HEADER BLOOD CLOTTING 07-JUN-25 9P0X TITLE NANODISC-EMBEDDED HUMAN TF/FVIIA/XK1 IN COMPLEX WITH 10H10 FAB TITLE 2 (NANODISC-SUBTRACTED) COMPND MOL_ID: 1; COMPND 2 MOLECULE: FACTOR VII LIGHT CHAIN; COMPND 3 CHAIN: V; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FACTOR X LIGHT CHAIN; COMPND 7 CHAIN: X; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: COAGULATION FACTOR VII HEAVY CHAIN; COMPND 11 CHAIN: S; COMPND 12 SYNONYM: PROCONVERTIN,SERUM PROTHROMBIN CONVERSION ACCELERATOR,SPCA; COMPND 13 EC: 3.4.21.21; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: TISSUE FACTOR,MALTOSE/MALTODEXTRIN-BINDING PERIPLASMIC COMPND 17 PROTEIN; COMPND 18 CHAIN: T; COMPND 19 SYNONYM: TF,COAGULATION FACTOR III,THROMBOPLASTIN,MMBP,MALTODEXTRIN- COMPND 20 BINDING PROTEIN,MALTOSE-BINDING PROTEIN,MBP; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: TISSUE FACTOR PATHWAY INHIBITOR; COMPND 24 CHAIN: K; COMPND 25 SYNONYM: TFPI,EXTRINSIC PATHWAY INHIBITOR,EPI,LIPOPROTEIN-ASSOCIATED COMPND 26 COAGULATION INHIBITOR,LACI; COMPND 27 ENGINEERED: YES; COMPND 28 MOL_ID: 6; COMPND 29 MOLECULE: HUMAN 10H10 ANTIBODY FAB HEAVY CHAIN; COMPND 30 CHAIN: H; COMPND 31 MOL_ID: 7; COMPND 32 MOLECULE: HUMAN 10H10 ANTIBODY FAB LIGHT CHAIN; COMPND 33 CHAIN: L SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: F7; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: F10; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 19 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(+); SOURCE 22 MOL_ID: 3; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: F7; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 30 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 31 MOL_ID: 4; SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 33 ORGANISM_COMMON: HUMAN; SOURCE 34 ORGANISM_TAXID: 9606, 562; SOURCE 35 GENE: F3, MALE, Z5632, ECS5017; SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 37 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 38 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PET-26B(+); SOURCE 41 MOL_ID: 5; SOURCE 42 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 43 ORGANISM_COMMON: HUMAN; SOURCE 44 ORGANISM_TAXID: 9606; SOURCE 45 GENE: TFPI, LACI, TFPI1; SOURCE 46 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 47 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 48 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 49 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 50 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 51 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 52 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(+); SOURCE 53 MOL_ID: 6; SOURCE 54 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 55 ORGANISM_COMMON: MOUSE; SOURCE 56 ORGANISM_TAXID: 10090; SOURCE 57 STRAIN: BALB/C; SOURCE 58 MOL_ID: 7; SOURCE 59 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 60 ORGANISM_COMMON: MOUSE; SOURCE 61 ORGANISM_TAXID: 10090; SOURCE 62 STRAIN: BALB/C KEYWDS COMPLEX, NANODISC, BLOOD CLOTTING EXPDTA ELECTRON MICROSCOPY AUTHOR A.L.PHOTENHAUER,J.C.SEDZRO,M.D.OHI,J.H.MORRISSEY REVDAT 1 27-AUG-25 9P0X 0 JRNL AUTH J.C.SEDZRO,A.L.PHOTENHAUER,F.BIRKLE,K.MEZE,A.MORTENSON, JRNL AUTH 2 C.DUCKWORTH,P.C.WEN,S.KEARNS,M.A.CIANFROCCO,E.TAJKHORSHID, JRNL AUTH 3 M.D.OHI,J.H.MORRISSEY JRNL TITL CRYO-EM STRUCTURE OF THE TISSUE FACTOR/FACTOR VIIA COMPLEX JRNL TITL 2 WITH A FACTOR X MIMETIC REVEALS A NOVEL ALLOSTERIC JRNL TITL 3 MECHANISM. JRNL REF BLOOD 2025 JRNL REFN ESSN 1528-0020 JRNL PMID 40811856 JRNL DOI 10.1182/BLOOD.2025029430 REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 1DAN REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : CRYSTAL STRUCTURES WERE RIGID-BODY FIT INTO REMARK 3 THE DENSITY MAP AND MODEL OPTIMIZATION WAS THEN CARRIED OUT WITH REMARK 3 PHENIX REAL-SPACE REFINE. MANUAL REFINEMENT IN COOT WAS REMARK 3 PERFORMED TO ENSURE THAT THE BACKBONE TRACES FOLLOWED THE REMARK 3 DENSITY IN REGIONS WHERE THE MAP WAS HIGH ENOUGH RESOLUTION TO REMARK 3 TRACE THE BACKBONE. SECONDARY STRUCTURE RESTRAINTS WERE USED TO REMARK 3 ENSURE THAT ALPHA-HELICES AND BETA-SHEETS DID NOT DEVIATE FAR REMARK 3 FROM THEIR EXPECTED GEOMETRY. A FINAL CHECK OF MOLPROBITY AND REMARK 3 CROSS CORRELATION WAS DONE TO ENSURE MODEL QUALITY. 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) : 3.700 REMARK 3 NUMBER OF PARTICLES : 20107 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 9P0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1000296731. 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 : COMPLEX OF FACTOR VIIA, XK1 AND REMARK 245 THE FAB FRAGMENT OF ANTIBODY REMARK 245 10H10, ALL BOUND TO TISSUE REMARK 245 FACTOR EMBEDDED IN A NANODISC REMARK 245 MEMBRANE BILAYER.; HUMAN 10H10 REMARK 245 ANTIBODY FAB; XK1 CHIMERIC REMARK 245 PROTEIN; HUMAN FACTOR VIIA REMARK 245 (FVIIA); HUMAN MBP-TAGGED REMARK 245 TISSUE FACTOR 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 : 7.40 REMARK 245 SAMPLE DETAILS : MAP WITH NANODISC SUBTRACTED. REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 7132 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) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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 : 105000 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: V, X, S, T, K, H, L 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 VAL T 83 REMARK 465 GLU T 84 REMARK 465 SER T 85 REMARK 465 THR T 86 REMARK 465 GLY T 211 REMARK 465 GLN T 212 REMARK 465 GLU T 213 REMARK 465 LYS T 214 REMARK 465 GLY T 215 REMARK 465 GLU T 216 REMARK 465 PHE T 217 REMARK 465 ARG T 218 REMARK 465 GLU T 219 REMARK 465 ILE T 220 REMARK 465 PHE T 221 REMARK 465 TYR T 222 REMARK 465 ILE T 223 REMARK 465 ILE T 224 REMARK 465 GLY T 225 REMARK 465 ALA T 226 REMARK 465 VAL T 227 REMARK 465 VAL T 228 REMARK 465 PHE T 229 REMARK 465 VAL T 230 REMARK 465 VAL T 231 REMARK 465 ILE T 232 REMARK 465 ILE T 233 REMARK 465 LEU T 234 REMARK 465 VAL T 235 REMARK 465 ILE T 236 REMARK 465 ILE T 237 REMARK 465 LEU T 238 REMARK 465 ALA T 239 REMARK 465 ILE T 240 REMARK 465 SER T 241 REMARK 465 LEU T 242 REMARK 465 HIS T 243 REMARK 465 LYS T 244 REMARK 465 GLY T 245 REMARK 465 SER T 246 REMARK 465 GLY T 247 REMARK 465 SER T 248 REMARK 465 GLY T 249 REMARK 465 MET T 250 REMARK 465 LYS T 251 REMARK 465 ILE T 252 REMARK 465 GLU T 253 REMARK 465 GLU T 254 REMARK 465 GLY T 255 REMARK 465 LYS T 256 REMARK 465 LEU T 257 REMARK 465 VAL T 258 REMARK 465 ILE T 259 REMARK 465 TRP T 260 REMARK 465 ILE T 261 REMARK 465 ASN T 262 REMARK 465 GLY T 263 REMARK 465 ASP T 264 REMARK 465 LYS T 265 REMARK 465 GLY T 266 REMARK 465 TYR T 267 REMARK 465 ASN T 268 REMARK 465 GLY T 269 REMARK 465 LEU T 270 REMARK 465 ALA T 271 REMARK 465 GLU T 272 REMARK 465 VAL T 273 REMARK 465 GLY T 274 REMARK 465 LYS T 275 REMARK 465 LYS T 276 REMARK 465 PHE T 277 REMARK 465 GLU T 278 REMARK 465 LYS T 279 REMARK 465 ASP T 280 REMARK 465 THR T 281 REMARK 465 GLY T 282 REMARK 465 ILE T 283 REMARK 465 LYS T 284 REMARK 465 VAL T 285 REMARK 465 THR T 286 REMARK 465 VAL T 287 REMARK 465 GLU T 288 REMARK 465 HIS T 289 REMARK 465 PRO T 290 REMARK 465 ASP T 291 REMARK 465 LYS T 292 REMARK 465 LEU T 293 REMARK 465 GLU T 294 REMARK 465 GLU T 295 REMARK 465 LYS T 296 REMARK 465 PHE T 297 REMARK 465 PRO T 298 REMARK 465 GLN T 299 REMARK 465 VAL T 300 REMARK 465 ALA T 301 REMARK 465 ALA T 302 REMARK 465 THR T 303 REMARK 465 GLY T 304 REMARK 465 ASP T 305 REMARK 465 GLY T 306 REMARK 465 PRO T 307 REMARK 465 ASP T 308 REMARK 465 ILE T 309 REMARK 465 ILE T 310 REMARK 465 PHE T 311 REMARK 465 TRP T 312 REMARK 465 ALA T 313 REMARK 465 HIS T 314 REMARK 465 ASP T 315 REMARK 465 ARG T 316 REMARK 465 PHE T 317 REMARK 465 GLY T 318 REMARK 465 GLY T 319 REMARK 465 TYR T 320 REMARK 465 ALA T 321 REMARK 465 GLN T 322 REMARK 465 SER T 323 REMARK 465 GLY T 324 REMARK 465 LEU T 325 REMARK 465 LEU T 326 REMARK 465 ALA T 327 REMARK 465 GLU T 328 REMARK 465 ILE T 329 REMARK 465 THR T 330 REMARK 465 PRO T 331 REMARK 465 ASP T 332 REMARK 465 LYS T 333 REMARK 465 ALA T 334 REMARK 465 PHE T 335 REMARK 465 GLN T 336 REMARK 465 ASP T 337 REMARK 465 LYS T 338 REMARK 465 LEU T 339 REMARK 465 TYR T 340 REMARK 465 PRO T 341 REMARK 465 PHE T 342 REMARK 465 THR T 343 REMARK 465 TRP T 344 REMARK 465 ASP T 345 REMARK 465 ALA T 346 REMARK 465 VAL T 347 REMARK 465 ARG T 348 REMARK 465 TYR T 349 REMARK 465 ASN T 350 REMARK 465 GLY T 351 REMARK 465 LYS T 352 REMARK 465 LEU T 353 REMARK 465 ILE T 354 REMARK 465 ALA T 355 REMARK 465 TYR T 356 REMARK 465 PRO T 357 REMARK 465 ILE T 358 REMARK 465 ALA T 359 REMARK 465 VAL T 360 REMARK 465 GLU T 361 REMARK 465 ALA T 362 REMARK 465 LEU T 363 REMARK 465 SER T 364 REMARK 465 LEU T 365 REMARK 465 ILE T 366 REMARK 465 TYR T 367 REMARK 465 ASN T 368 REMARK 465 LYS T 369 REMARK 465 ASP T 370 REMARK 465 LEU T 371 REMARK 465 LEU T 372 REMARK 465 PRO T 373 REMARK 465 ASN T 374 REMARK 465 PRO T 375 REMARK 465 PRO T 376 REMARK 465 LYS T 377 REMARK 465 THR T 378 REMARK 465 TRP T 379 REMARK 465 GLU T 380 REMARK 465 GLU T 381 REMARK 465 ILE T 382 REMARK 465 PRO T 383 REMARK 465 ALA T 384 REMARK 465 LEU T 385 REMARK 465 ASP T 386 REMARK 465 LYS T 387 REMARK 465 GLU T 388 REMARK 465 LEU T 389 REMARK 465 LYS T 390 REMARK 465 ALA T 391 REMARK 465 LYS T 392 REMARK 465 GLY T 393 REMARK 465 LYS T 394 REMARK 465 SER T 395 REMARK 465 ALA T 396 REMARK 465 LEU T 397 REMARK 465 MET T 398 REMARK 465 PHE T 399 REMARK 465 ASN T 400 REMARK 465 LEU T 401 REMARK 465 GLN T 402 REMARK 465 GLU T 403 REMARK 465 PRO T 404 REMARK 465 TYR T 405 REMARK 465 PHE T 406 REMARK 465 THR T 407 REMARK 465 TRP T 408 REMARK 465 PRO T 409 REMARK 465 LEU T 410 REMARK 465 ILE T 411 REMARK 465 ALA T 412 REMARK 465 ALA T 413 REMARK 465 ASP T 414 REMARK 465 GLY T 415 REMARK 465 GLY T 416 REMARK 465 TYR T 417 REMARK 465 ALA T 418 REMARK 465 PHE T 419 REMARK 465 LYS T 420 REMARK 465 TYR T 421 REMARK 465 GLU T 422 REMARK 465 ASN T 423 REMARK 465 GLY T 424 REMARK 465 LYS T 425 REMARK 465 TYR T 426 REMARK 465 ASP T 427 REMARK 465 ILE T 428 REMARK 465 LYS T 429 REMARK 465 ASP T 430 REMARK 465 VAL T 431 REMARK 465 GLY T 432 REMARK 465 VAL T 433 REMARK 465 ASP T 434 REMARK 465 ASN T 435 REMARK 465 ALA T 436 REMARK 465 GLY T 437 REMARK 465 ALA T 438 REMARK 465 LYS T 439 REMARK 465 ALA T 440 REMARK 465 GLY T 441 REMARK 465 LEU T 442 REMARK 465 THR T 443 REMARK 465 PHE T 444 REMARK 465 LEU T 445 REMARK 465 VAL T 446 REMARK 465 ASP T 447 REMARK 465 LEU T 448 REMARK 465 ILE T 449 REMARK 465 LYS T 450 REMARK 465 ASN T 451 REMARK 465 LYS T 452 REMARK 465 HIS T 453 REMARK 465 MET T 454 REMARK 465 ASN T 455 REMARK 465 ALA T 456 REMARK 465 ASP T 457 REMARK 465 THR T 458 REMARK 465 ASP T 459 REMARK 465 TYR T 460 REMARK 465 SER T 461 REMARK 465 ILE T 462 REMARK 465 ALA T 463 REMARK 465 GLU T 464 REMARK 465 ALA T 465 REMARK 465 ALA T 466 REMARK 465 PHE T 467 REMARK 465 ASN T 468 REMARK 465 LYS T 469 REMARK 465 GLY T 470 REMARK 465 GLU T 471 REMARK 465 THR T 472 REMARK 465 ALA T 473 REMARK 465 MET T 474 REMARK 465 THR T 475 REMARK 465 ILE T 476 REMARK 465 ASN T 477 REMARK 465 GLY T 478 REMARK 465 PRO T 479 REMARK 465 TRP T 480 REMARK 465 ALA T 481 REMARK 465 TRP T 482 REMARK 465 SER T 483 REMARK 465 ASN T 484 REMARK 465 ILE T 485 REMARK 465 ASP T 486 REMARK 465 THR T 487 REMARK 465 SER T 488 REMARK 465 LYS T 489 REMARK 465 VAL T 490 REMARK 465 ASN T 491 REMARK 465 TYR T 492 REMARK 465 GLY T 493 REMARK 465 VAL T 494 REMARK 465 THR T 495 REMARK 465 VAL T 496 REMARK 465 LEU T 497 REMARK 465 PRO T 498 REMARK 465 THR T 499 REMARK 465 PHE T 500 REMARK 465 LYS T 501 REMARK 465 GLY T 502 REMARK 465 GLN T 503 REMARK 465 PRO T 504 REMARK 465 SER T 505 REMARK 465 LYS T 506 REMARK 465 PRO T 507 REMARK 465 PHE T 508 REMARK 465 VAL T 509 REMARK 465 GLY T 510 REMARK 465 VAL T 511 REMARK 465 LEU T 512 REMARK 465 SER T 513 REMARK 465 ALA T 514 REMARK 465 GLY T 515 REMARK 465 ILE T 516 REMARK 465 ASN T 517 REMARK 465 ALA T 518 REMARK 465 ALA T 519 REMARK 465 SER T 520 REMARK 465 PRO T 521 REMARK 465 ASN T 522 REMARK 465 LYS T 523 REMARK 465 GLU T 524 REMARK 465 LEU T 525 REMARK 465 ALA T 526 REMARK 465 LYS T 527 REMARK 465 GLU T 528 REMARK 465 PHE T 529 REMARK 465 LEU T 530 REMARK 465 GLU T 531 REMARK 465 ASN T 532 REMARK 465 TYR T 533 REMARK 465 LEU T 534 REMARK 465 LEU T 535 REMARK 465 THR T 536 REMARK 465 ASP T 537 REMARK 465 GLU T 538 REMARK 465 GLY T 539 REMARK 465 LEU T 540 REMARK 465 GLU T 541 REMARK 465 ALA T 542 REMARK 465 VAL T 543 REMARK 465 ASN T 544 REMARK 465 LYS T 545 REMARK 465 ASP T 546 REMARK 465 LYS T 547 REMARK 465 PRO T 548 REMARK 465 LEU T 549 REMARK 465 GLY T 550 REMARK 465 ALA T 551 REMARK 465 VAL T 552 REMARK 465 ALA T 553 REMARK 465 LEU T 554 REMARK 465 LYS T 555 REMARK 465 SER T 556 REMARK 465 TYR T 557 REMARK 465 GLU T 558 REMARK 465 GLU T 559 REMARK 465 GLU T 560 REMARK 465 LEU T 561 REMARK 465 ALA T 562 REMARK 465 LYS T 563 REMARK 465 ASP T 564 REMARK 465 PRO T 565 REMARK 465 ARG T 566 REMARK 465 ILE T 567 REMARK 465 ALA T 568 REMARK 465 ALA T 569 REMARK 465 THR T 570 REMARK 465 MET T 571 REMARK 465 GLU T 572 REMARK 465 ASN T 573 REMARK 465 ALA T 574 REMARK 465 GLN T 575 REMARK 465 LYS T 576 REMARK 465 GLY T 577 REMARK 465 GLU T 578 REMARK 465 ILE T 579 REMARK 465 MET T 580 REMARK 465 PRO T 581 REMARK 465 ASN T 582 REMARK 465 ILE T 583 REMARK 465 PRO T 584 REMARK 465 GLN T 585 REMARK 465 MET T 586 REMARK 465 SER T 587 REMARK 465 ALA T 588 REMARK 465 PHE T 589 REMARK 465 TRP T 590 REMARK 465 TYR T 591 REMARK 465 ALA T 592 REMARK 465 VAL T 593 REMARK 465 ARG T 594 REMARK 465 THR T 595 REMARK 465 ALA T 596 REMARK 465 VAL T 597 REMARK 465 ILE T 598 REMARK 465 ASN T 599 REMARK 465 ALA T 600 REMARK 465 ALA T 601 REMARK 465 SER T 602 REMARK 465 GLY T 603 REMARK 465 ARG T 604 REMARK 465 GLN T 605 REMARK 465 THR T 606 REMARK 465 VAL T 607 REMARK 465 ASP T 608 REMARK 465 GLU T 609 REMARK 465 ALA T 610 REMARK 465 LEU T 611 REMARK 465 LYS T 612 REMARK 465 ASP T 613 REMARK 465 ALA T 614 REMARK 465 GLN T 615 REMARK 465 THR T 616 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 ASN X 105 CG OD1 ND2 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 CYS K 72 CA - CB - SG ANGL. DEV. = 7.8 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 LEU V 5 93.04 48.23 REMARK 500 CGU V 19 -76.94 -127.04 REMARK 500 GLN V 49 40.45 -86.41 REMARK 500 CGU X 7 -60.54 71.43 REMARK 500 MET X 18 -52.90 -142.65 REMARK 500 CGU X 20 -153.36 -105.27 REMARK 500 CGU X 32 -85.92 64.02 REMARK 500 ASP X 48 116.09 -165.12 REMARK 500 GLN X 56 -169.36 -79.58 REMARK 500 TYR X 68 70.13 59.67 REMARK 500 ARG X 86 45.74 -84.27 REMARK 500 LYS X 87 -11.11 69.77 REMARK 500 ASN X 93 53.91 38.01 REMARK 500 PHE X 99 -179.08 -174.01 REMARK 500 ILE S 183 -64.12 -92.61 REMARK 500 ASN S 184 -70.10 -121.61 REMARK 500 THR S 185 -51.17 -131.61 REMARK 500 GLU S 215 148.59 -173.20 REMARK 500 LEU S 273D 47.53 -83.70 REMARK 500 ARG S 277 -9.74 73.29 REMARK 500 TRP S 284 34.02 -98.16 REMARK 500 LYS S 316 40.02 -108.54 REMARK 500 CYS S 340 -66.08 -109.61 REMARK 500 LYS S 341 -18.17 -145.06 REMARK 500 ARG S 392 30.77 -98.50 REMARK 500 TYR T 51 13.78 58.87 REMARK 500 ARG T 136 -156.00 -145.72 REMARK 500 ASN T 137 85.39 -68.43 REMARK 500 SER T 163 -123.78 42.28 REMARK 500 LEU K 19 -9.68 74.21 REMARK 500 GLN K 63 31.28 -96.87 REMARK 500 CYS K 76 -61.80 -97.88 REMARK 500 TYR H 101 -61.11 -94.08 REMARK 500 TYR H 102 45.69 -87.90 REMARK 500 ASN H 104 47.14 37.02 REMARK 500 SER H 197 -159.78 -158.98 REMARK 500 PRO H 219 -177.01 -68.22 REMARK 500 SER L 58 -15.48 -141.02 REMARK 500 PRO L 147 -162.86 -76.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA V 206 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN V 2 OD1 REMARK 620 2 CGU V 20 OE11 146.0 REMARK 620 3 CGU V 20 OE21 130.3 66.5 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA V 205 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU V 6 OE22 REMARK 620 2 CGU V 16 OE11 84.1 REMARK 620 3 CGU V 16 OE12 129.8 50.4 REMARK 620 4 CGU V 20 OE21 76.2 69.9 101.5 REMARK 620 5 CGU V 20 OE22 126.3 93.6 82.1 53.4 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA V 202 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU V 7 OE11 REMARK 620 2 CGU V 7 OE12 42.9 REMARK 620 3 CGU V 7 OE22 94.6 99.4 REMARK 620 4 CGU V 26 OE21 110.8 95.7 153.9 REMARK 620 5 CGU V 26 OE22 70.6 77.2 161.9 43.4 REMARK 620 6 CGU V 29 OE11 66.1 108.2 94.4 101.1 70.4 REMARK 620 7 CGU V 29 OE12 113.9 156.1 73.8 99.9 102.0 51.0 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA V 203 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU V 7 OE11 REMARK 620 2 CGU V 16 OE21 95.1 REMARK 620 3 CGU V 16 OE22 122.7 42.7 REMARK 620 4 CGU V 26 OE22 75.6 84.0 120.7 REMARK 620 5 CGU V 29 OE11 74.0 156.9 158.9 73.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG V 204 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU V 7 OE11 REMARK 620 2 CGU V 7 OE12 46.9 REMARK 620 3 CGU V 16 OE21 82.6 112.6 REMARK 620 4 CGU V 26 OE12 166.6 146.4 89.9 REMARK 620 5 CGU V 26 OE22 64.7 102.1 86.6 104.0 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG V 207 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU V 14 OE12 REMARK 620 2 CGU V 14 OE21 94.3 REMARK 620 3 CGU V 19 OE11 116.7 78.0 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG V 201 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU V 25 OE21 REMARK 620 2 CGU V 29 OE12 75.4 REMARK 620 3 CGU V 29 OE21 94.2 82.7 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA V 210 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP V 46 OD2 REMARK 620 2 GLY V 47 O 93.9 REMARK 620 3 GLN V 49 OE1 97.2 89.7 REMARK 620 4 ASP V 63 OD1 153.4 111.5 76.1 REMARK 620 5 ASP V 63 OD2 140.2 81.4 122.1 55.6 REMARK 620 6 GLN V 64 O 77.0 165.3 80.1 76.5 113.0 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA X 204 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA X 1 O REMARK 620 2 ASN X 2 OD1 125.9 REMARK 620 3 CGU X 6 OE12 84.5 89.0 REMARK 620 4 CGU X 16 OE12 66.9 161.4 78.4 REMARK 620 5 CGU X 26 OE12 143.9 86.1 79.4 78.2 REMARK 620 6 CGU X 26 OE21 112.8 71.5 159.1 118.4 91.5 REMARK 620 7 CGU X 26 OE22 96.7 119.3 141.6 67.1 77.5 51.5 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA X 205 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA X 1 O REMARK 620 2 CGU X 6 OE22 83.1 REMARK 620 3 CGU X 20 OE21 164.1 99.5 REMARK 620 4 CGU X 20 OE22 126.9 144.5 57.5 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA X 202 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN X 2 OD1 REMARK 620 2 CGU X 7 OE21 74.8 REMARK 620 3 CGU X 7 OE22 123.4 56.0 REMARK 620 4 CGU X 25 OE21 148.2 126.3 70.3 REMARK 620 5 CGU X 25 OE22 119.4 162.7 114.8 46.7 REMARK 620 6 CGU X 26 OE11 111.7 74.7 82.6 97.9 90.1 REMARK 620 7 CGU X 26 OE12 68.0 64.2 107.5 139.8 110.2 43.7 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA X 203 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU X 6 OE11 REMARK 620 2 CGU X 7 OE21 95.1 REMARK 620 3 CGU X 26 OE11 121.0 71.9 REMARK 620 4 CGU X 26 OE12 65.0 75.2 56.0 REMARK 620 5 CGU X 29 OE21 163.0 99.1 72.7 127.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA X 201 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU X 7 OE11 REMARK 620 2 CGU X 29 OE12 139.9 REMARK 620 3 CGU X 29 OE22 75.9 83.1 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG X 207 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU X 14 OE21 REMARK 620 2 CGU X 19 OE11 123.5 REMARK 620 3 CGU X 19 OE12 75.7 48.3 REMARK 620 4 CGU X 19 OE21 132.2 68.6 94.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA X 206 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CGU X 20 OE11 REMARK 620 2 CGU X 20 OE21 83.4 REMARK 620 3 CGU X 20 OE22 91.0 45.6 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA S 501 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU S 210 OE1 REMARK 620 2 GLU S 210 OE2 56.7 REMARK 620 3 ASP S 212 O 65.6 75.7 REMARK 620 4 GLU S 215 O 137.6 129.4 75.5 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-71090 RELATED DB: EMDB REMARK 900 NANODISC-EMBEDDED HUMAN TF/FVIIA/XK1 IN COMPLEX WITH 10H10 FAB REMARK 900 (NANODISC-SUBTRACTED) DBREF 9P0X V 1 142 UNP P08709 FA7_HUMAN 61 202 DBREF 9P0X X 1 131 UNP P00742 FA10_HUMAN 41 171 DBREF 9P0X S 153 406 UNP P08709 FA7_HUMAN 213 466 DBREF 9P0X T 6 244 UNP P13726 TF_HUMAN 38 276 DBREF 9P0X T 251 616 UNP P0AEY0 MALE_ECO57 27 392 DBREF 9P0X K 12 79 UNP P10646 TFPI1_HUMAN 40 107 DBREF 9P0X H 1 221 PDB 9P0X 9P0X 1 221 DBREF 9P0X L 1 220 PDB 9P0X 9P0X 1 220 SEQADV 9P0X GLY T 245 UNP P13726 LINKER SEQADV 9P0X SER T 246 UNP P13726 LINKER SEQADV 9P0X GLY T 247 UNP P13726 LINKER SEQADV 9P0X SER T 248 UNP P13726 LINKER SEQADV 9P0X GLY T 249 UNP P13726 LINKER SEQADV 9P0X MET T 250 UNP P13726 LINKER SEQRES 1 V 142 ALA ASN ALA PHE LEU CGU CGU LEU ARG PRO GLY SER LEU SEQRES 2 V 142 CGU ARG CGU CYS LYS CGU CGU GLN CYS SER PHE CGU CGU SEQRES 3 V 142 ALA ARG CGU ILE PHE LYS ASP ALA CGU ARG THR LYS LEU SEQRES 4 V 142 PHE TRP ILE SER TYR SER ASP GLY ASP GLN CYS ALA SER SEQRES 5 V 142 SER PRO CYS GLN ASN GLY GLY SER CYS LYS ASP GLN LEU SEQRES 6 V 142 GLN SER TYR ILE CYS PHE CYS LEU PRO ALA PHE GLU GLY SEQRES 7 V 142 ARG ASN CYS GLU THR HIS LYS ASP ASP GLN LEU ILE CYS SEQRES 8 V 142 VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS SER ASP SEQRES 9 V 142 HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS GLU GLY SEQRES 10 V 142 TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR PRO THR SEQRES 11 V 142 VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU GLU SEQRES 1 X 131 ALA ASN SER PHE LEU CGU CGU MET LYS LYS GLY HIS LEU SEQRES 2 X 131 CGU ARG CGU CYS MET CGU CGU THR CYS SER TYR CGU CGU SEQRES 3 X 131 ALA ARG CGU VAL PHE CGU ASP SER ASP LYS THR ASN CGU SEQRES 4 X 131 PHE TRP ASN LYS TYR LYS ASP GLY ASP GLN CYS GLU THR SEQRES 5 X 131 SER PRO CYS GLN ASN GLN GLY LYS CYS LYS ASP GLY LEU SEQRES 6 X 131 GLY GLU TYR THR CYS THR CYS LEU GLU GLY PHE GLU GLY SEQRES 7 X 131 LYS ASN CYS GLU LEU PHE THR ARG LYS LEU CYS SER LEU SEQRES 8 X 131 ASP ASN GLY ASP CYS ASP GLN PHE CYS HIS GLU GLU GLN SEQRES 9 X 131 ASN SER VAL VAL CYS SER CYS ALA ARG GLY TYR THR LEU SEQRES 10 X 131 ALA ASP ASN GLY LYS ALA CYS ILE PRO THR GLY PRO TYR SEQRES 11 X 131 PRO SEQRES 1 S 254 ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO SEQRES 2 S 254 TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS SEQRES 3 S 254 GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA SEQRES 4 S 254 ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU SEQRES 5 S 254 ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP SEQRES 6 S 254 GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE SEQRES 7 S 254 PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE SEQRES 8 S 254 ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP SEQRES 9 S 254 HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER SEQRES 10 S 254 GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER SEQRES 11 S 254 GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU SEQRES 12 S 254 GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN SEQRES 13 S 254 ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO SEQRES 14 S 254 ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP SEQRES 15 S 254 GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO SEQRES 16 S 254 HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY SEQRES 17 S 254 ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS SEQRES 18 S 254 PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP SEQRES 19 S 254 LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL SEQRES 20 S 254 LEU LEU ARG ALA PRO PHE PRO SEQRES 1 T 611 THR VAL ALA ALA TYR ASN LEU THR TRP LYS SER THR ASN SEQRES 2 T 611 PHE LYS THR ILE LEU GLU TRP GLU PRO LYS PRO VAL ASN SEQRES 3 T 611 GLN VAL TYR THR VAL GLN ILE SER THR LYS SER GLY ASP SEQRES 4 T 611 TRP LYS SER LYS CYS PHE TYR THR THR ASP THR GLU CYS SEQRES 5 T 611 ASP LEU THR ASP GLU ILE VAL LYS ASP VAL LYS GLN THR SEQRES 6 T 611 TYR LEU ALA ARG VAL PHE SER TYR PRO ALA GLY ASN VAL SEQRES 7 T 611 GLU SER THR GLY SER ALA GLY GLU PRO LEU TYR GLU ASN SEQRES 8 T 611 SER PRO GLU PHE THR PRO TYR LEU GLU THR ASN LEU GLY SEQRES 9 T 611 GLN PRO THR ILE GLN SER PHE GLU GLN VAL GLY THR LYS SEQRES 10 T 611 VAL ASN VAL THR VAL GLU ASP GLU ARG THR LEU VAL ARG SEQRES 11 T 611 ARG ASN ASN THR PHE LEU SER LEU ARG ASP VAL PHE GLY SEQRES 12 T 611 LYS ASP LEU ILE TYR THR LEU TYR TYR TRP LYS SER SER SEQRES 13 T 611 SER SER GLY LYS LYS THR ALA LYS THR ASN THR ASN GLU SEQRES 14 T 611 PHE LEU ILE ASP VAL ASP LYS GLY GLU ASN TYR CYS PHE SEQRES 15 T 611 SER VAL GLN ALA VAL ILE PRO SER ARG THR VAL ASN ARG SEQRES 16 T 611 LYS SER THR ASP SER PRO VAL GLU CYS MET GLY GLN GLU SEQRES 17 T 611 LYS GLY GLU PHE ARG GLU ILE PHE TYR ILE ILE GLY ALA SEQRES 18 T 611 VAL VAL PHE VAL VAL ILE ILE LEU VAL ILE ILE LEU ALA SEQRES 19 T 611 ILE SER LEU HIS LYS GLY SER GLY SER GLY MET LYS ILE SEQRES 20 T 611 GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN GLY ASP LYS SEQRES 21 T 611 GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS LYS PHE GLU SEQRES 22 T 611 LYS ASP THR GLY ILE LYS VAL THR VAL GLU HIS PRO ASP SEQRES 23 T 611 LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA ALA THR GLY SEQRES 24 T 611 ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS ASP ARG PHE SEQRES 25 T 611 GLY GLY TYR ALA GLN SER GLY LEU LEU ALA GLU ILE THR SEQRES 26 T 611 PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR PRO PHE THR SEQRES 27 T 611 TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU ILE ALA TYR SEQRES 28 T 611 PRO ILE ALA VAL GLU ALA LEU SER LEU ILE TYR ASN LYS SEQRES 29 T 611 ASP LEU LEU PRO ASN PRO PRO LYS THR TRP GLU GLU ILE SEQRES 30 T 611 PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS GLY LYS SER SEQRES 31 T 611 ALA LEU MET PHE ASN LEU GLN GLU PRO TYR PHE THR TRP SEQRES 32 T 611 PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA PHE LYS TYR SEQRES 33 T 611 GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL GLY VAL ASP SEQRES 34 T 611 ASN ALA GLY ALA LYS ALA GLY LEU THR PHE LEU VAL ASP SEQRES 35 T 611 LEU ILE LYS ASN LYS HIS MET ASN ALA ASP THR ASP TYR SEQRES 36 T 611 SER ILE ALA GLU ALA ALA PHE ASN LYS GLY GLU THR ALA SEQRES 37 T 611 MET THR ILE ASN GLY PRO TRP ALA TRP SER ASN ILE ASP SEQRES 38 T 611 THR SER LYS VAL ASN TYR GLY VAL THR VAL LEU PRO THR SEQRES 39 T 611 PHE LYS GLY GLN PRO SER LYS PRO PHE VAL GLY VAL LEU SEQRES 40 T 611 SER ALA GLY ILE ASN ALA ALA SER PRO ASN LYS GLU LEU SEQRES 41 T 611 ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU THR ASP GLU SEQRES 42 T 611 GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO LEU GLY ALA SEQRES 43 T 611 VAL ALA LEU LYS SER TYR GLU GLU GLU LEU ALA LYS ASP SEQRES 44 T 611 PRO ARG ILE ALA ALA THR MET GLU ASN ALA GLN LYS GLY SEQRES 45 T 611 GLU ILE MET PRO ASN ILE PRO GLN MET SER ALA PHE TRP SEQRES 46 T 611 TYR ALA VAL ARG THR ALA VAL ILE ASN ALA ALA SER GLY SEQRES 47 T 611 ARG GLN THR VAL ASP GLU ALA LEU LYS ASP ALA GLN THR SEQRES 1 K 68 THR ASP THR GLU LEU PRO PRO LEU LYS LEU MET HIS SER SEQRES 2 K 68 PHE CYS ALA PHE LYS ALA ASP ASP GLY PRO CYS LYS ALA SEQRES 3 K 68 ILE MET LYS ARG PHE PHE PHE ASN ILE PHE THR ARG GLN SEQRES 4 K 68 CYS GLU GLU PHE ILE TYR GLY GLY CYS GLU GLY ASN GLN SEQRES 5 K 68 ASN ARG PHE GLU SER LEU GLU GLU CYS LYS LYS MET CYS SEQRES 6 K 68 THR ARG ASP SEQRES 1 H 221 GLN VAL HIS LEU GLN GLN SER GLY ALA GLU LEU MET LYS SEQRES 2 H 221 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 221 TYR THR PHE ILE THR TYR TRP ILE GLU TRP VAL LYS GLN SEQRES 4 H 221 ARG PRO GLY HIS GLY LEU GLU TRP ILE GLY ASP ILE LEU SEQRES 5 H 221 PRO GLY SER GLY SER THR ASN TYR ASN GLU ASN PHE LYS SEQRES 6 H 221 GLY LYS ALA THR PHE THR ALA ASP SER SER SER ASN THR SEQRES 7 H 221 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 221 ALA VAL TYR TYR CYS ALA ARG SER GLY TYR TYR GLY ASN SEQRES 9 H 221 SER GLY PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 221 VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO SEQRES 11 H 221 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL SEQRES 12 H 221 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO SEQRES 13 H 221 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY SEQRES 14 H 221 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR SEQRES 15 H 221 THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP SEQRES 16 H 221 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SEQRES 17 H 221 SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP SEQRES 1 L 220 ASP ILE VAL MET THR GLN SER PRO SER SER LEU THR VAL SEQRES 2 L 220 THR ALA GLY GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 L 220 GLN SER LEU LEU SER SER GLY ASN GLN LYS ASN TYR LEU SEQRES 4 L 220 THR TRP TYR GLN GLN ILE PRO GLY GLN PRO PRO LYS LEU SEQRES 5 L 220 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 220 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 220 LEU THR ILE ASN SER VAL GLN ALA GLU ASP LEU ALA VAL SEQRES 8 L 220 TYR TYR CYS GLN ASN ASP TYR THR TYR PRO LEU THR PHE SEQRES 9 L 220 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 L 220 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 L 220 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 L 220 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 L 220 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER ALA SEQRES 14 L 220 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 L 220 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 L 220 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 L 220 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS MODRES 9P0X CGU V 6 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 7 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 14 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 16 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 19 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 20 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 25 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 26 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 29 GLU MODIFIED RESIDUE MODRES 9P0X CGU V 35 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 6 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 7 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 14 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 16 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 19 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 20 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 25 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 26 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 29 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 32 GLU MODIFIED RESIDUE MODRES 9P0X CGU X 39 GLU MODIFIED RESIDUE HET CGU V 6 12 HET CGU V 7 12 HET CGU V 14 12 HET CGU V 16 12 HET CGU V 19 12 HET CGU V 20 12 HET CGU V 25 12 HET CGU V 26 12 HET CGU V 29 12 HET CGU V 35 12 HET CGU X 6 12 HET CGU X 7 12 HET CGU X 14 12 HET CGU X 16 12 HET CGU X 19 12 HET CGU X 20 12 HET CGU X 25 12 HET CGU X 26 12 HET CGU X 29 12 HET CGU X 32 12 HET CGU X 39 12 HET MG V 201 1 HET CA V 202 1 HET CA V 203 1 HET MG V 204 1 HET CA V 205 1 HET CA V 206 1 HET MG V 207 1 HET BGC V 208 11 HET FUC V 209 10 HET CA V 210 1 HET CA X 201 1 HET CA X 202 1 HET CA X 203 1 HET CA X 204 1 HET CA X 205 1 HET CA X 206 1 HET MG X 207 1 HET CA S 501 1 HETNAM CGU GAMMA-CARBOXY-GLUTAMIC ACID HETNAM MG MAGNESIUM ION HETNAM CA CALCIUM ION HETNAM BGC BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 1 CGU 21(C6 H9 N O6) FORMUL 8 MG 4(MG 2+) FORMUL 9 CA 12(CA 2+) FORMUL 15 BGC C6 H12 O6 FORMUL 16 FUC C6 H12 O5 HELIX 1 AA1 SER V 12 LYS V 18 1 7 HELIX 2 AA2 SER V 23 LYS V 32 1 10 HELIX 3 AA3 ASP V 33 SER V 45 1 13 HELIX 4 AA4 ASP V 86 GLN V 88 5 3 HELIX 5 AA5 LEU X 13 MET X 18 1 6 HELIX 6 AA6 SER X 23 CGU X 32 1 10 HELIX 7 AA7 ASP X 33 LYS X 45 1 13 HELIX 8 AA8 LEU X 91 CYS X 96 1 6 HELIX 9 AA9 ALA S 191 PHE S 195 5 5 HELIX 10 AB1 ASN S 200D ARG S 202 5 3 HELIX 11 AB2 GLU S 265 THR S 272C 1 8 HELIX 12 AB3 MET S 306 SER S 314 1 9 HELIX 13 AB4 ARG S 379 GLN S 382 5 4 HELIX 14 AB5 TYR S 383 ARG S 392 1 10 HELIX 15 AB6 LEU T 59 VAL T 64 1 6 HELIX 16 AB7 THR T 101 THR T 106 1 6 HELIX 17 AB8 LEU T 143 GLY T 148 1 6 HELIX 18 AB9 LYS T 149 LEU T 151 5 3 HELIX 19 AC1 SER K 24 PHE K 28 5 5 HELIX 20 AC2 SER K 68 THR K 77 1 10 HELIX 21 AC3 THR H 28 TYR H 32 5 5 HELIX 22 AC4 GLU H 62 LYS H 65 5 4 HELIX 23 AC5 THR H 87 SER H 91 5 5 HELIX 24 AC6 GLN L 85 LEU L 89 5 5 HELIX 25 AC7 SER L 127 GLY L 134 1 8 HELIX 26 AC8 THR L 188 GLU L 193 1 6 SHEET 1 AA1 2 SER V 60 GLN V 64 0 SHEET 2 AA1 2 SER V 67 PHE V 71 -1 O SER V 67 N GLN V 64 SHEET 1 AA2 2 PHE V 76 GLU V 77 0 SHEET 2 AA2 2 THR V 83 HIS V 84 -1 O THR V 83 N GLU V 77 SHEET 1 AA3 2 TYR V 101 SER V 103 0 SHEET 2 AA3 2 SER V 111 ARG V 113 -1 N SER V 111 O SER V 103 SHEET 1 AA4 2 TYR V 118 LEU V 120 0 SHEET 2 AA4 2 CYS V 127 PRO V 129 -1 O THR V 128 N SER V 119 SHEET 1 AA5 2 PHE X 99 HIS X 101 0 SHEET 2 AA5 2 VAL X 108 SER X 110 -1 O VAL X 108 N HIS X 101 SHEET 1 AA6 7 LYS S 157 VAL S 158 0 SHEET 2 AA6 7 MET S 298 VAL S 302 -1 O VAL S 299 N LYS S 157 SHEET 3 AA6 7 SER S 279 GLY S 283 -1 N VAL S 281 O LEU S 300 SHEET 4 AA6 7 PRO S 347 HIS S 351 -1 O ALA S 349 N LEU S 280 SHEET 5 AA6 7 TRP S 356 VAL S 362 -1 O GLY S 360 N HIS S 348 SHEET 6 AA6 7 GLY S 375 THR S 378 -1 O THR S 378 N ILE S 361 SHEET 7 AA6 7 CYS S 329 ALA S 330 -1 N ALA S 330 O GLY S 375 SHEET 1 AA7 6 ALA S 175 CYS S 178 0 SHEET 2 AA7 6 VAL S 168 VAL S 172 -1 N LEU S 170 O CYS S 178 SHEET 3 AA7 6 LEU S 204 LEU S 208 -1 O ILE S 205 N LEU S 171 SHEET 4 AA7 6 GLN S 221 PRO S 231 -1 O GLN S 221 N LEU S 208 SHEET 5 AA7 6 ALA S 244 LEU S 248 -1 O ARG S 247 N GLN S 227 SHEET 6 AA7 6 TRP S 187 SER S 190 -1 N VAL S 188 O LEU S 246 SHEET 1 AA8 5 ALA S 175 CYS S 178 0 SHEET 2 AA8 5 VAL S 168 VAL S 172 -1 N LEU S 170 O CYS S 178 SHEET 3 AA8 5 LEU S 204 LEU S 208 -1 O ILE S 205 N LEU S 171 SHEET 4 AA8 5 GLN S 221 PRO S 231 -1 O GLN S 221 N LEU S 208 SHEET 5 AA8 5 LEU S 400 ALA S 403 1 O LEU S 401 N VAL S 228 SHEET 1 AA9 3 THR T 13 THR T 17 0 SHEET 2 AA9 3 LYS T 20 GLU T 24 -1 O ILE T 22 N LYS T 15 SHEET 3 AA9 3 GLU T 56 ASP T 58 -1 O CYS T 57 N LEU T 23 SHEET 1 AB1 4 LYS T 46 THR T 52 0 SHEET 2 AB1 4 GLN T 32 SER T 39 -1 N VAL T 36 O LYS T 48 SHEET 3 AB1 4 LEU T 72 PRO T 79 -1 O LEU T 72 N SER T 39 SHEET 4 AB1 4 GLU T 95 ASN T 96 -1 O GLU T 95 N VAL T 75 SHEET 1 AB2 3 ILE T 113 VAL T 119 0 SHEET 2 AB2 3 LYS T 122 VAL T 127 -1 O LYS T 122 N VAL T 119 SHEET 3 AB2 3 ILE T 177 ASP T 178 -1 O ILE T 177 N VAL T 123 SHEET 1 AB3 2 ARG T 131 ARG T 136 0 SHEET 2 AB3 2 THR T 139 SER T 142 -1 O LEU T 141 N VAL T 134 SHEET 1 AB4 2 TYR T 153 TYR T 157 0 SHEET 2 AB4 2 LYS T 166 THR T 170 -1 O LYS T 166 N TYR T 157 SHEET 1 AB5 2 CYS T 186 PHE T 187 0 SHEET 2 AB5 2 GLU T 208 CYS T 209 -1 O GLU T 208 N PHE T 187 SHEET 1 AB6 2 MET K 39 ASN K 45 0 SHEET 2 AB6 2 GLN K 50 TYR K 56 -1 O GLU K 52 N PHE K 43 SHEET 1 AB7 4 HIS H 3 GLN H 6 0 SHEET 2 AB7 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AB7 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AB7 4 ALA H 68 ASP H 73 -1 N THR H 69 O GLN H 82 SHEET 1 AB8 5 GLU H 10 MET H 12 0 SHEET 2 AB8 5 THR H 114 VAL H 118 1 O THR H 117 N GLU H 10 SHEET 3 AB8 5 ALA H 92 SER H 99 -1 N ALA H 92 O VAL H 116 SHEET 4 AB8 5 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AB8 5 GLU H 46 TRP H 47 -1 O GLU H 46 N LYS H 38 SHEET 1 AB9 4 GLU H 10 MET H 12 0 SHEET 2 AB9 4 THR H 114 VAL H 118 1 O THR H 117 N GLU H 10 SHEET 3 AB9 4 ALA H 92 SER H 99 -1 N ALA H 92 O VAL H 116 SHEET 4 AB9 4 PHE H 107 TRP H 110 -1 O TYR H 109 N ARG H 98 SHEET 1 AC1 2 GLY H 49 ILE H 51 0 SHEET 2 AC1 2 THR H 58 TYR H 60 -1 O ASN H 59 N ASP H 50 SHEET 1 AC2 4 TYR H 129 PRO H 130 0 SHEET 2 AC2 4 CYS H 147 TYR H 152 -1 O LEU H 148 N TYR H 129 SHEET 3 AC2 4 TYR H 182 LEU H 184 -1 O LEU H 184 N VAL H 149 SHEET 4 AC2 4 VAL H 176 LEU H 177 -1 N VAL H 176 O THR H 183 SHEET 1 AC3 3 MET H 142 LEU H 145 0 SHEET 2 AC3 3 SER H 186 PRO H 191 -1 O VAL H 190 N VAL H 143 SHEET 3 AC3 3 VAL H 170 THR H 172 -1 N HIS H 171 O SER H 187 SHEET 1 AC4 3 THR H 158 TRP H 161 0 SHEET 2 AC4 3 VAL H 200 HIS H 206 -1 O ALA H 205 N THR H 158 SHEET 3 AC4 3 THR H 211 VAL H 213 -1 O VAL H 213 N VAL H 204 SHEET 1 AC5 3 THR H 158 TRP H 161 0 SHEET 2 AC5 3 VAL H 200 HIS H 206 -1 O ALA H 205 N THR H 158 SHEET 3 AC5 3 LYS H 216 ILE H 217 -1 O ILE H 217 N VAL H 200 SHEET 1 AC6 4 MET L 4 GLN L 6 0 SHEET 2 AC6 4 VAL L 19 SER L 25 -1 O LYS L 24 N THR L 5 SHEET 3 AC6 4 ASP L 76 ILE L 81 -1 O ILE L 81 N VAL L 19 SHEET 4 AC6 4 THR L 69 SER L 71 -1 N THR L 69 O THR L 80 SHEET 1 AC7 2 SER L 10 VAL L 13 0 SHEET 2 AC7 2 LYS L 109 LEU L 112 1 O GLU L 111 N VAL L 13 SHEET 1 AC8 2 LEU L 30 SER L 31 0 SHEET 2 AC8 2 LYS L 36 ASN L 37 -1 O LYS L 36 N SER L 31 SHEET 1 AC9 4 THR L 59 ARG L 60 0 SHEET 2 AC9 4 LYS L 51 TYR L 55 -1 N TYR L 55 O THR L 59 SHEET 3 AC9 4 LEU L 39 GLN L 44 -1 N GLN L 43 O LYS L 51 SHEET 4 AC9 4 VAL L 91 ASN L 96 -1 O VAL L 91 N GLN L 44 SHEET 1 AD1 4 SER L 122 PHE L 124 0 SHEET 2 AD1 4 VAL L 138 PHE L 141 -1 O PHE L 141 N SER L 122 SHEET 3 AD1 4 SER L 182 LEU L 185 -1 O LEU L 185 N VAL L 138 SHEET 4 AD1 4 VAL L 165 LEU L 166 -1 N LEU L 166 O THR L 184 SHEET 1 AD2 4 SER L 159 GLU L 160 0 SHEET 2 AD2 4 ILE L 150 ILE L 156 -1 N ILE L 156 O SER L 159 SHEET 3 AD2 4 SER L 197 HIS L 204 -1 O THR L 199 N LYS L 155 SHEET 4 AD2 4 ILE L 211 ASN L 216 -1 O PHE L 215 N TYR L 198 SSBOND 1 CYS V 17 CYS V 22 1555 1555 2.03 SSBOND 2 CYS V 50 CYS V 61 1555 1555 2.03 SSBOND 3 CYS V 55 CYS V 70 1555 1555 2.03 SSBOND 4 CYS V 72 CYS V 81 1555 1555 2.03 SSBOND 5 CYS V 91 CYS V 102 1555 1555 2.03 SSBOND 6 CYS V 98 CYS V 112 1555 1555 2.03 SSBOND 7 CYS V 114 CYS V 127 1555 1555 2.03 SSBOND 8 CYS V 135 CYS S 262 1555 1555 2.03 SSBOND 9 CYS X 17 CYS X 22 1555 1555 2.03 SSBOND 10 CYS X 50 CYS X 61 1555 1555 2.03 SSBOND 11 CYS X 55 CYS X 70 1555 1555 2.04 SSBOND 12 CYS X 72 CYS X 81 1555 1555 2.03 SSBOND 13 CYS X 89 CYS X 100 1555 1555 2.04 SSBOND 14 CYS X 96 CYS X 109 1555 1555 2.02 SSBOND 15 CYS X 111 CYS X 124 1555 1555 2.03 SSBOND 16 CYS S 159 CYS S 164 1555 1555 2.04 SSBOND 17 CYS S 178 CYS S 194 1555 1555 2.03 SSBOND 18 CYS S 310 CYS S 329 1555 1555 2.03 SSBOND 19 CYS S 340 CYS S 368 1555 1555 2.03 SSBOND 20 CYS T 49 CYS T 57 1555 1555 2.03 SSBOND 21 CYS T 186 CYS T 209 1555 1555 2.03 SSBOND 22 CYS K 26 CYS K 76 1555 1555 2.03 SSBOND 23 CYS K 35 CYS K 59 1555 1555 2.03 SSBOND 24 CYS K 51 CYS K 72 1555 1555 2.03 SSBOND 25 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 26 CYS H 147 CYS H 202 1555 1555 2.04 SSBOND 27 CYS L 23 CYS L 94 1555 1555 2.03 SSBOND 28 CYS L 140 CYS L 200 1555 1555 2.04 LINK C LEU V 5 N CGU V 6 1555 1555 1.33 LINK C CGU V 6 N CGU V 7 1555 1555 1.33 LINK C CGU V 7 N LEU V 8 1555 1555 1.33 LINK C LEU V 13 N CGU V 14 1555 1555 1.33 LINK C CGU V 14 N ARG V 15 1555 1555 1.33 LINK C ARG V 15 N CGU V 16 1555 1555 1.33 LINK C CGU V 16 N CYS V 17 1555 1555 1.33 LINK C LYS V 18 N CGU V 19 1555 1555 1.33 LINK C CGU V 19 N CGU V 20 1555 1555 1.33 LINK C CGU V 20 N GLN V 21 1555 1555 1.33 LINK C PHE V 24 N CGU V 25 1555 1555 1.33 LINK C CGU V 25 N CGU V 26 1555 1555 1.33 LINK C CGU V 26 N ALA V 27 1555 1555 1.33 LINK C ARG V 28 N CGU V 29 1555 1555 1.33 LINK C CGU V 29 N ILE V 30 1555 1555 1.33 LINK C ALA V 34 N CGU V 35 1555 1555 1.33 LINK C CGU V 35 N ARG V 36 1555 1555 1.33 LINK OG SER V 52 C1 BGC V 208 1555 1555 1.38 LINK OG SER V 60 C1 FUC V 209 1555 1555 1.37 LINK C LEU X 5 N CGU X 6 1555 1555 1.33 LINK C CGU X 6 N CGU X 7 1555 1555 1.33 LINK C CGU X 7 N MET X 8 1555 1555 1.33 LINK C LEU X 13 N CGU X 14 1555 1555 1.33 LINK C CGU X 14 N ARG X 15 1555 1555 1.33 LINK C ARG X 15 N CGU X 16 1555 1555 1.33 LINK C CGU X 16 N CYS X 17 1555 1555 1.33 LINK C MET X 18 N CGU X 19 1555 1555 1.33 LINK C CGU X 19 N CGU X 20 1555 1555 1.33 LINK C CGU X 20 N THR X 21 1555 1555 1.33 LINK C TYR X 24 N CGU X 25 1555 1555 1.33 LINK C CGU X 25 N CGU X 26 1555 1555 1.33 LINK C CGU X 26 N ALA X 27 1555 1555 1.33 LINK C ARG X 28 N CGU X 29 1555 1555 1.33 LINK C CGU X 29 N VAL X 30 1555 1555 1.33 LINK C PHE X 31 N CGU X 32 1555 1555 1.33 LINK C CGU X 32 N ASP X 33 1555 1555 1.33 LINK C ASN X 38 N CGU X 39 1555 1555 1.33 LINK C CGU X 39 N PHE X 40 1555 1555 1.33 LINK OD1 ASN V 2 CA CA V 206 1555 1555 2.91 LINK OE22 CGU V 6 CA CA V 205 1555 1555 2.33 LINK OE11 CGU V 7 CA CA V 202 1555 1555 2.63 LINK OE12 CGU V 7 CA CA V 202 1555 1555 3.17 LINK OE22 CGU V 7 CA CA V 202 1555 1555 2.45 LINK OE11 CGU V 7 CA CA V 203 1555 1555 2.34 LINK OE11 CGU V 7 MG MG V 204 1555 1555 2.97 LINK OE12 CGU V 7 MG MG V 204 1555 1555 2.24 LINK OE12 CGU V 14 MG MG V 207 1555 1555 1.97 LINK OE21 CGU V 14 MG MG V 207 1555 1555 2.82 LINK OE21 CGU V 16 CA CA V 203 1555 1555 2.71 LINK OE22 CGU V 16 CA CA V 203 1555 1555 3.15 LINK OE21 CGU V 16 MG MG V 204 1555 1555 2.67 LINK OE11 CGU V 16 CA CA V 205 1555 1555 2.36 LINK OE12 CGU V 16 CA CA V 205 1555 1555 2.70 LINK OE11 CGU V 19 MG MG V 207 1555 1555 2.60 LINK OE21 CGU V 20 CA CA V 205 1555 1555 2.54 LINK OE22 CGU V 20 CA CA V 205 1555 1555 2.28 LINK OE11 CGU V 20 CA CA V 206 1555 1555 2.27 LINK OE21 CGU V 20 CA CA V 206 1555 1555 3.05 LINK OE21 CGU V 25 MG MG V 201 1555 1555 2.57 LINK OE21 CGU V 26 CA CA V 202 1555 1555 3.17 LINK OE22 CGU V 26 CA CA V 202 1555 1555 2.27 LINK OE22 CGU V 26 CA CA V 203 1555 1555 2.31 LINK OE12 CGU V 26 MG MG V 204 1555 1555 2.65 LINK OE22 CGU V 26 MG MG V 204 1555 1555 2.22 LINK OE12 CGU V 29 MG MG V 201 1555 1555 1.96 LINK OE21 CGU V 29 MG MG V 201 1555 1555 2.71 LINK OE11 CGU V 29 CA CA V 202 1555 1555 2.61 LINK OE12 CGU V 29 CA CA V 202 1555 1555 2.45 LINK OE11 CGU V 29 CA CA V 203 1555 1555 2.41 LINK OD2 ASP V 46 CA CA V 210 1555 1555 2.37 LINK O GLY V 47 CA CA V 210 1555 1555 2.29 LINK OE1 GLN V 49 CA CA V 210 1555 1555 2.43 LINK OD1 ASP V 63 CA CA V 210 1555 1555 2.32 LINK OD2 ASP V 63 CA CA V 210 1555 1555 2.37 LINK O GLN V 64 CA CA V 210 1555 1555 2.31 LINK O ALA X 1 CA CA X 204 1555 1555 2.29 LINK O ALA X 1 CA CA X 205 1555 1555 2.19 LINK OD1 ASN X 2 CA CA X 202 1555 1555 2.32 LINK OD1 ASN X 2 CA CA X 204 1555 1555 2.32 LINK OE11 CGU X 6 CA CA X 203 1555 1555 3.09 LINK OE12 CGU X 6 CA CA X 204 1555 1555 2.23 LINK OE22 CGU X 6 CA CA X 205 1555 1555 2.22 LINK OE11 CGU X 7 CA CA X 201 1555 1555 2.75 LINK OE21 CGU X 7 CA CA X 202 1555 1555 2.35 LINK OE22 CGU X 7 CA CA X 202 1555 1555 2.27 LINK OE21 CGU X 7 CA CA X 203 1555 1555 2.57 LINK OE21 CGU X 14 MG MG X 207 1555 1555 2.65 LINK OE12 CGU X 16 CA CA X 204 1555 1555 2.80 LINK OE11 CGU X 19 MG MG X 207 1555 1555 2.92 LINK OE12 CGU X 19 MG MG X 207 1555 1555 1.96 LINK OE21 CGU X 19 MG MG X 207 1555 1555 2.50 LINK OE21 CGU X 20 CA CA X 205 1555 1555 2.28 LINK OE22 CGU X 20 CA CA X 205 1555 1555 2.26 LINK OE11 CGU X 20 CA CA X 206 1555 1555 2.52 LINK OE21 CGU X 20 CA CA X 206 1555 1555 2.31 LINK OE22 CGU X 20 CA CA X 206 1555 1555 3.04 LINK OE21 CGU X 25 CA CA X 202 1555 1555 2.43 LINK OE22 CGU X 25 CA CA X 202 1555 1555 2.94 LINK OE11 CGU X 26 CA CA X 202 1555 1555 2.37 LINK OE12 CGU X 26 CA CA X 202 1555 1555 3.15 LINK OE11 CGU X 26 CA CA X 203 1555 1555 2.30 LINK OE12 CGU X 26 CA CA X 203 1555 1555 2.34 LINK OE12 CGU X 26 CA CA X 204 1555 1555 2.28 LINK OE21 CGU X 26 CA CA X 204 1555 1555 2.57 LINK OE22 CGU X 26 CA CA X 204 1555 1555 2.46 LINK OE12 CGU X 29 CA CA X 201 1555 1555 2.96 LINK OE22 CGU X 29 CA CA X 201 1555 1555 2.33 LINK OE21 CGU X 29 CA CA X 203 1555 1555 2.41 LINK OE1 GLU S 210 CA CA S 501 1555 1555 2.31 LINK OE2 GLU S 210 CA CA S 501 1555 1555 2.31 LINK O ASP S 212 CA CA S 501 1555 1555 2.80 LINK O GLU S 215 CA CA S 501 1555 1555 2.30 CISPEP 1 PHE S 405 PRO S 406 0 -0.25 CISPEP 2 PHE H 153 PRO H 154 0 -4.21 CISPEP 3 GLU H 155 PRO H 156 0 -1.86 CISPEP 4 TRP H 195 PRO H 196 0 3.73 CISPEP 5 TYR L 100 PRO L 101 0 0.09 CISPEP 6 TYR L 146 PRO L 147 0 -1.84 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