMARK 500 OG SER H 17 O MET H 82 2.18 REMARK 500 OG SER E 17 O MET E 82 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A 631 N - CA - C ANGL. DEV. = 19.4 DEGREES REMARK 500 ASN A 641 CB - CA - C ANGL. DEV. = 13.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 31 47.13 -101.85 REMARK 500 LYS A 41 37.02 -97.30 REMARK 500 PHE A 86 99.96 -67.91 REMARK 500 ASN A 87 -62.55 -92.90 REMARK 500 GLU A 132 77.34 -105.26 REMARK 500 ILE A 231 -65.19 -106.55 REMARK 500 GLU A 324 -166.10 -126.73 REMARK 500 ASP A 428 33.14 -97.17 REMARK 500 PRO A 561 -6.54 -53.79 REMARK 500 ASP A 571 42.36 79.79 REMARK 500 ASP A 663 -61.32 -102.26 REMARK 500 ALA A 783 36.91 -95.68 REMARK 500 LYS A 795 31.27 -94.32 REMARK 500 PHE A 855 116.14 -161.19 REMARK 500 LEU A 945 30.48 -94.65 REMARK 500 SER B 31 55.38 -115.97 REMARK 500 THR B 33 30.23 -141.61 REMARK 500 TYR B 38 103.90 -58.28 REMARK 500 ASP B 53 -168.50 -162.79 REMARK 500 CYS B 166 80.93 -69.05 REMARK 500 PRO B 561 -1.91 -55.27 REMARK 500 HIS B 625 59.64 -64.69 REMARK 500 TRP B 633 17.48 52.21 REMARK 500 SER B 640 8.62 -44.16 REMARK 500 ASN B 641 50.87 -93.32 REMARK 500 ASP B 663 -60.00 -102.01 REMARK 500 ASN B 703 113.95 -162.69 REMARK 500 ASN B 710 36.79 -148.97 REMARK 500 ALA B 783 36.12 -96.71 REMARK 500 LYS B 795 37.43 -97.79 REMARK 500 SER C 31 53.57 -117.40 REMARK 500 THR C 33 28.29 -141.19 REMARK 500 SER C 94 118.88 -160.52 REMARK 500 ASN C 99 76.91 -101.07 REMARK 500 SER C 316 -155.38 -143.82 REMARK 500 ASP C 428 33.05 -97.17 REMARK 500 ALA C 626 -151.53 -82.01 REMARK 500 THR C 632 -28.98 93.25 REMARK 500 ASP C 663 -61.65 -100.88 REMARK 500 ASN C 710 32.13 -141.01 REMARK 500 ALA C 783 38.88 -96.25 REMARK 500 LYS C 795 38.74 -98.60 REMARK 500 PHE C 855 -109.22 -92.65 REMARK 500 LEU C 945 33.39 -93.90 REMARK 500 LEU C1049 -60.20 -101.39 REMARK 500 THR C1100 -35.37 -130.06 REMARK 500 GLU C1111 88.83 -154.87 REMARK 500 GLU E 26 -8.56 73.11 REMARK 500 ALA E 91 -179.83 -171.05 REMARK 500 PRO F 43 -176.64 -65.77 REMARK 500 REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: D_1300056151 RELATED DB: PDB-DEV REMARK 900 RELATED ID: EMD-63263 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF SARS-COV-2 JN.1 SPIKE GLYCOPROTEIN IN COMPLEX REMARK 900 WITH F61R2-780 FAB DBREF 9LOY A 4 1208 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 9LOY B 4 1208 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 9LOY C 4 1208 UNP P0DTC2 SPIKE_SARS2 1 1208 DBREF 9LOY E 1 117 PDB 9LOY 9LOY 1 117 DBREF 9LOY F 1 106 PDB 9LOY 9LOY 1 106 DBREF 9LOY H 1 117 PDB 9LOY 9LOY 1 117 DBREF 9LOY I 1 106 PDB 9LOY 9LOY 1 106 SEQADV 9LOY ILE A 22 UNP P0DTC2 THR 19 VARIANT SEQADV 9LOY THR A 24 UNP P0DTC2 ARG 21 CONFLICT SEQADV 9LOY A UNP P0DTC2 LEU 24 DELETION SEQADV 9LOY A UNP P0DTC2 PRO 25 DELETION SEQADV 9LOY A UNP P0DTC2 PRO 26 DELETION SEQADV 9LOY SER A 27 UNP P0DTC2 ALA 27 CONFLICT SEQADV 9LOY LEU A 50 UNP P0DTC2 SER 50 CONFLICT SEQADV 9LOY A UNP P0DTC2 HIS 69 DELETION SEQADV 9LOY A UNP P0DTC2 VAL 70 DELETION SEQADV 9LOY PHE A 127 UNP P0DTC2 VAL 127 CONFLICT SEQADV 9LOY ASP A 142 UNP P0DTC2 GLY 142 VARIANT SEQADV 9LOY A UNP P0DTC2 TYR 145 DELETION SEQADV 9LOY SER A 157 UNP P0DTC2 PHE 157 CONFLICT SEQADV 9LOY GLY A 158 UNP P0DTC2 ARG 158 CONFLICT SEQADV 9LOY A UNP P0DTC2 ASN 211 DELETION SEQADV 9LOY ILE A 212 UNP P0DTC2 LEU 212 CONFLICT SEQADV 9LOY GLY A 213 UNP P0DTC2 VAL 213 VARIANT SEQADV 9LOY PHE A 216 UNP P0DTC2 LEU 216 CONFLICT SEQADV 9LOY ASN A 245 UNP P0DTC2 HIS 245 CONFLICT SEQADV 9LOY ASP A 264 UNP P0DTC2 ALA 264 CONFLICT SEQADV 9LOY VAL A 332 UNP P0DTC2 ILE 332 CONFLICT SEQADV 9LOY HIS A 339 UNP P0DTC2 GLY 339 VARIANT SEQADV 9LOY THR A 356 UNP P0DTC2 LYS 356 CONFLICT SEQADV 9LOY PHE A 371 UNP P0DTC2 SER 371 VARIANT SEQADV 9LOY PRO A 373 UNP P0DTC2 SER 373 VARIANT SEQADV 9LOY PHE A 375 UNP P0DTC2 SER 375 VARIANT SEQADV 9LOY ALA A 376 UNP P0DTC2 THR 376 VARIANT SEQADV 9LOY LYS A 403 UNP P0DTC2 ARG 403 CONFLICT SEQADV 9LOY ASN A 405 UNP P0DTC2 ASP 405 VARIANT SEQADV 9LOY SER A 408 UNP P0DTC2 ARG 408 VARIANT SEQADV 9LOY ASN A 417 UNP P0DTC2 LYS 417 VARIANT SEQADV 9LOY LYS A 440 UNP P0DTC2 ASN 440 VARIANT SEQADV 9LOY HIS A 445 UNP P0DTC2 VAL 445 CONFLICT SEQADV 9LOY SER A 446 UNP P0DTC2 GLY 446 VARIANT SEQADV 9LOY ASP A 450 UNP P0DTC2 ASN 450 CONFLICT SEQADV 9LOY TRP A 452 UNP P0DTC2 LEU 452 CONFLICT SEQADV 9LOY SER A 455 UNP P0DTC2 LEU 455 CONFLICT SEQADV 9LOY LYS A 460 UNP P0DTC2 ASN 460 VARIANT SEQADV 9LOY ASN A 477 UNP P0DTC2 SER 477 VARIANT SEQADV 9LOY LYS A 478 UNP P0DTC2 THR 478 VARIANT SEQADV 9LOY LYS A 481 UNP P0DTC2 ASN 481 CONFLICT SEQADV 9LOY A UNP P0DTC2 VAL 483 DELETION SEQADV 9LOY LYS A 484 UNP P0DTC2 GLU 484 VARIANT SEQADV 9LOY PRO A 486 UNP P0DTC2 PHE 486 VARIANT SEQADV 9LOY ARG A 498 UNP P0DTC2 GLN 498 VARIANT SEQADV 9LOY TYR A 501 UNP P0DTC2 ASN 501 VARIANT SEQADV 9LOY HIS A 505 UNP P0DTC2 TYR 505 VARIANT SEQADV 9LOY LYS A 554 UNP P0DTC2 GLU 554 CONFLICT SEQADV 9LOY VAL A 570 UNP P0DTC2 ALA 570 CONFLICT SEQADV 9LOY GLY A 614 UNP P0DTC2 ASP 614 VARIANT SEQADV 9LOY SER A 621 UNP P0DTC2 PRO 621 CONFLICT SEQADV 9LOY TYR A 655 UNP P0DTC2 HIS 655 VARIANT SEQADV 9LOY LYS A 679 UNP P0DTC2 ASN 679 VARIANT SEQADV 9LOY ARG A 681 UNP P0DTC2 PRO 681 VARIANT SEQADV 9LOY GLY A 682 UNP P0DTC2 ARG 682 CONFLICT SEQADV 9LOY SER A 683 UNP P0DTC2 ARG 683 CONFLICT SEQADV 9LOY SER A 685 UNP P0DTC2 ARG 685 CONFLICT SEQADV 9LOY LYS A 764 UNP P0DTC2 ASN 764 VARIANT SEQADV 9LOY TYR A 796 UNP P0DTC2 ASP 796 VARIANT SEQADV 9LOY PRO A 817 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 9LOY PRO A 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 9LOY PRO A 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 9LOY PHE A 939 UNP P0DTC2 SER 939 CONFLICT SEQADV 9LOY PRO A 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 9LOY HIS A 954 UNP P0DTC2 GLN 954 VARIANT SEQADV 9LOY LYS A 969 UNP P0DTC2 ASN 969 VARIANT SEQADV 9LOY PRO A 986 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 9LOY PRO A 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 9LOY LEU A 1143 UNP P0DTC2 PRO 1143 CONFLICT SEQADV 9LOY ILE B 22 UNP P0DTC2 THR 19 VARIANT SEQADV 9LOY THR B 24 UNP P0DTC2 ARG 21 CONFLICT SEQADV 9LOY B UNP P0DTC2 LEU 24 DELETION SEQADV 9LOY B UNP P0DTC2 PRO 25 DELETION SEQADV 9LOY B UNP P0DTC2 PRO 26 DELETION SEQADV 9LOY SER B 27 UNP P0DTC2 ALA 27 CONFLICT SEQADV 9LOY LEU B 50 UNP P0DTC2 SER 50 CONFLICT SEQADV 9LOY B UNP P0DTC2 HIS 69 DELETION SEQADV 9LOY B UNP P0DTC2 VAL 70 DELETION SEQADV 9LOY PHE B 127 UNP P0DTC2 VAL 127 CONFLICT SEQADV 9LOY ASP B 143 UNP P0DTC2 GLY 142 VARIANT SEQADV 9LOY B UNP P0DTC2 TYR 145 DELETION SEQADV 9LOY SER B 157 UNP P0DTC2 PHE 157 CONFLICT SEQADV 9LOY GLY B 158 UNP P0DTC2 ARG 158 CONFLICT SEQADV 9LOY B UNP P0DTC2 ASN 211 DELETION SEQADV 9LOY ILE B 211 UNP P0DTC2 LEU 212 CONFLICT SEQADV 9LOY GLY B 213 UNP P0DTC2 VAL 213 VARIANT SEQADV 9LOY PHE B 216 UNP P0DTC2 LEU 216 CONFLICT SEQADV 9LOY ASN B 245 UNP P0DTC2 HIS 245 CONFLICT SEQADV 9LOY ASP B 264 UNP P0DTC2 ALA 264 CONFLICT SEQADV 9LOY VAL B 333 UNP P0DTC2 ILE 332 CONFLICT SEQADV 9LOY HIS B 340 UNP P0DTC2 GLY 339 VARIANT SEQADV 9LOY THR B 357 UNP P0DTC2 LYS 356 CONFLICT SEQADV 9LOY PHE B 372 UNP P0DTC2 SER 371 VARIANT SEQADV 9LOY PRO B 374 UNP P0DTC2 SER 373 VARIANT SEQADV 9LOY PHE B 376 UNP P0DTC2 SER 375 VARIANT SEQADV 9LOY ALA B 377 UNP P0DTC2 THR 376 VARIANT SEQADV 9LOY LYS B 404 UNP P0DTC2 ARG 403 CONFLICT SEQADV 9LOY ASN B 406 UNP P0DTC2 ASP 405 VARIANT SEQADV 9LOY SER B 409 UNP P0DTC2 ARG 408 VARIANT SEQADV 9LOY ASN B 418 UNP P0DTC2 LYS 417 VARIANT SEQADV 9LOY LYS B 441 UNP P0DTC2 ASN 440 VARIANT SEQADV 9LOY HIS B 446 UNP P0DTC2 VAL 445 CONFLICT SEQADV 9LOY SER B 447 UNP P0DTC2 GLY 446 VARIANT SEQADV 9LOY ASP B 451 UNP P0DTC2 ASN 450 CONFLICT SEQADV 9LOY TRP B 453 UNP P0DTC2 LEU 452 CONFLICT SEQADV 9LOY SER B 456 UNP P0DTC2 LEU 455 CONFLICT SEQADV 9LOY LYS B 461 UNP P0DTC2 ASN 460 VARIANT SEQADV 9LOY ASN B 478 UNP P0DTC2 SER 477 VARIANT SEQADV 9LOY LYS B 479 UNP P0DTC2 THR 478 VARIANT SEQADV 9LOY LYS B 482 UNP P0DTC2 ASN 481 CONFLICT SEQADV 9LOY B UNP P0DTC2 VAL 483 DELETION SEQADV 9LOY LYS B 484 UNP P0DTC2 GLU 484 VARIANT SEQADV 9LOY PRO B 486 UNP P0DTC2 PHE 486 VARIANT SEQADV 9LOY ARG B 498 UNP P0DTC2 GLN 498 VARIANT SEQADV 9LOY TYR B 501 UNP P0DTC2 ASN 501 VARIANT SEQADV 9LOY HIS B 505 UNP P0DTC2 TYR 505 VARIANT SEQADV 9LOY LYS B 554 UNP P0DTC2 GLU 554 CONFLICT SEQADV 9LOY VAL B 570 UNP P0DTC2 ALA 570 CONFLICT SEQADV 9LOY GLY B 614 UNP P0DTC2 ASP 614 VARIANT SEQADV 9LOY SER B 621 UNP P0DTC2 PRO 621 CONFLICT SEQADV 9LOY TYR B 655 UNP P0DTC2 HIS 655 VARIANT SEQADV 9LOY LYS B 679 UNP P0DTC2 ASN 679 VARIANT SEQADV 9LOY ARG B 681 UNP P0DTC2 PRO 681 VARIANT SEQADV 9LOY GLY B 682 UNP P0DTC2 ARG 682 CONFLICT SEQADV 9LOY SER B 683 UNP P0DTC2 ARG 683 CONFLICT SEQADV 9LOY SER B 685 UNP P0DTC2 ARG 685 CONFLICT SEQADV 9LOY LYS B 764 UNP P0DTC2 ASN 764 VARIANT SEQADV 9LOY TYR B 796 UNP P0DTC2 ASP 796 VARIANT SEQADV 9LOY PRO B 817 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 9LOY PRO B 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 9LOY PRO B 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 9LOY PHE B 939 UNP P0DTC2 SER 939 CONFLICT SEQADV 9LOY PRO B 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 9LOY HIS B 954 UNP P0DTC2 GLN 954 VARIANT SEQADV 9LOY LYS B 969 UNP P0DTC2 ASN 969 VARIANT SEQADV 9LOY PRO B 986 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 9LOY PRO B 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 9LOY LEU B 1143 UNP P0DTC2 PRO 1143 CONFLICT SEQADV 9LOY ILE C 22 UNP P0DTC2 THR 19 VARIANT SEQADV 9LOY THR C 24 UNP P0DTC2 ARG 21 CONFLICT SEQADV 9LOY C UNP P0DTC2 LEU 24 DELETION SEQADV 9LOY C UNP P0DTC2 PRO 25 DELETION SEQADV 9LOY C UNP P0DTC2 PRO 26 DELETION SEQADV 9LOY SER C 27 UNP P0DTC2 ALA 27 CONFLICT SEQADV 9LOY LEU C 50 UNP P0DTC2 SER 50 CONFLICT SEQADV 9LOY C UNP P0DTC2 HIS 69 DELETION SEQADV 9LOY C UNP P0DTC2 VAL 70 DELETION SEQADV 9LOY PHE C 127 UNP P0DTC2 VAL 127 CONFLICT SEQADV 9LOY ASP C 142 UNP P0DTC2 GLY 142 VARIANT SEQADV 9LOY C UNP P0DTC2 TYR 145 DELETION SEQADV 9LOY SER C 157 UNP P0DTC2 PHE 157 CONFLICT SEQADV 9LOY GLY C 158 UNP P0DTC2 ARG 158 CONFLICT SEQADV 9LOY C UNP P0DTC2 ASN 211 DELETION SEQADV 9LOY ILE C 211 UNP P0DTC2 LEU 212 CONFLICT SEQADV 9LOY GLY C 213 UNP P0DTC2 VAL 213 VARIANT SEQADV 9LOY PHE C 216 UNP P0DTC2 LEU 216 CONFLICT SEQADV 9LOY ASN C 245 UNP P0DTC2 HIS 245 CONFLICT SEQADV 9LOY ASP C 264 UNP P0DTC2 ALA 264 CONFLICT SEQADV 9LOY VAL C 332 UNP P0DTC2 ILE 332 CONFLICT SEQADV 9LOY HIS C 339 UNP P0DTC2 GLY 339 VARIANT SEQADV 9LOY THR C 356 UNP P0DTC2 LYS 356 CONFLICT SEQADV 9LOY PHE C 371 UNP P0DTC2 SER 371 VARIANT SEQADV 9LOY PRO C 373 UNP P0DTC2 SER 373 VARIANT SEQADV 9LOY PHE C 375 UNP P0DTC2 SER 375 VARIANT SEQADV 9LOY ALA C 376 UNP P0DTC2 THR 376 VARIANT SEQADV 9LOY LYS C 403 UNP P0DTC2 ARG 403 CONFLICT SEQADV 9LOY ASN C 405 UNP P0DTC2 ASP 405 VARIANT SEQADV 9LOY SER C 408 UNP P0DTC2 ARG 408 VARIANT SEQADV 9LOY ASN C 417 UNP P0DTC2 LYS 417 VARIANT SEQADV 9LOY LYS C 440 UNP P0DTC2 ASN 440 VARIANT SEQADV 9LOY HIS C 445 UNP P0DTC2 VAL 445 CONFLICT SEQADV 9LOY SER C 446 UNP P0DTC2 GLY 446 VARIANT SEQADV 9LOY ASP C 450 UNP P0DTC2 ASN 450 CONFLICT SEQADV 9LOY TRP C 452 UNP P0DTC2 LEU 452 CONFLICT SEQADV 9LOY SER C 455 UNP P0DTC2 LEU 455 CONFLICT SEQADV 9LOY LYS C 460 UNP P0DTC2 ASN 460 VARIANT SEQADV 9LOY ASN C 477 UNP P0DTC2 SER 477 VARIANT SEQADV 9LOY LYS C 478 UNP P0DTC2 THR 478 VARIANT SEQADV 9LOY LYS C 481 UNP P0DTC2 ASN 481 CONFLICT SEQADV 9LOY C UNP P0DTC2 VAL 483 DELETION SEQADV 9LOY LYS C 484 UNP P0DTC2 GLU 484 VARIANT SEQADV 9LOY PRO C 486 UNP P0DTC2 PHE 486 VARIANT SEQADV 9LOY ARG C 498 UNP P0DTC2 GLN 498 VARIANT SEQADV 9LOY TYR C 501 UNP P0DTC2 ASN 501 VARIANT SEQADV 9LOY HIS C 505 UNP P0DTC2 TYR 505 VARIANT SEQADV 9LOY LYS C 554 UNP P0DTC2 GLU 554 CONFLICT SEQADV 9LOY VAL C 570 UNP P0DTC2 ALA 570 CONFLICT SEQADV 9LOY GLY C 614 UNP P0DTC2 ASP 614 VARIANT SEQADV 9LOY SER C 621 UNP P0DTC2 PRO 621 CONFLICT SEQADV 9LOY TYR C 655 UNP P0DTC2 HIS 655 VARIANT SEQADV 9LOY LYS C 679 UNP P0DTC2 ASN 679 VARIANT SEQADV 9LOY ARG C 681 UNP P0DTC2 PRO 681 VARIANT SEQADV 9LOY GLY C 682 UNP P0DTC2 ARG 682 CONFLICT SEQADV 9LOY SER C 683 UNP P0DTC2 ARG 683 CONFLICT SEQADV 9LOY SER C 685 UNP P0DTC2 ARG 685 CONFLICT SEQADV 9LOY LYS C 764 UNP P0DTC2 ASN 764 VARIANT SEQADV 9LOY TYR C 796 UNP P0DTC2 ASP 796 VARIANT SEQADV 9LOY PRO C 817 UNP P0DTC2 PHE 817 ENGINEERED MUTATION SEQADV 9LOY PRO C 892 UNP P0DTC2 ALA 892 ENGINEERED MUTATION SEQADV 9LOY PRO C 899 UNP P0DTC2 ALA 899 ENGINEERED MUTATION SEQADV 9LOY PHE C 939 UNP P0DTC2 SER 939 CONFLICT SEQADV 9LOY PRO C 942 UNP P0DTC2 ALA 942 ENGINEERED MUTATION SEQADV 9LOY HIS C 954 UNP P0DTC2 GLN 954 VARIANT SEQADV 9LOY LYS C 969 UNP P0DTC2 ASN 969 VARIANT SEQADV 9LOY PRO C 986 UNP P0DTC2 LYS 986 ENGINEERED MUTATION SEQADV 9LOY PRO C 987 UNP P0DTC2 VAL 987 ENGINEERED MUTATION SEQADV 9LOY LEU C 1143 UNP P0DTC2 PRO 1143 CONFLICT SEQRES 1 A 1200 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 A 1200 GLN CYS VAL ASN LEU ILE THR THR THR GLN SER TYR THR SEQRES 3 A 1200 ASN SER PHE THR ARG GLY VAL TYR TYR PRO ASP LYS VAL SEQRES 4 A 1200 PHE ARG SER SER VAL LEU HIS LEU THR GLN ASP LEU PHE SEQRES 5 A 1200 LEU PRO PHE PHE SER ASN VAL THR TRP PHE HIS ALA ILE SEQRES 6 A 1200 SER GLY THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL SEQRES 7 A 1200 LEU PRO PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU SEQRES 8 A 1200 LYS SER ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR SEQRES 9 A 1200 LEU ASP SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN SEQRES 10 A 1200 ALA THR ASN VAL PHE ILE LYS VAL CYS GLU PHE GLN PHE SEQRES 11 A 1200 CYS ASN ASP PRO PHE LEU ASP VAL TYR HIS LYS ASN ASN SEQRES 12 A 1200 LYS SER TRP MET GLU SER GLU SER GLY VAL TYR SER SER SEQRES 13 A 1200 ALA ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE SEQRES 14 A 1200 LEU MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN SEQRES 15 A 1200 LEU ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE SEQRES 16 A 1200 LYS ILE TYR SER LYS HIS THR PRO ILE ILE GLY ARG ASP SEQRES 17 A 1200 PHE PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP SEQRES 18 A 1200 LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU SEQRES 19 A 1200 LEU ALA LEU ASN ARG SER TYR LEU THR PRO GLY ASP SER SEQRES 20 A 1200 SER SER GLY TRP THR ALA GLY ALA ALA ASP TYR TYR VAL SEQRES 21 A 1200 GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN SEQRES 22 A 1200 GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU SEQRES 23 A 1200 ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE SEQRES 24 A 1200 THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG SEQRES 25 A 1200 VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN VAL SEQRES 26 A 1200 THR ASN LEU CYS PRO PHE HIS GLU VAL PHE ASN ALA THR SEQRES 27 A 1200 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG THR ARG ILE SEQRES 28 A 1200 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN PHE SEQRES 29 A 1200 ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER PRO SEQRES 30 A 1200 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 31 A 1200 ASP SER PHE VAL ILE LYS GLY ASN GLU VAL SER GLN ILE SEQRES 32 A 1200 ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR SEQRES 33 A 1200 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 34 A 1200 ASN SER ASN LYS LEU ASP SER LYS HIS SER GLY ASN TYR SEQRES 35 A 1200 ASP TYR TRP TYR ARG SER PHE ARG LYS SER LYS LEU LYS SEQRES 36 A 1200 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 37 A 1200 GLY ASN LYS PRO CYS LYS GLY LYS GLY PRO ASN CYS TYR SEQRES 38 A 1200 PHE PRO LEU GLN SER TYR GLY PHE ARG PRO THR TYR GLY SEQRES 39 A 1200 VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 40 A 1200 GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO LYS SEQRES 41 A 1200 LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN PHE SEQRES 42 A 1200 ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR LYS SEQRES 43 A 1200 SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY ARG SEQRES 44 A 1200 ASP ILE VAL ASP THR THR ASP ALA VAL ARG ASP PRO GLN SEQRES 45 A 1200 THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE GLY SEQRES 46 A 1200 GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER ASN SEQRES 47 A 1200 GLN VAL ALA VAL LEU TYR GLN GLY VAL ASN CYS THR GLU SEQRES 48 A 1200 VAL SER VAL ALA ILE HIS ALA ASP GLN LEU THR PRO THR SEQRES 49 A 1200 TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN THR SEQRES 50 A 1200 ARG ALA GLY CYS LEU ILE GLY ALA GLU TYR VAL ASN ASN SEQRES 51 A 1200 SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE CYS SEQRES 52 A 1200 ALA SER TYR GLN THR GLN THR LYS SER ARG GLY SER ALA SEQRES 53 A 1200 SER SER VAL ALA SER GLN SER ILE ILE ALA TYR THR MET SEQRES 54 A 1200 SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN ASN SEQRES 55 A 1200 SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL THR SEQRES 56 A 1200 THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER VAL SEQRES 57 A 1200 ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU CYS SEQRES 58 A 1200 SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR GLN SEQRES 59 A 1200 LEU LYS ARG ALA LEU THR GLY ILE ALA VAL GLU GLN ASP SEQRES 60 A 1200 LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE SEQRES 61 A 1200 TYR LYS THR PRO PRO ILE LYS TYR PHE GLY GLY PHE ASN SEQRES 62 A 1200 PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER LYS SEQRES 63 A 1200 ARG SER PRO ILE GLU ASP LEU LEU PHE ASN LYS VAL THR SEQRES 64 A 1200 LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS SEQRES 65 A 1200 LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN SEQRES 66 A 1200 LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU THR SEQRES 67 A 1200 ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU ALA SEQRES 68 A 1200 GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY PRO SEQRES 69 A 1200 ALA LEU GLN ILE PRO PHE PRO MET GLN MET ALA TYR ARG SEQRES 70 A 1200 PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR GLU SEQRES 71 A 1200 ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA ILE SEQRES 72 A 1200 GLY LYS ILE GLN ASP SER LEU PHE SER THR PRO SER ALA SEQRES 73 A 1200 LEU GLY LYS LEU GLN ASP VAL VAL ASN HIS ASN ALA GLN SEQRES 74 A 1200 ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER LYS PHE SEQRES 75 A 1200 GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER ARG SEQRES 76 A 1200 LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG LEU SEQRES 77 A 1200 ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL THR SEQRES 78 A 1200 GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER ALA SEQRES 79 A 1200 ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU GLY SEQRES 80 A 1200 GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS SEQRES 81 A 1200 LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL VAL SEQRES 82 A 1200 PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS ASN SEQRES 83 A 1200 PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA SEQRES 84 A 1200 HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY THR SEQRES 85 A 1200 HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO GLN SEQRES 86 A 1200 ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN CYS SEQRES 87 A 1200 ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR ASP SEQRES 88 A 1200 PRO LEU GLN LEU GLU LEU ASP SER PHE LYS GLU GLU LEU SEQRES 89 A 1200 ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL ASP SEQRES 90 A 1200 LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL ASN SEQRES 91 A 1200 ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA LYS SEQRES 92 A 1200 ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU GLY SEQRES 93 A 1200 LYS TYR GLU GLN SEQRES 1 B 1200 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 B 1200 GLN CYS VAL ASN LEU ILE THR THR THR GLN SER TYR THR SEQRES 3 B 1200 ASN SER PHE THR ARG GLY VAL TYR TYR PRO ASP LYS VAL SEQRES 4 B 1200 PHE ARG SER SER VAL LEU HIS LEU THR GLN ASP LEU PHE SEQRES 5 B 1200 LEU PRO PHE PHE SER ASN VAL THR TRP PHE HIS ALA ILE SEQRES 6 B 1200 SER GLY THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL SEQRES 7 B 1200 LEU PRO PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU SEQRES 8 B 1200 LYS SER ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR SEQRES 9 B 1200 LEU ASP SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN SEQRES 10 B 1200 ALA THR ASN VAL PHE ILE LYS VAL CYS GLU PHE GLN PHE SEQRES 11 B 1200 CYS ASN ASP PRO PHE LEU ASP VAL TYR HIS LYS ASN ASN SEQRES 12 B 1200 LYS SER TRP MET GLU SER GLU SER GLY VAL TYR SER SER SEQRES 13 B 1200 ALA ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE SEQRES 14 B 1200 LEU MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN SEQRES 15 B 1200 LEU ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE SEQRES 16 B 1200 LYS ILE TYR SER LYS HIS THR PRO ILE ILE GLY ARG ASP SEQRES 17 B 1200 PHE PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP SEQRES 18 B 1200 LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU SEQRES 19 B 1200 LEU ALA LEU ASN ARG SER TYR LEU THR PRO GLY ASP SER SEQRES 20 B 1200 SER SER GLY TRP THR ALA GLY ALA ALA ASP TYR TYR VAL SEQRES 21 B 1200 GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN SEQRES 22 B 1200 GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU SEQRES 23 B 1200 ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE SEQRES 24 B 1200 THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG SEQRES 25 B 1200 VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN VAL SEQRES 26 B 1200 THR ASN LEU CYS PRO PHE HIS GLU VAL PHE ASN ALA THR SEQRES 27 B 1200 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG THR ARG ILE SEQRES 28 B 1200 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN PHE SEQRES 29 B 1200 ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER PRO SEQRES 30 B 1200 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 31 B 1200 ASP SER PHE VAL ILE LYS GLY ASN GLU VAL SER GLN ILE SEQRES 32 B 1200 ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR SEQRES 33 B 1200 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 34 B 1200 ASN SER ASN LYS LEU ASP SER LYS HIS SER GLY ASN TYR SEQRES 35 B 1200 ASP TYR TRP TYR ARG SER PHE ARG LYS SER LYS LEU LYS SEQRES 36 B 1200 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 37 B 1200 GLY ASN LYS PRO CYS LYS GLY LYS GLY PRO ASN CYS TYR SEQRES 38 B 1200 PHE PRO LEU GLN SER TYR GLY PHE ARG PRO THR TYR GLY SEQRES 39 B 1200 VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 40 B 1200 GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO LYS SEQRES 41 B 1200 LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN PHE SEQRES 42 B 1200 ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR LYS SEQRES 43 B 1200 SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY ARG SEQRES 44 B 1200 ASP ILE VAL ASP THR THR ASP ALA VAL ARG ASP PRO GLN SEQRES 45 B 1200 THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE GLY SEQRES 46 B 1200 GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER ASN SEQRES 47 B 1200 GLN VAL ALA VAL LEU TYR GLN GLY VAL ASN CYS THR GLU SEQRES 48 B 1200 VAL SER VAL ALA ILE HIS ALA ASP GLN LEU THR PRO THR SEQRES 49 B 1200 TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN THR SEQRES 50 B 1200 ARG ALA GLY CYS LEU ILE GLY ALA GLU TYR VAL ASN ASN SEQRES 51 B 1200 SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE CYS SEQRES 52 B 1200 ALA SER TYR GLN THR GLN THR LYS SER ARG GLY SER ALA SEQRES 53 B 1200 SER SER VAL ALA SER GLN SER ILE ILE ALA TYR THR MET SEQRES 54 B 1200 SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN ASN SEQRES 55 B 1200 SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL THR SEQRES 56 B 1200 THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER VAL SEQRES 57 B 1200 ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU CYS SEQRES 58 B 1200 SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR GLN SEQRES 59 B 1200 LEU LYS ARG ALA LEU THR GLY ILE ALA VAL GLU GLN ASP SEQRES 60 B 1200 LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE SEQRES 61 B 1200 TYR LYS THR PRO PRO ILE LYS TYR PHE GLY GLY PHE ASN SEQRES 62 B 1200 PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER LYS SEQRES 63 B 1200 ARG SER PRO ILE GLU ASP LEU LEU PHE ASN LYS VAL THR SEQRES 64 B 1200 LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS SEQRES 65 B 1200 LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN SEQRES 66 B 1200 LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU THR SEQRES 67 B 1200 ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU ALA SEQRES 68 B 1200 GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY PRO SEQRES 69 B 1200 ALA LEU GLN ILE PRO PHE PRO MET GLN MET ALA TYR ARG SEQRES 70 B 1200 PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR GLU SEQRES 71 B 1200 ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA ILE SEQRES 72 B 1200 GLY LYS ILE GLN ASP SER LEU PHE SER THR PRO SER ALA SEQRES 73 B 1200 LEU GLY LYS LEU GLN ASP VAL VAL ASN HIS ASN ALA GLN SEQRES 74 B 1200 ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER LYS PHE SEQRES 75 B 1200 GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER ARG SEQRES 76 B 1200 LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG LEU SEQRES 77 B 1200 ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL THR SEQRES 78 B 1200 GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER ALA SEQRES 79 B 1200 ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU GLY SEQRES 80 B 1200 GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS SEQRES 81 B 1200 LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL VAL SEQRES 82 B 1200 PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS ASN SEQRES 83 B 1200 PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA SEQRES 84 B 1200 HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY THR SEQRES 85 B 1200 HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO GLN SEQRES 86 B 1200 ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN CYS SEQRES 87 B 1200 ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR ASP SEQRES 88 B 1200 PRO LEU GLN LEU GLU LEU ASP SER PHE LYS GLU GLU LEU SEQRES 89 B 1200 ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL ASP SEQRES 90 B 1200 LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL ASN SEQRES 91 B 1200 ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA LYS SEQRES 92 B 1200 ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU GLY SEQRES 93 B 1200 LYS TYR GLU GLN SEQRES 1 C 1200 MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER SEQRES 2 C 1200 GLN CYS VAL ASN LEU ILE THR THR THR GLN SER TYR THR SEQRES 3 C 1200 ASN SER PHE THR ARG GLY VAL TYR TYR PRO ASP LYS VAL SEQRES 4 C 1200 PHE ARG SER SER VAL LEU HIS LEU THR GLN ASP LEU PHE SEQRES 5 C 1200 LEU PRO PHE PHE SER ASN VAL THR TRP PHE HIS ALA ILE SEQRES 6 C 1200 SER GLY THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL SEQRES 7 C 1200 LEU PRO PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU SEQRES 8 C 1200 LYS SER ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR SEQRES 9 C 1200 LEU ASP SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN SEQRES 10 C 1200 ALA THR ASN VAL PHE ILE LYS VAL CYS GLU PHE GLN PHE SEQRES 11 C 1200 CYS ASN ASP PRO PHE LEU ASP VAL TYR HIS LYS ASN ASN SEQRES 12 C 1200 LYS SER TRP MET GLU SER GLU SER GLY VAL TYR SER SER SEQRES 13 C 1200 ALA ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE SEQRES 14 C 1200 LEU MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN SEQRES 15 C 1200 LEU ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE SEQRES 16 C 1200 LYS ILE TYR SER LYS HIS THR PRO ILE ILE GLY ARG ASP SEQRES 17 C 1200 PHE PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP SEQRES 18 C 1200 LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU SEQRES 19 C 1200 LEU ALA LEU ASN ARG SER TYR LEU THR PRO GLY ASP SER SEQRES 20 C 1200 SER SER GLY TRP THR ALA GLY ALA ALA ASP TYR TYR VAL SEQRES 21 C 1200 GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN SEQRES 22 C 1200 GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU SEQRES 23 C 1200 ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE SEQRES 24 C 1200 THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG SEQRES 25 C 1200 VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN VAL SEQRES 26 C 1200 THR ASN LEU CYS PRO PHE HIS GLU VAL PHE ASN ALA THR SEQRES 27 C 1200 ARG PHE ALA SER VAL TYR ALA TRP ASN ARG THR ARG ILE SEQRES 28 C 1200 SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN PHE SEQRES 29 C 1200 ALA PRO PHE PHE ALA PHE LYS CYS TYR GLY VAL SER PRO SEQRES 30 C 1200 THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA SEQRES 31 C 1200 ASP SER PHE VAL ILE LYS GLY ASN GLU VAL SER GLN ILE SEQRES 32 C 1200 ALA PRO GLY GLN THR GLY ASN ILE ALA ASP TYR ASN TYR SEQRES 33 C 1200 LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP SEQRES 34 C 1200 ASN SER ASN LYS LEU ASP SER LYS HIS SER GLY ASN TYR SEQRES 35 C 1200 ASP TYR TRP TYR ARG SER PHE ARG LYS SER LYS LEU LYS SEQRES 36 C 1200 PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA SEQRES 37 C 1200 GLY ASN LYS PRO CYS LYS GLY LYS GLY PRO ASN CYS TYR SEQRES 38 C 1200 PHE PRO LEU GLN SER TYR GLY PHE ARG PRO THR TYR GLY SEQRES 39 C 1200 VAL GLY HIS GLN PRO TYR ARG VAL VAL VAL LEU SER PHE SEQRES 40 C 1200 GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO LYS SEQRES 41 C 1200 LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN PHE SEQRES 42 C 1200 ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR LYS SEQRES 43 C 1200 SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY ARG SEQRES 44 C 1200 ASP ILE VAL ASP THR THR ASP ALA VAL ARG ASP PRO GLN SEQRES 45 C 1200 THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE GLY SEQRES 46 C 1200 GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER ASN SEQRES 47 C 1200 GLN VAL ALA VAL LEU TYR GLN GLY VAL ASN CYS THR GLU SEQRES 48 C 1200 VAL SER VAL ALA ILE HIS ALA ASP GLN LEU THR PRO THR SEQRES 49 C 1200 TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN THR SEQRES 50 C 1200 ARG ALA GLY CYS LEU ILE GLY ALA GLU TYR VAL ASN ASN SEQRES 51 C 1200 SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE CYS SEQRES 52 C 1200 ALA SER TYR GLN THR GLN THR LYS SER ARG GLY SER ALA SEQRES 53 C 1200 SER SER VAL ALA SER GLN SER ILE ILE ALA TYR THR MET SEQRES 54 C 1200 SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN ASN SEQRES 55 C 1200 SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL THR SEQRES 56 C 1200 THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER VAL SEQRES 57 C 1200 ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU CYS SEQRES 58 C 1200 SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR GLN SEQRES 59 C 1200 LEU LYS ARG ALA LEU THR GLY ILE ALA VAL GLU GLN ASP SEQRES 60 C 1200 LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN ILE SEQRES 61 C 1200 TYR LYS THR PRO PRO ILE LYS TYR PHE GLY GLY PHE ASN SEQRES 62 C 1200 PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER LYS SEQRES 63 C 1200 ARG SER PRO ILE GLU ASP LEU LEU PHE ASN LYS VAL THR SEQRES 64 C 1200 LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP CYS SEQRES 65 C 1200 LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA GLN SEQRES 66 C 1200 LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU THR SEQRES 67 C 1200 ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU ALA SEQRES 68 C 1200 GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY PRO SEQRES 69 C 1200 ALA LEU GLN ILE PRO PHE PRO MET GLN MET ALA TYR ARG SEQRES 70 C 1200 PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR GLU SEQRES 71 C 1200 ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA ILE SEQRES 72 C 1200 GLY LYS ILE GLN ASP SER LEU PHE SER THR PRO SER ALA SEQRES 73 C 1200 LEU GLY LYS LEU GLN ASP VAL VAL ASN HIS ASN ALA GLN SEQRES 74 C 1200 ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER LYS PHE SEQRES 75 C 1200 GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER ARG SEQRES 76 C 1200 LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG LEU SEQRES 77 C 1200 ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL THR SEQRES 78 C 1200 GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER ALA SEQRES 79 C 1200 ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU GLY SEQRES 80 C 1200 GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR HIS SEQRES 81 C 1200 LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL VAL SEQRES 82 C 1200 PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS ASN SEQRES 83 C 1200 PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS ALA SEQRES 84 C 1200 HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY THR SEQRES 85 C 1200 HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO GLN SEQRES 86 C 1200 ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN CYS SEQRES 87 C 1200 ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR ASP SEQRES 88 C 1200 PRO LEU GLN LEU GLU LEU ASP SER PHE LYS GLU GLU LEU SEQRES 89 C 1200 ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL ASP SEQRES 90 C 1200 LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL ASN SEQRES 91 C 1200 ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA LYS SEQRES 92 C 1200 ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU GLY SEQRES 93 C 1200 LYS TYR GLU GLN SEQRES 1 E 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 117 PRO GLY GLY SER LEU ARG LEU SER CYS GLU ALA SER GLU SEQRES 3 E 117 ILE ILE VAL ASN ARG ASN TYR MET ASN TRP VAL ARG GLN SEQRES 4 E 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ILE ILE TYR SEQRES 5 E 117 PRO GLY GLY SER THR PHE TYR ALA ASP SER VAL LYS GLY SEQRES 6 E 117 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR MET SEQRES 7 E 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 E 117 VAL TYR TYR CYS ALA ARG SER TYR GLY ASP PHE TYR VAL SEQRES 9 E 117 ASP PHE TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 F 106 VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SER PRO SEQRES 2 F 106 GLY GLU ARG ALA THR LEU SER CYS ARG ALA THR GLN SER SEQRES 3 F 106 ILE PRO SER THR TYR LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 F 106 GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SER SEQRES 5 F 106 ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SER GLY SEQRES 6 F 106 SER GLY THR ASP PHE THR LEU SER ILE ASN ARG LEU GLU SEQRES 7 F 106 PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN HIS TYR GLY SEQRES 8 F 106 THR SER PRO PHE THR PHE GLY PRO GLY THR LYS VAL ASP SEQRES 9 F 106 ILE LYS SEQRES 1 H 117 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 117 PRO GLY GLY SER LEU ARG LEU SER CYS GLU ALA SER GLU SEQRES 3 H 117 ILE ILE VAL ASN ARG ASN TYR MET ASN TRP VAL ARG GLN SEQRES 4 H 117 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ILE ILE TYR SEQRES 5 H 117 PRO GLY GLY SER THR PHE TYR ALA ASP SER VAL LYS GLY SEQRES 6 H 117 ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR MET SEQRES 7 H 117 TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR ALA SEQRES 8 H 117 VAL TYR TYR CYS ALA ARG SER TYR GLY ASP PHE TYR VAL SEQRES 9 H 117 ASP PHE TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 1 I 106 VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SER PRO SEQRES 2 I 106 GLY GLU ARG ALA THR LEU SER CYS ARG ALA THR GLN SER SEQRES 3 I 106 ILE PRO SER THR TYR LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 4 I 106 GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SER SEQRES 5 I 106 ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SER GLY SEQRES 6 I 106 SER GLY THR ASP PHE THR LEU SER ILE ASN ARG LEU GLU SEQRES 7 I 106 PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN HIS TYR GLY SEQRES 8 I 106 THR SER PRO PHE THR PHE GLY PRO GLY THR LYS VAL ASP SEQRES 9 I 106 ILE LYS HET NAG A1301 14 HET NAG A1302 14 HET NAG A1303 14 HET NAG A1304 14 HET NAG A1305 14 HET NAG A1306 14 HET NAG A1307 14 HET NAG A1308 14 HET NAG A1309 14 HET NAG B1301 14 HET NAG B1302 14 HET NAG B1303 14 HET NAG B1304 14 HET NAG B1305 14 HET NAG B1306 14 HET NAG B1307 14 HET NAG C1301 14 HET NAG C1302 14 HET NAG C1303 14 HET NAG C1304 14 HET NAG C1305 14 HET NAG C1306 14 HET NAG C1307 14 HET NAG C1308 14 HET NAG C1309 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 8 NAG 25(C8 H15 N O6) HELIX 1 AA1 ASP A 294 LYS A 304 1 11 HELIX 2 AA2 PHE A 338 ASN A 343 1 6 HELIX 3 AA3 TYR A 351 TRP A 353 5 3 HELIX 4 AA4 ASP A 364 PHE A 371 5 8 HELIX 5 AA5 SER A 383 LEU A 387 5 5 HELIX 6 AA6 ASN A 405 ILE A 410 5 6 HELIX 7 AA7 ASN A 616 ALA A 626 1 11 HELIX 8 AA8 ASP A 737 GLY A 744 1 8 HELIX 9 AA9 SER A 746 GLN A 755 1 10 HELIX 10 AB1 SER A 758 ALA A 783 1 26 HELIX 11 AB2 SER A 816 VAL A 826 1 11 HELIX 12 AB3 THR A 866 GLY A 885 1 20 HELIX 13 AB4 PRO A 897 ILE A 909 1 13 HELIX 14 AB5 THR A 912 ASN A 919 1 8 HELIX 15 AB6 ASN A 919 THR A 941 1 23 HELIX 16 AB7 PRO A 942 ALA A 944 5 3 HELIX 17 AB8 LEU A 945 GLN A 965 1 21 HELIX 18 AB9 LEU A 966 SER A 968 5 3 HELIX 19 AC1 VAL A 976 LEU A 984 1 9 HELIX 20 AC2 ASP A 985 VAL A 1033 1 49 HELIX 21 AC3 ASP B 294 LYS B 304 1 11 HELIX 22 AC4 ASN B 616 ILE B 624 1 9 HELIX 23 AC5 ASP B 737 GLY B 744 1 8 HELIX 24 AC6 SER B 746 GLN B 755 1 10 HELIX 25 AC7 SER B 758 ALA B 783 1 26 HELIX 26 AC8 SER B 816 VAL B 826 1 11 HELIX 27 AC9 THR B 866 GLY B 885 1 20 HELIX 28 AD1 PRO B 897 ILE B 909 1 13 HELIX 29 AD2 THR B 912 GLU B 918 1 7 HELIX 30 AD3 ASN B 919 THR B 941 1 23 HELIX 31 AD4 PRO B 942 ALA B 944 5 3 HELIX 32 AD5 LEU B 945 GLN B 965 1 21 HELIX 33 AD6 LEU B 966 SER B 968 5 3 HELIX 34 AD7 VAL B 976 LEU B 984 1 9 HELIX 35 AD8 ASP B 985 VAL B 1033 1 49 HELIX 36 AD9 ASP C 294 LYS C 304 1 11 HELIX 37 AE1 PHE C 338 ASN C 343 1 6 HELIX 38 AE2 TYR C 351 TRP C 353 5 3 HELIX 39 AE3 ASP C 364 PHE C 371 5 8 HELIX 40 AE4 SER C 383 LEU C 387 5 5 HELIX 41 AE5 ASN C 405 ILE C 410 5 6 HELIX 42 AE6 ASN C 616 ALA C 626 1 11 HELIX 43 AE7 THR C 638 SER C 640 5 3 HELIX 44 AE8 ASP C 737 GLY C 744 1 8 HELIX 45 AE9 THR C 747 GLN C 755 1 9 HELIX 46 AF1 SER C 758 ALA C 783 1 26 HELIX 47 AF2 SER C 816 VAL C 826 1 11 HELIX 48 AF3 THR C 866 GLY C 885 1 20 HELIX 49 AF4 PRO C 897 ILE C 909 1 13 HELIX 50 AF5 GLN C 913 GLU C 918 1 6 HELIX 51 AF6 ASN C 919 THR C 941 1 23 HELIX 52 AF7 LEU C 945 GLN C 965 1 21 HELIX 53 AF8 LEU C 966 SER C 968 5 3 HELIX 54 AF9 VAL C 976 LEU C 984 1 9 HELIX 55 AG1 ASP C 985 VAL C 1033 1 49 HELIX 56 AG2 ILE E 28 ASN E 32 5 5 HELIX 57 AG3 ASP E 61 LYS E 64 5 4 HELIX 58 AG4 PRO F 28 TYR F 31 5 4 HELIX 59 AG5 ILE H 28 ASN H 32 5 5 HELIX 60 AG6 ASP H 61 LYS H 64 5 4 HELIX 61 AG7 PRO I 28 TYR I 31 5 4 SHEET 1 AA1 7 THR A 29 ASN A 30 0 SHEET 2 AA1 7 ASN A 61 PHE A 65 -1 O VAL A 62 N THR A 29 SHEET 3 AA1 7 TYR A 265 VAL A 267 -1 O TYR A 265 N PHE A 65 SHEET 4 AA1 7 VAL A 90 SER A 94 -1 N ALA A 93 O TYR A 266 SHEET 5 AA1 7 ARG A 190 ILE A 197 -1 O PHE A 194 N VAL A 90 SHEET 6 AA1 7 TYR A 200 HIS A 207 -1 O TYR A 200 N ILE A 197 SHEET 7 AA1 7 GLU A 224 PRO A 230 -1 O LEU A 226 N ILE A 203 SHEET 1 AA2 2 VAL A 42 PHE A 43 0 SHEET 2 AA2 2 PHE B 565 GLY B 566 1 O PHE B 565 N PHE A 43 SHEET 1 AA3 3 LEU A 48 PHE A 55 0 SHEET 2 AA3 3 GLN A 271 TYR A 279 -1 O GLN A 271 N PHE A 55 SHEET 3 AA3 3 ILE A 285 ASP A 287 -1 O THR A 286 N LYS A 278 SHEET 1 AA4 5 PHE A 168 SER A 172 0 SHEET 2 AA4 5 VAL A 126 VAL A 130 -1 N VAL A 130 O PHE A 168 SHEET 3 AA4 5 LEU A 118 ASN A 121 -1 N VAL A 120 O PHE A 127 SHEET 4 AA4 5 GLY A 103 PHE A 106 -1 N TRP A 104 O ILE A 119 SHEET 5 AA4 5 PHE A 238 LEU A 241 -1 O LEU A 241 N GLY A 103 SHEET 1 AA5 5 GLY A 311 ARG A 319 0 SHEET 2 AA5 5 PHE A 592 THR A 599 -1 O GLY A 593 N PHE A 318 SHEET 3 AA5 5 ALA A 609 GLN A 613 -1 O ALA A 609 N ILE A 598 SHEET 4 AA5 5 GLY A 648 ILE A 651 -1 O ILE A 651 N VAL A 610 SHEET 5 AA5 5 VAL A 642 THR A 645 -1 N PHE A 643 O LEU A 650 SHEET 1 AA6 7 GLU A 324 SER A 325 0 SHEET 2 AA6 7 VAL A 539 PHE A 543 1 O ASN A 540 N GLU A 324 SHEET 3 AA6 7 LEU A 546 LYS A 554 -1 O GLY A 550 N VAL A 539 SHEET 4 AA6 7 ILE A 584 THR A 588 -1 O THR A 588 N VAL A 551 SHEET 5 AA6 7 THR A 573 ARG A 577 -1 N VAL A 576 O LEU A 585 SHEET 6 AA6 7 PHE A 565 ARG A 567 -1 N GLY A 566 O ALA A 575 SHEET 7 AA6 7 VAL C 42 PHE C 43 1 O PHE C 43 N PHE A 565 SHEET 1 AA7 3 ALA A 348 SER A 349 0 SHEET 2 AA7 3 ASN A 394 LYS A 403 1 O VAL A 401 N ALA A 348 SHEET 3 AA7 3 ASN A 354 ILE A 358 -1 N ILE A 358 O VAL A 395 SHEET 1 AA8 5 ALA A 348 SER A 349 0 SHEET 2 AA8 5 ASN A 394 LYS A 403 1 O VAL A 401 N ALA A 348 SHEET 3 AA8 5 PRO A 507 GLU A 516 -1 O VAL A 510 N PHE A 400 SHEET 4 AA8 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA8 5 ALA A 376 TYR A 380 -1 N LYS A 378 O VAL A 433 SHEET 1 AA9 2 TRP A 452 ARG A 454 0 SHEET 2 AA9 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AB1 2 TYR A 473 GLN A 474 0 SHEET 2 AB1 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AB2 4 GLU A 654 TYR A 655 0 SHEET 2 AB2 4 SER A 689 THR A 696 1 O ALA A 694 N GLU A 654 SHEET 3 AB2 4 ILE A 670 GLN A 677 -1 N SER A 673 O ILE A 693 SHEET 4 AB2 4 ILE A 664 GLY A 667 -1 N ILE A 666 O ILE A 670 SHEET 1 AB3 2 GLU A 702 SER A 704 0 SHEET 2 AB3 2 ILE C 788 LYS C 790 1 O ILE C 788 N ASN A 703 SHEET 1 AB4 3 SER A 711 PRO A 728 0 SHEET 2 AB4 3 GLY A1059 ALA A1078 -1 O VAL A1068 N THR A 719 SHEET 3 AB4 3 TYR A1047 ALA A1056 -1 N GLN A1054 O VAL A1061 SHEET 1 AB5 5 SER A 711 PRO A 728 0 SHEET 2 AB5 5 GLY A1059 ALA A1078 -1 O VAL A1068 N THR A 719 SHEET 3 AB5 5 VAL A1094 SER A1097 -1 O SER A1097 N THR A1076 SHEET 4 AB5 5 TRP A1102 GLN A1106 -1 O PHE A1103 N VAL A1096 SHEET 5 AB5 5 PHE A1109 GLN A1113 -1 O GLN A1113 N VAL A1104 SHEET 1 AB6 2 LYS A 733 VAL A 736 0 SHEET 2 AB6 2 LEU A 858 LEU A 861 -1 O LEU A 861 N LYS A 733 SHEET 1 AB7 2 ILE A 788 LYS A 790 0 SHEET 2 AB7 2 GLU B 702 SER B 704 1 O ASN B 703 N ILE A 788 SHEET 1 AB8 4 THR A1120 ASN A1125 0 SHEET 2 AB8 4 LYS A1086 PRO A1090 -1 N PHE A1089 O PHE A1121 SHEET 3 AB8 4 ILE A1081 HIS A1083 -1 N HIS A1083 O LYS A1086 SHEET 4 AB8 4 VAL A1133 ASN A1134 1 O VAL A1133 N CYS A1082 SHEET 1 AB9 2 THR B 29 ASN B 30 0 SHEET 2 AB9 2 ASN B 61 VAL B 62 -1 O VAL B 62 N THR B 29 SHEET 1 AC1 4 VAL B 42 PHE B 43 0 SHEET 2 AC1 4 PHE C 565 ARG C 567 1 O ARG C 567 N PHE B 43 SHEET 3 AC1 4 THR C 573 ARG C 577 -1 O ASP C 574 N GLY C 566 SHEET 4 AC1 4 ILE C 584 ASP C 586 -1 O LEU C 585 N VAL C 576 SHEET 1 AC2 3 VAL B 47 PHE B 55 0 SHEET 2 AC2 3 GLN B 271 TYR B 279 -1 O GLN B 271 N PHE B 55 SHEET 3 AC2 3 ILE B 285 ASP B 290 -1 O ASP B 287 N LYS B 278 SHEET 1 AC3 5 GLU B 224 PRO B 230 0 SHEET 2 AC3 5 TYR B 200 PRO B 209 -1 N PHE B 201 O LEU B 229 SHEET 3 AC3 5 ASN B 188 ILE B 197 -1 N LEU B 189 O THR B 208 SHEET 4 AC3 5 VAL B 90 PHE B 92 -1 N VAL B 90 O PHE B 194 SHEET 5 AC3 5 VAL B 267 TYR B 269 -1 O GLY B 268 N TYR B 91 SHEET 1 AC4 5 VAL B 171 SER B 172 0 SHEET 2 AC4 5 VAL B 126 LYS B 129 -1 N VAL B 126 O SER B 172 SHEET 3 AC4 5 LEU B 117 ASN B 121 -1 N VAL B 120 O PHE B 127 SHEET 4 AC4 5 ILE B 101 GLY B 107 -1 N PHE B 106 O LEU B 117 SHEET 5 AC4 5 ARG B 237 LEU B 242 -1 O LEU B 241 N GLY B 103 SHEET 1 AC5 5 GLY B 311 ARG B 319 0 SHEET 2 AC5 5 PHE B 592 THR B 599 -1 O VAL B 597 N TYR B 313 SHEET 3 AC5 5 ALA B 609 GLN B 613 -1 O ALA B 609 N ILE B 598 SHEET 4 AC5 5 GLY B 648 ILE B 651 -1 O CYS B 649 N TYR B 612 SHEET 5 AC5 5 VAL B 642 THR B 645 -1 N PHE B 643 O LEU B 650 SHEET 1 AC6 3 SER B 325 ILE B 326 0 SHEET 2 AC6 3 VAL B 539 PHE B 541 1 O ASN B 540 N ILE B 326 SHEET 3 AC6 3 THR B 549 GLY B 550 -1 O GLY B 550 N VAL B 539 SHEET 1 AC7 2 ALA B 575 ARG B 577 0 SHEET 2 AC7 2 ILE B 584 ASP B 586 -1 O LEU B 585 N VAL B 576 SHEET 1 AC8 4 GLU B 654 TYR B 655 0 SHEET 2 AC8 4 SER B 689 THR B 696 1 O ALA B 694 N GLU B 654 SHEET 3 AC8 4 ILE B 670 GLN B 677 -1 N GLN B 677 O SER B 689 SHEET 4 AC8 4 ILE B 664 GLY B 667 -1 N ILE B 666 O ILE B 670 SHEET 1 AC9 3 SER B 711 PRO B 728 0 SHEET 2 AC9 3 GLY B1059 ALA B1078 -1 O PHE B1075 N ILE B 712 SHEET 3 AC9 3 TYR B1047 ALA B1056 -1 N MET B1050 O VAL B1065 SHEET 1 AD1 5 SER B 711 PRO B 728 0 SHEET 2 AD1 5 GLY B1059 ALA B1078 -1 O PHE B1075 N ILE B 712 SHEET 3 AD1 5 VAL B1094 SER B1097 -1 O SER B1097 N THR B1076 SHEET 4 AD1 5 TRP B1102 THR B1105 -1 O PHE B1103 N VAL B1096 SHEET 5 AD1 5 GLN B1113 ILE B1114 -1 O GLN B1113 N VAL B1104 SHEET 1 AD2 2 LYS B 733 VAL B 736 0 SHEET 2 AD2 2 LEU B 858 LEU B 861 -1 O THR B 859 N SER B 735 SHEET 1 AD3 2 ILE B 788 LYS B 790 0 SHEET 2 AD3 2 GLU C 702 SER C 704 1 O ASN C 703 N ILE B 788 SHEET 1 AD4 4 THR B1120 VAL B1122 0 SHEET 2 AD4 4 LYS B1086 PRO B1090 -1 N PHE B1089 O PHE B1121 SHEET 3 AD4 4 ILE B1081 HIS B1083 -1 N HIS B1083 O LYS B1086 SHEET 4 AD4 4 VAL B1133 ASN B1134 1 O VAL B1133 N CYS B1082 SHEET 1 AD5 7 THR C 29 ASN C 30 0 SHEET 2 AD5 7 ASN C 61 PHE C 65 -1 O VAL C 62 N THR C 29 SHEET 3 AD5 7 TYR C 265 TYR C 269 -1 O TYR C 265 N PHE C 65 SHEET 4 AD5 7 VAL C 90 THR C 95 -1 N TYR C 91 O GLY C 268 SHEET 5 AD5 7 ASN C 188 ILE C 197 -1 O PHE C 192 N PHE C 92 SHEET 6 AD5 7 TYR C 200 PRO C 209 -1 O THR C 208 N LEU C 189 SHEET 7 AD5 7 GLU C 224 LEU C 229 -1 O LEU C 226 N ILE C 203 SHEET 1 AD6 3 LEU C 48 PHE C 55 0 SHEET 2 AD6 3 GLN C 271 TYR C 279 -1 O GLN C 271 N PHE C 55 SHEET 3 AD6 3 ILE C 285 ASP C 290 -1 O VAL C 289 N LEU C 276 SHEET 1 AD7 6 LEU C 84 PRO C 85 0 SHEET 2 AD7 6 ARG C 237 LEU C 241 -1 O PHE C 238 N LEU C 84 SHEET 3 AD7 6 GLY C 103 GLY C 107 -1 N GLY C 107 O ARG C 237 SHEET 4 AD7 6 SER C 116 ASN C 122 -1 O ILE C 119 N TRP C 104 SHEET 5 AD7 6 ASN C 125 CYS C 131 -1 O PHE C 127 N VAL C 120 SHEET 6 AD7 6 PHE C 168 SER C 172 -1 O TYR C 170 N ILE C 128 SHEET 1 AD8 5 GLY C 311 ARG C 319 0 SHEET 2 AD8 5 PHE C 592 THR C 599 -1 O VAL C 597 N TYR C 313 SHEET 3 AD8 5 ALA C 609 GLN C 613 -1 O ALA C 609 N ILE C 598 SHEET 4 AD8 5 GLY C 648 ILE C 651 -1 O CYS C 649 N TYR C 612 SHEET 5 AD8 5 VAL C 642 GLN C 644 -1 N PHE C 643 O LEU C 650 SHEET 1 AD9 3 GLU C 324 SER C 325 0 SHEET 2 AD9 3 CYS C 538 PHE C 543 1 O ASN C 540 N GLU C 324 SHEET 3 AD9 3 LEU C 546 VAL C 551 -1 O LEU C 546 N PHE C 543 SHEET 1 AE1 3 ALA C 348 SER C 349 0 SHEET 2 AE1 3 ASN C 394 LYS C 403 1 O VAL C 401 N ALA C 348 SHEET 3 AE1 3 ASN C 354 ILE C 358 -1 N ILE C 358 O VAL C 395 SHEET 1 AE2 5 ALA C 348 SER C 349 0 SHEET 2 AE2 5 ASN C 394 LYS C 403 1 O VAL C 401 N ALA C 348 SHEET 3 AE2 5 PRO C 507 GLU C 516 -1 O VAL C 510 N PHE C 400 SHEET 4 AE2 5 GLY C 431 ASN C 437 -1 N ILE C 434 O VAL C 511 SHEET 5 AE2 5 ALA C 376 TYR C 380 -1 N LYS C 378 O VAL C 433 SHEET 1 AE3 2 TRP C 452 ARG C 454 0 SHEET 2 AE3 2 LEU C 492 SER C 494 -1 O GLN C 493 N TYR C 453 SHEET 1 AE4 2 TYR C 473 GLN C 474 0 SHEET 2 AE4 2 CYS C 488 TYR C 489 -1 O TYR C 489 N TYR C 473 SHEET 1 AE5 4 GLU C 654 TYR C 655 0 SHEET 2 AE5 4 GLN C 690 THR C 696 1 O ALA C 694 N GLU C 654 SHEET 3 AE5 4 ILE C 670 THR C 676 -1 N CYS C 671 O TYR C 695 SHEET 4 AE5 4 ILE C 664 GLY C 667 -1 N ILE C 666 O ILE C 670 SHEET 1 AE6 3 SER C 711 PRO C 728 0 SHEET 2 AE6 3 GLY C1059 ALA C1078 -1 O PHE C1075 N ILE C 712 SHEET 3 AE6 3 TYR C1047 ALA C1056 -1 N MET C1050 O VAL C1065 SHEET 1 AE7 4 SER C 711 PRO C 728 0 SHEET 2 AE7 4 GLY C1059 ALA C1078 -1 O PHE C1075 N ILE C 712 SHEET 3 AE7 4 VAL C1094 SER C1097 -1 O SER C1097 N THR C1076 SHEET 4 AE7 4 TRP C1102 THR C1105 -1 O PHE C1103 N VAL C1096 SHEET 1 AE8 2 LYS C 733 VAL C 736 0 SHEET 2 AE8 2 LEU C 858 LEU C 861 -1 O LEU C 861 N LYS C 733 SHEET 1 AE9 4 THR C1120 ASN C1125 0 SHEET 2 AE9 4 LYS C1086 PRO C1090 -1 N PHE C1089 O PHE C1121 SHEET 3 AE9 4 ILE C1081 HIS C1083 -1 N ILE C1081 O HIS C1088 SHEET 4 AE9 4 VAL C1133 ASN C1134 1 O VAL C1133 N CYS C1082 SHEET 1 AF1 4 GLN E 3 SER E 7 0 SHEET 2 AF1 4 LEU E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AF1 4 THR E 77 MET E 82 -1 O MET E 82 N LEU E 18 SHEET 4 AF1 4 PHE E 67 ASP E 72 -1 N THR E 68 O GLN E 81 SHEET 1 AF2 6 LEU E 11 VAL E 12 0 SHEET 2 AF2 6 THR E 111 VAL E 115 1 O THR E 114 N VAL E 12 SHEET 3 AF2 6 ALA E 91 TYR E 99 -1 N ALA E 91 O VAL E 113 SHEET 4 AF2 6 MET E 34 ARG E 38 -1 N VAL E 37 O TYR E 94 SHEET 5 AF2 6 GLU E 46 ILE E 51 -1 O ILE E 51 N MET E 34 SHEET 6 AF2 6 THR E 57 TYR E 59 -1 O PHE E 58 N ILE E 50 SHEET 1 AF3 4 LEU E 11 VAL E 12 0 SHEET 2 AF3 4 THR E 111 VAL E 115 1 O THR E 114 N VAL E 12 SHEET 3 AF3 4 ALA E 91 TYR E 99 -1 N ALA E 91 O VAL E 113 SHEET 4 AF3 4 TYR E 103 TRP E 107 -1 O TYR E 103 N TYR E 99 SHEET 1 AF4 6 THR F 8 LEU F 11 0 SHEET 2 AF4 6 THR F 101 ILE F 105 1 O ASP F 104 N LEU F 11 SHEET 3 AF4 6 VAL F 84 HIS F 89 -1 N TYR F 85 O THR F 101 SHEET 4 AF4 6 ALA F 33 GLN F 37 -1 N TYR F 35 O TYR F 86 SHEET 5 AF4 6 ARG F 44 TYR F 48 -1 O ARG F 44 N GLN F 36 SHEET 6 AF4 6 SER F 52 ARG F 53 -1 O SER F 52 N TYR F 48 SHEET 1 AF5 4 THR F 8 LEU F 11 0 SHEET 2 AF5 4 THR F 101 ILE F 105 1 O ASP F 104 N LEU F 11 SHEET 3 AF5 4 VAL F 84 HIS F 89 -1 N TYR F 85 O THR F 101 SHEET 4 AF5 4 THR F 96 PHE F 97 -1 O THR F 96 N HIS F 89 SHEET 1 AF6 3 ALA F 17 ARG F 22 0 SHEET 2 AF6 3 ASP F 69 ILE F 74 -1 O ILE F 74 N ALA F 17 SHEET 3 AF6 3 PHE F 61 SER F 66 -1 N SER F 62 O SER F 73 SHEET 1 AF7 4 GLN H 3 SER H 7 0 SHEET 2 AF7 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AF7 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AF7 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AF8 6 LEU H 11 VAL H 12 0 SHEET 2 AF8 6 THR H 111 VAL H 115 1 O THR H 114 N VAL H 12 SHEET 3 AF8 6 ALA H 91 TYR H 99 -1 N ALA H 91 O VAL H 113 SHEET 4 AF8 6 MET H 34 ARG H 38 -1 N VAL H 37 O TYR H 94 SHEET 5 AF8 6 GLU H 46 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AF8 6 THR H 57 TYR H 59 -1 O PHE H 58 N ILE H 50 SHEET 1 AF9 4 LEU H 11 VAL H 12 0 SHEET 2 AF9 4 THR H 111 VAL H 115 1 O THR H 114 N VAL H 12 SHEET 3 AF9 4 ALA H 91 TYR H 99 -1 N ALA H 91 O VAL H 113 SHEET 4 AF9 4 TYR H 103 TRP H 107 -1 O TYR H 103 N TYR H 99 SHEET 1 AG1 6 THR I 8 LEU I 11 0 SHEET 2 AG1 6 THR I 101 ILE I 105 1 O ASP I 104 N LEU I 11 SHEET 3 AG1 6 VAL I 84 HIS I 89 -1 N TYR I 85 O THR I 101 SHEET 4 AG1 6 ALA I 33 GLN I 37 -1 N TYR I 35 O TYR I 86 SHEET 5 AG1 6 ARG I 44 TYR I 48 -1 O ARG I 44 N GLN I 36 SHEET 6 AG1 6 SER I 52 ARG I 53 -1 O SER I 52 N TYR I 48 SHEET 1 AG2 4 THR I 8 LEU I 11 0 SHEET 2 AG2 4 THR I 101 ILE I 105 1 O ASP I 104 N LEU I 11 SHEET 3 AG2 4 VAL I 84 HIS I 89 -1 N TYR I 85 O THR I 101 SHEET 4 AG2 4 THR I 96 PHE I 97 -1 O THR I 96 N HIS I 89 SHEET 1 AG3 3 ALA I 17 ARG I 22 0 SHEET 2 AG3 3 ASP I 69 ILE I 74 -1 O ILE I 74 N ALA I 17 SHEET 3 AG3 3 PHE I 61 SER I 66 -1 N SER I 62 O SER I 73 SSBOND 1 CYS A 131 CYS A 166 1555 1555 2.04 SSBOND 2 CYS A 291 CYS A 301 1555 1555 2.02 SSBOND 3 CYS A 336 CYS A 361 1555 1555 2.03 SSBOND 4 CYS A 379 CYS A 432 1555 1555 2.03 SSBOND 5 CYS A 391 CYS A 525 1555 1555 2.03 SSBOND 6 CYS A 480 CYS A 488 1555 1555 2.03 SSBOND 7 CYS A 538 CYS A 590 1555 1555 2.04 SSBOND 8 CYS A 617 CYS A 649 1555 1555 2.04 SSBOND 9 CYS A 662 CYS A 671 1555 1555 2.04 SSBOND 10 CYS A 738 CYS A 760 1555 1555 2.04 SSBOND 11 CYS A 743 CYS A 749 1555 1555 2.04 SSBOND 12 CYS A 1032 CYS A 1043 1555 1555 2.03 SSBOND 13 CYS A 1082 CYS A 1126 1555 1555 2.03 SSBOND 14 CYS B 131 CYS B 166 1555 1555 2.03 SSBOND 15 CYS B 291 CYS B 301 1555 1555 2.02 SSBOND 16 CYS B 538 CYS B 590 1555 1555 2.02 SSBOND 17 CYS B 617 CYS B 649 1555 1555 2.04 SSBOND 18 CYS B 662 CYS B 671 1555 1555 2.04 SSBOND 19 CYS B 738 CYS B 760 1555 1555 2.04 SSBOND 20 CYS B 743 CYS B 749 1555 1555 2.03 SSBOND 21 CYS B 1032 CYS B 1043 1555 1555 2.02 SSBOND 22 CYS B 1082 CYS B 1126 1555 1555 2.02 SSBOND 23 CYS C 131 CYS C 166 1555 1555 2.03 SSBOND 24 CYS C 291 CYS C 301 1555 1555 2.02 SSBOND 25 CYS C 336 CYS C 361 1555 1555 2.03 SSBOND 26 CYS C 379 CYS C 432 1555 1555 2.03 SSBOND 27 CYS C 391 CYS C 525 1555 1555 2.03 SSBOND 28 CYS C 480 CYS C 488 1555 1555 2.03 SSBOND 29 CYS C 538 CYS C 590 1555 1555 2.03 SSBOND 30 CYS C 617 CYS C 649 1555 1555 2.05 SSBOND 31 CYS C 662 CYS C 671 1555 1555 2.04 SSBOND 32 CYS C 738 CYS C 760 1555 1555 2.04 SSBOND 33 CYS C 743 CYS C 749 1555 1555 2.03 SSBOND 34 CYS C 1032 CYS C 1043 1555 1555 2.03 SSBOND 35 CYS C 1082 CYS C 1126 1555 1555 2.03 SSBOND 36 CYS E 22 CYS E 95 1555 1555 2.03 SSBOND 37 CYS F 21 CYS F 87 1555 1555 2.03 SSBOND 38 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 39 CYS I 21 CYS I 87 1555 1555 2.03 LINK ND2 ASN A 282 C1 NAG A1301 1555 1555 1.45 LINK ND2 ASN A 343 C1 NAG A1307 1555 1555 1.43 LINK ND2 ASN A 354 C1 NAG A1308 1555 1555 1.44 LINK ND2 ASN A 616 C1 NAG A1309 1555 1555 1.43 LINK ND2 ASN A 709 C1 NAG A1302 1555 1555 1.44 LINK ND2 ASN A 717 C1 NAG A1303 1555 1555 1.43 LINK ND2 ASN A 801 C1 NAG A1304 1555 1555 1.44 LINK ND2 ASN A1098 C1 NAG A1305 1555 1555 1.43 LINK ND2 ASN A1134 C1 NAG A1306 1555 1555 1.42 LINK ND2 ASN B 282 C1 NAG B1301 1555 1555 1.44 LINK ND2 ASN B 616 C1 NAG B1302 1555 1555 1.43 LINK ND2 ASN B 709 C1 NAG B1303 1555 1555 1.44 LINK ND2 ASN B 717 C1 NAG B1304 1555 1555 1.42 LINK ND2 ASN B 801 C1 NAG B1305 1555 1555 1.43 LINK ND2 ASN B1098 C1 NAG B1306 1555 1555 1.44 LINK ND2 ASN B1134 C1 NAG B1307 1555 1555 1.42 LINK ND2 ASN C 282 C1 NAG C1301 1555 1555 1.42 LINK ND2 ASN C 343 C1 NAG C1308 1555 1555 1.44 LINK ND2 ASN C 354 C1 NAG C1309 1555 1555 1.43 LINK ND2 ASN C 616 C1 NAG C1302 1555 1555 1.42 LINK ND2 ASN C 709 C1 NAG C1303 1555 1555 1.43 LINK ND2 ASN C 717 C1 NAG C1304 1555 1555 1.43 LINK ND2 ASN C 801 C1 NAG C1305 1555 1555 1.43 LINK ND2 ASN C1098 C1 NAG C1306 1555 1555 1.43 LINK ND2 ASN C1134 C1 NAG C1307 1555 1555 1.43 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000