HEADER IMMUNE SYSTEM 11-FEB-25 9NAB TITLE CRYO-EM STRUCTURE OF THE ALPHA5BETA1 INTEGRIN HEADPIECE WITH OS2966 TITLE 2 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTEGRIN BETA-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FIBRONECTIN RECEPTOR SUBUNIT BETA,GLYCOPROTEIN IIA,GPIIA, COMPND 5 VLA-4 SUBUNIT BETA; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HUMAN INTEGRIN ALPHA 5; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: IGG HEAVY CHAIN; COMPND 13 CHAIN: D; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: IGG LIGHT CHAIN; COMPND 17 CHAIN: C; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ITGB1, FNRB, MDF2, MSK12; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_TAXID: 10090; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 20 ORGANISM_TAXID: 10090; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INTEGRIN ANTIBODY, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR L.WANG,C.ZHANG REVDAT 1 23-JUL-25 9NAB 0 JRNL AUTH N.SONG,S.CHEN,L.WANG,J.DANG,X.CAO,S.SINGH,L.YANG,J.WANG, JRNL AUTH 2 S.T.ROSEN,Y.WANG,C.D.CHEN,C.ZHANG,M.FENG JRNL TITL ITGB1 REGULATES TRIPLE-NEGATIVE BREAST CANCER DEVELOPMENT BY JRNL TITL 2 MODULATING THE TUMOR MICROENVIRONMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.540 REMARK 3 NUMBER OF PARTICLES : 191874 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 9NAB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000292804. 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 : HUMAN INTEGRIN ALPHA5BETA1 REMARK 245 HEADPIECE IN COMPLEX WITH THE REMARK 245 FAB FRAGMENT OF OS2966 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 : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C 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 GLN A 21 REMARK 465 THR A 22 REMARK 465 ASP A 23 REMARK 465 GLU A 24 REMARK 465 ASN A 25 REMARK 465 ARG A 26 REMARK 465 CYS A 27 REMARK 465 LEU A 28 REMARK 465 LYS A 29 REMARK 465 ALA A 30 REMARK 465 ASN A 31 REMARK 465 ALA A 32 REMARK 465 LYS A 33 REMARK 465 SER A 34 REMARK 465 CYS A 35 REMARK 465 GLY A 36 REMARK 465 GLU A 37 REMARK 465 CYS A 38 REMARK 465 ILE A 39 REMARK 465 GLN A 40 REMARK 465 ALA A 41 REMARK 465 GLY A 42 REMARK 465 PRO A 43 REMARK 465 ASN A 44 REMARK 465 CYS A 45 REMARK 465 GLY A 46 REMARK 465 TRP A 47 REMARK 465 CYS A 48 REMARK 465 THR A 49 REMARK 465 ASN A 50 REMARK 465 SER A 51 REMARK 465 THR A 52 REMARK 465 PHE A 53 REMARK 465 LEU A 54 REMARK 465 GLN A 55 REMARK 465 GLU A 56 REMARK 465 GLY A 57 REMARK 465 MET A 58 REMARK 465 PRO A 59 REMARK 465 THR A 60 REMARK 465 SER A 61 REMARK 465 ALA A 62 REMARK 465 ARG A 63 REMARK 465 CYS A 64 REMARK 465 ASP A 65 REMARK 465 ASP A 66 REMARK 465 LEU A 67 REMARK 465 GLU A 68 REMARK 465 ALA A 69 REMARK 465 LEU A 70 REMARK 465 LYS A 71 REMARK 465 LYS A 72 REMARK 465 LYS A 73 REMARK 465 GLY A 74 REMARK 465 CYS A 75 REMARK 465 PRO A 76 REMARK 465 PRO A 77 REMARK 465 ASP A 78 REMARK 465 ASP A 79 REMARK 465 ILE A 80 REMARK 465 GLU A 81 REMARK 465 ASN A 82 REMARK 465 PRO A 83 REMARK 465 ARG A 84 REMARK 465 ARG A 98 REMARK 465 SER A 99 REMARK 465 LYS A 100 REMARK 465 GLY A 101 REMARK 465 THR A 102 REMARK 465 ALA A 103 REMARK 465 GLU A 104 REMARK 465 LYS A 105 REMARK 465 LEU A 106 REMARK 465 LYS A 107 REMARK 465 PRO A 108 REMARK 465 GLU A 109 REMARK 465 ASP A 110 REMARK 465 LYS A 434 REMARK 465 CYS A 435 REMARK 465 PRO A 436 REMARK 465 LYS A 437 REMARK 465 LYS A 438 REMARK 465 ASP A 439 REMARK 465 ILE A 461 REMARK 465 CYS A 462 REMARK 465 GLU A 463 REMARK 465 CYS A 464 REMARK 465 GLU A 465 REMARK 465 GLY A 466 REMARK 465 GLY A 467 REMARK 465 LEU A 468 REMARK 465 GLU A 469 REMARK 465 ASN A 470 REMARK 465 LEU A 471 REMARK 465 TYR A 472 REMARK 465 PHE A 473 REMARK 465 GLN A 474 REMARK 465 GLY A 475 REMARK 465 GLY A 476 REMARK 465 LYS A 477 REMARK 465 ASN A 478 REMARK 465 ALA A 479 REMARK 465 GLN A 480 REMARK 465 CYS A 481 REMARK 465 LYS A 482 REMARK 465 LYS A 483 REMARK 465 LYS A 484 REMARK 465 LEU A 485 REMARK 465 GLN A 486 REMARK 465 ALA A 487 REMARK 465 LEU A 488 REMARK 465 LYS A 489 REMARK 465 LYS A 490 REMARK 465 LYS A 491 REMARK 465 ASN A 492 REMARK 465 ALA A 493 REMARK 465 GLN A 494 REMARK 465 LEU A 495 REMARK 465 LYS A 496 REMARK 465 TRP A 497 REMARK 465 LYS A 498 REMARK 465 LEU A 499 REMARK 465 GLN A 500 REMARK 465 ALA A 501 REMARK 465 LEU A 502 REMARK 465 LYS A 503 REMARK 465 LYS A 504 REMARK 465 LYS A 505 REMARK 465 LEU A 506 REMARK 465 ALA A 507 REMARK 465 GLN A 508 REMARK 465 GLY A 509 REMARK 465 GLY A 510 REMARK 465 HIS A 511 REMARK 465 HIS A 512 REMARK 465 HIS A 513 REMARK 465 HIS A 514 REMARK 465 HIS A 515 REMARK 465 HIS A 516 REMARK 465 HIS A 517 REMARK 465 HIS A 518 REMARK 465 PHE B 42 REMARK 465 ASN B 43 REMARK 465 LEU B 44 REMARK 465 ASP B 45 REMARK 465 ALA B 46 REMARK 465 GLU B 47 REMARK 465 GLY B 70 REMARK 465 THR B 71 REMARK 465 ASP B 72 REMARK 465 GLY B 73 REMARK 465 PRO B 100 REMARK 465 TRP B 101 REMARK 465 GLY B 102 REMARK 465 ALA B 103 REMARK 465 SER B 104 REMARK 465 PRO B 105 REMARK 465 THR B 106 REMARK 465 SER B 123 REMARK 465 SER B 124 REMARK 465 LEU B 125 REMARK 465 SER B 126 REMARK 465 SER B 127 REMARK 465 SER B 128 REMARK 465 GLU B 129 REMARK 465 GLY B 130 REMARK 465 ARG B 490 REMARK 465 PRO B 491 REMARK 465 ILE B 492 REMARK 465 VAL B 493 REMARK 465 SER B 494 REMARK 465 ALA B 495 REMARK 465 SER B 496 REMARK 465 ALA B 497 REMARK 465 SER B 498 REMARK 465 LEU B 499 REMARK 465 THR B 500 REMARK 465 ILE B 501 REMARK 465 PHE B 502 REMARK 465 PRO B 503 REMARK 465 ALA B 504 REMARK 465 MET B 505 REMARK 465 PHE B 506 REMARK 465 ASN B 507 REMARK 465 PRO B 508 REMARK 465 GLU B 509 REMARK 465 GLU B 510 REMARK 465 ARG B 511 REMARK 465 SER B 512 REMARK 465 CYS B 513 REMARK 465 SER B 514 REMARK 465 LEU B 515 REMARK 465 GLU B 516 REMARK 465 GLY B 517 REMARK 465 ASN B 518 REMARK 465 PRO B 519 REMARK 465 VAL B 520 REMARK 465 ALA B 521 REMARK 465 CYS B 522 REMARK 465 ILE B 523 REMARK 465 ASN B 524 REMARK 465 LEU B 525 REMARK 465 SER B 526 REMARK 465 PHE B 527 REMARK 465 CYS B 528 REMARK 465 LEU B 529 REMARK 465 ASN B 530 REMARK 465 ALA B 531 REMARK 465 SER B 532 REMARK 465 GLY B 533 REMARK 465 LYS B 534 REMARK 465 HIS B 535 REMARK 465 VAL B 536 REMARK 465 ALA B 537 REMARK 465 ASP B 538 REMARK 465 SER B 539 REMARK 465 ILE B 540 REMARK 465 GLY B 541 REMARK 465 PHE B 542 REMARK 465 THR B 543 REMARK 465 VAL B 544 REMARK 465 GLU B 545 REMARK 465 LEU B 546 REMARK 465 GLN B 547 REMARK 465 LEU B 548 REMARK 465 ASP B 549 REMARK 465 TRP B 550 REMARK 465 GLN B 551 REMARK 465 LYS B 552 REMARK 465 GLN B 553 REMARK 465 LYS B 554 REMARK 465 GLY B 555 REMARK 465 GLY B 556 REMARK 465 VAL B 557 REMARK 465 ARG B 558 REMARK 465 ARG B 559 REMARK 465 ALA B 560 REMARK 465 LEU B 561 REMARK 465 PHE B 562 REMARK 465 LEU B 563 REMARK 465 ALA B 564 REMARK 465 SER B 565 REMARK 465 ARG B 566 REMARK 465 GLN B 567 REMARK 465 ALA B 568 REMARK 465 THR B 569 REMARK 465 LEU B 570 REMARK 465 THR B 571 REMARK 465 GLN B 572 REMARK 465 THR B 573 REMARK 465 LEU B 574 REMARK 465 LEU B 575 REMARK 465 ILE B 576 REMARK 465 GLN B 577 REMARK 465 ASN B 578 REMARK 465 GLY B 579 REMARK 465 ALA B 580 REMARK 465 ARG B 581 REMARK 465 GLU B 582 REMARK 465 ASP B 583 REMARK 465 CYS B 584 REMARK 465 ARG B 585 REMARK 465 GLU B 586 REMARK 465 MET B 587 REMARK 465 LYS B 588 REMARK 465 ILE B 589 REMARK 465 TYR B 590 REMARK 465 LEU B 591 REMARK 465 ARG B 592 REMARK 465 ASN B 593 REMARK 465 GLU B 594 REMARK 465 SER B 595 REMARK 465 GLU B 596 REMARK 465 PHE B 597 REMARK 465 ARG B 598 REMARK 465 ASP B 599 REMARK 465 LYS B 600 REMARK 465 LEU B 601 REMARK 465 SER B 602 REMARK 465 PRO B 603 REMARK 465 ILE B 604 REMARK 465 HIS B 605 REMARK 465 ILE B 606 REMARK 465 ALA B 607 REMARK 465 LEU B 608 REMARK 465 ASN B 609 REMARK 465 PHE B 610 REMARK 465 SER B 611 REMARK 465 LEU B 612 REMARK 465 ASP B 613 REMARK 465 PRO B 614 REMARK 465 GLN B 615 REMARK 465 ALA B 616 REMARK 465 PRO B 617 REMARK 465 VAL B 618 REMARK 465 ASP B 619 REMARK 465 SER B 620 REMARK 465 HIS B 621 REMARK 465 GLY B 622 REMARK 465 LEU B 623 REMARK 465 ARG B 624 REMARK 465 PRO B 625 REMARK 465 ALA B 626 REMARK 465 LEU B 627 REMARK 465 HIS B 628 REMARK 465 TYR B 629 REMARK 465 GLN B 630 REMARK 465 SER B 631 REMARK 465 LYS B 632 REMARK 465 SER B 633 REMARK 465 ARG B 634 REMARK 465 ILE B 635 REMARK 465 GLU B 636 REMARK 465 ASP B 637 REMARK 465 LYS B 638 REMARK 465 ALA B 639 REMARK 465 GLN B 640 REMARK 465 ILE B 641 REMARK 465 LEU B 642 REMARK 465 LEU B 643 REMARK 465 ASP B 644 REMARK 465 CYS B 645 REMARK 465 GLY B 646 REMARK 465 GLU B 647 REMARK 465 ASP B 648 REMARK 465 ASN B 649 REMARK 465 ILE B 650 REMARK 465 CYS B 651 REMARK 465 VAL B 652 REMARK 465 PRO B 653 REMARK 465 ASP B 654 REMARK 465 LEU B 655 REMARK 465 GLN B 656 REMARK 465 LEU B 657 REMARK 465 GLU B 658 REMARK 465 VAL B 659 REMARK 465 PHE B 660 REMARK 465 GLY B 661 REMARK 465 GLU B 662 REMARK 465 GLN B 663 REMARK 465 ASN B 664 REMARK 465 GLY B 665 REMARK 465 GLY B 666 REMARK 465 LEU B 667 REMARK 465 GLU B 668 REMARK 465 ASN B 669 REMARK 465 LEU B 670 REMARK 465 TYR B 671 REMARK 465 PHE B 672 REMARK 465 GLN B 673 REMARK 465 GLY B 674 REMARK 465 GLY B 675 REMARK 465 GLU B 676 REMARK 465 ASN B 677 REMARK 465 ALA B 678 REMARK 465 GLN B 679 REMARK 465 CYS B 680 REMARK 465 GLU B 681 REMARK 465 LYS B 682 REMARK 465 GLU B 683 REMARK 465 LEU B 684 REMARK 465 GLN B 685 REMARK 465 ALA B 686 REMARK 465 LEU B 687 REMARK 465 GLU B 688 REMARK 465 LYS B 689 REMARK 465 GLU B 690 REMARK 465 ASN B 691 REMARK 465 ALA B 692 REMARK 465 GLN B 693 REMARK 465 LEU B 694 REMARK 465 GLU B 695 REMARK 465 TRP B 696 REMARK 465 GLU B 697 REMARK 465 LEU B 698 REMARK 465 GLN B 699 REMARK 465 ALA B 700 REMARK 465 LEU B 701 REMARK 465 GLU B 702 REMARK 465 LYS B 703 REMARK 465 GLU B 704 REMARK 465 LEU B 705 REMARK 465 ALA B 706 REMARK 465 GLN B 707 REMARK 465 TRP B 708 REMARK 465 SER B 709 REMARK 465 HIS B 710 REMARK 465 PRO B 711 REMARK 465 GLN B 712 REMARK 465 PHE B 713 REMARK 465 GLU B 714 REMARK 465 LYS B 715 REMARK 465 GLY B 716 REMARK 465 GLY B 717 REMARK 465 GLY B 718 REMARK 465 SER B 719 REMARK 465 GLY B 720 REMARK 465 GLY B 721 REMARK 465 GLY B 722 REMARK 465 SER B 723 REMARK 465 GLY B 724 REMARK 465 GLY B 725 REMARK 465 SER B 726 REMARK 465 ALA B 727 REMARK 465 TRP B 728 REMARK 465 SER B 729 REMARK 465 HIS B 730 REMARK 465 PRO B 731 REMARK 465 GLN B 732 REMARK 465 PHE B 733 REMARK 465 GLU B 734 REMARK 465 LYS B 735 REMARK 465 PRO D 153 REMARK 465 CYS D 154 REMARK 465 SER D 155 REMARK 465 ARG D 156 REMARK 465 SER D 157 REMARK 465 THR D 158 REMARK 465 SER D 159 REMARK 465 GLU D 160 REMARK 465 SER D 161 REMARK 465 THR D 162 REMARK 465 ALA D 163 REMARK 465 ALA D 164 REMARK 465 THR D 178 REMARK 465 VAL D 179 REMARK 465 SER D 180 REMARK 465 TRP D 181 REMARK 465 ASN D 182 REMARK 465 SER D 183 REMARK 465 GLY D 184 REMARK 465 ALA D 185 REMARK 465 LEU D 186 REMARK 465 THR D 187 REMARK 465 SER D 188 REMARK 465 GLY D 189 REMARK 465 VAL D 190 REMARK 465 HIS D 191 REMARK 465 THR D 192 REMARK 465 VAL D 209 REMARK 465 THR D 210 REMARK 465 VAL D 211 REMARK 465 PRO D 212 REMARK 465 SER D 213 REMARK 465 SER D 214 REMARK 465 SER D 215 REMARK 465 LEU D 216 REMARK 465 GLY D 217 REMARK 465 THR D 218 REMARK 465 LYS D 219 REMARK 465 THR D 220 REMARK 465 LYS D 241 REMARK 465 TYR D 242 REMARK 465 GLY D 243 REMARK 465 PRO D 244 REMARK 465 PRO D 245 REMARK 465 CYS D 246 REMARK 465 PRO D 247 REMARK 465 PRO D 248 REMARK 465 CYS D 249 REMARK 465 ASP C 29 REMARK 465 ALA C 140 REMARK 465 PRO C 141 REMARK 465 SER C 142 REMARK 465 VAL C 143 REMARK 465 PHE C 144 REMARK 465 ILE C 145 REMARK 465 PHE C 146 REMARK 465 PRO C 147 REMARK 465 PRO C 148 REMARK 465 SER C 149 REMARK 465 ASP C 150 REMARK 465 GLU C 151 REMARK 465 GLN C 152 REMARK 465 LEU C 153 REMARK 465 LYS C 154 REMARK 465 SER C 155 REMARK 465 GLY C 156 REMARK 465 THR C 157 REMARK 465 ALA C 158 REMARK 465 GLU C 171 REMARK 465 ALA C 172 REMARK 465 LYS C 173 REMARK 465 VAL C 174 REMARK 465 GLN C 175 REMARK 465 TRP C 176 REMARK 465 LYS C 177 REMARK 465 VAL C 178 REMARK 465 ASP C 179 REMARK 465 ASN C 180 REMARK 465 ALA C 181 REMARK 465 LEU C 182 REMARK 465 GLN C 183 REMARK 465 SER C 184 REMARK 465 GLY C 185 REMARK 465 THR C 208 REMARK 465 LEU C 209 REMARK 465 SER C 210 REMARK 465 LYS C 211 REMARK 465 ALA C 212 REMARK 465 ASP C 213 REMARK 465 TYR C 214 REMARK 465 GLU C 215 REMARK 465 LYS C 216 REMARK 465 HIS C 217 REMARK 465 LYS C 218 REMARK 465 VAL C 219 REMARK 465 TYR C 220 REMARK 465 ALA C 221 REMARK 465 CYS C 222 REMARK 465 GLU C 223 REMARK 465 VAL C 224 REMARK 465 THR C 225 REMARK 465 HIS C 226 REMARK 465 GLN C 227 REMARK 465 GLY C 228 REMARK 465 LEU C 229 REMARK 465 SER C 230 REMARK 465 SER C 231 REMARK 465 PRO C 232 REMARK 465 VAL C 233 REMARK 465 THR C 234 REMARK 465 LYS C 235 REMARK 465 SER C 236 REMARK 465 PHE C 237 REMARK 465 ASN C 238 REMARK 465 ARG C 239 REMARK 465 GLY C 240 REMARK 465 GLU C 241 REMARK 465 CYS C 242 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 LEU A 458 CA - CB - CG ANGL. DEV. = 16.3 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 ARG A 124 -91.24 -129.59 REMARK 500 VAL A 188 -64.92 -123.64 REMARK 500 THR A 191 50.48 -91.62 REMARK 500 MET A 310 33.63 -96.01 REMARK 500 PRO A 343 2.64 -66.69 REMARK 500 VAL A 344 -61.79 -99.65 REMARK 500 SER A 432 -113.04 57.89 REMARK 500 SER B 58 12.40 -141.60 REMARK 500 ARG B 68 80.54 -161.07 REMARK 500 SER B 170 54.75 -94.32 REMARK 500 ASN B 182 60.23 60.23 REMARK 500 ALA B 199 -5.99 74.87 REMARK 500 THR B 299 13.04 54.93 REMARK 500 ARG B 312 -141.80 49.98 REMARK 500 ASP B 352 116.76 -161.59 REMARK 500 ASP B 387 150.29 -48.25 REMARK 500 ALA B 459 115.64 -162.08 REMARK 500 ASP D 120 -11.86 74.72 REMARK 500 TYR D 122 -135.17 57.63 REMARK 500 SER D 140 33.82 -99.23 REMARK 500 ASN C 60 64.27 -100.35 REMARK 500 ALA C 79 -7.78 72.52 REMARK 500 HIS C 80 -32.43 -131.30 REMARK 500 ASN C 166 61.65 61.77 REMARK 500 PRO C 169 -162.10 -77.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 122 0.17 SIDE CHAIN REMARK 500 ARG A 124 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49184 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE ALPHA5BETA1 INTEGRIN HEADPIECE WITH OS2966 REMARK 900 FAB DBREF 9NAB A 21 465 UNP P05556 ITB1_HUMAN 21 465 DBREF 9NAB B 42 735 PDB 9NAB 9NAB 42 735 DBREF 9NAB D 20 249 PDB 9NAB 9NAB 20 249 DBREF 9NAB C 29 242 PDB 9NAB 9NAB 29 242 SEQADV 9NAB GLY A 466 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLY A 467 UNP P05556 EXPRESSION TAG SEQADV 9NAB LEU A 468 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLU A 469 UNP P05556 EXPRESSION TAG SEQADV 9NAB ASN A 470 UNP P05556 EXPRESSION TAG SEQADV 9NAB LEU A 471 UNP P05556 EXPRESSION TAG SEQADV 9NAB TYR A 472 UNP P05556 EXPRESSION TAG SEQADV 9NAB PHE A 473 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLN A 474 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLY A 475 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLY A 476 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 477 UNP P05556 EXPRESSION TAG SEQADV 9NAB ASN A 478 UNP P05556 EXPRESSION TAG SEQADV 9NAB ALA A 479 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLN A 480 UNP P05556 EXPRESSION TAG SEQADV 9NAB CYS A 481 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 482 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 483 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 484 UNP P05556 EXPRESSION TAG SEQADV 9NAB LEU A 485 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLN A 486 UNP P05556 EXPRESSION TAG SEQADV 9NAB ALA A 487 UNP P05556 EXPRESSION TAG SEQADV 9NAB LEU A 488 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 489 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 490 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 491 UNP P05556 EXPRESSION TAG SEQADV 9NAB ASN A 492 UNP P05556 EXPRESSION TAG SEQADV 9NAB ALA A 493 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLN A 494 UNP P05556 EXPRESSION TAG SEQADV 9NAB LEU A 495 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 496 UNP P05556 EXPRESSION TAG SEQADV 9NAB TRP A 497 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 498 UNP P05556 EXPRESSION TAG SEQADV 9NAB LEU A 499 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLN A 500 UNP P05556 EXPRESSION TAG SEQADV 9NAB ALA A 501 UNP P05556 EXPRESSION TAG SEQADV 9NAB LEU A 502 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 503 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 504 UNP P05556 EXPRESSION TAG SEQADV 9NAB LYS A 505 UNP P05556 EXPRESSION TAG SEQADV 9NAB LEU A 506 UNP P05556 EXPRESSION TAG SEQADV 9NAB ALA A 507 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLN A 508 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLY A 509 UNP P05556 EXPRESSION TAG SEQADV 9NAB GLY A 510 UNP P05556 EXPRESSION TAG SEQADV 9NAB HIS A 511 UNP P05556 EXPRESSION TAG SEQADV 9NAB HIS A 512 UNP P05556 EXPRESSION TAG SEQADV 9NAB HIS A 513 UNP P05556 EXPRESSION TAG SEQADV 9NAB HIS A 514 UNP P05556 EXPRESSION TAG SEQADV 9NAB HIS A 515 UNP P05556 EXPRESSION TAG SEQADV 9NAB HIS A 516 UNP P05556 EXPRESSION TAG SEQADV 9NAB HIS A 517 UNP P05556 EXPRESSION TAG SEQADV 9NAB HIS A 518 UNP P05556 EXPRESSION TAG SEQRES 1 A 498 GLN THR ASP GLU ASN ARG CYS LEU LYS ALA ASN ALA LYS SEQRES 2 A 498 SER CYS GLY GLU CYS ILE GLN ALA GLY PRO ASN CYS GLY SEQRES 3 A 498 TRP CYS THR ASN SER THR PHE LEU GLN GLU GLY MET PRO SEQRES 4 A 498 THR SER ALA ARG CYS ASP ASP LEU GLU ALA LEU LYS LYS SEQRES 5 A 498 LYS GLY CYS PRO PRO ASP ASP ILE GLU ASN PRO ARG GLY SEQRES 6 A 498 SER LYS ASP ILE LYS LYS ASN LYS ASN VAL THR ASN ARG SEQRES 7 A 498 SER LYS GLY THR ALA GLU LYS LEU LYS PRO GLU ASP ILE SEQRES 8 A 498 THR GLN ILE GLN PRO GLN GLN LEU VAL LEU ARG LEU ARG SEQRES 9 A 498 SER GLY GLU PRO GLN THR PHE THR LEU LYS PHE LYS ARG SEQRES 10 A 498 ALA GLU ASP TYR PRO ILE ASP LEU TYR TYR LEU MET ASP SEQRES 11 A 498 LEU SER TYR SER MET LYS ASP ASP LEU GLU ASN VAL LYS SEQRES 12 A 498 SER LEU GLY THR ASP LEU MET ASN GLU MET ARG ARG ILE SEQRES 13 A 498 THR SER ASP PHE ARG ILE GLY PHE GLY SER PHE VAL GLU SEQRES 14 A 498 LYS THR VAL MET PRO TYR ILE SER THR THR PRO ALA LYS SEQRES 15 A 498 LEU ARG ASN PRO CYS THR SER GLU GLN ASN CYS THR SER SEQRES 16 A 498 PRO PHE SER TYR LYS ASN VAL LEU SER LEU THR ASN LYS SEQRES 17 A 498 GLY GLU VAL PHE ASN GLU LEU VAL GLY LYS GLN ARG ILE SEQRES 18 A 498 SER GLY ASN LEU ASP SER PRO GLU GLY GLY PHE ASP ALA SEQRES 19 A 498 ILE MET GLN VAL ALA VAL CYS GLY SER LEU ILE GLY TRP SEQRES 20 A 498 ARG ASN VAL THR ARG LEU LEU VAL PHE SER THR ASP ALA SEQRES 21 A 498 GLY PHE HIS PHE ALA GLY ASP GLY LYS LEU GLY GLY ILE SEQRES 22 A 498 VAL LEU PRO ASN ASP GLY GLN CYS HIS LEU GLU ASN ASN SEQRES 23 A 498 MET TYR THR MET SER HIS TYR TYR ASP TYR PRO SER ILE SEQRES 24 A 498 ALA HIS LEU VAL GLN LYS LEU SER GLU ASN ASN ILE GLN SEQRES 25 A 498 THR ILE PHE ALA VAL THR GLU GLU PHE GLN PRO VAL TYR SEQRES 26 A 498 LYS GLU LEU LYS ASN LEU ILE PRO LYS SER ALA VAL GLY SEQRES 27 A 498 THR LEU SER ALA ASN SER SER ASN VAL ILE GLN LEU ILE SEQRES 28 A 498 ILE ASP ALA TYR ASN SER LEU SER SER GLU VAL ILE LEU SEQRES 29 A 498 GLU ASN GLY LYS LEU SER GLU GLY VAL THR ILE SER TYR SEQRES 30 A 498 LYS SER TYR CYS LYS ASN GLY VAL ASN GLY THR GLY GLU SEQRES 31 A 498 ASN GLY ARG LYS CYS SER ASN ILE SER ILE GLY ASP GLU SEQRES 32 A 498 VAL GLN PHE GLU ILE SER ILE THR SER ASN LYS CYS PRO SEQRES 33 A 498 LYS LYS ASP SER ASP SER PHE LYS ILE ARG PRO LEU GLY SEQRES 34 A 498 PHE THR GLU GLU VAL GLU VAL ILE LEU GLN TYR ILE CYS SEQRES 35 A 498 GLU CYS GLU GLY GLY LEU GLU ASN LEU TYR PHE GLN GLY SEQRES 36 A 498 GLY LYS ASN ALA GLN CYS LYS LYS LYS LEU GLN ALA LEU SEQRES 37 A 498 LYS LYS LYS ASN ALA GLN LEU LYS TRP LYS LEU GLN ALA SEQRES 38 A 498 LEU LYS LYS LYS LEU ALA GLN GLY GLY HIS HIS HIS HIS SEQRES 39 A 498 HIS HIS HIS HIS SEQRES 1 B 694 PHE ASN LEU ASP ALA GLU ALA PRO ALA VAL LEU SER GLY SEQRES 2 B 694 PRO PRO GLY SER PHE PHE GLY PHE SER VAL GLU PHE TYR SEQRES 3 B 694 ARG PRO GLY THR ASP GLY VAL SER VAL LEU VAL GLY ALA SEQRES 4 B 694 PRO LYS ALA ASN THR SER GLN PRO GLY VAL LEU GLN GLY SEQRES 5 B 694 GLY ALA VAL TYR LEU CYS PRO TRP GLY ALA SER PRO THR SEQRES 6 B 694 GLN CYS THR PRO ILE GLU PHE ASP SER LYS GLY SER ARG SEQRES 7 B 694 LEU LEU GLU SER SER LEU SER SER SER GLU GLY GLU GLU SEQRES 8 B 694 PRO VAL GLU TYR LYS SER LEU GLN TRP PHE GLY ALA THR SEQRES 9 B 694 VAL ARG ALA HIS GLY SER SER ILE LEU ALA CYS ALA PRO SEQRES 10 B 694 LEU TYR SER TRP ARG THR GLU LYS GLU PRO LEU SER ASP SEQRES 11 B 694 PRO VAL GLY THR CYS TYR LEU SER THR ASP ASN PHE THR SEQRES 12 B 694 ARG ILE LEU GLU TYR ALA PRO CYS ARG SER ASP PHE SER SEQRES 13 B 694 TRP ALA ALA GLY GLN GLY TYR CYS GLN GLY GLY PHE SER SEQRES 14 B 694 ALA GLU PHE THR LYS THR GLY ARG VAL VAL LEU GLY GLY SEQRES 15 B 694 PRO GLY SER TYR PHE TRP GLN GLY GLN ILE LEU SER ALA SEQRES 16 B 694 THR GLN GLU GLN ILE ALA GLU SER TYR TYR PRO GLU TYR SEQRES 17 B 694 LEU ILE ASN LEU VAL GLN GLY GLN LEU GLN THR ARG GLN SEQRES 18 B 694 ALA SER SER ILE TYR ASP ASP SER TYR LEU GLY TYR SER SEQRES 19 B 694 VAL ALA VAL GLY GLU PHE SER GLY ASP ASP THR GLU ASP SEQRES 20 B 694 PHE VAL ALA GLY VAL PRO LYS GLY ASN LEU THR TYR GLY SEQRES 21 B 694 TYR VAL THR ILE LEU ASN GLY SER ASP ILE ARG SER LEU SEQRES 22 B 694 TYR ASN PHE SER GLY GLU GLN MET ALA SER TYR PHE GLY SEQRES 23 B 694 TYR ALA VAL ALA ALA THR ASP VAL ASN GLY ASP GLY LEU SEQRES 24 B 694 ASP ASP LEU LEU VAL GLY ALA PRO LEU LEU MET ASP ARG SEQRES 25 B 694 THR PRO ASP GLY ARG PRO GLN GLU VAL GLY ARG VAL TYR SEQRES 26 B 694 VAL TYR LEU GLN HIS PRO ALA GLY ILE GLU PRO THR PRO SEQRES 27 B 694 THR LEU THR LEU THR GLY HIS ASP GLU PHE GLY ARG PHE SEQRES 28 B 694 GLY SER SER LEU THR PRO LEU GLY ASP LEU ASP GLN ASP SEQRES 29 B 694 GLY TYR ASN ASP VAL ALA ILE GLY ALA PRO PHE GLY GLY SEQRES 30 B 694 GLU THR GLN GLN GLY VAL VAL PHE VAL PHE PRO GLY GLY SEQRES 31 B 694 PRO GLY GLY LEU GLY SER LYS PRO SER GLN VAL LEU GLN SEQRES 32 B 694 PRO LEU TRP ALA ALA SER HIS THR PRO ASP PHE PHE GLY SEQRES 33 B 694 SER ALA LEU ARG GLY GLY ARG ASP LEU ASP GLY ASN GLY SEQRES 34 B 694 TYR PRO ASP LEU ILE VAL GLY SER PHE GLY VAL ASP LYS SEQRES 35 B 694 ALA VAL VAL TYR ARG GLY ARG PRO ILE VAL SER ALA SER SEQRES 36 B 694 ALA SER LEU THR ILE PHE PRO ALA MET PHE ASN PRO GLU SEQRES 37 B 694 GLU ARG SER CYS SER LEU GLU GLY ASN PRO VAL ALA CYS SEQRES 38 B 694 ILE ASN LEU SER PHE CYS LEU ASN ALA SER GLY LYS HIS SEQRES 39 B 694 VAL ALA ASP SER ILE GLY PHE THR VAL GLU LEU GLN LEU SEQRES 40 B 694 ASP TRP GLN LYS GLN LYS GLY GLY VAL ARG ARG ALA LEU SEQRES 41 B 694 PHE LEU ALA SER ARG GLN ALA THR LEU THR GLN THR LEU SEQRES 42 B 694 LEU ILE GLN ASN GLY ALA ARG GLU ASP CYS ARG GLU MET SEQRES 43 B 694 LYS ILE TYR LEU ARG ASN GLU SER GLU PHE ARG ASP LYS SEQRES 44 B 694 LEU SER PRO ILE HIS ILE ALA LEU ASN PHE SER LEU ASP SEQRES 45 B 694 PRO GLN ALA PRO VAL ASP SER HIS GLY LEU ARG PRO ALA SEQRES 46 B 694 LEU HIS TYR GLN SER LYS SER ARG ILE GLU ASP LYS ALA SEQRES 47 B 694 GLN ILE LEU LEU ASP CYS GLY GLU ASP ASN ILE CYS VAL SEQRES 48 B 694 PRO ASP LEU GLN LEU GLU VAL PHE GLY GLU GLN ASN GLY SEQRES 49 B 694 GLY LEU GLU ASN LEU TYR PHE GLN GLY GLY GLU ASN ALA SEQRES 50 B 694 GLN CYS GLU LYS GLU LEU GLN ALA LEU GLU LYS GLU ASN SEQRES 51 B 694 ALA GLN LEU GLU TRP GLU LEU GLN ALA LEU GLU LYS GLU SEQRES 52 B 694 LEU ALA GLN TRP SER HIS PRO GLN PHE GLU LYS GLY GLY SEQRES 53 B 694 GLY SER GLY GLY GLY SER GLY GLY SER ALA TRP SER HIS SEQRES 54 B 694 PRO GLN PHE GLU LYS SEQRES 1 D 230 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU VAL GLY ARG SEQRES 2 D 230 PRO GLY SER SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 D 230 TYR THR PHE THR GLY TYR ILE LEU SER TRP VAL LYS GLN SEQRES 4 D 230 SER PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP VAL ASP SEQRES 5 D 230 PRO GLU TYR GLY SER THR ASP SER ALA GLU LYS PHE LYS SEQRES 6 D 230 LYS ARG ALA THR LEU THR ALA ASP ILE SER SER ASN THR SEQRES 7 D 230 ALA TYR ILE GLN LEU SER SER LEU THR SER GLU ASP THR SEQRES 8 D 230 ALA THR TYR PHE CYS THR ARG TYR TYR ASP GLY TYR TYR SEQRES 9 D 230 ARG ARG TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 D 230 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 D 230 PRO LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR SEQRES 12 D 230 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 D 230 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 D 230 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 D 230 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 D 230 SER LEU GLY THR LYS THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 D 230 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 D 230 LYS TYR GLY PRO PRO CYS PRO PRO CYS SEQRES 1 C 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 C 214 SER LEU GLY ASP ILE VAL SER ILE GLU CYS LEU ALA SER SEQRES 3 C 214 GLU GLY ILE SER ASN ASN LEU ALA TRP HIS GLN GLN LYS SEQRES 4 C 214 PRO GLY LYS SER PRO GLN LEU LEU ILE TYR GLY ALA HIS SEQRES 5 C 214 SER LEU HIS ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 C 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE SER GLY MET SEQRES 7 C 214 GLN PRO GLU ASP GLU GLY VAL TYR TYR CYS GLN GLN GLY SEQRES 8 C 214 TYR LYS TYR PRO ILE THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 C 214 GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 C 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 C 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 C 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 C 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 C 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 C 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 C 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 C 214 PHE ASN ARG GLY GLU CYS HELIX 1 AA1 SER A 152 SER A 154 5 3 HELIX 2 AA2 MET A 155 SER A 164 1 10 HELIX 3 AA3 LEU A 165 ARG A 174 1 10 HELIX 4 AA4 THR A 199 ASN A 205 1 7 HELIX 5 AA5 LYS A 228 GLN A 239 1 12 HELIX 6 AA6 GLY A 251 CYS A 261 1 11 HELIX 7 AA7 CYS A 261 GLY A 266 1 6 HELIX 8 AA8 GLY A 286 LEU A 290 5 5 HELIX 9 AA9 SER A 318 ASN A 329 1 12 HELIX 10 AB1 PHE A 341 ILE A 352 1 12 HELIX 11 AB2 ASN A 366 SER A 380 1 15 HELIX 12 AB3 CYS A 401 VAL A 405 5 5 HELIX 13 AB4 GLY B 225 GLN B 230 1 6 HELIX 14 AB5 THR B 237 SER B 244 1 8 HELIX 15 AB6 SER B 264 ASP B 268 5 5 HELIX 16 AB7 LYS B 295 TYR B 300 1 6 HELIX 17 AB8 THR D 106 THR D 110 5 5 HELIX 18 AB9 GLN C 107 GLU C 111 5 5 SHEET 1 AA1 4 ILE A 114 GLN A 115 0 SHEET 2 AA1 4 LYS A 134 LYS A 136 -1 O LYS A 134 N GLN A 115 SHEET 3 AA1 4 GLU A 423 ILE A 430 -1 O VAL A 424 N PHE A 135 SHEET 4 AA1 4 ILE A 395 SER A 396 -1 N SER A 396 O SER A 429 SHEET 1 AA2 3 GLN A 129 THR A 132 0 SHEET 2 AA2 3 GLU A 423 ILE A 430 -1 O ILE A 430 N GLN A 129 SHEET 3 AA2 3 SER A 399 TYR A 400 -1 N TYR A 400 O GLN A 425 SHEET 1 AA3 4 GLN A 118 LEU A 119 0 SHEET 2 AA3 4 VAL A 454 ILE A 457 1 O GLU A 455 N LEU A 119 SHEET 3 AA3 4 SER A 442 PRO A 447 -1 N ILE A 445 O VAL A 454 SHEET 4 AA3 4 LEU A 384 GLU A 385 -1 N GLU A 385 O ARG A 446 SHEET 1 AA4 6 LYS A 220 THR A 226 0 SHEET 2 AA4 6 PHE A 180 PHE A 187 -1 N PHE A 184 O LEU A 223 SHEET 3 AA4 6 ILE A 143 ASP A 150 1 N TYR A 147 O GLY A 183 SHEET 4 AA4 6 THR A 271 THR A 278 1 O THR A 271 N ASP A 144 SHEET 5 AA4 6 ILE A 331 THR A 338 1 O GLN A 332 N ARG A 272 SHEET 6 AA4 6 GLY A 358 LEU A 360 1 O GLY A 358 N VAL A 337 SHEET 1 AA5 4 ALA B 50 VAL B 51 0 SHEET 2 AA5 4 LYS B 483 TYR B 487 -1 O VAL B 486 N ALA B 50 SHEET 3 AA5 4 LEU B 474 SER B 478 -1 N SER B 478 O LYS B 483 SHEET 4 AA5 4 ALA B 459 GLY B 462 -1 N ARG B 461 O ILE B 475 SHEET 1 AA6 2 VAL B 78 ALA B 80 0 SHEET 2 AA6 2 ALA B 95 TYR B 97 -1 O ALA B 95 N ALA B 80 SHEET 1 AA7 2 GLU B 135 TYR B 136 0 SHEET 2 AA7 2 SER B 161 TRP B 162 -1 O SER B 161 N TYR B 136 SHEET 1 AA8 4 ALA B 148 HIS B 149 0 SHEET 2 AA8 4 SER B 152 ALA B 157 -1 O SER B 152 N HIS B 149 SHEET 3 AA8 4 THR B 175 THR B 180 -1 O TYR B 177 N ALA B 155 SHEET 4 AA8 4 ARG B 185 TYR B 189 -1 O LEU B 187 N LEU B 178 SHEET 1 AA9 3 SER B 210 PHE B 213 0 SHEET 2 AA9 3 VAL B 219 GLY B 223 -1 O GLY B 222 N SER B 210 SHEET 3 AA9 3 GLN B 232 ALA B 236 -1 O LEU B 234 N LEU B 221 SHEET 1 AB1 3 VAL B 276 GLY B 279 0 SHEET 2 AB1 3 ASP B 288 VAL B 293 -1 O VAL B 290 N ALA B 277 SHEET 3 AB1 3 TYR B 302 LEU B 306 -1 O LEU B 306 N PHE B 289 SHEET 1 AB2 4 VAL B 330 THR B 333 0 SHEET 2 AB2 4 ASP B 342 ALA B 347 -1 N ASP B 342 O THR B 333 SHEET 3 AB2 4 ARG B 364 TYR B 368 -1 O TYR B 366 N VAL B 345 SHEET 4 AB2 4 LEU B 381 THR B 384 -1 O LEU B 383 N VAL B 365 SHEET 1 AB3 2 GLN B 370 HIS B 371 0 SHEET 2 AB3 2 GLY B 374 ILE B 375 -1 O GLY B 374 N HIS B 371 SHEET 1 AB4 4 THR B 397 GLY B 400 0 SHEET 2 AB4 4 ASP B 409 GLY B 413 -1 O ASP B 409 N LEU B 399 SHEET 3 AB4 4 VAL B 425 VAL B 427 -1 O PHE B 426 N ILE B 412 SHEET 4 AB4 4 GLN B 441 LEU B 443 -1 O LEU B 443 N VAL B 425 SHEET 1 AB5 2 GLY B 430 GLY B 431 0 SHEET 2 AB5 2 GLY B 434 LEU B 435 -1 O GLY B 434 N GLY B 431 SHEET 1 AB6 2 GLN D 22 GLN D 25 0 SHEET 2 AB6 2 CYS D 41 SER D 44 -1 O LYS D 42 N GLN D 24 SHEET 1 AB7 6 VAL D 30 GLY D 31 0 SHEET 2 AB7 6 THR D 134 VAL D 138 1 O THR D 137 N GLY D 31 SHEET 3 AB7 6 ALA D 111 TYR D 118 -1 N TYR D 113 O THR D 134 SHEET 4 AB7 6 LEU D 53 GLN D 58 -1 N SER D 54 O THR D 116 SHEET 5 AB7 6 GLU D 65 VAL D 70 -1 O VAL D 70 N LEU D 53 SHEET 6 AB7 6 ASP D 78 SER D 79 -1 O ASP D 78 N TRP D 69 SHEET 1 AB8 4 VAL D 30 GLY D 31 0 SHEET 2 AB8 4 THR D 134 VAL D 138 1 O THR D 137 N GLY D 31 SHEET 3 AB8 4 ALA D 111 TYR D 118 -1 N TYR D 113 O THR D 134 SHEET 4 AB8 4 PHE D 127 TRP D 130 -1 O TYR D 129 N ARG D 117 SHEET 1 AB9 3 LYS D 38 ILE D 39 0 SHEET 2 AB9 3 THR D 97 LEU D 102 -1 O ILE D 100 N ILE D 39 SHEET 3 AB9 3 ALA D 87 ASP D 92 -1 N THR D 90 O TYR D 99 SHEET 1 AC1 4 SER D 147 VAL D 148 0 SHEET 2 AC1 4 LEU D 168 TYR D 172 -1 O LYS D 170 N SER D 147 SHEET 3 AC1 4 TYR D 203 SER D 206 -1 O TYR D 203 N TYR D 172 SHEET 4 AC1 4 VAL D 196 LEU D 197 -1 N VAL D 196 O SER D 204 SHEET 1 AC2 2 ILE D 222 VAL D 225 0 SHEET 2 AC2 2 VAL D 234 LYS D 237 -1 O VAL D 234 N VAL D 225 SHEET 1 AC3 6 SER C 38 LEU C 39 0 SHEET 2 AC3 6 THR C 130 LEU C 132 1 O LYS C 131 N LEU C 39 SHEET 3 AC3 6 VAL C 113 GLN C 118 -1 N TYR C 114 O THR C 130 SHEET 4 AC3 6 LEU C 61 GLN C 66 -1 N ALA C 62 O GLN C 117 SHEET 5 AC3 6 GLN C 73 TYR C 77 -1 O LEU C 75 N TRP C 63 SHEET 6 AC3 6 SER C 81 LEU C 82 -1 O SER C 81 N TYR C 77 SHEET 1 AC4 3 VAL C 47 GLU C 50 0 SHEET 2 AC4 3 GLN C 98 ILE C 103 -1 O LEU C 101 N ILE C 49 SHEET 3 AC4 3 PHE C 90 SER C 95 -1 N SER C 91 O LYS C 102 SHEET 1 AC5 2 VAL C 161 ASN C 165 0 SHEET 2 AC5 2 SER C 202 THR C 206 -1 O LEU C 203 N LEU C 164 SSBOND 1 CYS A 207 CYS A 213 1555 1555 2.03 SSBOND 2 CYS A 261 CYS A 301 1555 1555 2.03 SSBOND 3 CYS A 401 CYS A 415 1555 1555 2.03 SSBOND 4 CYS B 99 CYS B 108 1555 1555 2.03 SSBOND 5 CYS B 156 CYS B 176 1555 1555 2.03 SSBOND 6 CYS B 192 CYS B 205 1555 1555 2.03 SSBOND 7 CYS D 41 CYS D 115 1555 1555 2.03 SSBOND 8 CYS D 167 CYS D 223 1555 1555 2.03 SSBOND 9 CYS C 51 CYS C 116 1555 1555 2.03 CISPEP 1 GLN A 115 PRO A 116 0 2.51 CISPEP 2 MET A 193 PRO A 194 0 -3.74 CISPEP 3 PHE D 173 PRO D 174 0 -7.79 CISPEP 4 GLU D 175 PRO D 176 0 -1.97 CISPEP 5 SER C 35 PRO C 36 0 -3.68 CISPEP 6 TYR C 122 PRO C 123 0 7.47 CISPEP 7 TYR C 168 PRO C 169 0 -11.00 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