HEADER ANTIVIRAL PROTEIN 13-JUL-23 8TGV TITLE CRYOEM STRUCTURE OF FAB HC84.26-HCV E2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN E2; COMPND 3 CHAIN: A, D, G; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HC84.26 HEAVY CHAIN; COMPND 7 CHAIN: E, B, I, K; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HC84.26 LIGHT CHAIN; COMPND 11 CHAIN: F, C, J, L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HEPACIVIRUS C; SOURCE 3 ORGANISM_TAXID: 11103; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL: HEK293; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.4 TOPO; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS HCV, E2, FAB, ANTIVIRAL, COMPLEX, ANTIVIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.SHAHID,J.LIQUN,Y.LIU,S.S.HASAN,R.A.MARIUZZA REVDAT 1 24-JUL-24 8TGV 0 JRNL AUTH S.SHAHID,J.LIQUN,Y.LIU,S.S.HASAN,R.A.MARIUZZA JRNL TITL CRYOEM STRUCTURE OF FAB HC84.26-HCV E2 COMPLEX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC 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) : 3.750 REMARK 3 NUMBER OF PARTICLES : 180188 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8TGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-23. REMARK 100 THE DEPOSITION ID IS D_1000275844. 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 : HCV E2-HC84.26 COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50 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 : 9653 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN 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 : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : 81000 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: UNDECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, F, D, B, C, G, I, J, K, REMARK 350 AND CHAINS: L, Z, H, M, N 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 363 REMARK 465 GLU A 364 REMARK 465 THR A 365 REMARK 465 ASP A 366 REMARK 465 THR A 367 REMARK 465 LEU A 368 REMARK 465 LEU A 369 REMARK 465 LEU A 370 REMARK 465 TRP A 371 REMARK 465 VAL A 372 REMARK 465 LEU A 373 REMARK 465 LEU A 374 REMARK 465 LEU A 375 REMARK 465 TRP A 376 REMARK 465 VAL A 377 REMARK 465 PRO A 378 REMARK 465 GLY A 379 REMARK 465 SER A 380 REMARK 465 THR A 381 REMARK 465 GLY A 382 REMARK 465 ASP A 383 REMARK 465 SER A 384 REMARK 465 THR A 385 REMARK 465 HIS A 386 REMARK 465 VAL A 387 REMARK 465 THR A 388 REMARK 465 GLY A 389 REMARK 465 GLY A 390 REMARK 465 THR A 391 REMARK 465 ALA A 392 REMARK 465 SER A 393 REMARK 465 HIS A 394 REMARK 465 THR A 395 REMARK 465 THR A 396 REMARK 465 ARG A 397 REMARK 465 HIS A 398 REMARK 465 PHE A 399 REMARK 465 ALA A 400 REMARK 465 SER A 401 REMARK 465 LEU A 402 REMARK 465 PHE A 403 REMARK 465 SER A 404 REMARK 465 SER A 405 REMARK 465 GLY A 406 REMARK 465 ALA A 407 REMARK 465 SER A 408 REMARK 465 GLN A 409 REMARK 465 ARG A 410 REMARK 465 VAL A 411 REMARK 465 GLN A 412 REMARK 465 LEU A 413 REMARK 465 ILE A 414 REMARK 465 GLN A 467 REMARK 465 GLY A 468 REMARK 465 TRP A 469 REMARK 465 GLY A 470 REMARK 465 PRO A 471 REMARK 465 ILE A 472 REMARK 465 THR A 473 REMARK 465 TYR A 474 REMARK 465 ALA A 475 REMARK 465 GLU A 476 REMARK 465 GLY A 477 REMARK 465 GLY A 575 REMARK 465 ASN A 576 REMARK 465 ASN A 577 REMARK 465 GLY A 647 REMARK 465 HIS A 648 REMARK 465 HIS A 649 REMARK 465 HIS A 650 REMARK 465 HIS A 651 REMARK 465 HIS A 652 REMARK 465 HIS A 653 REMARK 465 MET E -20 REMARK 465 GLU E -19 REMARK 465 THR E -18 REMARK 465 ASP E -17 REMARK 465 THR E -16 REMARK 465 LEU E -15 REMARK 465 LEU E -14 REMARK 465 LEU E -13 REMARK 465 TRP E -12 REMARK 465 VAL E -11 REMARK 465 LEU E -10 REMARK 465 LEU E -9 REMARK 465 LEU E -8 REMARK 465 TRP E -7 REMARK 465 VAL E -6 REMARK 465 PRO E -5 REMARK 465 GLY E -4 REMARK 465 SER E -3 REMARK 465 THR E -2 REMARK 465 GLY E -1 REMARK 465 ASP E 0 REMARK 465 GLN E 1 REMARK 465 VAL E 2 REMARK 465 GLN E 3 REMARK 465 PRO E 4 REMARK 465 VAL E 5 REMARK 465 GLN E 6 REMARK 465 SER E 7 REMARK 465 GLY E 8 REMARK 465 ALA E 9 REMARK 465 ASP E 222 REMARK 465 LYS E 223 REMARK 465 THR E 224 REMARK 465 ALA E 225 REMARK 465 GLY E 226 REMARK 465 TRP E 227 REMARK 465 SER E 228 REMARK 465 HIS E 229 REMARK 465 PRO E 230 REMARK 465 GLN E 231 REMARK 465 PHE E 232 REMARK 465 GLU E 233 REMARK 465 LYS E 234 REMARK 465 MET F -20 REMARK 465 GLU F -19 REMARK 465 THR F -18 REMARK 465 ASP F -17 REMARK 465 THR F -16 REMARK 465 LEU F -15 REMARK 465 LEU F -14 REMARK 465 LEU F -13 REMARK 465 TRP F -12 REMARK 465 VAL F -11 REMARK 465 LEU F -10 REMARK 465 LEU F -9 REMARK 465 LEU F -8 REMARK 465 TRP F -7 REMARK 465 VAL F -6 REMARK 465 PRO F -5 REMARK 465 GLY F -4 REMARK 465 SER F -3 REMARK 465 THR F -2 REMARK 465 GLY F -1 REMARK 465 ASP F 0 REMARK 465 MET D 363 REMARK 465 GLU D 364 REMARK 465 THR D 365 REMARK 465 ASP D 366 REMARK 465 THR D 367 REMARK 465 LEU D 368 REMARK 465 LEU D 369 REMARK 465 LEU D 370 REMARK 465 TRP D 371 REMARK 465 VAL D 372 REMARK 465 LEU D 373 REMARK 465 LEU D 374 REMARK 465 LEU D 375 REMARK 465 TRP D 376 REMARK 465 VAL D 377 REMARK 465 PRO D 378 REMARK 465 GLY D 379 REMARK 465 SER D 380 REMARK 465 THR D 381 REMARK 465 GLY D 382 REMARK 465 ASP D 383 REMARK 465 SER D 384 REMARK 465 THR D 385 REMARK 465 HIS D 386 REMARK 465 VAL D 387 REMARK 465 THR D 388 REMARK 465 GLY D 389 REMARK 465 GLY D 390 REMARK 465 THR D 391 REMARK 465 ALA D 392 REMARK 465 SER D 393 REMARK 465 HIS D 394 REMARK 465 THR D 395 REMARK 465 THR D 396 REMARK 465 ARG D 397 REMARK 465 HIS D 398 REMARK 465 PHE D 399 REMARK 465 ALA D 400 REMARK 465 SER D 401 REMARK 465 LEU D 402 REMARK 465 PHE D 403 REMARK 465 SER D 404 REMARK 465 SER D 405 REMARK 465 GLY D 406 REMARK 465 ALA D 407 REMARK 465 SER D 408 REMARK 465 GLN D 409 REMARK 465 ARG D 410 REMARK 465 VAL D 411 REMARK 465 GLN D 412 REMARK 465 LEU D 413 REMARK 465 ILE D 414 REMARK 465 ASN D 415 REMARK 465 ASP D 463 REMARK 465 GLU D 464 REMARK 465 PHE D 465 REMARK 465 ALA D 466 REMARK 465 GLN D 467 REMARK 465 GLY D 468 REMARK 465 TRP D 469 REMARK 465 GLY D 470 REMARK 465 PRO D 471 REMARK 465 ILE D 472 REMARK 465 THR D 473 REMARK 465 TYR D 474 REMARK 465 ALA D 475 REMARK 465 GLU D 476 REMARK 465 GLY D 477 REMARK 465 HIS D 478 REMARK 465 GLY D 479 REMARK 465 SER D 480 REMARK 465 ASP D 481 REMARK 465 GLN D 482 REMARK 465 ARG D 483 REMARK 465 PHE D 522 REMARK 465 GLY D 523 REMARK 465 ALA D 524 REMARK 465 GLU D 533 REMARK 465 THR D 534 REMARK 465 ASP D 535 REMARK 465 VAL D 536 REMARK 465 LEU D 537 REMARK 465 ILE D 538 REMARK 465 LEU D 539 REMARK 465 ASN D 540 REMARK 465 ASN D 541 REMARK 465 ILE D 571 REMARK 465 GLY D 572 REMARK 465 GLY D 573 REMARK 465 VAL D 574 REMARK 465 GLY D 575 REMARK 465 ASN D 576 REMARK 465 ASN D 577 REMARK 465 THR D 578 REMARK 465 LEU D 579 REMARK 465 THR D 580 REMARK 465 CYS D 581 REMARK 465 PRO D 582 REMARK 465 THR D 583 REMARK 465 ASP D 584 REMARK 465 CYS D 585 REMARK 465 PHE D 586 REMARK 465 ARG D 587 REMARK 465 LYS D 588 REMARK 465 HIS D 589 REMARK 465 PRO D 590 REMARK 465 GLU D 591 REMARK 465 VAL D 633 REMARK 465 GLY D 634 REMARK 465 GLY D 635 REMARK 465 GLY D 647 REMARK 465 HIS D 648 REMARK 465 HIS D 649 REMARK 465 HIS D 650 REMARK 465 HIS D 651 REMARK 465 HIS D 652 REMARK 465 HIS D 653 REMARK 465 MET B -20 REMARK 465 GLU B -19 REMARK 465 THR B -18 REMARK 465 ASP B -17 REMARK 465 THR B -16 REMARK 465 LEU B -15 REMARK 465 LEU B -14 REMARK 465 LEU B -13 REMARK 465 TRP B -12 REMARK 465 VAL B -11 REMARK 465 LEU B -10 REMARK 465 LEU B -9 REMARK 465 LEU B -8 REMARK 465 TRP B -7 REMARK 465 VAL B -6 REMARK 465 PRO B -5 REMARK 465 GLY B -4 REMARK 465 SER B -3 REMARK 465 THR B -2 REMARK 465 GLY B -1 REMARK 465 ASP B 0 REMARK 465 GLN B 1 REMARK 465 VAL B 2 REMARK 465 GLN B 3 REMARK 465 PRO B 4 REMARK 465 VAL B 5 REMARK 465 GLN B 6 REMARK 465 SER B 7 REMARK 465 GLY B 8 REMARK 465 LYS B 223 REMARK 465 THR B 224 REMARK 465 ALA B 225 REMARK 465 GLY B 226 REMARK 465 TRP B 227 REMARK 465 SER B 228 REMARK 465 HIS B 229 REMARK 465 PRO B 230 REMARK 465 GLN B 231 REMARK 465 PHE B 232 REMARK 465 GLU B 233 REMARK 465 LYS B 234 REMARK 465 MET C -20 REMARK 465 GLU C -19 REMARK 465 THR C -18 REMARK 465 ASP C -17 REMARK 465 THR C -16 REMARK 465 LEU C -15 REMARK 465 LEU C -14 REMARK 465 LEU C -13 REMARK 465 TRP C -12 REMARK 465 VAL C -11 REMARK 465 LEU C -10 REMARK 465 LEU C -9 REMARK 465 LEU C -8 REMARK 465 TRP C -7 REMARK 465 VAL C -6 REMARK 465 PRO C -5 REMARK 465 GLY C -4 REMARK 465 SER C -3 REMARK 465 THR C -2 REMARK 465 GLY C -1 REMARK 465 ASP C 0 REMARK 465 MET G 363 REMARK 465 GLU G 364 REMARK 465 THR G 365 REMARK 465 ASP G 366 REMARK 465 THR G 367 REMARK 465 LEU G 368 REMARK 465 LEU G 369 REMARK 465 LEU G 370 REMARK 465 TRP G 371 REMARK 465 VAL G 372 REMARK 465 LEU G 373 REMARK 465 LEU G 374 REMARK 465 LEU G 375 REMARK 465 TRP G 376 REMARK 465 VAL G 377 REMARK 465 PRO G 378 REMARK 465 GLY G 379 REMARK 465 SER G 380 REMARK 465 THR G 381 REMARK 465 GLY G 382 REMARK 465 ASP G 383 REMARK 465 SER G 384 REMARK 465 THR G 385 REMARK 465 HIS G 386 REMARK 465 VAL G 387 REMARK 465 THR G 388 REMARK 465 GLY G 389 REMARK 465 GLY G 390 REMARK 465 THR G 391 REMARK 465 ALA G 392 REMARK 465 SER G 393 REMARK 465 HIS G 394 REMARK 465 THR G 395 REMARK 465 THR G 396 REMARK 465 ARG G 397 REMARK 465 HIS G 398 REMARK 465 PHE G 399 REMARK 465 ALA G 400 REMARK 465 SER G 401 REMARK 465 LEU G 402 REMARK 465 PHE G 403 REMARK 465 SER G 404 REMARK 465 SER G 405 REMARK 465 GLY G 406 REMARK 465 ALA G 407 REMARK 465 SER G 408 REMARK 465 GLN G 409 REMARK 465 ARG G 410 REMARK 465 VAL G 411 REMARK 465 GLN G 412 REMARK 465 LEU G 413 REMARK 465 ILE G 414 REMARK 465 ASN G 415 REMARK 465 THR G 416 REMARK 465 PRO G 461 REMARK 465 ILE G 462 REMARK 465 ASP G 463 REMARK 465 GLU G 464 REMARK 465 PHE G 465 REMARK 465 ALA G 466 REMARK 465 GLN G 467 REMARK 465 GLY G 468 REMARK 465 TRP G 469 REMARK 465 GLY G 470 REMARK 465 PRO G 471 REMARK 465 ILE G 472 REMARK 465 THR G 473 REMARK 465 TYR G 474 REMARK 465 ALA G 475 REMARK 465 GLU G 476 REMARK 465 GLY G 477 REMARK 465 HIS G 478 REMARK 465 GLY G 479 REMARK 465 SER G 480 REMARK 465 ASP G 481 REMARK 465 GLN G 482 REMARK 465 ARG G 483 REMARK 465 GLY G 517 REMARK 465 THR G 518 REMARK 465 THR G 519 REMARK 465 ASP G 520 REMARK 465 ARG G 521 REMARK 465 PHE G 522 REMARK 465 GLY G 523 REMARK 465 ALA G 524 REMARK 465 PRO G 525 REMARK 465 ASN G 570 REMARK 465 ILE G 571 REMARK 465 GLY G 572 REMARK 465 GLY G 573 REMARK 465 VAL G 574 REMARK 465 GLY G 575 REMARK 465 ASN G 576 REMARK 465 ASN G 577 REMARK 465 THR G 578 REMARK 465 LEU G 579 REMARK 465 PHE G 586 REMARK 465 ARG G 587 REMARK 465 LYS G 588 REMARK 465 HIS G 589 REMARK 465 PRO G 590 REMARK 465 GLU G 591 REMARK 465 ALA G 592 REMARK 465 LYS G 628 REMARK 465 VAL G 629 REMARK 465 ARG G 630 REMARK 465 MET G 631 REMARK 465 TYR G 632 REMARK 465 VAL G 633 REMARK 465 GLY G 634 REMARK 465 GLY G 635 REMARK 465 VAL G 636 REMARK 465 GLU G 637 REMARK 465 HIS G 638 REMARK 465 GLY G 647 REMARK 465 HIS G 648 REMARK 465 HIS G 649 REMARK 465 HIS G 650 REMARK 465 HIS G 651 REMARK 465 HIS G 652 REMARK 465 HIS G 653 REMARK 465 MET I -20 REMARK 465 GLU I -19 REMARK 465 THR I -18 REMARK 465 ASP I -17 REMARK 465 THR I -16 REMARK 465 LEU I -15 REMARK 465 LEU I -14 REMARK 465 LEU I -13 REMARK 465 TRP I -12 REMARK 465 VAL I -11 REMARK 465 LEU I -10 REMARK 465 LEU I -9 REMARK 465 LEU I -8 REMARK 465 TRP I -7 REMARK 465 VAL I -6 REMARK 465 PRO I -5 REMARK 465 GLY I -4 REMARK 465 SER I -3 REMARK 465 THR I -2 REMARK 465 GLY I -1 REMARK 465 ASP I 0 REMARK 465 GLN I 1 REMARK 465 VAL I 2 REMARK 465 GLN I 3 REMARK 465 PRO I 4 REMARK 465 VAL I 5 REMARK 465 GLN I 6 REMARK 465 SER I 7 REMARK 465 GLY I 8 REMARK 465 ALA I 9 REMARK 465 LYS I 223 REMARK 465 THR I 224 REMARK 465 ALA I 225 REMARK 465 GLY I 226 REMARK 465 TRP I 227 REMARK 465 SER I 228 REMARK 465 HIS I 229 REMARK 465 PRO I 230 REMARK 465 GLN I 231 REMARK 465 PHE I 232 REMARK 465 GLU I 233 REMARK 465 LYS I 234 REMARK 465 MET J -20 REMARK 465 GLU J -19 REMARK 465 THR J -18 REMARK 465 ASP J -17 REMARK 465 THR J -16 REMARK 465 LEU J -15 REMARK 465 LEU J -14 REMARK 465 LEU J -13 REMARK 465 TRP J -12 REMARK 465 VAL J -11 REMARK 465 LEU J -10 REMARK 465 LEU J -9 REMARK 465 LEU J -8 REMARK 465 TRP J -7 REMARK 465 VAL J -6 REMARK 465 PRO J -5 REMARK 465 GLY J -4 REMARK 465 SER J -3 REMARK 465 THR J -2 REMARK 465 GLY J -1 REMARK 465 ASP J 0 REMARK 465 MET K -20 REMARK 465 GLU K -19 REMARK 465 THR K -18 REMARK 465 ASP K -17 REMARK 465 THR K -16 REMARK 465 LEU K -15 REMARK 465 LEU K -14 REMARK 465 LEU K -13 REMARK 465 TRP K -12 REMARK 465 VAL K -11 REMARK 465 LEU K -10 REMARK 465 LEU K -9 REMARK 465 LEU K -8 REMARK 465 TRP K -7 REMARK 465 VAL K -6 REMARK 465 PRO K -5 REMARK 465 GLY K -4 REMARK 465 SER K -3 REMARK 465 THR K -2 REMARK 465 GLY K -1 REMARK 465 ASP K 0 REMARK 465 GLN K 1 REMARK 465 VAL K 2 REMARK 465 GLN K 3 REMARK 465 PRO K 4 REMARK 465 VAL K 5 REMARK 465 GLN K 6 REMARK 465 SER K 7 REMARK 465 GLY K 8 REMARK 465 ALA K 9 REMARK 465 GLU K 10 REMARK 465 GLU K 23 REMARK 465 ALA K 24 REMARK 465 SER K 25 REMARK 465 GLY K 26 REMARK 465 GLY K 27 REMARK 465 THR K 28 REMARK 465 HIS K 29 REMARK 465 SER K 30 REMARK 465 ASN K 31 REMARK 465 ASP K 54 REMARK 465 PHE K 55 REMARK 465 ARG K 56 REMARK 465 THR K 57 REMARK 465 ASP K 73 REMARK 465 GLU K 74 REMARK 465 SER K 75 REMARK 465 THR K 76 REMARK 465 SER K 77 REMARK 465 LEU K 78 REMARK 465 ASP K 222 REMARK 465 LYS K 223 REMARK 465 THR K 224 REMARK 465 ALA K 225 REMARK 465 GLY K 226 REMARK 465 TRP K 227 REMARK 465 SER K 228 REMARK 465 HIS K 229 REMARK 465 PRO K 230 REMARK 465 GLN K 231 REMARK 465 PHE K 232 REMARK 465 GLU K 233 REMARK 465 LYS K 234 REMARK 465 MET L -20 REMARK 465 GLU L -19 REMARK 465 THR L -18 REMARK 465 ASP L -17 REMARK 465 THR L -16 REMARK 465 LEU L -15 REMARK 465 LEU L -14 REMARK 465 LEU L -13 REMARK 465 TRP L -12 REMARK 465 VAL L -11 REMARK 465 LEU L -10 REMARK 465 LEU L -9 REMARK 465 LEU L -8 REMARK 465 TRP L -7 REMARK 465 VAL L -6 REMARK 465 PRO L -5 REMARK 465 GLY L -4 REMARK 465 SER L -3 REMARK 465 THR L -2 REMARK 465 GLY L -1 REMARK 465 ASP L 0 REMARK 465 SER L 1 REMARK 465 TYR L 2 REMARK 465 VAL L 3 REMARK 465 LEU L 4 REMARK 465 SER L 55 REMARK 465 GLY L 56 REMARK 465 ILE L 57 REMARK 465 SER L 92 REMARK 465 SER L 93 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 A 415 CG OD1 ND2 REMARK 470 SER A 419 OG REMARK 470 TRP A 420 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 420 CZ3 CH2 REMARK 470 ASP A 431 CG OD1 OD2 REMARK 470 SER A 432 OG REMARK 470 ARG A 460 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 462 CG1 CG2 CD1 REMARK 470 ASP A 463 CG OD1 OD2 REMARK 470 GLU A 464 CG CD OE1 OE2 REMARK 470 HIS A 478 CG ND1 CD2 CE1 NE2 REMARK 470 SER A 480 OG REMARK 470 GLN A 482 CG CD OE1 NE2 REMARK 470 ARG A 483 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 492 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 522 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 531 CG CD OE1 OE2 REMARK 470 ASP A 535 CG OD1 OD2 REMARK 470 GLN A 546 CG CD OE1 NE2 REMARK 470 ILE A 571 CG1 CG2 CD1 REMARK 470 VAL A 574 CG1 CG2 REMARK 470 THR A 578 OG1 CG2 REMARK 470 LEU A 579 CG CD1 CD2 REMARK 470 THR A 580 OG1 CG2 REMARK 470 ASP A 584 CG OD1 OD2 REMARK 470 ARG A 587 CG CD NE CZ NH1 NH2 REMARK 470 HIS A 589 CG ND1 CD2 CE1 NE2 REMARK 470 GLU A 591 CG CD OE1 OE2 REMARK 470 LYS A 596 CG CD CE NZ REMARK 470 ARG A 630 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 13 CG CD CE NZ REMARK 470 LYS E 134 CG CD CE NZ REMARK 470 SER E 137 OG REMARK 470 GLU F 59 CG CD OE1 OE2 REMARK 470 LYS F 168 CG CD CE NZ REMARK 470 CYS F 213 O REMARK 470 THR D 416 OG1 CG2 REMARK 470 ASN D 417 CG OD1 ND2 REMARK 470 SER D 419 OG REMARK 470 TRP D 420 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP D 420 CZ3 CH2 REMARK 470 ASP D 431 CG OD1 OD2 REMARK 470 SER D 432 OG REMARK 470 HIS D 434 CG ND1 CD2 CE1 NE2 REMARK 470 PHE D 437 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU D 438 CG CD1 CD2 REMARK 470 SER D 450 OG REMARK 470 GLU D 454 CG CD OE1 OE2 REMARK 470 ARG D 455 CG CD NE CZ NH1 NH2 REMARK 470 MET D 456 CG SD CE REMARK 470 HIS D 458 CG ND1 CD2 CE1 NE2 REMARK 470 ARG D 460 CG CD NE CZ NH1 NH2 REMARK 470 ILE D 462 CG1 CG2 CD1 REMARK 470 HIS D 488 CG ND1 CD2 CE1 NE2 REMARK 470 GLN D 493 CG CD OE1 NE2 REMARK 470 THR D 496 OG1 CG2 REMARK 470 GLN D 501 CG CD OE1 NE2 REMARK 470 VAL D 502 CG1 CG2 REMARK 470 ASP D 520 CG OD1 OD2 REMARK 470 ARG D 521 CG CD NE CZ NH1 NH2 REMARK 470 GLU D 531 CG CD OE1 OE2 REMARK 470 GLN D 546 CG CD OE1 NE2 REMARK 470 ASN D 548 CG OD1 ND2 REMARK 470 PHE D 550 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS D 562 CG CD CE NZ REMARK 470 ASN D 570 CG OD1 ND2 REMARK 470 TYR D 594 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR D 595 OG1 CG2 REMARK 470 LYS D 596 CG CD CE NZ REMARK 470 LEU D 603 CG CD1 CD2 REMARK 470 THR D 604 OG1 CG2 REMARK 470 ILE D 626 CG1 CG2 CD1 REMARK 470 PHE D 627 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS D 628 CG CD CE NZ REMARK 470 ARG D 630 CG CD NE CZ NH1 NH2 REMARK 470 MET D 631 CG SD CE REMARK 470 TYR D 632 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL D 636 CG1 CG2 REMARK 470 GLU D 637 CG CD OE1 OE2 REMARK 470 ARG D 639 CG CD NE CZ NH1 NH2 REMARK 470 LEU D 640 CG CD1 CD2 REMARK 470 ILE D 646 CG1 CG2 CD1 REMARK 470 GLU B 10 CG CD OE1 OE2 REMARK 470 LYS B 13 CG CD CE NZ REMARK 470 LYS B 19 CG CD CE NZ REMARK 470 GLU B 23 CG CD OE1 OE2 REMARK 470 GLU B 46 CG CD OE1 OE2 REMARK 470 ASP B 54 CG OD1 OD2 REMARK 470 ARG B 56 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 134 CG CD CE NZ REMARK 470 THR B 136 OG1 CG2 REMARK 470 SER B 137 OG REMARK 470 ASP B 222 CG OD1 OD2 REMARK 470 LYS C 26 CG CD CE NZ REMARK 470 ASP C 29 CG OD1 OD2 REMARK 470 ASP C 166 CG OD1 OD2 REMARK 470 SER C 167 OG REMARK 470 LYS C 168 CG CD CE NZ REMARK 470 CYS C 213 O REMARK 470 SER G 419 OG REMARK 470 THR G 425 OG1 CG2 REMARK 470 ASP G 431 CG OD1 OD2 REMARK 470 HIS G 434 CG ND1 CD2 CE1 NE2 REMARK 470 THR G 435 OG1 CG2 REMARK 470 GLU G 454 CG CD OE1 OE2 REMARK 470 ARG G 455 CG CD NE CZ NH1 NH2 REMARK 470 HIS G 458 CG ND1 CD2 CE1 NE2 REMARK 470 ARG G 460 CG CD NE CZ NH1 NH2 REMARK 470 TYR G 485 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR G 496 OG1 CG2 REMARK 470 SER G 500 OG REMARK 470 TYR G 507 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL G 516 CG1 CG2 REMARK 470 GLU G 531 CG CD OE1 OE2 REMARK 470 ASN G 532 CG OD1 ND2 REMARK 470 GLU G 533 CG CD OE1 OE2 REMARK 470 THR G 534 OG1 CG2 REMARK 470 ASP G 535 CG OD1 OD2 REMARK 470 ILE G 538 CG1 CG2 CD1 REMARK 470 ASN G 540 CG OD1 ND2 REMARK 470 GLN G 546 CG CD OE1 NE2 REMARK 470 THR G 580 OG1 CG2 REMARK 470 ASP G 584 CG OD1 OD2 REMARK 470 THR G 593 OG1 CG2 REMARK 470 TYR G 594 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR G 595 OG1 CG2 REMARK 470 LYS G 596 CG CD CE NZ REMARK 470 LEU G 603 CG CD1 CD2 REMARK 470 ARG G 606 CG CD NE CZ NH1 NH2 REMARK 470 VAL G 609 CG1 CG2 REMARK 470 ASP G 610 CG OD1 OD2 REMARK 470 THR G 625 OG1 CG2 REMARK 470 ILE G 626 CG1 CG2 CD1 REMARK 470 ARG G 639 CG CD NE CZ NH1 NH2 REMARK 470 LEU G 640 CG CD1 CD2 REMARK 470 ARG I 56 CG CD NE CZ NH1 NH2 REMARK 470 SER I 75 OG REMARK 470 ARG I 103 CG CD NE CZ NH1 NH2 REMARK 470 SER I 135 OG REMARK 470 SER I 137 OG REMARK 470 ASP I 222 O CG OD1 OD2 REMARK 470 LYS J 52 CG CD CE NZ REMARK 470 GLU J 59 CG CD OE1 OE2 REMARK 470 SER J 167 OG REMARK 470 LYS J 168 CG CD CE NZ REMARK 470 CYS J 213 O REMARK 470 VAL K 11 CG1 CG2 REMARK 470 LYS K 13 CG CD CE NZ REMARK 470 LYS K 19 CG CD CE NZ REMARK 470 GLU K 46 CG CD OE1 OE2 REMARK 470 ILE K 52 CG1 CG2 CD1 REMARK 470 GLN K 62 CG CD OE1 NE2 REMARK 470 GLN K 65 CG CD OE1 NE2 REMARK 470 THR K 71 OG1 CG2 REMARK 470 GLU K 82 CG CD OE1 OE2 REMARK 470 TYR K 95 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG K 103 CG CD NE CZ NH1 NH2 REMARK 470 THR K 113 OG1 CG2 REMARK 470 SER K 135 OG REMARK 470 SER K 137 OG REMARK 470 THR L 5 OG1 CG2 REMARK 470 ILE L 20 CG1 CG2 CD1 REMARK 470 LYS L 26 CG CD CE NZ REMARK 470 LYS L 30 CG CD CE NZ REMARK 470 GLN L 37 CG CD OE1 NE2 REMARK 470 ARG L 38 CG CD NE CZ NH1 NH2 REMARK 470 VAL L 46 CG1 CG2 REMARK 470 LEU L 47 CG CD1 CD2 REMARK 470 LYS L 52 CG CD CE NZ REMARK 470 GLU L 59 CG CD OE1 OE2 REMARK 470 ARG L 60 CG CD NE CZ NH1 NH2 REMARK 470 SER L 64 OG REMARK 470 SER L 66 OG REMARK 470 LEU L 72 CG CD1 CD2 REMARK 470 SER L 75 OG REMARK 470 GLN L 78 CG CD OE1 NE2 REMARK 470 ASP L 81 CG OD1 OD2 REMARK 470 ASP L 91 CG OD1 OD2 REMARK 470 VAL L 96 CG1 CG2 REMARK 470 LYS L 102 CG CD CE NZ REMARK 470 ASP L 166 CG OD1 OD2 REMARK 470 SER L 167 OG REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 SER L 181 OG REMARK 470 LYS L 182 CG CD CE NZ REMARK 470 GLU L 212 CG CD OE1 OE2 REMARK 470 CYS L 213 O 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 HH TYR C 2 O ASP C 25 1.57 REMARK 500 H CYS G 508 O VAL G 514 1.57 REMARK 500 OD1 ASN G 556 H PHE G 560 1.59 REMARK 500 O GLN L 36 H VAL L 44 1.59 REMARK 500 OD2 ASP E 73 HG1 THR E 76 1.60 REMARK 500 O GLN F 123 OG SER F 126 1.99 REMARK 500 OH TYR C 2 O ASP C 25 2.07 REMARK 500 N THR D 416 O VAL D 515 2.17 REMARK 500 NH1 ARG I 38 OD1 ASP I 90 2.18 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 ILE A 422 -68.73 -100.31 REMARK 500 LEU A 427 76.12 -100.15 REMARK 500 SER A 480 29.47 -140.37 REMARK 500 ASN A 548 -142.11 69.74 REMARK 500 CYS A 552 -179.88 -172.72 REMARK 500 ASN A 570 -167.63 64.25 REMARK 500 ASP A 584 -108.74 55.90 REMARK 500 GLN E 43 11.29 -140.13 REMARK 500 PHE E 51 137.89 -170.43 REMARK 500 MET E 59 116.21 -163.37 REMARK 500 TYR E 108 65.60 60.59 REMARK 500 ALA E 119 -132.33 34.68 REMARK 500 ASP E 149 61.27 61.55 REMARK 500 ASP F 50 -76.32 70.20 REMARK 500 ALA F 143 137.12 -170.16 REMARK 500 HIS F 188 164.73 63.67 REMARK 500 LEU D 427 53.24 -91.77 REMARK 500 ASN D 548 -151.03 69.11 REMARK 500 CYS D 552 -176.97 -171.50 REMARK 500 TYR B 32 160.39 178.38 REMARK 500 PRO B 41 109.64 -55.67 REMARK 500 PHE B 64 33.04 -97.90 REMARK 500 ASN B 85 60.47 61.34 REMARK 500 ALA B 119 -167.72 56.82 REMARK 500 SER B 178 51.76 -92.51 REMARK 500 ASP C 50 -77.39 69.32 REMARK 500 LYS C 168 48.19 -87.89 REMARK 500 SER C 170 10.90 -140.20 REMARK 500 ALA C 183 -2.52 81.37 REMARK 500 LYS C 187 -169.53 -123.49 REMARK 500 ARG G 424 -9.70 -58.10 REMARK 500 LEU G 427 67.43 -101.02 REMARK 500 ASN G 548 -137.05 68.06 REMARK 500 ASP G 584 -111.56 53.31 REMARK 500 SER I 30 -62.32 -95.48 REMARK 500 ASN I 85 60.88 61.26 REMARK 500 ASP I 149 60.24 61.54 REMARK 500 PHE I 151 142.96 -171.19 REMARK 500 SER I 220 -166.40 -78.54 REMARK 500 LYS J 26 16.28 56.68 REMARK 500 ASP J 50 -76.81 70.78 REMARK 500 LYS J 168 50.31 -90.90 REMARK 500 SER J 173 119.61 -164.70 REMARK 500 ALA K 92 -175.15 -171.79 REMARK 500 ALA K 119 170.77 175.09 REMARK 500 ASP K 149 60.40 63.13 REMARK 500 SER K 193 34.12 -98.69 REMARK 500 ASP L 50 -74.07 66.34 REMARK 500 ARG L 107 148.45 72.36 REMARK 500 ALA L 152 110.60 -160.83 REMARK 500 REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-41245 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF FAB HC84.26-HCV E2 COMPLEX DBREF 8TGV A 384 645 UNP X4ZFZ7 X4ZFZ7_9HEPC 206 467 DBREF 8TGV E -20 234 PDB 8TGV 8TGV -20 234 DBREF 8TGV F -20 213 PDB 8TGV 8TGV -20 213 DBREF 8TGV D 384 645 UNP X4ZFZ7 X4ZFZ7_9HEPC 206 467 DBREF 8TGV B -20 234 PDB 8TGV 8TGV -20 234 DBREF 8TGV C -20 213 PDB 8TGV 8TGV -20 213 DBREF 8TGV G 384 645 UNP X4ZFZ7 X4ZFZ7_9HEPC 206 467 DBREF 8TGV I -20 234 PDB 8TGV 8TGV -20 234 DBREF 8TGV J -20 213 PDB 8TGV 8TGV -20 213 DBREF 8TGV K -20 234 PDB 8TGV 8TGV -20 234 DBREF 8TGV L -20 213 PDB 8TGV 8TGV -20 213 SEQADV 8TGV MET A 363 UNP X4ZFZ7 INITIATING METHIONINE SEQADV 8TGV GLU A 364 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR A 365 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ASP A 366 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR A 367 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU A 368 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU A 369 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU A 370 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV TRP A 371 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV VAL A 372 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU A 373 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU A 374 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU A 375 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV TRP A 376 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV VAL A 377 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV PRO A 378 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY A 379 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV SER A 380 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR A 381 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY A 382 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ASP A 383 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ILE A 646 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY A 647 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS A 648 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS A 649 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS A 650 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS A 651 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS A 652 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS A 653 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV MET D 363 UNP X4ZFZ7 INITIATING METHIONINE SEQADV 8TGV GLU D 364 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR D 365 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ASP D 366 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR D 367 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU D 368 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU D 369 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU D 370 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV TRP D 371 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV VAL D 372 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU D 373 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU D 374 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU D 375 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV TRP D 376 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV VAL D 377 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV PRO D 378 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY D 379 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV SER D 380 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR D 381 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY D 382 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ASP D 383 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ILE D 646 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY D 647 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS D 648 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS D 649 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS D 650 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS D 651 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS D 652 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS D 653 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV MET G 363 UNP X4ZFZ7 INITIATING METHIONINE SEQADV 8TGV GLU G 364 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR G 365 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ASP G 366 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR G 367 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU G 368 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU G 369 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU G 370 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV TRP G 371 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV VAL G 372 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU G 373 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU G 374 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV LEU G 375 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV TRP G 376 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV VAL G 377 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV PRO G 378 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY G 379 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV SER G 380 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV THR G 381 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY G 382 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ASP G 383 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV ILE G 646 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV GLY G 647 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS G 648 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS G 649 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS G 650 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS G 651 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS G 652 UNP X4ZFZ7 EXPRESSION TAG SEQADV 8TGV HIS G 653 UNP X4ZFZ7 EXPRESSION TAG SEQRES 1 A 291 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 A 291 TRP VAL PRO GLY SER THR GLY ASP SER THR HIS VAL THR SEQRES 3 A 291 GLY GLY THR ALA SER HIS THR THR ARG HIS PHE ALA SER SEQRES 4 A 291 LEU PHE SER SER GLY ALA SER GLN ARG VAL GLN LEU ILE SEQRES 5 A 291 ASN THR ASN GLY SER TRP HIS ILE ASN ARG THR ALA LEU SEQRES 6 A 291 ASN CYS ASN ASP SER LEU HIS THR GLY PHE LEU ALA ALA SEQRES 7 A 291 LEU PHE TYR THR HIS LYS PHE ASN ALA SER GLY CYS PRO SEQRES 8 A 291 GLU ARG MET ALA HIS CYS ARG PRO ILE ASP GLU PHE ALA SEQRES 9 A 291 GLN GLY TRP GLY PRO ILE THR TYR ALA GLU GLY HIS GLY SEQRES 10 A 291 SER ASP GLN ARG PRO TYR CYS TRP HIS TYR ALA PRO ARG SEQRES 11 A 291 GLN CYS GLY THR ILE PRO ALA SER GLN VAL CYS GLY PRO SEQRES 12 A 291 VAL TYR CYS PHE THR PRO SER PRO VAL VAL VAL GLY THR SEQRES 13 A 291 THR ASP ARG PHE GLY ALA PRO THR TYR THR TRP GLY GLU SEQRES 14 A 291 ASN GLU THR ASP VAL LEU ILE LEU ASN ASN THR ARG PRO SEQRES 15 A 291 PRO GLN GLY ASN TRP PHE GLY CYS THR TRP MET ASN SER SEQRES 16 A 291 THR GLY PHE THR LYS THR CYS GLY GLY PRO PRO CYS ASN SEQRES 17 A 291 ILE GLY GLY VAL GLY ASN ASN THR LEU THR CYS PRO THR SEQRES 18 A 291 ASP CYS PHE ARG LYS HIS PRO GLU ALA THR TYR THR LYS SEQRES 19 A 291 CYS GLY SER GLY PRO TRP LEU THR PRO ARG CYS LEU VAL SEQRES 20 A 291 ASP TYR PRO TYR ARG LEU TRP HIS TYR PRO CYS THR VAL SEQRES 21 A 291 ASN PHE THR ILE PHE LYS VAL ARG MET TYR VAL GLY GLY SEQRES 22 A 291 VAL GLU HIS ARG LEU ASN ALA ALA CYS ASN ILE GLY HIS SEQRES 23 A 291 HIS HIS HIS HIS HIS SEQRES 1 E 255 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 E 255 TRP VAL PRO GLY SER THR GLY ASP GLN VAL GLN PRO VAL SEQRES 3 E 255 GLN SER GLY ALA GLU VAL LYS LYS PRO GLY SER SER VAL SEQRES 4 E 255 LYS VAL SER CYS GLU ALA SER GLY GLY THR HIS SER ASN SEQRES 5 E 255 TYR VAL ILE THR TRP VAL ARG GLN ALA PRO GLY GLN GLY SEQRES 6 E 255 LEU GLU TRP MET GLY GLY PHE ILE PRO ASP PHE ARG THR SEQRES 7 E 255 ALA MET TYR ALA GLN GLY PHE GLN GLY ARG VAL THR ILE SEQRES 8 E 255 THR ALA ASP GLU SER THR SER LEU ALA TYR MET GLU LEU SEQRES 9 E 255 THR ASN LEU ARG SER GLU ASP THR ALA VAL TYR TYR CYS SEQRES 10 E 255 ALA ARG GLY PRO LEU SER ARG GLY TYR TYR ASP TYR TRP SEQRES 11 E 255 GLY PRO GLY THR LEU VAL THR VAL SER ALA SER THR LYS SEQRES 12 E 255 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 13 E 255 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 14 E 255 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 15 E 255 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 16 E 255 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 17 E 255 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 18 E 255 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 19 E 255 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR ALA GLY SEQRES 20 E 255 TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 F 234 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 F 234 TRP VAL PRO GLY SER THR GLY ASP SER TYR VAL LEU THR SEQRES 3 F 234 GLN PRO PRO SER VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 4 F 234 SER ILE THR CYS SER GLY ASP LYS LEU GLY ASP LYS TYR SEQRES 5 F 234 VAL SER TRP TYR GLN GLN ARG PRO GLY GLN SER PRO VAL SEQRES 6 F 234 LEU VAL LEU TYR GLN ASP SER LYS ARG PRO SER GLY ILE SEQRES 7 F 234 PRO GLU ARG PHE SER GLY SER ASN SER GLY ASN THR ALA SEQRES 8 F 234 THR LEU THR ILE SER GLY THR GLN ALA MET ASP GLU ALA SEQRES 9 F 234 ASP TYR TYR CYS GLN ALA TRP ASP SER SER ALA LEU VAL SEQRES 10 F 234 PHE GLY GLY GLY THR LYS LEU THR VAL LEU ARG THR VAL SEQRES 11 F 234 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 12 F 234 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 13 F 234 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 14 F 234 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 15 F 234 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 16 F 234 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 17 F 234 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 18 F 234 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 291 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 D 291 TRP VAL PRO GLY SER THR GLY ASP SER THR HIS VAL THR SEQRES 3 D 291 GLY GLY THR ALA SER HIS THR THR ARG HIS PHE ALA SER SEQRES 4 D 291 LEU PHE SER SER GLY ALA SER GLN ARG VAL GLN LEU ILE SEQRES 5 D 291 ASN THR ASN GLY SER TRP HIS ILE ASN ARG THR ALA LEU SEQRES 6 D 291 ASN CYS ASN ASP SER LEU HIS THR GLY PHE LEU ALA ALA SEQRES 7 D 291 LEU PHE TYR THR HIS LYS PHE ASN ALA SER GLY CYS PRO SEQRES 8 D 291 GLU ARG MET ALA HIS CYS ARG PRO ILE ASP GLU PHE ALA SEQRES 9 D 291 GLN GLY TRP GLY PRO ILE THR TYR ALA GLU GLY HIS GLY SEQRES 10 D 291 SER ASP GLN ARG PRO TYR CYS TRP HIS TYR ALA PRO ARG SEQRES 11 D 291 GLN CYS GLY THR ILE PRO ALA SER GLN VAL CYS GLY PRO SEQRES 12 D 291 VAL TYR CYS PHE THR PRO SER PRO VAL VAL VAL GLY THR SEQRES 13 D 291 THR ASP ARG PHE GLY ALA PRO THR TYR THR TRP GLY GLU SEQRES 14 D 291 ASN GLU THR ASP VAL LEU ILE LEU ASN ASN THR ARG PRO SEQRES 15 D 291 PRO GLN GLY ASN TRP PHE GLY CYS THR TRP MET ASN SER SEQRES 16 D 291 THR GLY PHE THR LYS THR CYS GLY GLY PRO PRO CYS ASN SEQRES 17 D 291 ILE GLY GLY VAL GLY ASN ASN THR LEU THR CYS PRO THR SEQRES 18 D 291 ASP CYS PHE ARG LYS HIS PRO GLU ALA THR TYR THR LYS SEQRES 19 D 291 CYS GLY SER GLY PRO TRP LEU THR PRO ARG CYS LEU VAL SEQRES 20 D 291 ASP TYR PRO TYR ARG LEU TRP HIS TYR PRO CYS THR VAL SEQRES 21 D 291 ASN PHE THR ILE PHE LYS VAL ARG MET TYR VAL GLY GLY SEQRES 22 D 291 VAL GLU HIS ARG LEU ASN ALA ALA CYS ASN ILE GLY HIS SEQRES 23 D 291 HIS HIS HIS HIS HIS SEQRES 1 B 255 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 B 255 TRP VAL PRO GLY SER THR GLY ASP GLN VAL GLN PRO VAL SEQRES 3 B 255 GLN SER GLY ALA GLU VAL LYS LYS PRO GLY SER SER VAL SEQRES 4 B 255 LYS VAL SER CYS GLU ALA SER GLY GLY THR HIS SER ASN SEQRES 5 B 255 TYR VAL ILE THR TRP VAL ARG GLN ALA PRO GLY GLN GLY SEQRES 6 B 255 LEU GLU TRP MET GLY GLY PHE ILE PRO ASP PHE ARG THR SEQRES 7 B 255 ALA MET TYR ALA GLN GLY PHE GLN GLY ARG VAL THR ILE SEQRES 8 B 255 THR ALA ASP GLU SER THR SER LEU ALA TYR MET GLU LEU SEQRES 9 B 255 THR ASN LEU ARG SER GLU ASP THR ALA VAL TYR TYR CYS SEQRES 10 B 255 ALA ARG GLY PRO LEU SER ARG GLY TYR TYR ASP TYR TRP SEQRES 11 B 255 GLY PRO GLY THR LEU VAL THR VAL SER ALA SER THR LYS SEQRES 12 B 255 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 13 B 255 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 14 B 255 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 15 B 255 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 16 B 255 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 17 B 255 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 18 B 255 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 19 B 255 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR ALA GLY SEQRES 20 B 255 TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 C 234 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 C 234 TRP VAL PRO GLY SER THR GLY ASP SER TYR VAL LEU THR SEQRES 3 C 234 GLN PRO PRO SER VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 4 C 234 SER ILE THR CYS SER GLY ASP LYS LEU GLY ASP LYS TYR SEQRES 5 C 234 VAL SER TRP TYR GLN GLN ARG PRO GLY GLN SER PRO VAL SEQRES 6 C 234 LEU VAL LEU TYR GLN ASP SER LYS ARG PRO SER GLY ILE SEQRES 7 C 234 PRO GLU ARG PHE SER GLY SER ASN SER GLY ASN THR ALA SEQRES 8 C 234 THR LEU THR ILE SER GLY THR GLN ALA MET ASP GLU ALA SEQRES 9 C 234 ASP TYR TYR CYS GLN ALA TRP ASP SER SER ALA LEU VAL SEQRES 10 C 234 PHE GLY GLY GLY THR LYS LEU THR VAL LEU ARG THR VAL SEQRES 11 C 234 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 12 C 234 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 13 C 234 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 14 C 234 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 15 C 234 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 16 C 234 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 17 C 234 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 18 C 234 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 291 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 G 291 TRP VAL PRO GLY SER THR GLY ASP SER THR HIS VAL THR SEQRES 3 G 291 GLY GLY THR ALA SER HIS THR THR ARG HIS PHE ALA SER SEQRES 4 G 291 LEU PHE SER SER GLY ALA SER GLN ARG VAL GLN LEU ILE SEQRES 5 G 291 ASN THR ASN GLY SER TRP HIS ILE ASN ARG THR ALA LEU SEQRES 6 G 291 ASN CYS ASN ASP SER LEU HIS THR GLY PHE LEU ALA ALA SEQRES 7 G 291 LEU PHE TYR THR HIS LYS PHE ASN ALA SER GLY CYS PRO SEQRES 8 G 291 GLU ARG MET ALA HIS CYS ARG PRO ILE ASP GLU PHE ALA SEQRES 9 G 291 GLN GLY TRP GLY PRO ILE THR TYR ALA GLU GLY HIS GLY SEQRES 10 G 291 SER ASP GLN ARG PRO TYR CYS TRP HIS TYR ALA PRO ARG SEQRES 11 G 291 GLN CYS GLY THR ILE PRO ALA SER GLN VAL CYS GLY PRO SEQRES 12 G 291 VAL TYR CYS PHE THR PRO SER PRO VAL VAL VAL GLY THR SEQRES 13 G 291 THR ASP ARG PHE GLY ALA PRO THR TYR THR TRP GLY GLU SEQRES 14 G 291 ASN GLU THR ASP VAL LEU ILE LEU ASN ASN THR ARG PRO SEQRES 15 G 291 PRO GLN GLY ASN TRP PHE GLY CYS THR TRP MET ASN SER SEQRES 16 G 291 THR GLY PHE THR LYS THR CYS GLY GLY PRO PRO CYS ASN SEQRES 17 G 291 ILE GLY GLY VAL GLY ASN ASN THR LEU THR CYS PRO THR SEQRES 18 G 291 ASP CYS PHE ARG LYS HIS PRO GLU ALA THR TYR THR LYS SEQRES 19 G 291 CYS GLY SER GLY PRO TRP LEU THR PRO ARG CYS LEU VAL SEQRES 20 G 291 ASP TYR PRO TYR ARG LEU TRP HIS TYR PRO CYS THR VAL SEQRES 21 G 291 ASN PHE THR ILE PHE LYS VAL ARG MET TYR VAL GLY GLY SEQRES 22 G 291 VAL GLU HIS ARG LEU ASN ALA ALA CYS ASN ILE GLY HIS SEQRES 23 G 291 HIS HIS HIS HIS HIS SEQRES 1 I 255 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 I 255 TRP VAL PRO GLY SER THR GLY ASP GLN VAL GLN PRO VAL SEQRES 3 I 255 GLN SER GLY ALA GLU VAL LYS LYS PRO GLY SER SER VAL SEQRES 4 I 255 LYS VAL SER CYS GLU ALA SER GLY GLY THR HIS SER ASN SEQRES 5 I 255 TYR VAL ILE THR TRP VAL ARG GLN ALA PRO GLY GLN GLY SEQRES 6 I 255 LEU GLU TRP MET GLY GLY PHE ILE PRO ASP PHE ARG THR SEQRES 7 I 255 ALA MET TYR ALA GLN GLY PHE GLN GLY ARG VAL THR ILE SEQRES 8 I 255 THR ALA ASP GLU SER THR SER LEU ALA TYR MET GLU LEU SEQRES 9 I 255 THR ASN LEU ARG SER GLU ASP THR ALA VAL TYR TYR CYS SEQRES 10 I 255 ALA ARG GLY PRO LEU SER ARG GLY TYR TYR ASP TYR TRP SEQRES 11 I 255 GLY PRO GLY THR LEU VAL THR VAL SER ALA SER THR LYS SEQRES 12 I 255 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 13 I 255 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 14 I 255 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 15 I 255 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 16 I 255 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 17 I 255 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 18 I 255 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 19 I 255 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR ALA GLY SEQRES 20 I 255 TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 J 234 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 J 234 TRP VAL PRO GLY SER THR GLY ASP SER TYR VAL LEU THR SEQRES 3 J 234 GLN PRO PRO SER VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 4 J 234 SER ILE THR CYS SER GLY ASP LYS LEU GLY ASP LYS TYR SEQRES 5 J 234 VAL SER TRP TYR GLN GLN ARG PRO GLY GLN SER PRO VAL SEQRES 6 J 234 LEU VAL LEU TYR GLN ASP SER LYS ARG PRO SER GLY ILE SEQRES 7 J 234 PRO GLU ARG PHE SER GLY SER ASN SER GLY ASN THR ALA SEQRES 8 J 234 THR LEU THR ILE SER GLY THR GLN ALA MET ASP GLU ALA SEQRES 9 J 234 ASP TYR TYR CYS GLN ALA TRP ASP SER SER ALA LEU VAL SEQRES 10 J 234 PHE GLY GLY GLY THR LYS LEU THR VAL LEU ARG THR VAL SEQRES 11 J 234 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 12 J 234 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 13 J 234 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 14 J 234 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 15 J 234 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 16 J 234 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 17 J 234 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 18 J 234 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 K 255 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 K 255 TRP VAL PRO GLY SER THR GLY ASP GLN VAL GLN PRO VAL SEQRES 3 K 255 GLN SER GLY ALA GLU VAL LYS LYS PRO GLY SER SER VAL SEQRES 4 K 255 LYS VAL SER CYS GLU ALA SER GLY GLY THR HIS SER ASN SEQRES 5 K 255 TYR VAL ILE THR TRP VAL ARG GLN ALA PRO GLY GLN GLY SEQRES 6 K 255 LEU GLU TRP MET GLY GLY PHE ILE PRO ASP PHE ARG THR SEQRES 7 K 255 ALA MET TYR ALA GLN GLY PHE GLN GLY ARG VAL THR ILE SEQRES 8 K 255 THR ALA ASP GLU SER THR SER LEU ALA TYR MET GLU LEU SEQRES 9 K 255 THR ASN LEU ARG SER GLU ASP THR ALA VAL TYR TYR CYS SEQRES 10 K 255 ALA ARG GLY PRO LEU SER ARG GLY TYR TYR ASP TYR TRP SEQRES 11 K 255 GLY PRO GLY THR LEU VAL THR VAL SER ALA SER THR LYS SEQRES 12 K 255 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 13 K 255 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 14 K 255 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 15 K 255 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 16 K 255 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 17 K 255 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 18 K 255 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 19 K 255 LYS ARG VAL GLU PRO LYS SER CYS ASP LYS THR ALA GLY SEQRES 20 K 255 TRP SER HIS PRO GLN PHE GLU LYS SEQRES 1 L 234 MET GLU THR ASP THR LEU LEU LEU TRP VAL LEU LEU LEU SEQRES 2 L 234 TRP VAL PRO GLY SER THR GLY ASP SER TYR VAL LEU THR SEQRES 3 L 234 GLN PRO PRO SER VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 4 L 234 SER ILE THR CYS SER GLY ASP LYS LEU GLY ASP LYS TYR SEQRES 5 L 234 VAL SER TRP TYR GLN GLN ARG PRO GLY GLN SER PRO VAL SEQRES 6 L 234 LEU VAL LEU TYR GLN ASP SER LYS ARG PRO SER GLY ILE SEQRES 7 L 234 PRO GLU ARG PHE SER GLY SER ASN SER GLY ASN THR ALA SEQRES 8 L 234 THR LEU THR ILE SER GLY THR GLN ALA MET ASP GLU ALA SEQRES 9 L 234 ASP TYR TYR CYS GLN ALA TRP ASP SER SER ALA LEU VAL SEQRES 10 L 234 PHE GLY GLY GLY THR LYS LEU THR VAL LEU ARG THR VAL SEQRES 11 L 234 ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU SEQRES 12 L 234 GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU SEQRES 13 L 234 ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS SEQRES 14 L 234 VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER SEQRES 15 L 234 VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SEQRES 16 L 234 SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS SEQRES 17 L 234 HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SEQRES 18 L 234 SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG Z 1 26 HET NAG Z 2 26 HET BMA Z 3 21 HET NAG H 1 26 HET NAG H 2 27 HET NAG M 1 26 HET NAG M 2 27 HET NAG N 1 26 HET NAG N 2 27 HET NAG A 701 27 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 12 NAG 9(C8 H15 N O6) FORMUL 12 BMA C6 H12 O6 HELIX 1 AA1 LEU A 438 PHE A 442 5 5 HELIX 2 AA2 GLY A 451 ALA A 457 1 7 HELIX 3 AA3 THR A 593 GLY A 598 1 6 HELIX 4 AA4 TYR A 613 TYR A 618 1 6 HELIX 5 AA5 PRO A 619 VAL A 622 5 4 HELIX 6 AA6 ARG E 87 THR E 91 5 5 HELIX 7 AA7 SER E 161 ALA E 163 5 3 HELIX 8 AA8 PRO E 190 LEU E 194 5 5 HELIX 9 AA9 LYS F 26 LYS F 30 5 5 HELIX 10 AB1 GLN F 78 GLU F 82 5 5 HELIX 11 AB2 SER F 120 GLY F 127 1 8 HELIX 12 AB3 LYS F 182 LYS F 187 1 6 HELIX 13 AB4 PHE D 437 LEU D 441 5 5 HELIX 14 AB5 GLY D 451 ALA D 457 1 7 HELIX 15 AB6 ARG D 543 GLY D 547 5 5 HELIX 16 AB7 TYR D 613 TYR D 618 1 6 HELIX 17 AB8 PRO D 619 VAL D 622 5 4 HELIX 18 AB9 ARG B 87 THR B 91 5 5 HELIX 19 AC1 TRP B 159 ALA B 163 5 5 HELIX 20 AC2 PRO B 190 THR B 196 5 7 HELIX 21 AC3 LYS C 26 LYS C 30 5 5 HELIX 22 AC4 SER C 120 LYS C 125 1 6 HELIX 23 AC5 LEU G 438 PHE G 442 5 5 HELIX 24 AC6 GLY G 451 ALA G 457 1 7 HELIX 25 AC7 SER G 500 VAL G 502 5 3 HELIX 26 AC8 ARG G 543 GLY G 547 5 5 HELIX 27 AC9 TYR G 594 GLY G 598 1 5 HELIX 28 AD1 TYR G 613 TYR G 618 1 6 HELIX 29 AD2 PRO G 619 VAL G 622 5 4 HELIX 30 AD3 ARG I 87 THR I 91 5 5 HELIX 31 AD4 SER I 161 ALA I 163 5 3 HELIX 32 AD5 SER I 192 LEU I 194 5 3 HELIX 33 AD6 LYS I 206 ASN I 209 5 4 HELIX 34 AD7 LYS J 26 LYS J 30 5 5 HELIX 35 AD8 GLN J 78 GLU J 82 5 5 HELIX 36 AD9 GLN J 123 SER J 126 5 4 HELIX 37 AE1 LYS J 182 GLU J 186 1 5 HELIX 38 AE2 ARG K 87 THR K 91 5 5 HELIX 39 AE3 SER K 161 ALA K 163 5 3 HELIX 40 AE4 SER K 192 LEU K 194 5 3 HELIX 41 AE5 LYS K 206 ASN K 209 5 4 HELIX 42 AE6 GLU L 122 SER L 126 5 5 SHEET 1 AA1 2 THR A 496 PRO A 498 0 SHEET 2 AA1 2 VAL A 536 ILE A 538 -1 O LEU A 537 N ILE A 497 SHEET 1 AA2 4 PRO A 513 VAL A 515 0 SHEET 2 AA2 4 TYR A 507 PHE A 509 -1 N CYS A 508 O VAL A 514 SHEET 3 AA2 4 GLY A 551 ASN A 556 -1 O GLY A 551 N PHE A 509 SHEET 4 AA2 4 PHE A 560 GLY A 565 -1 O CYS A 564 N CYS A 552 SHEET 1 AA3 4 TRP A 602 THR A 604 0 SHEET 2 AA3 4 CYS A 607 VAL A 609 -1 O CYS A 607 N THR A 604 SHEET 3 AA3 4 VAL A 636 CYS A 644 -1 O ALA A 643 N LEU A 608 SHEET 4 AA3 4 PHE A 627 VAL A 633 -1 N VAL A 633 O VAL A 636 SHEET 1 AA4 3 SER E 17 GLU E 23 0 SHEET 2 AA4 3 LEU E 78 THR E 84 -1 O ALA E 79 N CYS E 22 SHEET 3 AA4 3 ILE E 70 ASP E 73 -1 N ASP E 73 O LEU E 78 SHEET 1 AA5 4 PHE E 55 TYR E 60 0 SHEET 2 AA5 4 GLU E 46 ILE E 52 -1 N GLY E 50 O MET E 59 SHEET 3 AA5 4 VAL E 33 GLN E 39 -1 N ARG E 38 O GLU E 46 SHEET 4 AA5 4 ARG E 98 GLY E 99 -1 O GLY E 99 N VAL E 33 SHEET 1 AA6 5 PHE E 55 TYR E 60 0 SHEET 2 AA6 5 GLU E 46 ILE E 52 -1 N GLY E 50 O MET E 59 SHEET 3 AA6 5 VAL E 33 GLN E 39 -1 N ARG E 38 O GLU E 46 SHEET 4 AA6 5 ALA E 92 TYR E 95 -1 O TYR E 95 N VAL E 37 SHEET 5 AA6 5 THR E 113 VAL E 115 -1 O THR E 113 N TYR E 94 SHEET 1 AA7 4 SER E 125 PRO E 128 0 SHEET 2 AA7 4 CYS E 145 TYR E 150 -1 O LEU E 146 N PHE E 127 SHEET 3 AA7 4 TYR E 181 SER E 185 -1 O LEU E 183 N VAL E 147 SHEET 4 AA7 4 VAL E 174 LEU E 175 -1 N VAL E 174 O SER E 182 SHEET 1 AA8 2 ALA E 141 ALA E 142 0 SHEET 2 AA8 2 THR E 188 VAL E 189 -1 O VAL E 189 N ALA E 141 SHEET 1 AA9 3 THR E 156 TRP E 159 0 SHEET 2 AA9 3 ILE E 200 HIS E 205 -1 O ASN E 204 N THR E 156 SHEET 3 AA9 3 THR E 210 ARG E 215 -1 O THR E 210 N HIS E 205 SHEET 1 AB1 5 SER F 9 VAL F 12 0 SHEET 2 AB1 5 THR F 101 VAL F 105 1 O LYS F 102 N VAL F 10 SHEET 3 AB1 5 ASP F 84 ASP F 91 -1 N TYR F 85 O THR F 101 SHEET 4 AB1 5 SER F 33 GLN F 37 -1 N GLN F 37 O ASP F 84 SHEET 5 AB1 5 VAL F 44 TYR F 48 -1 O VAL F 44 N GLN F 36 SHEET 1 AB2 4 SER F 9 VAL F 12 0 SHEET 2 AB2 4 THR F 101 VAL F 105 1 O LYS F 102 N VAL F 10 SHEET 3 AB2 4 ASP F 84 ASP F 91 -1 N TYR F 85 O THR F 101 SHEET 4 AB2 4 ALA F 94 PHE F 97 -1 O ALA F 94 N ASP F 91 SHEET 1 AB3 3 ALA F 18 SER F 23 0 SHEET 2 AB3 3 THR F 69 ILE F 74 -1 O LEU F 72 N ILE F 20 SHEET 3 AB3 3 SER F 62 SER F 66 -1 N SER F 62 O THR F 73 SHEET 1 AB4 4 SER F 113 PHE F 117 0 SHEET 2 AB4 4 THR F 128 PHE F 138 -1 O VAL F 132 N PHE F 117 SHEET 3 AB4 4 TYR F 172 SER F 181 -1 O LEU F 178 N VAL F 131 SHEET 4 AB4 4 SER F 158 VAL F 162 -1 N SER F 161 O SER F 175 SHEET 1 AB5 3 LYS F 144 VAL F 149 0 SHEET 2 AB5 3 VAL F 190 THR F 196 -1 O GLU F 194 N GLN F 146 SHEET 3 AB5 3 VAL F 204 THR F 205 -1 O VAL F 204 N VAL F 195 SHEET 1 AB6 3 LYS F 144 VAL F 149 0 SHEET 2 AB6 3 VAL F 190 THR F 196 -1 O GLU F 194 N GLN F 146 SHEET 3 AB6 3 PHE F 208 ASN F 209 -1 O PHE F 208 N TYR F 191 SHEET 1 AB7 4 PRO D 513 VAL D 516 0 SHEET 2 AB7 4 VAL D 506 PHE D 509 -1 N CYS D 508 O VAL D 514 SHEET 3 AB7 4 GLY D 551 MET D 555 -1 O THR D 553 N TYR D 507 SHEET 4 AB7 4 THR D 561 GLY D 565 -1 O CYS D 564 N CYS D 552 SHEET 1 AB8 4 TRP D 602 THR D 604 0 SHEET 2 AB8 4 CYS D 607 VAL D 609 -1 O CYS D 607 N THR D 604 SHEET 3 AB8 4 HIS D 638 CYS D 644 -1 O ALA D 643 N LEU D 608 SHEET 4 AB8 4 THR D 625 MET D 631 -1 N MET D 631 O HIS D 638 SHEET 1 AB9 3 SER B 17 GLU B 23 0 SHEET 2 AB9 3 LEU B 78 THR B 84 -1 O ALA B 79 N CYS B 22 SHEET 3 AB9 3 VAL B 68 ASP B 73 -1 N THR B 69 O GLU B 82 SHEET 1 AC1 5 ALA B 58 TYR B 60 0 SHEET 2 AC1 5 LEU B 45 PHE B 51 -1 N GLY B 50 O MET B 59 SHEET 3 AC1 5 VAL B 33 GLN B 39 -1 N ILE B 34 O PHE B 51 SHEET 4 AC1 5 ALA B 92 GLY B 99 -1 O TYR B 95 N VAL B 37 SHEET 5 AC1 5 THR B 113 VAL B 115 -1 O THR B 113 N TYR B 94 SHEET 1 AC2 4 SER B 125 LEU B 129 0 SHEET 2 AC2 4 ALA B 141 TYR B 150 -1 O LEU B 146 N PHE B 127 SHEET 3 AC2 4 TYR B 181 VAL B 189 -1 O LEU B 183 N VAL B 147 SHEET 4 AC2 4 VAL B 168 THR B 170 -1 N HIS B 169 O VAL B 186 SHEET 1 AC3 4 SER B 125 LEU B 129 0 SHEET 2 AC3 4 ALA B 141 TYR B 150 -1 O LEU B 146 N PHE B 127 SHEET 3 AC3 4 TYR B 181 VAL B 189 -1 O LEU B 183 N VAL B 147 SHEET 4 AC3 4 VAL B 174 LEU B 175 -1 N VAL B 174 O SER B 182 SHEET 1 AC4 3 VAL B 155 SER B 158 0 SHEET 2 AC4 3 ILE B 200 HIS B 205 -1 O ASN B 202 N SER B 158 SHEET 3 AC4 3 THR B 210 ARG B 215 -1 O VAL B 212 N VAL B 203 SHEET 1 AC5 5 SER C 9 VAL C 12 0 SHEET 2 AC5 5 THR C 101 VAL C 105 1 O THR C 104 N VAL C 10 SHEET 3 AC5 5 ALA C 83 ASP C 91 -1 N TYR C 85 O THR C 101 SHEET 4 AC5 5 SER C 33 GLN C 37 -1 N TYR C 35 O TYR C 86 SHEET 5 AC5 5 VAL C 44 TYR C 48 -1 O VAL C 44 N GLN C 36 SHEET 1 AC6 4 SER C 9 VAL C 12 0 SHEET 2 AC6 4 THR C 101 VAL C 105 1 O THR C 104 N VAL C 10 SHEET 3 AC6 4 ALA C 83 ASP C 91 -1 N TYR C 85 O THR C 101 SHEET 4 AC6 4 ALA C 94 PHE C 97 -1 O VAL C 96 N ALA C 89 SHEET 1 AC7 3 THR C 17 SER C 23 0 SHEET 2 AC7 3 THR C 69 SER C 75 -1 O ALA C 70 N CYS C 22 SHEET 3 AC7 3 SER C 62 SER C 66 -1 N SER C 62 O THR C 73 SHEET 1 AC8 4 VAL C 114 PHE C 117 0 SHEET 2 AC8 4 SER C 130 PHE C 138 -1 O LEU C 134 N PHE C 115 SHEET 3 AC8 4 TYR C 172 THR C 179 -1 O LEU C 174 N LEU C 135 SHEET 4 AC8 4 SER C 158 VAL C 162 -1 N GLN C 159 O THR C 177 SHEET 1 AC9 3 LYS C 144 VAL C 149 0 SHEET 2 AC9 3 VAL C 190 THR C 196 -1 O GLU C 194 N GLN C 146 SHEET 3 AC9 3 VAL C 204 ASN C 209 -1 O LYS C 206 N CYS C 193 SHEET 1 AD1 2 THR G 496 PRO G 498 0 SHEET 2 AD1 2 VAL G 536 ILE G 538 -1 O LEU G 537 N ILE G 497 SHEET 1 AD2 2 TYR G 507 PHE G 509 0 SHEET 2 AD2 2 PRO G 513 VAL G 515 -1 O VAL G 514 N CYS G 508 SHEET 1 AD3 2 GLY G 551 MET G 555 0 SHEET 2 AD3 2 THR G 561 GLY G 565 -1 O CYS G 564 N CYS G 552 SHEET 1 AD4 2 LEU G 608 VAL G 609 0 SHEET 2 AD4 2 ALA G 642 ALA G 643 -1 O ALA G 643 N LEU G 608 SHEET 1 AD5 3 SER I 17 GLU I 23 0 SHEET 2 AD5 3 LEU I 78 THR I 84 -1 O ALA I 79 N CYS I 22 SHEET 3 AD5 3 VAL I 68 ASP I 73 -1 N THR I 69 O GLU I 82 SHEET 1 AD6 5 ALA I 58 TYR I 60 0 SHEET 2 AD6 5 GLU I 46 PHE I 51 -1 N GLY I 50 O MET I 59 SHEET 3 AD6 5 VAL I 33 GLN I 39 -1 N ARG I 38 O GLU I 46 SHEET 4 AD6 5 VAL I 93 GLY I 99 -1 O TYR I 95 N VAL I 37 SHEET 5 AD6 5 THR I 113 LEU I 114 -1 O THR I 113 N TYR I 94 SHEET 1 AD7 4 SER I 125 PRO I 128 0 SHEET 2 AD7 4 THR I 140 TYR I 150 -1 O LEU I 146 N PHE I 127 SHEET 3 AD7 4 TYR I 181 PRO I 190 -1 O LEU I 183 N VAL I 147 SHEET 4 AD7 4 HIS I 169 THR I 170 -1 N HIS I 169 O VAL I 186 SHEET 1 AD8 4 SER I 125 PRO I 128 0 SHEET 2 AD8 4 THR I 140 TYR I 150 -1 O LEU I 146 N PHE I 127 SHEET 3 AD8 4 TYR I 181 PRO I 190 -1 O LEU I 183 N VAL I 147 SHEET 4 AD8 4 VAL I 174 LEU I 175 -1 N VAL I 174 O SER I 182 SHEET 1 AD9 3 THR I 156 TRP I 159 0 SHEET 2 AD9 3 TYR I 199 HIS I 205 -1 O ASN I 204 N THR I 156 SHEET 3 AD9 3 THR I 210 VAL I 216 -1 O THR I 210 N HIS I 205 SHEET 1 AE1 5 SER J 9 SER J 11 0 SHEET 2 AE1 5 THR J 101 THR J 104 1 O LYS J 102 N VAL J 10 SHEET 3 AE1 5 ASP J 84 ASP J 91 -1 N TYR J 85 O THR J 101 SHEET 4 AE1 5 VAL J 32 GLN J 37 -1 N GLN J 37 O ASP J 84 SHEET 5 AE1 5 VAL J 44 TYR J 48 -1 O VAL J 44 N GLN J 36 SHEET 1 AE2 4 SER J 9 SER J 11 0 SHEET 2 AE2 4 THR J 101 THR J 104 1 O LYS J 102 N VAL J 10 SHEET 3 AE2 4 ASP J 84 ASP J 91 -1 N TYR J 85 O THR J 101 SHEET 4 AE2 4 ALA J 94 PHE J 97 -1 O ALA J 94 N ASP J 91 SHEET 1 AE3 3 ALA J 18 SER J 23 0 SHEET 2 AE3 3 THR J 69 ILE J 74 -1 O ALA J 70 N CYS J 22 SHEET 3 AE3 3 SER J 62 SER J 66 -1 N SER J 62 O THR J 73 SHEET 1 AE4 4 VAL J 114 PHE J 117 0 SHEET 2 AE4 4 THR J 128 PHE J 138 -1 O LEU J 134 N PHE J 115 SHEET 3 AE4 4 TYR J 172 SER J 181 -1 O LEU J 174 N LEU J 135 SHEET 4 AE4 4 SER J 158 VAL J 162 -1 N SER J 161 O SER J 175 SHEET 1 AE5 3 LYS J 144 VAL J 149 0 SHEET 2 AE5 3 TYR J 191 THR J 196 -1 O GLU J 194 N GLN J 146 SHEET 3 AE5 3 VAL J 204 SER J 207 -1 O LYS J 206 N CYS J 193 SHEET 1 AE6 3 SER K 17 SER K 21 0 SHEET 2 AE6 3 TYR K 80 THR K 84 -1 O LEU K 83 N VAL K 18 SHEET 3 AE6 3 VAL K 68 THR K 71 -1 N THR K 71 O TYR K 80 SHEET 1 AE7 5 MET K 59 TYR K 60 0 SHEET 2 AE7 5 GLU K 46 PHE K 51 -1 N GLY K 50 O MET K 59 SHEET 3 AE7 5 VAL K 33 GLN K 39 -1 N ARG K 38 O GLU K 46 SHEET 4 AE7 5 VAL K 93 GLY K 99 -1 O GLY K 99 N VAL K 33 SHEET 5 AE7 5 THR K 113 LEU K 114 -1 O THR K 113 N TYR K 94 SHEET 1 AE8 4 SER K 125 LEU K 129 0 SHEET 2 AE8 4 THR K 140 TYR K 150 -1 O LEU K 146 N PHE K 127 SHEET 3 AE8 4 TYR K 181 PRO K 190 -1 O LEU K 183 N VAL K 147 SHEET 4 AE8 4 VAL K 168 THR K 170 -1 N HIS K 169 O VAL K 186 SHEET 1 AE9 4 SER K 125 LEU K 129 0 SHEET 2 AE9 4 THR K 140 TYR K 150 -1 O LEU K 146 N PHE K 127 SHEET 3 AE9 4 TYR K 181 PRO K 190 -1 O LEU K 183 N VAL K 147 SHEET 4 AE9 4 VAL K 174 LEU K 175 -1 N VAL K 174 O SER K 182 SHEET 1 AF1 3 THR K 156 TRP K 159 0 SHEET 2 AF1 3 ILE K 200 HIS K 205 -1 O ASN K 202 N SER K 158 SHEET 3 AF1 3 THR K 210 ARG K 215 -1 O THR K 210 N HIS K 205 SHEET 1 AF2 5 SER L 9 VAL L 12 0 SHEET 2 AF2 5 THR L 101 VAL L 105 1 O LYS L 102 N VAL L 10 SHEET 3 AF2 5 ALA L 83 ALA L 89 -1 N TYR L 85 O THR L 101 SHEET 4 AF2 5 SER L 33 GLN L 37 -1 N SER L 33 O GLN L 88 SHEET 5 AF2 5 VAL L 44 LEU L 47 -1 O VAL L 44 N GLN L 36 SHEET 1 AF3 4 SER L 9 VAL L 12 0 SHEET 2 AF3 4 THR L 101 VAL L 105 1 O LYS L 102 N VAL L 10 SHEET 3 AF3 4 ALA L 83 ALA L 89 -1 N TYR L 85 O THR L 101 SHEET 4 AF3 4 VAL L 96 PHE L 97 -1 O VAL L 96 N ALA L 89 SHEET 1 AF4 3 ALA L 18 SER L 23 0 SHEET 2 AF4 3 THR L 69 ILE L 74 -1 O LEU L 72 N ILE L 20 SHEET 3 AF4 3 PHE L 61 SER L 66 -1 N SER L 62 O THR L 73 SHEET 1 AF5 4 VAL L 114 PHE L 117 0 SHEET 2 AF5 4 THR L 128 PHE L 138 -1 O LEU L 134 N PHE L 115 SHEET 3 AF5 4 TYR L 172 SER L 181 -1 O LEU L 174 N LEU L 135 SHEET 4 AF5 4 SER L 158 VAL L 162 -1 N GLN L 159 O THR L 177 SHEET 1 AF6 3 LYS L 144 TRP L 147 0 SHEET 2 AF6 3 VAL L 190 THR L 196 -1 O GLU L 194 N GLN L 146 SHEET 3 AF6 3 VAL L 204 ASN L 209 -1 O LYS L 206 N CYS L 193 SSBOND 1 CYS A 429 CYS A 503 1555 1555 2.03 SSBOND 2 CYS A 452 CYS A 620 1555 1555 2.03 SSBOND 3 CYS A 459 CYS A 486 1555 1555 2.03 SSBOND 4 CYS A 494 CYS A 564 1555 1555 2.03 SSBOND 5 CYS A 508 CYS A 552 1555 1555 2.04 SSBOND 6 CYS A 569 CYS A 597 1555 1555 2.03 SSBOND 7 CYS A 581 CYS A 585 1555 1555 2.03 SSBOND 8 CYS A 607 CYS A 644 1555 1555 2.03 SSBOND 9 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 10 CYS E 145 CYS E 201 1555 1555 2.03 SSBOND 11 CYS F 22 CYS F 87 1555 1555 2.04 SSBOND 12 CYS F 133 CYS F 193 1555 1555 2.03 SSBOND 13 CYS D 429 CYS D 503 1555 1555 2.03 SSBOND 14 CYS D 452 CYS D 620 1555 1555 2.03 SSBOND 15 CYS D 459 CYS D 486 1555 1555 2.03 SSBOND 16 CYS D 494 CYS D 564 1555 1555 2.03 SSBOND 17 CYS D 508 CYS D 552 1555 1555 2.03 SSBOND 18 CYS D 569 CYS D 597 1555 1555 2.03 SSBOND 19 CYS D 607 CYS D 644 1555 1555 2.03 SSBOND 20 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 21 CYS B 145 CYS B 201 1555 1555 2.03 SSBOND 22 CYS C 22 CYS C 87 1555 1555 2.03 SSBOND 23 CYS C 133 CYS C 193 1555 1555 2.04 SSBOND 24 CYS G 429 CYS G 503 1555 1555 2.03 SSBOND 25 CYS G 452 CYS G 620 1555 1555 2.03 SSBOND 26 CYS G 459 CYS G 486 1555 1555 2.03 SSBOND 27 CYS G 494 CYS G 564 1555 1555 2.03 SSBOND 28 CYS G 508 CYS G 552 1555 1555 2.04 SSBOND 29 CYS G 569 CYS G 597 1555 1555 2.03 SSBOND 30 CYS G 581 CYS G 585 1555 1555 2.03 SSBOND 31 CYS G 607 CYS G 644 1555 1555 2.03 SSBOND 32 CYS I 22 CYS I 96 1555 1555 2.03 SSBOND 33 CYS I 145 CYS I 201 1555 1555 2.03 SSBOND 34 CYS I 221 CYS L 213 1555 1555 2.03 SSBOND 35 CYS J 22 CYS J 87 1555 1555 2.04 SSBOND 36 CYS J 133 CYS J 193 1555 1555 2.04 SSBOND 37 CYS K 22 CYS K 96 1555 1555 2.03 SSBOND 38 CYS K 145 CYS K 201 1555 1555 2.03 SSBOND 39 CYS L 22 CYS L 87 1555 1555 2.03 SSBOND 40 CYS L 133 CYS L 193 1555 1555 2.04 LINK ND2 ASN A 423 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN A 540 C1 NAG A 701 1555 1555 1.45 LINK ND2 ASN A 556 C1 NAG H 1 1555 1555 1.45 LINK ND2 ASN D 423 C1 NAG M 1 1555 1555 1.45 LINK ND2 ASN G 423 C1 NAG N 1 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.46 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 CISPEP 1 THR A 510 PRO A 511 0 25.62 CISPEP 2 PHE E 151 PRO E 152 0 -0.67 CISPEP 3 GLU E 153 PRO E 154 0 -6.62 CISPEP 4 TYR F 139 PRO F 140 0 0.61 CISPEP 5 THR D 510 PRO D 511 0 22.41 CISPEP 6 PHE B 151 PRO B 152 0 -3.82 CISPEP 7 GLU B 153 PRO B 154 0 -1.54 CISPEP 8 THR G 510 PRO G 511 0 20.62 CISPEP 9 PHE I 151 PRO I 152 0 -2.91 CISPEP 10 GLU I 153 PRO I 154 0 -0.02 CISPEP 11 PHE K 151 PRO K 152 0 -0.57 CISPEP 12 GLU K 153 PRO K 154 0 -3.44 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