HEADER VIRAL PROTEIN/IMMUNE SYSTEM 29-DEC-23 8VGV TITLE DH270.6 FAB BOUND TO THE HIV-1 CH848 DE3 SOSIP CAVEAT 8VGV MAN O 6 HAS WRONG CHIRALITY AT ATOM C5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CH848 DE3 SOSIP GP120; COMPND 3 CHAIN: A, E, I; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CH848 DE3 SOSIP GP41; COMPND 8 CHAIN: B, F, J; COMPND 9 SYNONYM: ENV POLYPROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: DH270.6 ANTIBODY FAB HEAVY CHAIN; COMPND 13 CHAIN: C, G, K; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: DH270.6 ANTIBODY FAB LIGHT CHAIN; COMPND 17 CHAIN: D, H, L; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IMMUNOGEN, VACCINE, ANTIBODY, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.HENDERSON,P.ACHARYA REVDAT 1 02-OCT-24 8VGV 0 JRNL AUTH R.HENDERSON,B.F.HAYNES JRNL TITL ENGINEERING IMMUNOGENS THAT SELECT FOR SPECIFIC MUTATIONS IN JRNL TITL 2 HIV BROADLY NEUTRALIZING ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.600 REMARK 3 NUMBER OF PARTICLES : 236154 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 8VGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1000280211. 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 : ANTIBODY FAB BOUND HIV-1 REMARK 245 ECTODOMAIN 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 : 7.10 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 420.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 4710.00 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) : 6000.00 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: DODECAMERIC 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 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 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 ILE B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 MET B 565 REMARK 465 LEU B 566 REMARK 465 GLN B 567 REMARK 465 LEU B 568 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 ILE F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 MET F 565 REMARK 465 LEU F 566 REMARK 465 GLN F 567 REMARK 465 LEU F 568 REMARK 465 ILE J 548 REMARK 465 VAL J 549 REMARK 465 GLN J 550 REMARK 465 GLN J 551 REMARK 465 GLN J 552 REMARK 465 SER J 553 REMARK 465 ASN J 554 REMARK 465 LEU J 555 REMARK 465 LEU J 556 REMARK 465 ARG J 557 REMARK 465 ALA J 558 REMARK 465 ILE J 559 REMARK 465 GLU J 560 REMARK 465 ALA J 561 REMARK 465 GLN J 562 REMARK 465 GLN J 563 REMARK 465 HIS J 564 REMARK 465 MET J 565 REMARK 465 LEU J 566 REMARK 465 GLN J 567 REMARK 465 LEU J 568 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 O MET A 369 OG1 THR A 373 2.10 REMARK 500 O MET E 369 OG1 THR E 373 2.12 REMARK 500 O GLY H 94 OG1 THR H 98 2.15 REMARK 500 OG SER C 7 OG SER C 21 2.15 REMARK 500 O MET I 369 OG1 THR I 373 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ALA A 55 C - N - CA ANGL. DEV. = 19.1 DEGREES REMARK 500 PRO A 177 C - N - CD ANGL. DEV. = -20.0 DEGREES REMARK 500 VAL B 513 C - N - CA ANGL. DEV. = 19.2 DEGREES REMARK 500 ALA E 55 C - N - CA ANGL. DEV. = 18.8 DEGREES REMARK 500 PRO E 177 C - N - CD ANGL. DEV. = -21.5 DEGREES REMARK 500 VAL F 513 C - N - CA ANGL. DEV. = 19.7 DEGREES REMARK 500 ALA I 55 C - N - CA ANGL. DEV. = 18.9 DEGREES REMARK 500 PRO I 177 C - N - CD ANGL. DEV. = -22.0 DEGREES REMARK 500 VAL J 513 C - N - CA ANGL. DEV. = 18.7 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 LYS A 49 74.66 -100.02 REMARK 500 ALA A 55 64.36 66.15 REMARK 500 SER A 56 -168.47 -79.74 REMARK 500 ALA A 60 33.95 -99.62 REMARK 500 GLU A 62 -158.38 -80.52 REMARK 500 VAL A 85 78.31 54.01 REMARK 500 LEU A 122 32.85 -94.76 REMARK 500 THR A 138 -1.03 72.33 REMARK 500 PRO A 177 -48.43 44.67 REMARK 500 THR A 198 -32.53 -132.81 REMARK 500 GLN A 258 -8.08 75.40 REMARK 500 ASN A 377 46.91 -140.39 REMARK 500 SER A 462 -73.01 -80.42 REMARK 500 ASN A 463 4.66 56.62 REMARK 500 VAL B 513 135.12 49.38 REMARK 500 PHE B 522 148.54 -174.75 REMARK 500 LEU B 523 13.66 54.23 REMARK 500 THR B 529 142.67 70.78 REMARK 500 SER B 599 -67.07 -96.55 REMARK 500 LEU B 602 -10.91 74.22 REMARK 500 SER C 17 144.40 68.13 REMARK 500 LEU D 4 127.18 66.70 REMARK 500 ASN D 54 48.15 -140.73 REMARK 500 GLU E 62 -157.45 -79.71 REMARK 500 THR E 71 -6.31 -140.02 REMARK 500 VAL E 85 70.53 57.93 REMARK 500 LEU E 122 33.58 -97.76 REMARK 500 LYS E 137 -26.73 74.84 REMARK 500 THR E 138 -28.41 -153.74 REMARK 500 ALA E 172 145.40 -171.39 REMARK 500 PRO E 177 -44.67 46.42 REMARK 500 THR E 198 -33.59 -134.38 REMARK 500 PRO E 253 49.93 -84.50 REMARK 500 GLN E 258 -7.46 75.22 REMARK 500 ASN E 262 18.59 58.27 REMARK 500 ASN E 377 44.62 -140.56 REMARK 500 ARG E 432 32.36 -99.57 REMARK 500 SER E 462 -70.54 -80.86 REMARK 500 ASN E 463 4.57 58.30 REMARK 500 PRO E 493 -167.43 -71.85 REMARK 500 LEU E 494 61.71 67.87 REMARK 500 THR E 499 13.62 -141.21 REMARK 500 VAL F 513 138.70 50.05 REMARK 500 LEU F 523 13.89 54.04 REMARK 500 THR F 529 154.96 69.07 REMARK 500 SER F 599 -61.97 -99.15 REMARK 500 LEU F 602 -10.56 74.58 REMARK 500 TYR F 638 -2.12 69.38 REMARK 500 SER G 17 144.74 68.00 REMARK 500 LEU H 4 70.57 57.81 REMARK 500 REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 CYS A 119 VAL A 120 -146.50 REMARK 500 LYS A 176 PRO A 177 -144.65 REMARK 500 PHE A 376 ASN A 377 149.76 REMARK 500 THR A 450 GLY A 451 144.28 REMARK 500 PHE B 522 LEU B 523 145.84 REMARK 500 CYS E 119 VAL E 120 -147.25 REMARK 500 LYS E 176 PRO E 177 -142.86 REMARK 500 LYS E 327 GLN E 328 147.21 REMARK 500 THR E 450 GLY E 451 144.11 REMARK 500 CYS I 119 VAL I 120 -145.57 REMARK 500 LYS I 176 PRO I 177 -140.90 REMARK 500 ILE I 326 LYS I 327 -144.48 REMARK 500 LYS I 327 GLN I 328 149.95 REMARK 500 PHE I 376 ASN I 377 148.48 REMARK 500 THR I 450 GLY I 451 141.48 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43225 RELATED DB: EMDB REMARK 900 DH270.6 FAB BOUND TO THE HIV-1 CH848 DE3 SOSIP DBREF1 8VGV A 34 505 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGV A A0A1W6IPB2 30 489 DBREF1 8VGV B 512 664 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGV B A0A1W6IPB2 496 648 DBREF 8VGV C 1 126 PDB 8VGV 8VGV 1 126 DBREF 8VGV D 3 110 PDB 8VGV 8VGV 3 110 DBREF1 8VGV E 34 505 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGV E A0A1W6IPB2 30 489 DBREF1 8VGV F 512 664 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGV F A0A1W6IPB2 496 648 DBREF 8VGV G 1 126 PDB 8VGV 8VGV 1 126 DBREF 8VGV H 3 110 PDB 8VGV 8VGV 3 110 DBREF1 8VGV I 34 505 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGV I A0A1W6IPB2 30 489 DBREF1 8VGV J 512 664 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGV J A0A1W6IPB2 496 648 DBREF 8VGV K 1 126 PDB 8VGV 8VGV 1 126 DBREF 8VGV L 3 110 PDB 8VGV 8VGV 3 110 SEQADV 8VGV GLU A 32 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGV ASN A 33 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGV ASP A 133 UNP A0A1W6IPB ASN 129 CONFLICT SEQADV 8VGV THR A 138 UNP A0A1W6IPB ASN 134 CONFLICT SEQADV 8VGV CYS A 201 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8VGV CYS A 433 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8VGV LYS A 490 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8VGV GLU A 492 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8VGV VAL A 496 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8VGV ARG A 500 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8VGV CYS A 501 UNP A0A1W6IPB ALA 485 CONFLICT SEQADV 8VGV VAL B 513 UNP A0A1W6IPB ALA 497 CONFLICT SEQADV 8VGV ILE B 515 UNP A0A1W6IPB LEU 499 CONFLICT SEQADV 8VGV VAL B 518 UNP A0A1W6IPB LEU 502 CONFLICT SEQADV 8VGV MET B 535 UNP A0A1W6IPB ILE 519 CONFLICT SEQADV 8VGV ASN B 543 UNP A0A1W6IPB GLN 527 CONFLICT SEQADV 8VGV VAL B 583 UNP A0A1W6IPB LEU 567 CONFLICT SEQADV 8VGV ARG B 588 UNP A0A1W6IPB LYS 572 CONFLICT SEQADV 8VGV ILE B 595 UNP A0A1W6IPB MET 579 CONFLICT SEQADV 8VGV CYS B 605 UNP A0A1W6IPB THR 589 CONFLICT SEQADV 8VGV SER B 612 UNP A0A1W6IPB THR 596 CONFLICT SEQADV 8VGV ARG B 617 UNP A0A1W6IPB LYS 601 CONFLICT SEQADV 8VGV ASN B 618 UNP A0A1W6IPB SER 602 CONFLICT SEQADV 8VGV LEU B 619 UNP A0A1W6IPB GLU 603 CONFLICT SEQADV 8VGV SER B 620 UNP A0A1W6IPB THR 604 CONFLICT SEQADV 8VGV GLU B 621 UNP A0A1W6IPB ASP 605 CONFLICT SEQADV 8VGV LEU B 629 UNP A0A1W6IPB MET 613 CONFLICT SEQADV 8VGV ASP B 632 UNP A0A1W6IPB GLU 616 CONFLICT SEQADV 8VGV LYS B 633 UNP A0A1W6IPB ARG 617 CONFLICT SEQADV 8VGV GLN B 640 UNP A0A1W6IPB GLU 624 CONFLICT SEQADV 8VGV ILE B 641 UNP A0A1W6IPB THR 625 CONFLICT SEQADV 8VGV GLY B 644 UNP A0A1W6IPB LYS 628 CONFLICT SEQADV 8VGV GLU B 648 UNP A0A1W6IPB ASP 632 CONFLICT SEQADV 8VGV LYS B 655 UNP A0A1W6IPB ARG 639 CONFLICT SEQADV 8VGV GLU E 32 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGV ASN E 33 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGV ASP E 133 UNP A0A1W6IPB ASN 129 CONFLICT SEQADV 8VGV THR E 138 UNP A0A1W6IPB ASN 134 CONFLICT SEQADV 8VGV CYS E 201 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8VGV CYS E 433 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8VGV LYS E 490 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8VGV GLU E 492 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8VGV VAL E 496 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8VGV ARG E 500 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8VGV CYS E 501 UNP A0A1W6IPB ALA 485 CONFLICT SEQADV 8VGV VAL F 513 UNP A0A1W6IPB ALA 497 CONFLICT SEQADV 8VGV ILE F 515 UNP A0A1W6IPB LEU 499 CONFLICT SEQADV 8VGV VAL F 518 UNP A0A1W6IPB LEU 502 CONFLICT SEQADV 8VGV MET F 535 UNP A0A1W6IPB ILE 519 CONFLICT SEQADV 8VGV ASN F 543 UNP A0A1W6IPB GLN 527 CONFLICT SEQADV 8VGV VAL F 583 UNP A0A1W6IPB LEU 567 CONFLICT SEQADV 8VGV ARG F 588 UNP A0A1W6IPB LYS 572 CONFLICT SEQADV 8VGV ILE F 595 UNP A0A1W6IPB MET 579 CONFLICT SEQADV 8VGV CYS F 605 UNP A0A1W6IPB THR 589 CONFLICT SEQADV 8VGV SER F 612 UNP A0A1W6IPB THR 596 CONFLICT SEQADV 8VGV ARG F 617 UNP A0A1W6IPB LYS 601 CONFLICT SEQADV 8VGV ASN F 618 UNP A0A1W6IPB SER 602 CONFLICT SEQADV 8VGV LEU F 619 UNP A0A1W6IPB GLU 603 CONFLICT SEQADV 8VGV SER F 620 UNP A0A1W6IPB THR 604 CONFLICT SEQADV 8VGV GLU F 621 UNP A0A1W6IPB ASP 605 CONFLICT SEQADV 8VGV LEU F 629 UNP A0A1W6IPB MET 613 CONFLICT SEQADV 8VGV ASP F 632 UNP A0A1W6IPB GLU 616 CONFLICT SEQADV 8VGV LYS F 633 UNP A0A1W6IPB ARG 617 CONFLICT SEQADV 8VGV GLN F 640 UNP A0A1W6IPB GLU 624 CONFLICT SEQADV 8VGV ILE F 641 UNP A0A1W6IPB THR 625 CONFLICT SEQADV 8VGV GLY F 644 UNP A0A1W6IPB LYS 628 CONFLICT SEQADV 8VGV GLU F 648 UNP A0A1W6IPB ASP 632 CONFLICT SEQADV 8VGV LYS F 655 UNP A0A1W6IPB ARG 639 CONFLICT SEQADV 8VGV GLU I 32 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGV ASN I 33 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGV ASP I 133 UNP A0A1W6IPB ASN 129 CONFLICT SEQADV 8VGV THR I 138 UNP A0A1W6IPB ASN 134 CONFLICT SEQADV 8VGV CYS I 201 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8VGV CYS I 433 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8VGV LYS I 490 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8VGV GLU I 492 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8VGV VAL I 496 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8VGV ARG I 500 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8VGV CYS I 501 UNP A0A1W6IPB ALA 485 CONFLICT SEQADV 8VGV VAL J 513 UNP A0A1W6IPB ALA 497 CONFLICT SEQADV 8VGV ILE J 515 UNP A0A1W6IPB LEU 499 CONFLICT SEQADV 8VGV VAL J 518 UNP A0A1W6IPB LEU 502 CONFLICT SEQADV 8VGV MET J 535 UNP A0A1W6IPB ILE 519 CONFLICT SEQADV 8VGV ASN J 543 UNP A0A1W6IPB GLN 527 CONFLICT SEQADV 8VGV VAL J 583 UNP A0A1W6IPB LEU 567 CONFLICT SEQADV 8VGV ARG J 588 UNP A0A1W6IPB LYS 572 CONFLICT SEQADV 8VGV ILE J 595 UNP A0A1W6IPB MET 579 CONFLICT SEQADV 8VGV CYS J 605 UNP A0A1W6IPB THR 589 CONFLICT SEQADV 8VGV SER J 612 UNP A0A1W6IPB THR 596 CONFLICT SEQADV 8VGV ARG J 617 UNP A0A1W6IPB LYS 601 CONFLICT SEQADV 8VGV ASN J 618 UNP A0A1W6IPB SER 602 CONFLICT SEQADV 8VGV LEU J 619 UNP A0A1W6IPB GLU 603 CONFLICT SEQADV 8VGV SER J 620 UNP A0A1W6IPB THR 604 CONFLICT SEQADV 8VGV GLU J 621 UNP A0A1W6IPB ASP 605 CONFLICT SEQADV 8VGV LEU J 629 UNP A0A1W6IPB MET 613 CONFLICT SEQADV 8VGV ASP J 632 UNP A0A1W6IPB GLU 616 CONFLICT SEQADV 8VGV LYS J 633 UNP A0A1W6IPB ARG 617 CONFLICT SEQADV 8VGV GLN J 640 UNP A0A1W6IPB GLU 624 CONFLICT SEQADV 8VGV ILE J 641 UNP A0A1W6IPB THR 625 CONFLICT SEQADV 8VGV GLY J 644 UNP A0A1W6IPB LYS 628 CONFLICT SEQADV 8VGV GLU J 648 UNP A0A1W6IPB ASP 632 CONFLICT SEQADV 8VGV LYS J 655 UNP A0A1W6IPB ARG 639 CONFLICT SEQRES 1 A 462 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 A 462 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 A 462 ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP ALA SEQRES 4 A 462 THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN GLU SEQRES 5 A 462 LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 A 462 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE ILE SEQRES 7 A 462 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 A 462 THR PRO LEU CYS VAL THR LEU ILE CYS SER ASP ALA THR SEQRES 9 A 462 VAL LYS THR GLY THR VAL GLU GLU MET LYS ASN CYS SER SEQRES 10 A 462 PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS LYS SEQRES 11 A 462 GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO LEU SEQRES 12 A 462 SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE ASN SEQRES 13 A 462 CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS VAL SEQRES 14 A 462 THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA SEQRES 15 A 462 GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE ASN SEQRES 16 A 462 GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN CYS SEQRES 17 A 462 THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 A 462 LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE ARG SEQRES 19 A 462 SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE VAL SEQRES 20 A 462 HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG PRO SEQRES 21 A 462 ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO GLY SEQRES 22 A 462 GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE SEQRES 23 A 462 LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP ASN SEQRES 24 A 462 ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS HIS SEQRES 25 A 462 PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA GLY SEQRES 26 A 462 GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 A 462 GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE ASN SEQRES 28 A 462 GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SER SEQRES 29 A 462 ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG ILE SEQRES 30 A 462 LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG CYS SEQRES 31 A 462 MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS ARG SEQRES 32 A 462 SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY GLY SEQRES 33 A 462 THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA GLY SEQRES 34 A 462 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 35 A 462 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 36 A 462 THR ARG CYS LYS ARG ARG VAL SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 B 153 HIS MET LEU GLN LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 C 126 GLN VAL GLN LEU VAL GLN SER GLY ALA GLN MET LYS ASN SEQRES 2 C 126 PRO GLY ALA SER VAL LYS VAL SER CYS ALA PRO SER GLY SEQRES 3 C 126 TYR THR PHE THR ASP PHE TYR ILE HIS TRP LEU ARG GLN SEQRES 4 C 126 ALA PRO GLY GLN GLY LEU GLN TRP MET GLY TRP MET ASN SEQRES 5 C 126 PRO GLN THR GLY ARG THR ASN THR ALA ARG ASN PHE GLN SEQRES 6 C 126 GLY ARG VAL THR MET THR ARG ASP THR SER ILE GLY THR SEQRES 7 C 126 ALA TYR MET GLU LEU ARG SER LEU THR SER ASP ASP THR SEQRES 8 C 126 ALA ILE TYR TYR CYS THR THR GLY GLY TRP ILE SER LEU SEQRES 9 C 126 TYR TYR ASP SER SER TYR TYR PRO ASN PHE ASP HIS TRP SEQRES 10 C 126 GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 1 D 108 ALA LEU THR GLN PRO ALA SER VAL SER GLY SER PRO GLY SEQRES 2 D 108 GLN SER ILE THR ILE SER CYS THR GLY THR LYS TYR ASP SEQRES 3 D 108 VAL GLY SER HIS ASP LEU VAL SER TRP TYR GLN GLN TYR SEQRES 4 D 108 PRO GLY LYS VAL PRO LYS TYR MET ILE TYR GLU VAL ASN SEQRES 5 D 108 LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER GLY SER SEQRES 6 D 108 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 D 108 ARG ALA GLU ASP GLU ALA ASP TYR TYR CYS CYS SER PHE SEQRES 8 D 108 GLY GLY SER ALA THR VAL VAL CYS GLY GLY GLY THR LYS SEQRES 9 D 108 VAL THR VAL LEU SEQRES 1 E 462 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 E 462 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 E 462 ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP ALA SEQRES 4 E 462 THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN GLU SEQRES 5 E 462 LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 E 462 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE ILE SEQRES 7 E 462 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 E 462 THR PRO LEU CYS VAL THR LEU ILE CYS SER ASP ALA THR SEQRES 9 E 462 VAL LYS THR GLY THR VAL GLU GLU MET LYS ASN CYS SER SEQRES 10 E 462 PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS LYS SEQRES 11 E 462 GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO LEU SEQRES 12 E 462 SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE ASN SEQRES 13 E 462 CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS VAL SEQRES 14 E 462 THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA SEQRES 15 E 462 GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE ASN SEQRES 16 E 462 GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN CYS SEQRES 17 E 462 THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 E 462 LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE ARG SEQRES 19 E 462 SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE VAL SEQRES 20 E 462 HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG PRO SEQRES 21 E 462 ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO GLY SEQRES 22 E 462 GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE SEQRES 23 E 462 LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP ASN SEQRES 24 E 462 ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS HIS SEQRES 25 E 462 PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA GLY SEQRES 26 E 462 GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 E 462 GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE ASN SEQRES 28 E 462 GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SER SEQRES 29 E 462 ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG ILE SEQRES 30 E 462 LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG CYS SEQRES 31 E 462 MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS ARG SEQRES 32 E 462 SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY GLY SEQRES 33 E 462 THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA GLY SEQRES 34 E 462 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 35 E 462 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 36 E 462 THR ARG CYS LYS ARG ARG VAL SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 F 153 HIS MET LEU GLN LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 126 GLN VAL GLN LEU VAL GLN SER GLY ALA GLN MET LYS ASN SEQRES 2 G 126 PRO GLY ALA SER VAL LYS VAL SER CYS ALA PRO SER GLY SEQRES 3 G 126 TYR THR PHE THR ASP PHE TYR ILE HIS TRP LEU ARG GLN SEQRES 4 G 126 ALA PRO GLY GLN GLY LEU GLN TRP MET GLY TRP MET ASN SEQRES 5 G 126 PRO GLN THR GLY ARG THR ASN THR ALA ARG ASN PHE GLN SEQRES 6 G 126 GLY ARG VAL THR MET THR ARG ASP THR SER ILE GLY THR SEQRES 7 G 126 ALA TYR MET GLU LEU ARG SER LEU THR SER ASP ASP THR SEQRES 8 G 126 ALA ILE TYR TYR CYS THR THR GLY GLY TRP ILE SER LEU SEQRES 9 G 126 TYR TYR ASP SER SER TYR TYR PRO ASN PHE ASP HIS TRP SEQRES 10 G 126 GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 1 H 108 ALA LEU THR GLN PRO ALA SER VAL SER GLY SER PRO GLY SEQRES 2 H 108 GLN SER ILE THR ILE SER CYS THR GLY THR LYS TYR ASP SEQRES 3 H 108 VAL GLY SER HIS ASP LEU VAL SER TRP TYR GLN GLN TYR SEQRES 4 H 108 PRO GLY LYS VAL PRO LYS TYR MET ILE TYR GLU VAL ASN SEQRES 5 H 108 LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER GLY SER SEQRES 6 H 108 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 H 108 ARG ALA GLU ASP GLU ALA ASP TYR TYR CYS CYS SER PHE SEQRES 8 H 108 GLY GLY SER ALA THR VAL VAL CYS GLY GLY GLY THR LYS SEQRES 9 H 108 VAL THR VAL LEU SEQRES 1 I 462 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 I 462 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 I 462 ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP ALA SEQRES 4 I 462 THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN GLU SEQRES 5 I 462 LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 I 462 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE ILE SEQRES 7 I 462 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 I 462 THR PRO LEU CYS VAL THR LEU ILE CYS SER ASP ALA THR SEQRES 9 I 462 VAL LYS THR GLY THR VAL GLU GLU MET LYS ASN CYS SER SEQRES 10 I 462 PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS LYS SEQRES 11 I 462 GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO LEU SEQRES 12 I 462 SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE ASN SEQRES 13 I 462 CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS VAL SEQRES 14 I 462 THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA SEQRES 15 I 462 GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE ASN SEQRES 16 I 462 GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN CYS SEQRES 17 I 462 THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 I 462 LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE ARG SEQRES 19 I 462 SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE VAL SEQRES 20 I 462 HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG PRO SEQRES 21 I 462 ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO GLY SEQRES 22 I 462 GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE SEQRES 23 I 462 LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP ASN SEQRES 24 I 462 ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS HIS SEQRES 25 I 462 PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA GLY SEQRES 26 I 462 GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 I 462 GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE ASN SEQRES 28 I 462 GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SER SEQRES 29 I 462 ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG ILE SEQRES 30 I 462 LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG CYS SEQRES 31 I 462 MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS ARG SEQRES 32 I 462 SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY GLY SEQRES 33 I 462 THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA GLY SEQRES 34 I 462 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 35 I 462 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 36 I 462 THR ARG CYS LYS ARG ARG VAL SEQRES 1 J 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 J 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 J 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 J 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 J 153 HIS MET LEU GLN LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 J 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 J 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 J 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 J 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 J 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 J 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 J 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 K 126 GLN VAL GLN LEU VAL GLN SER GLY ALA GLN MET LYS ASN SEQRES 2 K 126 PRO GLY ALA SER VAL LYS VAL SER CYS ALA PRO SER GLY SEQRES 3 K 126 TYR THR PHE THR ASP PHE TYR ILE HIS TRP LEU ARG GLN SEQRES 4 K 126 ALA PRO GLY GLN GLY LEU GLN TRP MET GLY TRP MET ASN SEQRES 5 K 126 PRO GLN THR GLY ARG THR ASN THR ALA ARG ASN PHE GLN SEQRES 6 K 126 GLY ARG VAL THR MET THR ARG ASP THR SER ILE GLY THR SEQRES 7 K 126 ALA TYR MET GLU LEU ARG SER LEU THR SER ASP ASP THR SEQRES 8 K 126 ALA ILE TYR TYR CYS THR THR GLY GLY TRP ILE SER LEU SEQRES 9 K 126 TYR TYR ASP SER SER TYR TYR PRO ASN PHE ASP HIS TRP SEQRES 10 K 126 GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 1 L 108 ALA LEU THR GLN PRO ALA SER VAL SER GLY SER PRO GLY SEQRES 2 L 108 GLN SER ILE THR ILE SER CYS THR GLY THR LYS TYR ASP SEQRES 3 L 108 VAL GLY SER HIS ASP LEU VAL SER TRP TYR GLN GLN TYR SEQRES 4 L 108 PRO GLY LYS VAL PRO LYS TYR MET ILE TYR GLU VAL ASN SEQRES 5 L 108 LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER GLY SER SEQRES 6 L 108 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 L 108 ARG ALA GLU ASP GLU ALA ASP TYR TYR CYS CYS SER PHE SEQRES 8 L 108 GLY GLY SER ALA THR VAL VAL CYS GLY GLY GLY THR LYS SEQRES 9 L 108 VAL THR VAL LEU HET NAG M 1 27 HET NAG M 2 27 HET BMA M 3 21 HET MAN M 4 21 HET MAN M 5 21 HET MAN M 6 22 HET NAG N 1 27 HET NAG N 2 27 HET BMA N 3 22 HET NAG O 1 27 HET NAG O 2 27 HET BMA O 3 21 HET MAN O 4 21 HET MAN O 5 21 HET MAN O 6 22 HET NAG P 1 27 HET NAG P 2 27 HET BMA P 3 22 HET NAG Q 1 27 HET NAG Q 2 27 HET BMA Q 3 21 HET MAN Q 4 21 HET MAN Q 5 21 HET MAN Q 6 22 HET NAG R 1 27 HET NAG R 2 27 HET BMA R 3 22 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 13 NAG 12(C8 H15 N O6) FORMUL 13 BMA 6(C6 H12 O6) FORMUL 13 MAN 9(C6 H12 O6) HELIX 1 AA1 LYS A 63 VAL A 68 1 6 HELIX 2 AA2 ASP A 99 LYS A 117 1 19 HELIX 3 AA3 LEU A 122 CYS A 126 5 5 HELIX 4 AA4 THR A 135 GLY A 139 5 5 HELIX 5 AA5 ASN A 195 THR A 198 5 4 HELIX 6 AA6 GLU A 335 PHE A 353 1 19 HELIX 7 AA7 ASP A 368 THR A 373 1 6 HELIX 8 AA8 ASN A 377 GLU A 381 5 5 HELIX 9 AA9 ASN A 425 ARG A 432 5 8 HELIX 10 AB1 MET A 475 SER A 481 1 7 HELIX 11 AB2 GLY B 514 PHE B 519 1 6 HELIX 12 AB3 SER B 528 SER B 534 1 7 HELIX 13 AB4 THR B 536 ARG B 542 1 7 HELIX 14 AB5 THR B 569 TRP B 571 5 3 HELIX 15 AB6 GLY B 572 GLY B 597 1 26 HELIX 16 AB7 ASN B 611 SER B 615 5 5 HELIX 17 AB8 ASN B 618 MET B 626 1 9 HELIX 18 AB9 THR B 627 SER B 636 1 10 HELIX 19 AC1 TYR B 638 ASP B 664 1 27 HELIX 20 AC2 THR C 28 THR C 30 5 3 HELIX 21 AC3 ARG C 62 GLN C 65 5 4 HELIX 22 AC4 THR C 87 THR C 91 5 5 HELIX 23 AC5 ARG D 81 GLU D 85 5 5 HELIX 24 AC6 LYS E 63 VAL E 68 1 6 HELIX 25 AC7 ASP E 99 LYS E 117 1 19 HELIX 26 AC8 LEU E 122 CYS E 126 5 5 HELIX 27 AC9 ASN E 195 THR E 198 5 4 HELIX 28 AD1 GLU E 335 PHE E 353 1 19 HELIX 29 AD2 ASP E 368 THR E 373 1 6 HELIX 30 AD3 ASN E 377 GLU E 381 5 5 HELIX 31 AD4 ASN E 425 GLY E 429 5 5 HELIX 32 AD5 MET E 475 SER E 481 1 7 HELIX 33 AD6 GLY F 514 LEU F 520 1 7 HELIX 34 AD7 SER F 528 SER F 534 1 7 HELIX 35 AD8 THR F 536 ARG F 542 1 7 HELIX 36 AD9 ASN F 543 LEU F 545 5 3 HELIX 37 AE1 THR F 569 TRP F 571 5 3 HELIX 38 AE2 GLY F 572 GLY F 597 1 26 HELIX 39 AE3 ASN F 611 SER F 615 5 5 HELIX 40 AE4 ASN F 618 MET F 626 1 9 HELIX 41 AE5 THR F 627 SER F 636 1 10 HELIX 42 AE6 TYR F 638 ASP F 664 1 27 HELIX 43 AE7 THR G 28 THR G 30 5 3 HELIX 44 AE8 ARG G 62 GLN G 65 5 4 HELIX 45 AE9 THR G 87 THR G 91 5 5 HELIX 46 AF1 ARG H 81 GLU H 85 5 5 HELIX 47 AF2 LYS I 63 VAL I 68 1 6 HELIX 48 AF3 ASP I 99 LYS I 117 1 19 HELIX 49 AF4 LEU I 122 CYS I 126 5 5 HELIX 50 AF5 ASN I 195 THR I 198 5 4 HELIX 51 AF6 GLU I 335 PHE I 353 1 19 HELIX 52 AF7 ASP I 368 THR I 373 1 6 HELIX 53 AF8 ASN I 377 GLU I 381 5 5 HELIX 54 AF9 ASN I 425 ARG I 432 5 8 HELIX 55 AG1 MET I 475 SER I 481 1 7 HELIX 56 AG2 GLY J 514 PHE J 519 1 6 HELIX 57 AG3 SER J 528 SER J 534 1 7 HELIX 58 AG4 THR J 536 ARG J 542 1 7 HELIX 59 AG5 ASN J 543 LEU J 545 5 3 HELIX 60 AG6 THR J 569 TRP J 571 5 3 HELIX 61 AG7 GLY J 572 GLY J 597 1 26 HELIX 62 AG8 ASN J 611 SER J 615 5 5 HELIX 63 AG9 ASN J 618 MET J 626 1 9 HELIX 64 AH1 THR J 627 SER J 636 1 10 HELIX 65 AH2 TYR J 638 ASP J 664 1 27 HELIX 66 AH3 THR K 28 THR K 30 5 3 HELIX 67 AH4 ARG K 62 GLN K 65 5 4 HELIX 68 AH5 THR K 87 THR K 91 5 5 HELIX 69 AH6 ARG L 81 GLU L 85 5 5 SHEET 1 AA1 3 LEU A 494 PRO A 498 0 SHEET 2 AA1 3 TRP A 35 TYR A 40 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AA2 4 TRP A 45 GLU A 47 0 SHEET 2 AA2 4 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 4 TYR A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 SHEET 4 AA2 4 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 1 AA3 2 ALA A 55 SER A 56 0 SHEET 2 AA3 2 VAL A 75 PRO A 76 1 O VAL A 75 N SER A 56 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA5 5 GLU A 167 TYR A 175 0 SHEET 2 AA5 5 MET A 152 THR A 160 -1 N THR A 159 O LYS A 168 SHEET 3 AA5 5 LEU A 129 ASP A 133 -1 N ILE A 130 O SER A 156 SHEET 4 AA5 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA5 5 ILE A 179 PRO A 181 -1 N VAL A 180 O ARG A 192 SHEET 1 AA6 3 THR A 202 GLN A 203 0 SHEET 2 AA6 3 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA6 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA7 6 VAL A 271 ARG A 273 0 SHEET 2 AA7 6 ILE A 284 ARG A 298 -1 O ILE A 285 N ARG A 273 SHEET 3 AA7 6 HIS A 330 SER A 334 -1 O ASN A 332 N VAL A 295 SHEET 4 AA7 6 THR A 413 LYS A 421 -1 O LEU A 416 N CYS A 331 SHEET 5 AA7 6 PHE A 382 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 6 AA7 6 HIS A 374 SER A 375 -1 N HIS A 374 O CYS A 385 SHEET 1 AA8 6 VAL A 271 ARG A 273 0 SHEET 2 AA8 6 ILE A 284 ARG A 298 -1 O ILE A 285 N ARG A 273 SHEET 3 AA8 6 ILE A 443 ASP A 457 -1 O ILE A 449 N VAL A 292 SHEET 4 AA8 6 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AA8 6 THR A 357 TYR A 361 1 N LYS A 360 O PHE A 468 SHEET 6 AA8 6 GLY A 393 TYR A 395 -1 O TYR A 395 N ILE A 358 SHEET 1 AA9 2 LYS A 305 ILE A 309 0 SHEET 2 AA9 2 GLN A 315 ALA A 319 -1 O ALA A 319 N LYS A 305 SHEET 1 AB1 4 GLN C 3 GLN C 6 0 SHEET 2 AB1 4 VAL C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AB1 4 THR C 78 LEU C 83 -1 O ALA C 79 N CYS C 22 SHEET 4 AB1 4 VAL C 68 ASP C 73 -1 N THR C 69 O GLU C 82 SHEET 1 AB2 6 GLN C 10 LYS C 12 0 SHEET 2 AB2 6 THR C 121 VAL C 125 1 O LEU C 122 N GLN C 10 SHEET 3 AB2 6 ALA C 92 TRP C 101 -1 N TYR C 94 O THR C 121 SHEET 4 AB2 6 PHE C 32 GLN C 39 -1 N GLN C 39 O ILE C 93 SHEET 5 AB2 6 LEU C 45 MET C 51 -1 O GLY C 49 N TRP C 36 SHEET 6 AB2 6 THR C 58 THR C 60 -1 O ASN C 59 N TRP C 50 SHEET 1 AB3 5 SER D 9 GLY D 12 0 SHEET 2 AB3 5 THR D 105 VAL D 109 1 O LYS D 106 N VAL D 10 SHEET 3 AB3 5 ASP D 87 PHE D 93 -1 N TYR D 88 O THR D 105 SHEET 4 AB3 5 VAL D 35 GLN D 40 -1 N TYR D 38 O TYR D 89 SHEET 5 AB3 5 LYS D 47 ILE D 50 -1 O LYS D 47 N GLN D 39 SHEET 1 AB4 4 SER D 9 GLY D 12 0 SHEET 2 AB4 4 THR D 105 VAL D 109 1 O LYS D 106 N VAL D 10 SHEET 3 AB4 4 ASP D 87 PHE D 93 -1 N TYR D 88 O THR D 105 SHEET 4 AB4 4 VAL D 99 CYS D 101 -1 O VAL D 100 N SER D 92 SHEET 1 AB5 3 ILE D 18 THR D 23 0 SHEET 2 AB5 3 THR D 72 ILE D 77 -1 O ALA D 73 N CYS D 22 SHEET 3 AB5 3 PHE D 64 SER D 69 -1 N SER D 65 O THR D 76 SHEET 1 AB6 3 GLY E 495 PRO E 498 0 SHEET 2 AB6 3 TRP E 35 TYR E 39 -1 N THR E 37 O ALA E 497 SHEET 3 AB6 3 ILE F 603 PRO F 609 -1 O VAL F 608 N VAL E 36 SHEET 1 AB7 5 TRP E 45 GLU E 47 0 SHEET 2 AB7 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AB7 5 TYR E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AB7 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AB7 5 LEU E 84 VAL E 85 -1 N LEU E 84 O THR E 244 SHEET 1 AB8 2 ALA E 55 SER E 56 0 SHEET 2 AB8 2 VAL E 75 PRO E 76 1 O VAL E 75 N SER E 56 SHEET 1 AB9 2 GLU E 91 ASN E 94 0 SHEET 2 AB9 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AC1 3 LEU E 129 ILE E 130 0 SHEET 2 AC1 3 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 3 AC1 3 ILE E 179 PRO E 181 -1 N VAL E 180 O ARG E 192 SHEET 1 AC2 3 ASP E 133 VAL E 136 0 SHEET 2 AC2 3 GLY E 139 THR E 160 -1 O GLY E 139 N VAL E 136 SHEET 3 AC2 3 GLU E 167 TYR E 175 -1 O GLU E 170 N PHE E 157 SHEET 1 AC3 3 THR E 202 GLN E 203 0 SHEET 2 AC3 3 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC3 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC4 7 LEU E 259 LEU E 261 0 SHEET 2 AC4 7 ILE E 443 ASP E 457 -1 O GLY E 451 N LEU E 260 SHEET 3 AC4 7 ILE E 284 ARG E 298 -1 N VAL E 292 O ILE E 449 SHEET 4 AC4 7 HIS E 330 SER E 334 -1 O ASN E 332 N VAL E 295 SHEET 5 AC4 7 THR E 413 LYS E 421 -1 O LEU E 416 N CYS E 331 SHEET 6 AC4 7 PHE E 382 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AC4 7 HIS E 374 SER E 375 -1 N HIS E 374 O CYS E 385 SHEET 1 AC5 6 VAL E 271 ARG E 273 0 SHEET 2 AC5 6 ILE E 284 ARG E 298 -1 O ILE E 285 N ARG E 273 SHEET 3 AC5 6 ILE E 443 ASP E 457 -1 O ILE E 449 N VAL E 292 SHEET 4 AC5 6 THR E 465 PRO E 470 -1 O THR E 467 N ASP E 457 SHEET 5 AC5 6 THR E 357 TYR E 361 1 N LYS E 360 O PHE E 468 SHEET 6 AC5 6 THR E 394 TYR E 395 -1 O TYR E 395 N ILE E 358 SHEET 1 AC6 2 ASN E 302 ILE E 309 0 SHEET 2 AC6 2 GLN E 315 ILE E 322 -1 O ALA E 319 N LYS E 305 SHEET 1 AC7 4 GLN G 3 GLN G 6 0 SHEET 2 AC7 4 VAL G 18 SER G 25 -1 O ALA G 23 N VAL G 5 SHEET 3 AC7 4 THR G 78 LEU G 83 -1 O MET G 81 N VAL G 20 SHEET 4 AC7 4 VAL G 68 ASP G 73 -1 N THR G 71 O TYR G 80 SHEET 1 AC8 6 GLN G 10 LYS G 12 0 SHEET 2 AC8 6 THR G 121 VAL G 125 1 O LEU G 122 N GLN G 10 SHEET 3 AC8 6 ALA G 92 TRP G 101 -1 N TYR G 94 O THR G 121 SHEET 4 AC8 6 PHE G 32 GLN G 39 -1 N LEU G 37 O TYR G 95 SHEET 5 AC8 6 LEU G 45 MET G 51 -1 O GLN G 46 N ARG G 38 SHEET 6 AC8 6 THR G 58 THR G 60 -1 O ASN G 59 N TRP G 50 SHEET 1 AC9 5 SER H 9 GLY H 12 0 SHEET 2 AC9 5 THR H 105 VAL H 109 1 O LYS H 106 N VAL H 10 SHEET 3 AC9 5 ASP H 87 GLY H 94 -1 N TYR H 88 O THR H 105 SHEET 4 AC9 5 VAL H 35 GLN H 40 -1 N TYR H 38 O TYR H 89 SHEET 5 AC9 5 LYS H 47 ILE H 50 -1 O LYS H 47 N GLN H 39 SHEET 1 AD1 4 SER H 9 GLY H 12 0 SHEET 2 AD1 4 THR H 105 VAL H 109 1 O LYS H 106 N VAL H 10 SHEET 3 AD1 4 ASP H 87 GLY H 94 -1 N TYR H 88 O THR H 105 SHEET 4 AD1 4 THR H 98 CYS H 101 -1 O THR H 98 N GLY H 94 SHEET 1 AD2 3 ILE H 18 THR H 23 0 SHEET 2 AD2 3 THR H 72 ILE H 77 -1 O ALA H 73 N CYS H 22 SHEET 3 AD2 3 PHE H 64 SER H 69 -1 N SER H 65 O THR H 76 SHEET 1 AD3 3 LEU I 494 PRO I 498 0 SHEET 2 AD3 3 TRP I 35 TYR I 40 -1 N TYR I 39 O GLY I 495 SHEET 3 AD3 3 ILE J 603 PRO J 609 -1 O CYS J 604 N VAL I 38 SHEET 1 AD4 4 TRP I 45 GLU I 47 0 SHEET 2 AD4 4 TYR I 486 ILE I 491 -1 O LYS I 490 N LYS I 46 SHEET 3 AD4 4 TYR I 223 CYS I 228 -1 N LEU I 226 O LYS I 487 SHEET 4 AD4 4 VAL I 242 VAL I 245 -1 O SER I 243 N LYS I 227 SHEET 1 AD5 2 ALA I 55 SER I 56 0 SHEET 2 AD5 2 VAL I 75 PRO I 76 1 O VAL I 75 N SER I 56 SHEET 1 AD6 2 GLU I 91 PHE I 93 0 SHEET 2 AD6 2 GLY I 237 CYS I 239 -1 O CYS I 239 N GLU I 91 SHEET 1 AD7 5 GLU I 167 TYR I 175 0 SHEET 2 AD7 5 THR I 148 THR I 160 -1 N LYS I 153 O PHE I 174 SHEET 3 AD7 5 LEU I 129 THR I 135 -1 N ILE I 130 O SER I 156 SHEET 4 AD7 5 GLU I 190 LEU I 193 -1 O TYR I 191 N LEU I 129 SHEET 5 AD7 5 ILE I 179 PRO I 181 -1 N VAL I 180 O ARG I 192 SHEET 1 AD8 3 THR I 202 GLN I 203 0 SHEET 2 AD8 3 MET I 434 TYR I 435 1 O TYR I 435 N THR I 202 SHEET 3 AD8 3 ILE I 423 ILE I 424 -1 N ILE I 424 O MET I 434 SHEET 1 AD9 5 VAL I 271 ARG I 273 0 SHEET 2 AD9 5 ILE I 284 ARG I 298 -1 O ILE I 285 N ARG I 273 SHEET 3 AD9 5 ILE I 443 ASP I 457 -1 O ILE I 449 N VAL I 292 SHEET 4 AD9 5 THR I 465 PRO I 470 -1 O THR I 467 N ASP I 457 SHEET 5 AD9 5 THR I 357 TYR I 361 1 N LYS I 360 O PHE I 468 SHEET 1 AE1 6 VAL I 271 ARG I 273 0 SHEET 2 AE1 6 ILE I 284 ARG I 298 -1 O ILE I 285 N ARG I 273 SHEET 3 AE1 6 HIS I 330 SER I 334 -1 O ASN I 332 N VAL I 295 SHEET 4 AE1 6 THR I 413 LYS I 421 -1 O LEU I 416 N CYS I 331 SHEET 5 AE1 6 PHE I 382 CYS I 385 -1 N TYR I 384 O ARG I 419 SHEET 6 AE1 6 HIS I 374 SER I 375 -1 N HIS I 374 O CYS I 385 SHEET 1 AE2 2 LYS I 305 ARG I 308 0 SHEET 2 AE2 2 THR I 316 ALA I 319 -1 O ALA I 319 N LYS I 305 SHEET 1 AE3 4 GLN K 3 GLN K 6 0 SHEET 2 AE3 4 VAL K 18 SER K 25 -1 O ALA K 23 N VAL K 5 SHEET 3 AE3 4 THR K 78 LEU K 83 -1 O ALA K 79 N CYS K 22 SHEET 4 AE3 4 VAL K 68 ASP K 73 -1 N THR K 71 O TYR K 80 SHEET 1 AE4 6 GLN K 10 LYS K 12 0 SHEET 2 AE4 6 THR K 121 VAL K 125 1 O LEU K 122 N GLN K 10 SHEET 3 AE4 6 ALA K 92 TRP K 101 -1 N ALA K 92 O LEU K 123 SHEET 4 AE4 6 PHE K 32 GLN K 39 -1 N GLN K 39 O ILE K 93 SHEET 5 AE4 6 LEU K 45 MET K 51 -1 O GLN K 46 N ARG K 38 SHEET 6 AE4 6 THR K 58 THR K 60 -1 O ASN K 59 N TRP K 50 SHEET 1 AE5 5 SER L 9 GLY L 12 0 SHEET 2 AE5 5 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AE5 5 ASP L 87 PHE L 93 -1 N TYR L 88 O THR L 105 SHEET 4 AE5 5 VAL L 35 GLN L 40 -1 N TYR L 38 O TYR L 89 SHEET 5 AE5 5 LYS L 47 ILE L 50 -1 O LYS L 47 N GLN L 39 SHEET 1 AE6 4 SER L 9 GLY L 12 0 SHEET 2 AE6 4 THR L 105 VAL L 109 1 O LYS L 106 N VAL L 10 SHEET 3 AE6 4 ASP L 87 PHE L 93 -1 N TYR L 88 O THR L 105 SHEET 4 AE6 4 VAL L 99 CYS L 101 -1 O VAL L 100 N SER L 92 SHEET 1 AE7 3 ILE L 18 THR L 23 0 SHEET 2 AE7 3 THR L 72 ILE L 77 -1 O ALA L 73 N CYS L 22 SHEET 3 AE7 3 PHE L 64 SER L 69 -1 N SER L 69 O THR L 72 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 201 CYS A 433 1555 1555 2.04 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.04 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 11 CYS C 22 CYS C 96 1555 1555 2.04 SSBOND 12 CYS D 22 CYS D 90 1555 1555 2.03 SSBOND 13 CYS D 91 CYS D 101 1555 1555 2.03 SSBOND 14 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 15 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 16 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 17 CYS E 201 CYS E 433 1555 1555 2.04 SSBOND 18 CYS E 218 CYS E 247 1555 1555 2.02 SSBOND 19 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 20 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 21 CYS E 378 CYS E 445 1555 1555 2.05 SSBOND 22 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 23 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 24 CYS G 22 CYS G 96 1555 1555 2.03 SSBOND 25 CYS H 22 CYS H 90 1555 1555 2.03 SSBOND 26 CYS H 91 CYS H 101 1555 1555 2.03 SSBOND 27 CYS I 54 CYS I 74 1555 1555 2.03 SSBOND 28 CYS I 119 CYS I 205 1555 1555 2.03 SSBOND 29 CYS I 126 CYS I 196 1555 1555 2.03 SSBOND 30 CYS I 201 CYS I 433 1555 1555 2.03 SSBOND 31 CYS I 218 CYS I 247 1555 1555 2.03 SSBOND 32 CYS I 228 CYS I 239 1555 1555 2.03 SSBOND 33 CYS I 296 CYS I 331 1555 1555 2.03 SSBOND 34 CYS I 378 CYS I 445 1555 1555 2.04 SSBOND 35 CYS I 385 CYS I 418 1555 1555 2.03 SSBOND 36 CYS J 598 CYS J 604 1555 1555 2.04 SSBOND 37 CYS K 22 CYS K 96 1555 1555 2.03 SSBOND 38 CYS L 22 CYS L 90 1555 1555 2.03 SSBOND 39 CYS L 91 CYS L 101 1555 1555 2.03 LINK ND2 ASN A 301 C1 NAG N 1 1555 1555 1.45 LINK ND2 ASN A 332 C1 NAG M 1 1555 1555 1.43 LINK ND2 ASN E 301 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG O 1 1555 1555 1.43 LINK ND2 ASN I 301 C1 NAG R 1 1555 1555 1.45 LINK ND2 ASN I 332 C1 NAG Q 1 1555 1555 1.43 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 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 O2 MAN M 4 C1 MAN M 5 1555 1555 1.44 LINK O2 MAN M 5 C1 MAN M 6 1555 1555 1.46 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.44 LINK O2 MAN O 4 C1 MAN O 5 1555 1555 1.45 LINK O2 MAN O 5 C1 MAN O 6 1555 1555 1.46 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.44 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.44 LINK O2 MAN Q 4 C1 MAN Q 5 1555 1555 1.45 LINK O2 MAN Q 5 C1 MAN Q 6 1555 1555 1.46 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.46 CISPEP 1 CYS A 54 ALA A 55 0 14.98 CISPEP 2 LEU A 84 VAL A 85 0 9.33 CISPEP 3 SER A 388 ASN A 389 0 10.78 CISPEP 4 ILE A 449 THR A 450 0 6.76 CISPEP 5 ALA B 512 VAL B 513 0 -6.99 CISPEP 6 GLY B 597 CYS B 598 0 7.79 CISPEP 7 CYS B 598 SER B 599 0 -11.98 CISPEP 8 CYS E 54 ALA E 55 0 6.98 CISPEP 9 LEU E 84 VAL E 85 0 15.11 CISPEP 10 SER E 388 ASN E 389 0 7.95 CISPEP 11 ILE E 449 THR E 450 0 5.07 CISPEP 12 ALA F 512 VAL F 513 0 -7.31 CISPEP 13 GLY F 597 CYS F 598 0 6.98 CISPEP 14 CYS F 598 SER F 599 0 -3.46 CISPEP 15 CYS I 54 ALA I 55 0 12.43 CISPEP 16 LEU I 84 VAL I 85 0 10.56 CISPEP 17 SER I 388 ASN I 389 0 9.38 CISPEP 18 ILE I 449 THR I 450 0 0.35 CISPEP 19 ALA J 512 VAL J 513 0 -3.42 CISPEP 20 GLY J 597 CYS J 598 0 5.15 CISPEP 21 CYS J 598 SER J 599 0 -2.44 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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