HEADER VIRAL PROTEIN 18-DEC-24 9MLA TITLE PRE-FUSION HERV-K ENVELOPE PROTEIN TRIMER ECTODOMAIN IN COMPLEX WITH TITLE 2 KENV-6 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SURFACE PROTEIN; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: SU; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: PHOENIX CONSENSUS SEQUENCE (DEWANNIEUX, MARIE, ET AL. COMPND 8 2006). ENGINEERED V437C MUTATION; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: TRANSMEMBRANE PROTEIN,FIBRITIN; COMPND 11 CHAIN: D, E, F; COMPND 12 SYNONYM: TM,COLLAR PROTEIN,WHISKER ANTIGEN CONTROL PROTEIN; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES; COMPND 15 OTHER_DETAILS: PHOENIX CONSENSUS SEQUENCE (DEWANNIEUX, MARIE, ET AL. COMPND 16 2006). ENGINEERED V498C MUTATION. FUSION PROTEIN WITH ENTEROKINASE COMPND 17 SITE, GGS LINKERS, AND T4-FIBRITIN FOLDON TRIMERIZATION DOMAIN. C- COMPND 18 TERMINAL HRV-3C PROTEASE SITE AND TWIN-STREP II TAG.; COMPND 19 MOL_ID: 3; COMPND 20 MOLECULE: KENV-6 FAB HEAVY CHAIN; COMPND 21 CHAIN: G, H, I; COMPND 22 ENGINEERED: YES; COMPND 23 OTHER_DETAILS: CLEAVED FABS; COMPND 24 MOL_ID: 4; COMPND 25 MOLECULE: KENV-6 FAB LIGHT CHAIN; COMPND 26 CHAIN: J, K, L; COMPND 27 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: ERVK-25; SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: S2; SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1963; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 12 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4; SOURCE 13 ORGANISM_TAXID: 9606, 10665; SOURCE 14 GENE: ERVK-25; SOURCE 15 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: S2; SOURCE 18 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1963; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 21 ORGANISM_COMMON: MOUSE; SOURCE 22 ORGANISM_TAXID: 10090; SOURCE 23 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 27 ORGANISM_COMMON: MOUSE; SOURCE 28 ORGANISM_TAXID: 10090; SOURCE 29 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS HUMAN ENDOGENOUS RETROVIRUS K, GLYCOPROTEIN, HERV-K, ENVELOPE, PRE- KEYWDS 2 FUSION, FAB COMPLEX, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.SHEK,C.SUN,K.HASTIE,E.O.SAPHIRE REVDAT 1 30-JUL-25 9MLA 0 JRNL AUTH J.SHEK,C.SUN,K.HASTIE,E.O.SAPHIRE JRNL TITL HUMAN ENDOGENOUS RETROVIRUS HERV-K ENVELOPE GLYCOPROTEIN JRNL TITL 2 STRUCTURES IN PRE- AND POST-FUSION CONFORMATIONS BY CRYO-EM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.24 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER 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) : 2.240 REMARK 3 NUMBER OF PARTICLES : 479625 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9MLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291237. 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 : PRE-FUSION HERV-K ENVELOPE REMARK 245 GLYCOPROTEIN IN COMPLEX WITH REMARK 245 KENV-6 FABS; PRE-FUSION REMARK 245 STABILIZED HERV-K ENVELOPE REMARK 245 TRIMER; KENV-6 ANTIBODY FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.18 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 : FAB FRAGMENT GENERATED BY REMARK 245 PROTEOLYTIC CLEAVE OF KENV-6 IGG ANTIBODY REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 15947 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 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 : 2.70 REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : OTHER 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: 12-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 12-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j 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 ALA A 97 REMARK 465 ALA A 98 REMARK 465 ALA A 99 REMARK 465 LEU A 460 REMARK 465 ASN A 461 REMARK 465 ARG A 462 REMARK 465 ARG A 463 REMARK 465 ARG A 464 REMARK 465 ARG A 465 REMARK 465 ALA B 97 REMARK 465 ALA B 98 REMARK 465 ALA B 99 REMARK 465 LEU B 460 REMARK 465 ASN B 461 REMARK 465 ARG B 462 REMARK 465 ARG B 463 REMARK 465 ARG B 464 REMARK 465 ARG B 465 REMARK 465 ALA C 97 REMARK 465 ALA C 98 REMARK 465 ALA C 99 REMARK 465 LEU C 460 REMARK 465 ASN C 461 REMARK 465 ARG C 462 REMARK 465 ARG C 463 REMARK 465 ARG C 464 REMARK 465 ARG C 465 REMARK 465 LEU D 621 REMARK 465 ALA D 622 REMARK 465 ASN D 623 REMARK 465 LEU D 624 REMARK 465 ASN D 625 REMARK 465 PRO D 626 REMARK 465 VAL D 627 REMARK 465 THR D 628 REMARK 465 TRP D 629 REMARK 465 VAL D 630 REMARK 465 LYS D 631 REMARK 465 THR D 632 REMARK 465 ASP D 633 REMARK 465 ASP D 634 REMARK 465 ASP D 635 REMARK 465 ASP D 636 REMARK 465 LYS D 637 REMARK 465 ALA D 638 REMARK 465 GLY D 639 REMARK 465 GLY D 640 REMARK 465 SER D 641 REMARK 465 GLY D 642 REMARK 465 GLY D 643 REMARK 465 SER D 644 REMARK 465 GLY D 645 REMARK 465 GLY D 646 REMARK 465 SER D 647 REMARK 465 GLY D 648 REMARK 465 GLY D 649 REMARK 465 GLY D 650 REMARK 465 TYR D 651 REMARK 465 ILE D 652 REMARK 465 PRO D 653 REMARK 465 GLU D 654 REMARK 465 ALA D 655 REMARK 465 PRO D 656 REMARK 465 ARG D 657 REMARK 465 ASP D 658 REMARK 465 GLY D 659 REMARK 465 GLN D 660 REMARK 465 ALA D 661 REMARK 465 TYR D 662 REMARK 465 VAL D 663 REMARK 465 ARG D 664 REMARK 465 LYS D 665 REMARK 465 ASP D 666 REMARK 465 GLY D 667 REMARK 465 GLU D 668 REMARK 465 TRP D 669 REMARK 465 VAL D 670 REMARK 465 LEU D 671 REMARK 465 LEU D 672 REMARK 465 SER D 673 REMARK 465 THR D 674 REMARK 465 PHE D 675 REMARK 465 LEU D 676 REMARK 465 ALA D 677 REMARK 465 SER D 678 REMARK 465 GLY D 679 REMARK 465 LEU D 680 REMARK 465 GLU D 681 REMARK 465 VAL D 682 REMARK 465 LEU D 683 REMARK 465 PHE D 684 REMARK 465 GLN D 685 REMARK 465 GLY D 686 REMARK 465 PRO D 687 REMARK 465 GLY D 688 REMARK 465 ALA D 689 REMARK 465 GLY D 690 REMARK 465 TRP D 691 REMARK 465 SER D 692 REMARK 465 HIS D 693 REMARK 465 PRO D 694 REMARK 465 GLN D 695 REMARK 465 PHE D 696 REMARK 465 GLU D 697 REMARK 465 LYS D 698 REMARK 465 GLY D 699 REMARK 465 GLY D 700 REMARK 465 GLY D 701 REMARK 465 SER D 702 REMARK 465 GLY D 703 REMARK 465 GLY D 704 REMARK 465 GLY D 705 REMARK 465 SER D 706 REMARK 465 GLY D 707 REMARK 465 GLY D 708 REMARK 465 GLY D 709 REMARK 465 SER D 710 REMARK 465 TRP D 711 REMARK 465 SER D 712 REMARK 465 HIS D 713 REMARK 465 PRO D 714 REMARK 465 GLN D 715 REMARK 465 PHE D 716 REMARK 465 GLU D 717 REMARK 465 LYS D 718 REMARK 465 LEU E 621 REMARK 465 ALA E 622 REMARK 465 ASN E 623 REMARK 465 LEU E 624 REMARK 465 ASN E 625 REMARK 465 PRO E 626 REMARK 465 VAL E 627 REMARK 465 THR E 628 REMARK 465 TRP E 629 REMARK 465 VAL E 630 REMARK 465 LYS E 631 REMARK 465 THR E 632 REMARK 465 ASP E 633 REMARK 465 ASP E 634 REMARK 465 ASP E 635 REMARK 465 ASP E 636 REMARK 465 LYS E 637 REMARK 465 ALA E 638 REMARK 465 GLY E 639 REMARK 465 GLY E 640 REMARK 465 SER E 641 REMARK 465 GLY E 642 REMARK 465 GLY E 643 REMARK 465 SER E 644 REMARK 465 GLY E 645 REMARK 465 GLY E 646 REMARK 465 SER E 647 REMARK 465 GLY E 648 REMARK 465 GLY E 649 REMARK 465 GLY E 650 REMARK 465 TYR E 651 REMARK 465 ILE E 652 REMARK 465 PRO E 653 REMARK 465 GLU E 654 REMARK 465 ALA E 655 REMARK 465 PRO E 656 REMARK 465 ARG E 657 REMARK 465 ASP E 658 REMARK 465 GLY E 659 REMARK 465 GLN E 660 REMARK 465 ALA E 661 REMARK 465 TYR E 662 REMARK 465 VAL E 663 REMARK 465 ARG E 664 REMARK 465 LYS E 665 REMARK 465 ASP E 666 REMARK 465 GLY E 667 REMARK 465 GLU E 668 REMARK 465 TRP E 669 REMARK 465 VAL E 670 REMARK 465 LEU E 671 REMARK 465 LEU E 672 REMARK 465 SER E 673 REMARK 465 THR E 674 REMARK 465 PHE E 675 REMARK 465 LEU E 676 REMARK 465 ALA E 677 REMARK 465 SER E 678 REMARK 465 GLY E 679 REMARK 465 LEU E 680 REMARK 465 GLU E 681 REMARK 465 VAL E 682 REMARK 465 LEU E 683 REMARK 465 PHE E 684 REMARK 465 GLN E 685 REMARK 465 GLY E 686 REMARK 465 PRO E 687 REMARK 465 GLY E 688 REMARK 465 ALA E 689 REMARK 465 GLY E 690 REMARK 465 TRP E 691 REMARK 465 SER E 692 REMARK 465 HIS E 693 REMARK 465 PRO E 694 REMARK 465 GLN E 695 REMARK 465 PHE E 696 REMARK 465 GLU E 697 REMARK 465 LYS E 698 REMARK 465 GLY E 699 REMARK 465 GLY E 700 REMARK 465 GLY E 701 REMARK 465 SER E 702 REMARK 465 GLY E 703 REMARK 465 GLY E 704 REMARK 465 GLY E 705 REMARK 465 SER E 706 REMARK 465 GLY E 707 REMARK 465 GLY E 708 REMARK 465 GLY E 709 REMARK 465 SER E 710 REMARK 465 TRP E 711 REMARK 465 SER E 712 REMARK 465 HIS E 713 REMARK 465 PRO E 714 REMARK 465 GLN E 715 REMARK 465 PHE E 716 REMARK 465 GLU E 717 REMARK 465 LYS E 718 REMARK 465 LEU F 621 REMARK 465 ALA F 622 REMARK 465 ASN F 623 REMARK 465 LEU F 624 REMARK 465 ASN F 625 REMARK 465 PRO F 626 REMARK 465 VAL F 627 REMARK 465 THR F 628 REMARK 465 TRP F 629 REMARK 465 VAL F 630 REMARK 465 LYS F 631 REMARK 465 THR F 632 REMARK 465 ASP F 633 REMARK 465 ASP F 634 REMARK 465 ASP F 635 REMARK 465 ASP F 636 REMARK 465 LYS F 637 REMARK 465 ALA F 638 REMARK 465 GLY F 639 REMARK 465 GLY F 640 REMARK 465 SER F 641 REMARK 465 GLY F 642 REMARK 465 GLY F 643 REMARK 465 SER F 644 REMARK 465 GLY F 645 REMARK 465 GLY F 646 REMARK 465 SER F 647 REMARK 465 GLY F 648 REMARK 465 GLY F 649 REMARK 465 GLY F 650 REMARK 465 TYR F 651 REMARK 465 ILE F 652 REMARK 465 PRO F 653 REMARK 465 GLU F 654 REMARK 465 ALA F 655 REMARK 465 PRO F 656 REMARK 465 ARG F 657 REMARK 465 ASP F 658 REMARK 465 GLY F 659 REMARK 465 GLN F 660 REMARK 465 ALA F 661 REMARK 465 TYR F 662 REMARK 465 VAL F 663 REMARK 465 ARG F 664 REMARK 465 LYS F 665 REMARK 465 ASP F 666 REMARK 465 GLY F 667 REMARK 465 GLU F 668 REMARK 465 TRP F 669 REMARK 465 VAL F 670 REMARK 465 LEU F 671 REMARK 465 LEU F 672 REMARK 465 SER F 673 REMARK 465 THR F 674 REMARK 465 PHE F 675 REMARK 465 LEU F 676 REMARK 465 ALA F 677 REMARK 465 SER F 678 REMARK 465 GLY F 679 REMARK 465 LEU F 680 REMARK 465 GLU F 681 REMARK 465 VAL F 682 REMARK 465 LEU F 683 REMARK 465 PHE F 684 REMARK 465 GLN F 685 REMARK 465 GLY F 686 REMARK 465 PRO F 687 REMARK 465 GLY F 688 REMARK 465 ALA F 689 REMARK 465 GLY F 690 REMARK 465 TRP F 691 REMARK 465 SER F 692 REMARK 465 HIS F 693 REMARK 465 PRO F 694 REMARK 465 GLN F 695 REMARK 465 PHE F 696 REMARK 465 GLU F 697 REMARK 465 LYS F 698 REMARK 465 GLY F 699 REMARK 465 GLY F 700 REMARK 465 GLY F 701 REMARK 465 SER F 702 REMARK 465 GLY F 703 REMARK 465 GLY F 704 REMARK 465 GLY F 705 REMARK 465 SER F 706 REMARK 465 GLY F 707 REMARK 465 GLY F 708 REMARK 465 GLY F 709 REMARK 465 SER F 710 REMARK 465 TRP F 711 REMARK 465 SER F 712 REMARK 465 HIS F 713 REMARK 465 PRO F 714 REMARK 465 GLN F 715 REMARK 465 PHE F 716 REMARK 465 GLU F 717 REMARK 465 LYS F 718 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 LYS A 233 CG CD CE NZ REMARK 470 LYS A 236 CG CD CE NZ REMARK 470 LYS B 233 CG CD CE NZ REMARK 470 LYS B 236 CG CD CE NZ REMARK 470 LYS C 233 CG CD CE NZ REMARK 470 LYS C 236 CG CD CE NZ 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 OD1 ASP F 584 OG1 THR F 587 2.11 REMARK 500 OD1 ASP E 584 OG1 THR E 587 2.12 REMARK 500 OD1 ASP D 584 OG1 THR D 587 2.16 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 LYS A 236 150.68 71.34 REMARK 500 GLU A 239 -7.24 71.68 REMARK 500 ASN A 257 -165.50 -160.46 REMARK 500 CYS A 275 -4.20 68.30 REMARK 500 PRO B 111 48.38 -79.41 REMARK 500 ASN B 257 -165.05 -160.67 REMARK 500 CYS B 275 -4.12 69.29 REMARK 500 ASN C 257 -167.90 -163.22 REMARK 500 CYS C 275 -4.01 69.03 REMARK 500 GLU D 567 -8.31 74.44 REMARK 500 GLU D 583 25.11 -140.37 REMARK 500 GLU E 567 -8.00 74.43 REMARK 500 GLU E 583 29.29 -140.65 REMARK 500 GLU F 567 -8.20 74.56 REMARK 500 GLU F 583 29.02 -140.60 REMARK 500 TRP G 106 52.55 -93.46 REMARK 500 TRP H 106 51.32 -92.75 REMARK 500 TRP I 106 50.39 -91.31 REMARK 500 ALA J 54 -9.80 72.43 REMARK 500 SER J 70 -169.81 -100.67 REMARK 500 THR J 72 -5.76 71.72 REMARK 500 ALA K 54 -9.73 72.76 REMARK 500 THR K 72 -6.32 71.62 REMARK 500 ALA K 87 -174.61 -171.13 REMARK 500 LEU L 50 -61.25 -93.90 REMARK 500 ALA L 54 -9.07 71.74 REMARK 500 SER L 70 -168.39 -125.92 REMARK 500 THR L 72 -6.06 72.14 REMARK 500 TYR L 99 60.87 62.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48351 RELATED DB: EMDB REMARK 900 PRE-FUSION HERV-K ENVELOPE PROTEIN ECTODOMAIN IN COMPLEX WITH KENV- REMARK 900 6 FAB REMARK 900 RELATED ID: 9O4F RELATED DB: PDB REMARK 900 PRE-FUSION HERV-K ENVELOPE TRIMER WITHOUT THE FABS COMPLEXED REMARK 900 RELATED ID: 9MLK RELATED DB: PDB REMARK 900 POST-FUSIN HERV-K ENVELOPE TM. SAME CITATION. DBREF 9MLA A 97 465 UNP P61570 ENK25_HUMAN 97 465 DBREF 9MLA B 97 465 UNP P61570 ENK25_HUMAN 97 465 DBREF 9MLA C 97 465 UNP P61570 ENK25_HUMAN 97 465 DBREF 9MLA D 466 632 UNP P61570 ENK25_HUMAN 466 632 DBREF 9MLA D 651 676 UNP P10104 WAC_BPT4 459 484 DBREF 9MLA E 466 632 UNP P61570 ENK25_HUMAN 466 632 DBREF 9MLA E 651 676 UNP P10104 WAC_BPT4 459 484 DBREF 9MLA F 466 632 UNP P61570 ENK25_HUMAN 466 632 DBREF 9MLA F 651 676 UNP P10104 WAC_BPT4 459 484 DBREF 9MLA G 1 119 PDB 9MLA 9MLA 1 119 DBREF 9MLA H 1 119 PDB 9MLA 9MLA 1 119 DBREF 9MLA I 1 119 PDB 9MLA 9MLA 1 119 DBREF 9MLA J 1 107 PDB 9MLA 9MLA 1 107 DBREF 9MLA K 1 107 PDB 9MLA 9MLA 1 107 DBREF 9MLA L 1 107 PDB 9MLA 9MLA 1 107 SEQADV 9MLA ARG A 167 UNP P61570 THR 167 CONFLICT SEQADV 9MLA THR A 185 UNP P61570 ILE 185 CONFLICT SEQADV 9MLA ILE A 328 UNP P61570 VAL 328 CONFLICT SEQADV 9MLA CYS A 437 UNP P61570 VAL 437 ENGINEERED MUTATION SEQADV 9MLA ARG A 463 UNP P61570 SER 463 ENGINEERED MUTATION SEQADV 9MLA ARG A 464 UNP P61570 LYS 464 ENGINEERED MUTATION SEQADV 9MLA ARG B 167 UNP P61570 THR 167 CONFLICT SEQADV 9MLA THR B 185 UNP P61570 ILE 185 CONFLICT SEQADV 9MLA ILE B 328 UNP P61570 VAL 328 CONFLICT SEQADV 9MLA CYS B 437 UNP P61570 VAL 437 ENGINEERED MUTATION SEQADV 9MLA ARG B 463 UNP P61570 SER 463 ENGINEERED MUTATION SEQADV 9MLA ARG B 464 UNP P61570 LYS 464 ENGINEERED MUTATION SEQADV 9MLA ARG C 167 UNP P61570 THR 167 CONFLICT SEQADV 9MLA THR C 185 UNP P61570 ILE 185 CONFLICT SEQADV 9MLA ILE C 328 UNP P61570 VAL 328 CONFLICT SEQADV 9MLA CYS C 437 UNP P61570 VAL 437 ENGINEERED MUTATION SEQADV 9MLA ARG C 463 UNP P61570 SER 463 ENGINEERED MUTATION SEQADV 9MLA ARG C 464 UNP P61570 LYS 464 ENGINEERED MUTATION SEQADV 9MLA ALA D 484 UNP P61570 GLY 484 CONFLICT SEQADV 9MLA CYS D 498 UNP P61570 VAL 498 ENGINEERED MUTATION SEQADV 9MLA GLU D 599 UNP P61570 LYS 599 CONFLICT SEQADV 9MLA ASP D 633 UNP P61570 LINKER SEQADV 9MLA ASP D 634 UNP P61570 LINKER SEQADV 9MLA ASP D 635 UNP P61570 LINKER SEQADV 9MLA ASP D 636 UNP P61570 LINKER SEQADV 9MLA LYS D 637 UNP P61570 LINKER SEQADV 9MLA ALA D 638 UNP P61570 LINKER SEQADV 9MLA GLY D 639 UNP P61570 LINKER SEQADV 9MLA GLY D 640 UNP P61570 LINKER SEQADV 9MLA SER D 641 UNP P61570 LINKER SEQADV 9MLA GLY D 642 UNP P61570 LINKER SEQADV 9MLA GLY D 643 UNP P61570 LINKER SEQADV 9MLA SER D 644 UNP P61570 LINKER SEQADV 9MLA GLY D 645 UNP P61570 LINKER SEQADV 9MLA GLY D 646 UNP P61570 LINKER SEQADV 9MLA SER D 647 UNP P61570 LINKER SEQADV 9MLA GLY D 648 UNP P61570 LINKER SEQADV 9MLA GLY D 649 UNP P61570 LINKER SEQADV 9MLA GLY D 650 UNP P61570 LINKER SEQADV 9MLA LEU D 671 UNP P10104 PHE 479 CONFLICT SEQADV 9MLA ALA D 677 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER D 678 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 679 UNP P10104 EXPRESSION TAG SEQADV 9MLA LEU D 680 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU D 681 UNP P10104 EXPRESSION TAG SEQADV 9MLA VAL D 682 UNP P10104 EXPRESSION TAG SEQADV 9MLA LEU D 683 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE D 684 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN D 685 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 686 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO D 687 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 688 UNP P10104 EXPRESSION TAG SEQADV 9MLA ALA D 689 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 690 UNP P10104 EXPRESSION TAG SEQADV 9MLA TRP D 691 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER D 692 UNP P10104 EXPRESSION TAG SEQADV 9MLA HIS D 693 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO D 694 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN D 695 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE D 696 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU D 697 UNP P10104 EXPRESSION TAG SEQADV 9MLA LYS D 698 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 699 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 700 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 701 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER D 702 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 703 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 704 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 705 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER D 706 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 707 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 708 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY D 709 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER D 710 UNP P10104 EXPRESSION TAG SEQADV 9MLA TRP D 711 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER D 712 UNP P10104 EXPRESSION TAG SEQADV 9MLA HIS D 713 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO D 714 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN D 715 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE D 716 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU D 717 UNP P10104 EXPRESSION TAG SEQADV 9MLA LYS D 718 UNP P10104 EXPRESSION TAG SEQADV 9MLA ALA E 484 UNP P61570 GLY 484 CONFLICT SEQADV 9MLA CYS E 498 UNP P61570 VAL 498 ENGINEERED MUTATION SEQADV 9MLA GLU E 599 UNP P61570 LYS 599 CONFLICT SEQADV 9MLA ASP E 633 UNP P61570 LINKER SEQADV 9MLA ASP E 634 UNP P61570 LINKER SEQADV 9MLA ASP E 635 UNP P61570 LINKER SEQADV 9MLA ASP E 636 UNP P61570 LINKER SEQADV 9MLA LYS E 637 UNP P61570 LINKER SEQADV 9MLA ALA E 638 UNP P61570 LINKER SEQADV 9MLA GLY E 639 UNP P61570 LINKER SEQADV 9MLA GLY E 640 UNP P61570 LINKER SEQADV 9MLA SER E 641 UNP P61570 LINKER SEQADV 9MLA GLY E 642 UNP P61570 LINKER SEQADV 9MLA GLY E 643 UNP P61570 LINKER SEQADV 9MLA SER E 644 UNP P61570 LINKER SEQADV 9MLA GLY E 645 UNP P61570 LINKER SEQADV 9MLA GLY E 646 UNP P61570 LINKER SEQADV 9MLA SER E 647 UNP P61570 LINKER SEQADV 9MLA GLY E 648 UNP P61570 LINKER SEQADV 9MLA GLY E 649 UNP P61570 LINKER SEQADV 9MLA GLY E 650 UNP P61570 LINKER SEQADV 9MLA LEU E 671 UNP P10104 PHE 479 CONFLICT SEQADV 9MLA ALA E 677 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER E 678 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 679 UNP P10104 EXPRESSION TAG SEQADV 9MLA LEU E 680 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU E 681 UNP P10104 EXPRESSION TAG SEQADV 9MLA VAL E 682 UNP P10104 EXPRESSION TAG SEQADV 9MLA LEU E 683 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE E 684 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN E 685 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 686 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO E 687 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 688 UNP P10104 EXPRESSION TAG SEQADV 9MLA ALA E 689 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 690 UNP P10104 EXPRESSION TAG SEQADV 9MLA TRP E 691 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER E 692 UNP P10104 EXPRESSION TAG SEQADV 9MLA HIS E 693 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO E 694 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN E 695 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE E 696 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU E 697 UNP P10104 EXPRESSION TAG SEQADV 9MLA LYS E 698 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 699 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 700 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 701 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER E 702 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 703 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 704 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 705 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER E 706 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 707 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 708 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY E 709 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER E 710 UNP P10104 EXPRESSION TAG SEQADV 9MLA TRP E 711 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER E 712 UNP P10104 EXPRESSION TAG SEQADV 9MLA HIS E 713 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO E 714 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN E 715 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE E 716 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU E 717 UNP P10104 EXPRESSION TAG SEQADV 9MLA LYS E 718 UNP P10104 EXPRESSION TAG SEQADV 9MLA ALA F 484 UNP P61570 GLY 484 CONFLICT SEQADV 9MLA CYS F 498 UNP P61570 VAL 498 ENGINEERED MUTATION SEQADV 9MLA GLU F 599 UNP P61570 LYS 599 CONFLICT SEQADV 9MLA ASP F 633 UNP P61570 LINKER SEQADV 9MLA ASP F 634 UNP P61570 LINKER SEQADV 9MLA ASP F 635 UNP P61570 LINKER SEQADV 9MLA ASP F 636 UNP P61570 LINKER SEQADV 9MLA LYS F 637 UNP P61570 LINKER SEQADV 9MLA ALA F 638 UNP P61570 LINKER SEQADV 9MLA GLY F 639 UNP P61570 LINKER SEQADV 9MLA GLY F 640 UNP P61570 LINKER SEQADV 9MLA SER F 641 UNP P61570 LINKER SEQADV 9MLA GLY F 642 UNP P61570 LINKER SEQADV 9MLA GLY F 643 UNP P61570 LINKER SEQADV 9MLA SER F 644 UNP P61570 LINKER SEQADV 9MLA GLY F 645 UNP P61570 LINKER SEQADV 9MLA GLY F 646 UNP P61570 LINKER SEQADV 9MLA SER F 647 UNP P61570 LINKER SEQADV 9MLA GLY F 648 UNP P61570 LINKER SEQADV 9MLA GLY F 649 UNP P61570 LINKER SEQADV 9MLA GLY F 650 UNP P61570 LINKER SEQADV 9MLA LEU F 671 UNP P10104 PHE 479 CONFLICT SEQADV 9MLA ALA F 677 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER F 678 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 679 UNP P10104 EXPRESSION TAG SEQADV 9MLA LEU F 680 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU F 681 UNP P10104 EXPRESSION TAG SEQADV 9MLA VAL F 682 UNP P10104 EXPRESSION TAG SEQADV 9MLA LEU F 683 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE F 684 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN F 685 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 686 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO F 687 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 688 UNP P10104 EXPRESSION TAG SEQADV 9MLA ALA F 689 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 690 UNP P10104 EXPRESSION TAG SEQADV 9MLA TRP F 691 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER F 692 UNP P10104 EXPRESSION TAG SEQADV 9MLA HIS F 693 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO F 694 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN F 695 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE F 696 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU F 697 UNP P10104 EXPRESSION TAG SEQADV 9MLA LYS F 698 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 699 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 700 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 701 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER F 702 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 703 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 704 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 705 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER F 706 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 707 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 708 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLY F 709 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER F 710 UNP P10104 EXPRESSION TAG SEQADV 9MLA TRP F 711 UNP P10104 EXPRESSION TAG SEQADV 9MLA SER F 712 UNP P10104 EXPRESSION TAG SEQADV 9MLA HIS F 713 UNP P10104 EXPRESSION TAG SEQADV 9MLA PRO F 714 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLN F 715 UNP P10104 EXPRESSION TAG SEQADV 9MLA PHE F 716 UNP P10104 EXPRESSION TAG SEQADV 9MLA GLU F 717 UNP P10104 EXPRESSION TAG SEQADV 9MLA LYS F 718 UNP P10104 EXPRESSION TAG SEQRES 1 A 369 ALA ALA ALA ASN TYR THR TYR TRP ALA TYR VAL PRO PHE SEQRES 2 A 369 PRO PRO LEU ILE ARG ALA VAL THR TRP MET ASP ASN PRO SEQRES 3 A 369 ILE GLU VAL TYR VAL ASN ASP SER VAL TRP VAL PRO GLY SEQRES 4 A 369 PRO ILE ASP ASP ARG CYS PRO ALA LYS PRO GLU GLU GLU SEQRES 5 A 369 GLY MET MET ILE ASN ILE SER ILE GLY TYR ARG TYR PRO SEQRES 6 A 369 PRO ILE CYS LEU GLY ARG ALA PRO GLY CYS LEU MET PRO SEQRES 7 A 369 ALA VAL GLN ASN TRP LEU VAL GLU VAL PRO THR VAL SER SEQRES 8 A 369 PRO ILE SER ARG PHE THR TYR HIS MET VAL SER GLY MET SEQRES 9 A 369 SER LEU ARG PRO ARG VAL ASN TYR LEU GLN ASP PHE SER SEQRES 10 A 369 TYR GLN ARG SER LEU LYS PHE ARG PRO LYS GLY LYS PRO SEQRES 11 A 369 CYS PRO LYS GLU ILE PRO LYS GLU SER LYS ASN THR GLU SEQRES 12 A 369 VAL LEU VAL TRP GLU GLU CYS VAL ALA ASN SER ALA VAL SEQRES 13 A 369 ILE LEU GLN ASN ASN GLU PHE GLY THR ILE ILE ASP TRP SEQRES 14 A 369 ALA PRO ARG GLY GLN PHE TYR HIS ASN CYS SER GLY GLN SEQRES 15 A 369 THR GLN SER CYS PRO SER ALA GLN VAL SER PRO ALA VAL SEQRES 16 A 369 ASP SER ASP LEU THR GLU SER LEU ASP LYS HIS LYS HIS SEQRES 17 A 369 LYS LYS LEU GLN SER PHE TYR PRO TRP GLU TRP GLY GLU SEQRES 18 A 369 LYS GLY ILE SER THR PRO ARG PRO LYS ILE ILE SER PRO SEQRES 19 A 369 VAL SER GLY PRO GLU HIS PRO GLU LEU TRP ARG LEU THR SEQRES 20 A 369 VAL ALA SER HIS HIS ILE ARG ILE TRP SER GLY ASN GLN SEQRES 21 A 369 THR LEU GLU THR ARG ASP ARG LYS PRO PHE TYR THR VAL SEQRES 22 A 369 ASP LEU ASN SER SER LEU THR VAL PRO LEU GLN SER CYS SEQRES 23 A 369 VAL LYS PRO PRO TYR MET LEU VAL VAL GLY ASN ILE VAL SEQRES 24 A 369 ILE LYS PRO ASP SER GLN THR ILE THR CYS GLU ASN CYS SEQRES 25 A 369 ARG LEU LEU THR CYS ILE ASP SER THR PHE ASN TRP GLN SEQRES 26 A 369 HIS ARG ILE LEU LEU VAL ARG ALA ARG GLU GLY VAL TRP SEQRES 27 A 369 ILE PRO CYS SER MET ASP ARG PRO TRP GLU ALA SER PRO SEQRES 28 A 369 SER ILE HIS ILE LEU THR GLU VAL LEU LYS GLY VAL LEU SEQRES 29 A 369 ASN ARG ARG ARG ARG SEQRES 1 B 369 ALA ALA ALA ASN TYR THR TYR TRP ALA TYR VAL PRO PHE SEQRES 2 B 369 PRO PRO LEU ILE ARG ALA VAL THR TRP MET ASP ASN PRO SEQRES 3 B 369 ILE GLU VAL TYR VAL ASN ASP SER VAL TRP VAL PRO GLY SEQRES 4 B 369 PRO ILE ASP ASP ARG CYS PRO ALA LYS PRO GLU GLU GLU SEQRES 5 B 369 GLY MET MET ILE ASN ILE SER ILE GLY TYR ARG TYR PRO SEQRES 6 B 369 PRO ILE CYS LEU GLY ARG ALA PRO GLY CYS LEU MET PRO SEQRES 7 B 369 ALA VAL GLN ASN TRP LEU VAL GLU VAL PRO THR VAL SER SEQRES 8 B 369 PRO ILE SER ARG PHE THR TYR HIS MET VAL SER GLY MET SEQRES 9 B 369 SER LEU ARG PRO ARG VAL ASN TYR LEU GLN ASP PHE SER SEQRES 10 B 369 TYR GLN ARG SER LEU LYS PHE ARG PRO LYS GLY LYS PRO SEQRES 11 B 369 CYS PRO LYS GLU ILE PRO LYS GLU SER LYS ASN THR GLU SEQRES 12 B 369 VAL LEU VAL TRP GLU GLU CYS VAL ALA ASN SER ALA VAL SEQRES 13 B 369 ILE LEU GLN ASN ASN GLU PHE GLY THR ILE ILE ASP TRP SEQRES 14 B 369 ALA PRO ARG GLY GLN PHE TYR HIS ASN CYS SER GLY GLN SEQRES 15 B 369 THR GLN SER CYS PRO SER ALA GLN VAL SER PRO ALA VAL SEQRES 16 B 369 ASP SER ASP LEU THR GLU SER LEU ASP LYS HIS LYS HIS SEQRES 17 B 369 LYS LYS LEU GLN SER PHE TYR PRO TRP GLU TRP GLY GLU SEQRES 18 B 369 LYS GLY ILE SER THR PRO ARG PRO LYS ILE ILE SER PRO SEQRES 19 B 369 VAL SER GLY PRO GLU HIS PRO GLU LEU TRP ARG LEU THR SEQRES 20 B 369 VAL ALA SER HIS HIS ILE ARG ILE TRP SER GLY ASN GLN SEQRES 21 B 369 THR LEU GLU THR ARG ASP ARG LYS PRO PHE TYR THR VAL SEQRES 22 B 369 ASP LEU ASN SER SER LEU THR VAL PRO LEU GLN SER CYS SEQRES 23 B 369 VAL LYS PRO PRO TYR MET LEU VAL VAL GLY ASN ILE VAL SEQRES 24 B 369 ILE LYS PRO ASP SER GLN THR ILE THR CYS GLU ASN CYS SEQRES 25 B 369 ARG LEU LEU THR CYS ILE ASP SER THR PHE ASN TRP GLN SEQRES 26 B 369 HIS ARG ILE LEU LEU VAL ARG ALA ARG GLU GLY VAL TRP SEQRES 27 B 369 ILE PRO CYS SER MET ASP ARG PRO TRP GLU ALA SER PRO SEQRES 28 B 369 SER ILE HIS ILE LEU THR GLU VAL LEU LYS GLY VAL LEU SEQRES 29 B 369 ASN ARG ARG ARG ARG SEQRES 1 C 369 ALA ALA ALA ASN TYR THR TYR TRP ALA TYR VAL PRO PHE SEQRES 2 C 369 PRO PRO LEU ILE ARG ALA VAL THR TRP MET ASP ASN PRO SEQRES 3 C 369 ILE GLU VAL TYR VAL ASN ASP SER VAL TRP VAL PRO GLY SEQRES 4 C 369 PRO ILE ASP ASP ARG CYS PRO ALA LYS PRO GLU GLU GLU SEQRES 5 C 369 GLY MET MET ILE ASN ILE SER ILE GLY TYR ARG TYR PRO SEQRES 6 C 369 PRO ILE CYS LEU GLY ARG ALA PRO GLY CYS LEU MET PRO SEQRES 7 C 369 ALA VAL GLN ASN TRP LEU VAL GLU VAL PRO THR VAL SER SEQRES 8 C 369 PRO ILE SER ARG PHE THR TYR HIS MET VAL SER GLY MET SEQRES 9 C 369 SER LEU ARG PRO ARG VAL ASN TYR LEU GLN ASP PHE SER SEQRES 10 C 369 TYR GLN ARG SER LEU LYS PHE ARG PRO LYS GLY LYS PRO SEQRES 11 C 369 CYS PRO LYS GLU ILE PRO LYS GLU SER LYS ASN THR GLU SEQRES 12 C 369 VAL LEU VAL TRP GLU GLU CYS VAL ALA ASN SER ALA VAL SEQRES 13 C 369 ILE LEU GLN ASN ASN GLU PHE GLY THR ILE ILE ASP TRP SEQRES 14 C 369 ALA PRO ARG GLY GLN PHE TYR HIS ASN CYS SER GLY GLN SEQRES 15 C 369 THR GLN SER CYS PRO SER ALA GLN VAL SER PRO ALA VAL SEQRES 16 C 369 ASP SER ASP LEU THR GLU SER LEU ASP LYS HIS LYS HIS SEQRES 17 C 369 LYS LYS LEU GLN SER PHE TYR PRO TRP GLU TRP GLY GLU SEQRES 18 C 369 LYS GLY ILE SER THR PRO ARG PRO LYS ILE ILE SER PRO SEQRES 19 C 369 VAL SER GLY PRO GLU HIS PRO GLU LEU TRP ARG LEU THR SEQRES 20 C 369 VAL ALA SER HIS HIS ILE ARG ILE TRP SER GLY ASN GLN SEQRES 21 C 369 THR LEU GLU THR ARG ASP ARG LYS PRO PHE TYR THR VAL SEQRES 22 C 369 ASP LEU ASN SER SER LEU THR VAL PRO LEU GLN SER CYS SEQRES 23 C 369 VAL LYS PRO PRO TYR MET LEU VAL VAL GLY ASN ILE VAL SEQRES 24 C 369 ILE LYS PRO ASP SER GLN THR ILE THR CYS GLU ASN CYS SEQRES 25 C 369 ARG LEU LEU THR CYS ILE ASP SER THR PHE ASN TRP GLN SEQRES 26 C 369 HIS ARG ILE LEU LEU VAL ARG ALA ARG GLU GLY VAL TRP SEQRES 27 C 369 ILE PRO CYS SER MET ASP ARG PRO TRP GLU ALA SER PRO SEQRES 28 C 369 SER ILE HIS ILE LEU THR GLU VAL LEU LYS GLY VAL LEU SEQRES 29 C 369 ASN ARG ARG ARG ARG SEQRES 1 D 253 PHE ILE PHE THR LEU ILE ALA VAL ILE MET GLY LEU ILE SEQRES 2 D 253 ALA VAL THR ALA THR ALA ALA VAL ALA GLY VAL ALA LEU SEQRES 3 D 253 HIS SER SER VAL GLN SER CYS ASN PHE VAL ASN ASP TRP SEQRES 4 D 253 GLN LYS ASN SER THR ARG LEU TRP ASN SER GLN SER SER SEQRES 5 D 253 ILE ASP GLN LYS LEU ALA ASN GLN ILE ASN ASP LEU ARG SEQRES 6 D 253 GLN THR VAL ILE TRP MET GLY ASP ARG LEU MET SER LEU SEQRES 7 D 253 GLU HIS ARG PHE GLN LEU GLN CYS ASP TRP ASN THR SER SEQRES 8 D 253 ASP PHE CYS ILE THR PRO GLN ILE TYR ASN GLU SER GLU SEQRES 9 D 253 HIS HIS TRP ASP MET VAL ARG ARG HIS LEU GLN GLY ARG SEQRES 10 D 253 GLU ASP ASN LEU THR LEU ASP ILE SER LYS LEU LYS GLU SEQRES 11 D 253 GLN ILE PHE GLU ALA SER LYS ALA HIS LEU ASN LEU VAL SEQRES 12 D 253 PRO GLY THR GLU ALA ILE ALA GLY VAL ALA ASP GLY LEU SEQRES 13 D 253 ALA ASN LEU ASN PRO VAL THR TRP VAL LYS THR ASP ASP SEQRES 14 D 253 ASP ASP LYS ALA GLY GLY SER GLY GLY SER GLY GLY SER SEQRES 15 D 253 GLY GLY GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN SEQRES 16 D 253 ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER SEQRES 17 D 253 THR PHE LEU ALA SER GLY LEU GLU VAL LEU PHE GLN GLY SEQRES 18 D 253 PRO GLY ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY SEQRES 19 D 253 GLY GLY SER GLY GLY GLY SER GLY GLY GLY SER TRP SER SEQRES 20 D 253 HIS PRO GLN PHE GLU LYS SEQRES 1 E 253 PHE ILE PHE THR LEU ILE ALA VAL ILE MET GLY LEU ILE SEQRES 2 E 253 ALA VAL THR ALA THR ALA ALA VAL ALA GLY VAL ALA LEU SEQRES 3 E 253 HIS SER SER VAL GLN SER CYS ASN PHE VAL ASN ASP TRP SEQRES 4 E 253 GLN LYS ASN SER THR ARG LEU TRP ASN SER GLN SER SER SEQRES 5 E 253 ILE ASP GLN LYS LEU ALA ASN GLN ILE ASN ASP LEU ARG SEQRES 6 E 253 GLN THR VAL ILE TRP MET GLY ASP ARG LEU MET SER LEU SEQRES 7 E 253 GLU HIS ARG PHE GLN LEU GLN CYS ASP TRP ASN THR SER SEQRES 8 E 253 ASP PHE CYS ILE THR PRO GLN ILE TYR ASN GLU SER GLU SEQRES 9 E 253 HIS HIS TRP ASP MET VAL ARG ARG HIS LEU GLN GLY ARG SEQRES 10 E 253 GLU ASP ASN LEU THR LEU ASP ILE SER LYS LEU LYS GLU SEQRES 11 E 253 GLN ILE PHE GLU ALA SER LYS ALA HIS LEU ASN LEU VAL SEQRES 12 E 253 PRO GLY THR GLU ALA ILE ALA GLY VAL ALA ASP GLY LEU SEQRES 13 E 253 ALA ASN LEU ASN PRO VAL THR TRP VAL LYS THR ASP ASP SEQRES 14 E 253 ASP ASP LYS ALA GLY GLY SER GLY GLY SER GLY GLY SER SEQRES 15 E 253 GLY GLY GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN SEQRES 16 E 253 ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER SEQRES 17 E 253 THR PHE LEU ALA SER GLY LEU GLU VAL LEU PHE GLN GLY SEQRES 18 E 253 PRO GLY ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY SEQRES 19 E 253 GLY GLY SER GLY GLY GLY SER GLY GLY GLY SER TRP SER SEQRES 20 E 253 HIS PRO GLN PHE GLU LYS SEQRES 1 F 253 PHE ILE PHE THR LEU ILE ALA VAL ILE MET GLY LEU ILE SEQRES 2 F 253 ALA VAL THR ALA THR ALA ALA VAL ALA GLY VAL ALA LEU SEQRES 3 F 253 HIS SER SER VAL GLN SER CYS ASN PHE VAL ASN ASP TRP SEQRES 4 F 253 GLN LYS ASN SER THR ARG LEU TRP ASN SER GLN SER SER SEQRES 5 F 253 ILE ASP GLN LYS LEU ALA ASN GLN ILE ASN ASP LEU ARG SEQRES 6 F 253 GLN THR VAL ILE TRP MET GLY ASP ARG LEU MET SER LEU SEQRES 7 F 253 GLU HIS ARG PHE GLN LEU GLN CYS ASP TRP ASN THR SER SEQRES 8 F 253 ASP PHE CYS ILE THR PRO GLN ILE TYR ASN GLU SER GLU SEQRES 9 F 253 HIS HIS TRP ASP MET VAL ARG ARG HIS LEU GLN GLY ARG SEQRES 10 F 253 GLU ASP ASN LEU THR LEU ASP ILE SER LYS LEU LYS GLU SEQRES 11 F 253 GLN ILE PHE GLU ALA SER LYS ALA HIS LEU ASN LEU VAL SEQRES 12 F 253 PRO GLY THR GLU ALA ILE ALA GLY VAL ALA ASP GLY LEU SEQRES 13 F 253 ALA ASN LEU ASN PRO VAL THR TRP VAL LYS THR ASP ASP SEQRES 14 F 253 ASP ASP LYS ALA GLY GLY SER GLY GLY SER GLY GLY SER SEQRES 15 F 253 GLY GLY GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN SEQRES 16 F 253 ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER SEQRES 17 F 253 THR PHE LEU ALA SER GLY LEU GLU VAL LEU PHE GLN GLY SEQRES 18 F 253 PRO GLY ALA GLY TRP SER HIS PRO GLN PHE GLU LYS GLY SEQRES 19 F 253 GLY GLY SER GLY GLY GLY SER GLY GLY GLY SER TRP SER SEQRES 20 F 253 HIS PRO GLN PHE GLU LYS SEQRES 1 G 119 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 G 119 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 G 119 TYR THR PHE THR ILE TYR GLY MET ASN TRP LEU LYS GLN SEQRES 4 G 119 ALA PRO GLY LYS GLY LEU LYS TRP MET GLY TRP ILE ASN SEQRES 5 G 119 THR TYR THR GLY GLU PRO THR TYR ALA ASP ASP PHE LYS SEQRES 6 G 119 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR SEQRES 7 G 119 ALA TYR LEU GLN VAL ASN ASN LEU LYS ASN GLU ASP THR SEQRES 8 G 119 ALA THR TYR PHE CYS ALA LYS TYR TYR ASP GLY TYR TYR SEQRES 9 G 119 GLY TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR LEU SEQRES 10 G 119 THR VAL SEQRES 1 H 119 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 H 119 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 119 TYR THR PHE THR ILE TYR GLY MET ASN TRP LEU LYS GLN SEQRES 4 H 119 ALA PRO GLY LYS GLY LEU LYS TRP MET GLY TRP ILE ASN SEQRES 5 H 119 THR TYR THR GLY GLU PRO THR TYR ALA ASP ASP PHE LYS SEQRES 6 H 119 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR SEQRES 7 H 119 ALA TYR LEU GLN VAL ASN ASN LEU LYS ASN GLU ASP THR SEQRES 8 H 119 ALA THR TYR PHE CYS ALA LYS TYR TYR ASP GLY TYR TYR SEQRES 9 H 119 GLY TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR LEU SEQRES 10 H 119 THR VAL SEQRES 1 I 119 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 I 119 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 I 119 TYR THR PHE THR ILE TYR GLY MET ASN TRP LEU LYS GLN SEQRES 4 I 119 ALA PRO GLY LYS GLY LEU LYS TRP MET GLY TRP ILE ASN SEQRES 5 I 119 THR TYR THR GLY GLU PRO THR TYR ALA ASP ASP PHE LYS SEQRES 6 I 119 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR SEQRES 7 I 119 ALA TYR LEU GLN VAL ASN ASN LEU LYS ASN GLU ASP THR SEQRES 8 I 119 ALA THR TYR PHE CYS ALA LYS TYR TYR ASP GLY TYR TYR SEQRES 9 I 119 GLY TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR LEU SEQRES 10 I 119 THR VAL SEQRES 1 J 107 ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL THR SEQRES 2 J 107 LEU GLY GLN ARG ALA THR ILE SER CYS ARG GLY SER GLU SEQRES 3 J 107 SER VAL ASP SER TYR GLY ASN SER PHE MET HIS TRP TYR SEQRES 4 J 107 GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR SEQRES 5 J 107 ARG ALA SER ASN LEU GLU SER GLY ILE PRO ALA ARG PHE SEQRES 6 J 107 SER GLY SER GLY SER ARG THR ASP PHE THR LEU THR ILE SEQRES 7 J 107 ASN PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR CYS SEQRES 8 J 107 GLN GLN SER TYR GLU ASP PRO TYR THR PHE GLY GLY GLY SEQRES 9 J 107 THR LYS LEU SEQRES 1 K 107 ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL THR SEQRES 2 K 107 LEU GLY GLN ARG ALA THR ILE SER CYS ARG GLY SER GLU SEQRES 3 K 107 SER VAL ASP SER TYR GLY ASN SER PHE MET HIS TRP TYR SEQRES 4 K 107 GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR SEQRES 5 K 107 ARG ALA SER ASN LEU GLU SER GLY ILE PRO ALA ARG PHE SEQRES 6 K 107 SER GLY SER GLY SER ARG THR ASP PHE THR LEU THR ILE SEQRES 7 K 107 ASN PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR CYS SEQRES 8 K 107 GLN GLN SER TYR GLU ASP PRO TYR THR PHE GLY GLY GLY SEQRES 9 K 107 THR LYS LEU SEQRES 1 L 107 ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL THR SEQRES 2 L 107 LEU GLY GLN ARG ALA THR ILE SER CYS ARG GLY SER GLU SEQRES 3 L 107 SER VAL ASP SER TYR GLY ASN SER PHE MET HIS TRP TYR SEQRES 4 L 107 GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR SEQRES 5 L 107 ARG ALA SER ASN LEU GLU SER GLY ILE PRO ALA ARG PHE SEQRES 6 L 107 SER GLY SER GLY SER ARG THR ASP PHE THR LEU THR ILE SEQRES 7 L 107 ASN PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR CYS SEQRES 8 L 107 GLN GLN SER TYR GLU ASP PRO TYR THR PHE GLY GLY GLY SEQRES 9 L 107 THR LYS LEU HET NAG M 1 14 HET NAG M 2 14 HET BMA M 3 11 HET MAN M 4 11 HET MAN M 5 11 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET MAN R 4 11 HET MAN R 5 11 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET MAN W 4 11 HET MAN W 5 11 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET BMA b 3 11 HET NAG c 1 14 HET NAG c 2 14 HET BMA c 3 11 HET NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 HET FUC d 4 10 HET NAG e 1 14 HET NAG e 2 14 HET BMA e 3 11 HET NAG f 1 14 HET NAG f 2 14 HET BMA f 3 11 HET NAG g 1 14 HET NAG g 2 14 HET BMA g 3 11 HET FUC g 4 10 HET NAG h 1 14 HET NAG h 2 14 HET BMA h 3 11 HET NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET FUC j 4 10 HET NAG A 501 14 HET NAG B 501 14 HET NAG C 501 14 HET NAG D 801 14 HET NAG E 801 14 HET NAG F 801 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE 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 HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 13 NAG 54(C8 H15 N O6) FORMUL 13 BMA 12(C6 H12 O6) FORMUL 13 MAN 6(C6 H12 O6) FORMUL 30 FUC 3(C6 H12 O5) HELIX 1 AA1 LYS A 144 GLU A 148 5 5 HELIX 2 AA2 ASP A 292 GLU A 297 1 6 HELIX 3 AA3 GLU A 338 ALA A 345 1 8 HELIX 4 AA4 PRO A 447 VAL A 459 1 13 HELIX 5 AA5 LYS B 144 GLU B 148 5 5 HELIX 6 AA6 ASP B 292 GLU B 297 1 6 HELIX 7 AA7 GLU B 338 ALA B 345 1 8 HELIX 8 AA8 PRO B 447 VAL B 459 1 13 HELIX 9 AA9 ASP C 292 GLU C 297 1 6 HELIX 10 AB1 GLU C 338 ALA C 345 1 8 HELIX 11 AB2 PRO C 447 VAL C 459 1 13 HELIX 12 AB3 GLY D 476 HIS D 492 1 17 HELIX 13 AB4 CYS D 498 TRP D 512 1 15 HELIX 14 AB5 ASP D 519 ASN D 524 1 6 HELIX 15 AB6 LEU D 529 GLN D 548 1 20 HELIX 16 AB7 HIS D 571 GLN D 580 1 10 HELIX 17 AB8 ASP D 589 GLU D 599 1 11 HELIX 18 AB9 LYS D 602 LEU D 607 1 6 HELIX 19 AC1 GLY D 610 ALA D 618 1 9 HELIX 20 AC2 GLY E 476 HIS E 492 1 17 HELIX 21 AC3 CYS E 498 TRP E 512 1 15 HELIX 22 AC4 ASP E 519 ASN E 524 1 6 HELIX 23 AC5 LEU E 529 LEU E 549 1 21 HELIX 24 AC6 HIS E 571 GLN E 580 1 10 HELIX 25 AC7 ASP E 589 GLU E 599 1 11 HELIX 26 AC8 LYS E 602 LEU E 607 1 6 HELIX 27 AC9 GLY E 610 ALA E 618 1 9 HELIX 28 AD1 GLY F 476 HIS F 492 1 17 HELIX 29 AD2 CYS F 498 TRP F 512 1 15 HELIX 30 AD3 ASP F 519 ASN F 524 1 6 HELIX 31 AD4 LEU F 529 GLN F 548 1 20 HELIX 32 AD5 HIS F 571 GLY F 581 1 11 HELIX 33 AD6 ASP F 589 GLU F 599 1 11 HELIX 34 AD7 LYS F 602 LEU F 607 1 6 HELIX 35 AD8 GLY F 610 ALA F 618 1 9 HELIX 36 AD9 LYS G 87 THR G 91 5 5 HELIX 37 AE1 LYS I 87 THR I 91 5 5 HELIX 38 AE2 GLU J 82 VAL J 86 5 5 HELIX 39 AE3 GLU K 82 VAL K 86 5 5 HELIX 40 AE4 GLU L 82 VAL L 86 5 5 SHEET 1 AA1 4 GLN D 496 SER D 497 0 SHEET 2 AA1 4 VAL A 433 SER A 438 1 N SER A 438 O GLN D 496 SHEET 3 AA1 4 THR A 102 VAL A 107 -1 N TYR A 103 O CYS A 437 SHEET 4 AA1 4 CYS D 559 ILE D 564 -1 O CYS D 559 N TYR A 106 SHEET 1 AA2 5 ILE A 113 ALA A 115 0 SHEET 2 AA2 5 ARG A 423 ALA A 429 -1 O ARG A 428 N ARG A 114 SHEET 3 AA2 5 TYR A 387 GLY A 392 -1 N VAL A 390 O LEU A 425 SHEET 4 AA2 5 THR A 402 LEU A 411 -1 O LEU A 411 N LEU A 389 SHEET 5 AA2 5 CYS A 164 LEU A 165 0 SHEET 1 AA3 5 MET A 150 GLY A 157 0 SHEET 2 AA3 5 THR A 402 LEU A 411 -1 O ILE A 403 N ILE A 156 SHEET 3 AA3 5 TYR A 387 GLY A 392 -1 N LEU A 389 O LEU A 411 SHEET 4 AA3 5 ARG A 423 ALA A 429 -1 O LEU A 425 N VAL A 390 SHEET 5 AA3 5 VAL A 395 LYS A 397 0 SHEET 1 AA4 3 TYR A 126 VAL A 127 0 SHEET 2 AA4 3 SER A 381 CYS A 382 -1 O CYS A 382 N TYR A 126 SHEET 3 AA4 3 CYS A 413 ILE A 414 -1 O ILE A 414 N SER A 381 SHEET 1 AA5 5 PRO A 174 PRO A 184 0 SHEET 2 AA5 5 SER A 190 LEU A 202 -1 O SER A 201 N ALA A 175 SHEET 3 AA5 5 ILE A 349 ARG A 361 -1 O GLY A 354 N TYR A 194 SHEET 4 AA5 5 LYS A 364 VAL A 377 -1 O PHE A 366 N GLU A 359 SHEET 5 AA5 5 LYS A 303 SER A 309 -1 N LYS A 305 O LEU A 371 SHEET 1 AA6 2 VAL A 206 ASN A 207 0 SHEET 2 AA6 2 SER A 213 TYR A 214 -1 O SER A 213 N ASN A 207 SHEET 1 AA7 4 ARG A 216 SER A 217 0 SHEET 2 AA7 4 ALA A 251 ASN A 257 -1 O ALA A 251 N SER A 217 SHEET 3 AA7 4 GLY A 260 ASP A 264 -1 O ASP A 264 N VAL A 252 SHEET 4 AA7 4 PRO A 325 SER A 329 -1 O SER A 329 N THR A 261 SHEET 1 AA8 2 GLN A 270 TYR A 272 0 SHEET 2 AA8 2 GLU A 314 GLY A 316 -1 O GLU A 314 N TYR A 272 SHEET 1 AA9 4 GLN E 496 SER E 497 0 SHEET 2 AA9 4 VAL B 433 MET B 439 1 N SER B 438 O GLN E 496 SHEET 3 AA9 4 TYR B 101 VAL B 107 -1 N TYR B 101 O MET B 439 SHEET 4 AA9 4 CYS E 559 ILE E 564 -1 O CYS E 559 N TYR B 106 SHEET 1 AB1 5 ILE B 113 ALA B 115 0 SHEET 2 AB1 5 ARG B 423 ALA B 429 -1 O ARG B 428 N ARG B 114 SHEET 3 AB1 5 TYR B 387 GLY B 392 -1 N VAL B 390 O LEU B 425 SHEET 4 AB1 5 THR B 402 LEU B 411 -1 O LEU B 411 N LEU B 389 SHEET 5 AB1 5 CYS B 164 LEU B 165 0 SHEET 1 AB2 5 MET B 150 GLY B 157 0 SHEET 2 AB2 5 THR B 402 LEU B 411 -1 O ILE B 403 N ILE B 156 SHEET 3 AB2 5 TYR B 387 GLY B 392 -1 N LEU B 389 O LEU B 411 SHEET 4 AB2 5 ARG B 423 ALA B 429 -1 O LEU B 425 N VAL B 390 SHEET 5 AB2 5 VAL B 395 LYS B 397 0 SHEET 1 AB3 3 TYR B 126 VAL B 127 0 SHEET 2 AB3 3 SER B 381 CYS B 382 -1 O CYS B 382 N TYR B 126 SHEET 3 AB3 3 CYS B 413 ILE B 414 -1 O ILE B 414 N SER B 381 SHEET 1 AB4 5 PRO B 174 PRO B 184 0 SHEET 2 AB4 5 SER B 190 LEU B 202 -1 O SER B 201 N ALA B 175 SHEET 3 AB4 5 ILE B 349 ARG B 361 -1 O TRP B 352 N MET B 196 SHEET 4 AB4 5 LYS B 364 VAL B 377 -1 O PHE B 366 N GLU B 359 SHEET 5 AB4 5 LYS B 303 SER B 309 -1 N LYS B 305 O LEU B 371 SHEET 1 AB5 2 VAL B 206 ASN B 207 0 SHEET 2 AB5 2 SER B 213 TYR B 214 -1 O SER B 213 N ASN B 207 SHEET 1 AB6 4 ARG B 216 SER B 217 0 SHEET 2 AB6 4 ALA B 251 ASN B 257 -1 O ALA B 251 N SER B 217 SHEET 3 AB6 4 GLY B 260 ASP B 264 -1 O ASP B 264 N VAL B 252 SHEET 4 AB6 4 PRO B 325 SER B 329 -1 O LYS B 326 N ILE B 263 SHEET 1 AB7 2 GLN B 270 TYR B 272 0 SHEET 2 AB7 2 GLU B 314 GLY B 316 -1 O GLU B 314 N TYR B 272 SHEET 1 AB8 4 GLN F 496 SER F 497 0 SHEET 2 AB8 4 VAL C 433 SER C 438 1 N SER C 438 O GLN F 496 SHEET 3 AB8 4 THR C 102 VAL C 107 -1 N TYR C 103 O CYS C 437 SHEET 4 AB8 4 CYS F 559 ILE F 564 -1 O CYS F 559 N TYR C 106 SHEET 1 AB9 5 ILE C 113 ALA C 115 0 SHEET 2 AB9 5 ARG C 423 ALA C 429 -1 O ARG C 428 N ARG C 114 SHEET 3 AB9 5 TYR C 387 GLY C 392 -1 N VAL C 390 O LEU C 425 SHEET 4 AB9 5 THR C 402 LEU C 411 -1 O LEU C 411 N LEU C 389 SHEET 5 AB9 5 CYS C 164 LEU C 165 0 SHEET 1 AC1 5 MET C 150 GLY C 157 0 SHEET 2 AC1 5 THR C 402 LEU C 411 -1 O ILE C 403 N ILE C 156 SHEET 3 AC1 5 TYR C 387 GLY C 392 -1 N LEU C 389 O LEU C 411 SHEET 4 AC1 5 ARG C 423 ALA C 429 -1 O LEU C 425 N VAL C 390 SHEET 5 AC1 5 VAL C 395 LYS C 397 0 SHEET 1 AC2 3 TYR C 126 VAL C 127 0 SHEET 2 AC2 3 SER C 381 CYS C 382 -1 O CYS C 382 N TYR C 126 SHEET 3 AC2 3 CYS C 413 ILE C 414 -1 O ILE C 414 N SER C 381 SHEET 1 AC3 5 PRO C 174 PRO C 184 0 SHEET 2 AC3 5 SER C 190 LEU C 202 -1 O SER C 201 N ALA C 175 SHEET 3 AC3 5 ILE C 349 ARG C 361 -1 O TRP C 352 N MET C 196 SHEET 4 AC3 5 LYS C 364 VAL C 377 -1 O PHE C 366 N GLU C 359 SHEET 5 AC3 5 LYS C 303 SER C 309 -1 N LYS C 305 O LEU C 371 SHEET 1 AC4 2 VAL C 206 ASN C 207 0 SHEET 2 AC4 2 SER C 213 TYR C 214 -1 O SER C 213 N ASN C 207 SHEET 1 AC5 4 ARG C 216 SER C 217 0 SHEET 2 AC5 4 ALA C 251 ASN C 257 -1 O ALA C 251 N SER C 217 SHEET 3 AC5 4 GLY C 260 ASP C 264 -1 O ASP C 264 N VAL C 252 SHEET 4 AC5 4 PRO C 325 SER C 329 -1 O SER C 329 N THR C 261 SHEET 1 AC6 2 GLN C 270 TYR C 272 0 SHEET 2 AC6 2 GLU C 314 GLY C 316 -1 O GLU C 314 N TYR C 272 SHEET 1 AC7 4 GLN G 3 GLN G 6 0 SHEET 2 AC7 4 THR G 17 SER G 25 -1 O SER G 25 N GLN G 3 SHEET 3 AC7 4 THR G 78 ASN G 84 -1 O VAL G 83 N VAL G 18 SHEET 4 AC7 4 PHE G 68 GLU G 73 -1 N SER G 71 O TYR G 80 SHEET 1 AC8 2 GLU G 10 LEU G 11 0 SHEET 2 AC8 2 LEU G 117 THR G 118 1 O THR G 118 N GLU G 10 SHEET 1 AC9 5 PRO G 58 TYR G 60 0 SHEET 2 AC9 5 LEU G 45 ILE G 51 -1 N TRP G 50 O THR G 59 SHEET 3 AC9 5 MET G 34 GLN G 39 -1 N LYS G 38 O LYS G 46 SHEET 4 AC9 5 THR G 93 TYR G 99 -1 O PHE G 95 N LEU G 37 SHEET 5 AC9 5 PHE G 108 TRP G 111 -1 O VAL G 110 N LYS G 98 SHEET 1 AD1 4 GLN H 3 GLN H 6 0 SHEET 2 AD1 4 THR H 17 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AD1 4 THR H 78 ASN H 84 -1 O ALA H 79 N CYS H 22 SHEET 4 AD1 4 PHE H 68 GLU H 73 -1 N GLU H 73 O THR H 78 SHEET 1 AD2 2 GLU H 10 LEU H 11 0 SHEET 2 AD2 2 LEU H 117 THR H 118 1 O THR H 118 N GLU H 10 SHEET 1 AD3 5 PRO H 58 TYR H 60 0 SHEET 2 AD3 5 LEU H 45 ILE H 51 -1 N TRP H 50 O THR H 59 SHEET 3 AD3 5 MET H 34 GLN H 39 -1 N LYS H 38 O LYS H 46 SHEET 4 AD3 5 THR H 93 TYR H 99 -1 O PHE H 95 N LEU H 37 SHEET 5 AD3 5 PHE H 108 TRP H 111 -1 O VAL H 110 N LYS H 98 SHEET 1 AD4 2 GLU I 10 LEU I 11 0 SHEET 2 AD4 2 LEU I 117 THR I 118 1 O THR I 118 N GLU I 10 SHEET 1 AD5 3 THR I 17 LYS I 23 0 SHEET 2 AD5 3 THR I 78 ASN I 84 -1 O LEU I 81 N ILE I 20 SHEET 3 AD5 3 PHE I 68 GLU I 73 -1 N SER I 71 O TYR I 80 SHEET 1 AD6 5 PRO I 58 TYR I 60 0 SHEET 2 AD6 5 LEU I 45 ILE I 51 -1 N TRP I 50 O THR I 59 SHEET 3 AD6 5 MET I 34 GLN I 39 -1 N LYS I 38 O LYS I 46 SHEET 4 AD6 5 THR I 93 TYR I 99 -1 O PHE I 95 N LEU I 37 SHEET 5 AD6 5 PHE I 108 TRP I 111 -1 O VAL I 110 N LYS I 98 SHEET 1 AD7 4 LEU J 3 SER J 6 0 SHEET 2 AD7 4 ALA J 18 GLY J 24 -1 O SER J 21 N SER J 6 SHEET 3 AD7 4 ASP J 73 ILE J 78 -1 O PHE J 74 N CYS J 22 SHEET 4 AD7 4 PHE J 65 SER J 70 -1 N SER J 68 O THR J 75 SHEET 1 AD8 2 ASP J 29 SER J 30 0 SHEET 2 AD8 2 ASN J 33 SER J 34 -1 O ASN J 33 N SER J 30 SHEET 1 AD9 5 ASN J 56 LEU J 57 0 SHEET 2 AD9 5 LYS J 48 TYR J 52 -1 N TYR J 52 O ASN J 56 SHEET 3 AD9 5 MET J 36 GLN J 41 -1 N GLN J 40 O LYS J 48 SHEET 4 AD9 5 ALA J 87 GLN J 93 -1 O GLN J 92 N HIS J 37 SHEET 5 AD9 5 LYS J 106 LEU J 107 -1 O LEU J 107 N ALA J 87 SHEET 1 AE1 4 LEU K 3 SER K 6 0 SHEET 2 AE1 4 ALA K 18 GLY K 24 -1 O SER K 21 N SER K 6 SHEET 3 AE1 4 ASP K 73 ILE K 78 -1 O PHE K 74 N CYS K 22 SHEET 4 AE1 4 PHE K 65 SER K 70 -1 N SER K 68 O THR K 75 SHEET 1 AE2 2 ASP K 29 SER K 30 0 SHEET 2 AE2 2 ASN K 33 SER K 34 -1 O ASN K 33 N SER K 30 SHEET 1 AE3 4 ASN K 56 LEU K 57 0 SHEET 2 AE3 4 LYS K 48 TYR K 52 -1 N TYR K 52 O ASN K 56 SHEET 3 AE3 4 MET K 36 GLN K 41 -1 N GLN K 40 O LYS K 48 SHEET 4 AE3 4 THR K 88 GLN K 93 -1 O GLN K 92 N HIS K 37 SHEET 1 AE4 4 LEU L 3 SER L 6 0 SHEET 2 AE4 4 ALA L 18 GLY L 24 -1 O SER L 21 N SER L 6 SHEET 3 AE4 4 ASP L 73 ILE L 78 -1 O PHE L 74 N CYS L 22 SHEET 4 AE4 4 PHE L 65 SER L 70 -1 N SER L 70 O ASP L 73 SHEET 1 AE5 2 ASP L 29 SER L 30 0 SHEET 2 AE5 2 ASN L 33 SER L 34 -1 O ASN L 33 N SER L 30 SHEET 1 AE6 5 ASN L 56 LEU L 57 0 SHEET 2 AE6 5 LYS L 48 TYR L 52 -1 N TYR L 52 O ASN L 56 SHEET 3 AE6 5 MET L 36 GLN L 41 -1 N GLN L 40 O LYS L 48 SHEET 4 AE6 5 ALA L 87 GLN L 93 -1 O GLN L 92 N HIS L 37 SHEET 5 AE6 5 LYS L 106 LEU L 107 -1 O LEU L 107 N ALA L 87 SSBOND 1 CYS A 164 CYS A 171 1555 1555 2.04 SSBOND 2 CYS A 227 CYS A 246 1555 1555 2.03 SSBOND 3 CYS A 275 CYS A 282 1555 1555 2.04 SSBOND 4 CYS A 382 CYS A 413 1555 1555 2.03 SSBOND 5 CYS A 405 CYS A 408 1555 1555 2.02 SSBOND 6 CYS A 437 CYS D 498 1555 1555 2.04 SSBOND 7 CYS B 164 CYS B 171 1555 1555 2.04 SSBOND 8 CYS B 227 CYS B 246 1555 1555 2.03 SSBOND 9 CYS B 275 CYS B 282 1555 1555 2.04 SSBOND 10 CYS B 382 CYS B 413 1555 1555 2.03 SSBOND 11 CYS B 405 CYS B 408 1555 1555 2.02 SSBOND 12 CYS B 437 CYS E 498 1555 1555 2.04 SSBOND 13 CYS C 164 CYS C 171 1555 1555 2.04 SSBOND 14 CYS C 227 CYS C 246 1555 1555 2.03 SSBOND 15 CYS C 275 CYS C 282 1555 1555 2.04 SSBOND 16 CYS C 382 CYS C 413 1555 1555 2.03 SSBOND 17 CYS C 405 CYS C 408 1555 1555 2.02 SSBOND 18 CYS C 437 CYS F 498 1555 1555 2.03 SSBOND 19 CYS D 551 CYS D 559 1555 1555 2.03 SSBOND 20 CYS E 551 CYS E 559 1555 1555 2.03 SSBOND 21 CYS F 551 CYS F 559 1555 1555 2.03 SSBOND 22 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 23 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 24 CYS I 22 CYS I 96 1555 1555 2.03 SSBOND 25 CYS J 22 CYS J 91 1555 1555 2.03 SSBOND 26 CYS K 22 CYS K 91 1555 1555 2.03 SSBOND 27 CYS L 22 CYS L 91 1555 1555 2.03 LINK ND2 ASN A 100 C1 NAG A 501 1555 1555 1.44 LINK ND2 ASN A 128 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 153 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 274 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 355 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 372 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN B 100 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 128 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN B 153 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN B 274 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN B 355 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN B 372 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN C 100 C1 NAG C 501 1555 1555 1.44 LINK ND2 ASN C 128 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN C 153 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN C 274 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 355 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN C 372 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN D 507 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN D 554 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN D 566 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN D 585 C1 NAG D 801 1555 1555 1.44 LINK ND2 ASN E 507 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 554 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN E 566 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN E 585 C1 NAG E 801 1555 1555 1.44 LINK ND2 ASN F 507 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN F 554 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN F 566 C1 NAG j 1 1555 1555 1.44 LINK ND2 ASN F 585 C1 NAG F 801 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.44 LINK O3 BMA M 3 C1 MAN M 4 1555 1555 1.44 LINK O6 BMA M 3 C1 MAN M 5 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.44 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.44 LINK O6 BMA R 3 C1 MAN R 5 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.45 LINK O3 BMA W 3 C1 MAN W 4 1555 1555 1.45 LINK O6 BMA W 3 C1 MAN W 5 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.44 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG b 2 C1 BMA b 3 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O6 NAG d 1 C1 FUC d 4 1555 1555 1.44 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.45 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.45 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.44 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.44 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O6 NAG g 1 C1 FUC g 4 1555 1555 1.44 LINK O4 NAG g 2 C1 BMA g 3 1555 1555 1.45 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG h 2 C1 BMA h 3 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.44 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.44 LINK O6 NAG j 1 C1 FUC j 4 1555 1555 1.44 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.45 CISPEP 1 GLY A 135 PRO A 136 0 2.87 CISPEP 2 GLY A 316 GLU A 317 0 0.57 CISPEP 3 SER A 329 PRO A 330 0 0.69 CISPEP 4 PRO A 385 PRO A 386 0 6.76 CISPEP 5 GLY B 135 PRO B 136 0 3.55 CISPEP 6 GLY B 316 GLU B 317 0 2.10 CISPEP 7 SER B 329 PRO B 330 0 -0.40 CISPEP 8 PRO B 385 PRO B 386 0 6.30 CISPEP 9 GLY C 135 PRO C 136 0 4.30 CISPEP 10 GLY C 316 GLU C 317 0 2.19 CISPEP 11 SER C 329 PRO C 330 0 0.25 CISPEP 12 PRO C 385 PRO C 386 0 6.85 CISPEP 13 SER J 6 PRO J 7 0 -2.66 CISPEP 14 ASP J 97 PRO J 98 0 8.05 CISPEP 15 SER K 6 PRO K 7 0 -2.63 CISPEP 16 ASP K 97 PRO K 98 0 3.65 CISPEP 17 SER L 6 PRO L 7 0 -2.78 CISPEP 18 ASP L 97 PRO L 98 0 5.90 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