HEADER VIRAL PROTEIN/IMMUNE SYSTEM 22-MAY-23 8SXJ TITLE CH505 DISULFIDE STAPLED SOSIP BOUND TO CH235.12 FAB CAVEAT 8SXJ RESIDUES THR B 548 AND VAL B 570 THAT ARE NEXT TO EACH OTHER CAVEAT 2 8SXJ IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE CAVEAT 3 8SXJ BETWEEN C AND N IS 19.61. RESIDUES THR F 548 AND VAL F 570 CAVEAT 4 8SXJ THAT ARE NEXT TO EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT CAVEAT 5 8SXJ PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 19.58. CAVEAT 6 8SXJ RESIDUES TRP H 94 AND TRP H 96 THAT ARE NEXT TO EACH OTHER CAVEAT 7 8SXJ IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE CAVEAT 8 8SXJ BETWEEN C AND N IS 2.76. RESIDUES THR J 548 AND VAL J 570 CAVEAT 9 8SXJ THAT ARE NEXT TO EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT CAVEAT 10 8SXJ PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 19.59. CAVEAT 11 8SXJ RESIDUES TRP L 94 AND TRP L 96 THAT ARE NEXT TO EACH OTHER CAVEAT 12 8SXJ IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE CAVEAT 13 8SXJ BETWEEN C AND N IS 2.76. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 3 CHAIN: A, E, I; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HIV-1 GP41; COMPND 8 CHAIN: B, F, J; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: CH235.12 HEAVY CHAIN; COMPND 12 CHAIN: C, G, K; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: CH235.12 LIGHT CHAIN; COMPND 16 CHAIN: D, H, L; COMPND 17 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_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 4; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, ENVELOPE, ENV, ECTODOMAIN, FUSION PROTEIN, VIRAL PROTEIN, KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.HENDERSON JRNL AUTH A.L.BENNETT,R.EDWARDS,I.KOSHELEVA,C.SAUNDERS,Y.BILILIGN, JRNL AUTH 2 A.WILLIAMS,P.BUBPHAMALA,K.MANOSOURI,K.ANASTI,K.O.SAUNDERS, JRNL AUTH 3 S.M.ALAM,B.F.HAYNES,P.ACHARYA,R.HENDERSON JRNL TITL MICROSECOND DYNAMICS CONTROL THE HIV-1 ENVELOPE JRNL TITL 2 CONFORMATION. JRNL REF SCI ADV V. 10 J0396 2024 JRNL REFN ESSN 2375-2548 JRNL PMID 38306419 JRNL DOI 10.1126/SCIADV.ADJ0396 REMARK 2 REMARK 2 RESOLUTION. 4.00 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) : 4.000 REMARK 3 NUMBER OF PARTICLES : 116771 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 8SXJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000274572. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : HUMAN IMMUNODEFICIENCY VIRUS 1 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 TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 100.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2800.00 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) : 57.00 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) : 200 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 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 SER A 405 REMARK 465 THR A 406 REMARK 465 GLU A 407 REMARK 465 THR A 408 REMARK 465 SER E 405 REMARK 465 THR E 406 REMARK 465 GLU E 407 REMARK 465 THR E 408 REMARK 465 SER I 405 REMARK 465 THR I 406 REMARK 465 GLU I 407 REMARK 465 THR I 408 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 ARG A 169 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG A 192 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG A 344 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG A 456 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG B 542 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG B 579 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG B 617 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES REMARK 500 ARG C 66 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES REMARK 500 ARG D 24 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG E 192 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG E 344 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES REMARK 500 ARG F 542 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG F 579 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG F 617 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG G 66 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES REMARK 500 ARG H 24 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG I 166 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG I 169 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES REMARK 500 ARG I 192 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG I 344 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES REMARK 500 ARG I 432 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG J 542 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG J 579 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG J 617 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG K 66 NE - CZ - NH2 ANGL. DEV. = 4.7 DEGREES REMARK 500 ARG L 24 NE - CZ - NH2 ANGL. DEV. = 3.0 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 ALA A 60 -139.78 41.98 REMARK 500 TYR A 61 39.30 -73.14 REMARK 500 TRP A 69 -84.26 -85.43 REMARK 500 ALA A 73 -128.25 54.46 REMARK 500 VAL A 75 175.83 59.72 REMARK 500 ASN A 80 119.20 -166.32 REMARK 500 LEU A 122 23.30 -77.06 REMARK 500 ASN A 138 -1.31 59.00 REMARK 500 THR A 163 -143.33 54.35 REMARK 500 ARG A 166 13.17 59.55 REMARK 500 SER A 188 110.71 47.23 REMARK 500 CYS A 228 97.60 49.80 REMARK 500 GLN A 258 -55.89 62.12 REMARK 500 PRO A 313 46.20 -76.64 REMARK 500 ARG A 412 19.80 52.09 REMARK 500 TRP A 427 14.14 58.24 REMARK 500 ASN A 462 16.63 54.37 REMARK 500 GLU A 480 -34.18 -131.30 REMARK 500 GLU A 490 69.62 -119.67 REMARK 500 ALA B 525 109.61 -163.14 REMARK 500 ALA B 526 133.75 61.71 REMARK 500 ALA B 532 -135.65 51.95 REMARK 500 CYS B 598 52.48 -119.40 REMARK 500 LEU B 619 -21.04 58.99 REMARK 500 ASN B 625 85.79 -164.70 REMARK 500 MET B 626 -54.32 -141.73 REMARK 500 THR B 627 -132.64 -112.11 REMARK 500 LEU C 100C -134.57 -122.88 REMARK 500 ARG D 30 -137.66 50.72 REMARK 500 LEU D 47 -60.93 -104.68 REMARK 500 ALA D 51 8.32 54.78 REMARK 500 SER D 52 -28.86 -161.11 REMARK 500 PHE D 83 72.47 -68.53 REMARK 500 TRP D 94 -154.49 49.27 REMARK 500 ALA E 60 -139.66 41.97 REMARK 500 TYR E 61 39.08 -73.17 REMARK 500 TRP E 69 -84.57 -85.72 REMARK 500 ALA E 73 -128.19 54.52 REMARK 500 VAL E 75 175.93 59.80 REMARK 500 ASN E 80 119.12 -166.43 REMARK 500 SER E 188 108.29 49.12 REMARK 500 CYS E 228 96.56 49.42 REMARK 500 GLN E 258 -56.28 62.26 REMARK 500 ARG E 412 19.61 52.04 REMARK 500 TRP E 427 14.06 58.34 REMARK 500 ASP E 457 -179.30 -67.95 REMARK 500 ASN E 462 18.10 53.68 REMARK 500 GLU E 480 -33.71 -131.38 REMARK 500 GLU E 490 69.53 -119.87 REMARK 500 ALA F 525 109.56 -163.14 REMARK 500 REMARK 500 THIS ENTRY HAS 95 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG C 64 0.10 SIDE CHAIN REMARK 500 ARG E 192 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-40854 RELATED DB: EMDB REMARK 900 CH505 DISULFIDE STAPLED SOSIP BOUND TO CH235.12 FAB DBREF 8SXJ A 35 504 UNP M4M3Q1 M4M3Q1_9HIV1 31 483 DBREF 8SXJ B 518 664 PDB 8SXJ 8SXJ 518 664 DBREF 8SXJ C 1 113 PDB 8SXJ 8SXJ 1 113 DBREF 8SXJ D 1 106 PDB 8SXJ 8SXJ 1 106 DBREF 8SXJ E 35 504 UNP M4M3Q1 M4M3Q1_9HIV1 31 483 DBREF 8SXJ F 518 664 PDB 8SXJ 8SXJ 518 664 DBREF 8SXJ G 1 113 PDB 8SXJ 8SXJ 1 113 DBREF 8SXJ H 1 106 PDB 8SXJ 8SXJ 1 106 DBREF 8SXJ I 35 504 UNP M4M3Q1 M4M3Q1_9HIV1 31 483 DBREF 8SXJ J 518 664 PDB 8SXJ 8SXJ 518 664 DBREF 8SXJ K 1 113 PDB 8SXJ 8SXJ 1 113 DBREF 8SXJ L 1 106 PDB 8SXJ 8SXJ 1 106 SEQADV 8SXJ GLU A 32 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ ASN A 33 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ LEU A 34 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ ILE A 68 UNP M4M3Q1 VAL 64 CONFLICT SEQADV 8SXJ CYS A 127 UNP M4M3Q1 VAL 123 CONFLICT SEQADV 8SXJ CYS A 167 UNP M4M3Q1 ASP 154 CONFLICT SEQADV 8SXJ ASP A 197 UNP M4M3Q1 ASN 184 CONFLICT SEQADV 8SXJ VAL A 204 UNP M4M3Q1 ALA 191 CONFLICT SEQADV 8SXJ LEU A 208 UNP M4M3Q1 VAL 195 CONFLICT SEQADV 8SXJ LEU A 255 UNP M4M3Q1 VAL 242 CONFLICT SEQADV 8SXJ LYS A 279 UNP M4M3Q1 ASN 266 CONFLICT SEQADV 8SXJ TYR A 458 UNP M4M3Q1 GLY 437 CONFLICT SEQADV 8SXJ LYS A 488 UNP M4M3Q1 GLU 467 CONFLICT SEQADV 8SXJ ILE A 489 UNP M4M3Q1 VAL 468 CONFLICT SEQADV 8SXJ GLU A 490 UNP M4M3Q1 LYS 469 CONFLICT SEQADV 8SXJ ARG A 498 UNP M4M3Q1 ASN 477 CONFLICT SEQADV 8SXJ CYS A 499 UNP M4M3Q1 ALA 478 CONFLICT SEQADV 8SXJ LYS A 500 UNP M4M3Q1 ARG 479 CONFLICT SEQADV 8SXJ GLU E 32 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ ASN E 33 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ LEU E 34 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ ILE E 68 UNP M4M3Q1 VAL 64 CONFLICT SEQADV 8SXJ CYS E 127 UNP M4M3Q1 VAL 123 CONFLICT SEQADV 8SXJ CYS E 167 UNP M4M3Q1 ASP 154 CONFLICT SEQADV 8SXJ ASP E 197 UNP M4M3Q1 ASN 184 CONFLICT SEQADV 8SXJ VAL E 204 UNP M4M3Q1 ALA 191 CONFLICT SEQADV 8SXJ LEU E 208 UNP M4M3Q1 VAL 195 CONFLICT SEQADV 8SXJ LEU E 255 UNP M4M3Q1 VAL 242 CONFLICT SEQADV 8SXJ LYS E 279 UNP M4M3Q1 ASN 266 CONFLICT SEQADV 8SXJ TYR E 458 UNP M4M3Q1 GLY 437 CONFLICT SEQADV 8SXJ LYS E 488 UNP M4M3Q1 GLU 467 CONFLICT SEQADV 8SXJ ILE E 489 UNP M4M3Q1 VAL 468 CONFLICT SEQADV 8SXJ GLU E 490 UNP M4M3Q1 LYS 469 CONFLICT SEQADV 8SXJ ARG E 498 UNP M4M3Q1 ASN 477 CONFLICT SEQADV 8SXJ CYS E 499 UNP M4M3Q1 ALA 478 CONFLICT SEQADV 8SXJ LYS E 500 UNP M4M3Q1 ARG 479 CONFLICT SEQADV 8SXJ GLU I 32 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ ASN I 33 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ LEU I 34 UNP M4M3Q1 EXPRESSION TAG SEQADV 8SXJ ILE I 68 UNP M4M3Q1 VAL 64 CONFLICT SEQADV 8SXJ CYS I 127 UNP M4M3Q1 VAL 123 CONFLICT SEQADV 8SXJ CYS I 167 UNP M4M3Q1 ASP 154 CONFLICT SEQADV 8SXJ ASP I 197 UNP M4M3Q1 ASN 184 CONFLICT SEQADV 8SXJ VAL I 204 UNP M4M3Q1 ALA 191 CONFLICT SEQADV 8SXJ LEU I 208 UNP M4M3Q1 VAL 195 CONFLICT SEQADV 8SXJ LEU I 255 UNP M4M3Q1 VAL 242 CONFLICT SEQADV 8SXJ LYS I 279 UNP M4M3Q1 ASN 266 CONFLICT SEQADV 8SXJ TYR I 458 UNP M4M3Q1 GLY 437 CONFLICT SEQADV 8SXJ LYS I 488 UNP M4M3Q1 GLU 467 CONFLICT SEQADV 8SXJ ILE I 489 UNP M4M3Q1 VAL 468 CONFLICT SEQADV 8SXJ GLU I 490 UNP M4M3Q1 LYS 469 CONFLICT SEQADV 8SXJ ARG I 498 UNP M4M3Q1 ASN 477 CONFLICT SEQADV 8SXJ CYS I 499 UNP M4M3Q1 ALA 478 CONFLICT SEQADV 8SXJ LYS I 500 UNP M4M3Q1 ARG 479 CONFLICT SEQRES 1 A 456 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 A 456 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 A 456 ALA LYS ALA TYR GLU LYS GLU VAL HIS ASN ILE TRP ALA SEQRES 4 A 456 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 A 456 MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 A 456 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL ILE SEQRES 7 A 456 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 A 456 THR PRO LEU CYS CYS THR LEU ASN CYS THR ASN ALA THR SEQRES 9 A 456 ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN CYS SEQRES 10 A 456 SER PHE ASN ILE THR THR GLU LEU ARG CYS LYS ARG GLU SEQRES 11 A 456 LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL GLN SEQRES 12 A 456 LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN CYS SEQRES 13 A 456 ASP THR SER VAL ILE THR GLN VAL CYS PRO LYS LEU SER SEQRES 14 A 456 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 15 A 456 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR GLY SEQRES 16 A 456 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 17 A 456 HIS GLY ILE LYS PRO VAL LEU SER THR GLN LEU LEU LEU SEQRES 18 A 456 ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SER SEQRES 19 A 456 GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL HIS SEQRES 20 A 456 LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO ASN SEQRES 21 A 456 ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY GLN SEQRES 22 A 456 ALA PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE ARG SEQRES 23 A 456 GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN GLU SEQRES 24 A 456 THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR PHE SEQRES 25 A 456 PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY GLY SEQRES 26 A 456 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 27 A 456 GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN ARG SEQRES 28 A 456 THR TYR MET ALA ASN SER THR GLU THR ASN SER THR ARG SEQRES 29 A 456 THR ILE THR ILE HIS CYS ARG ILE LYS GLN ILE ILE ASN SEQRES 30 A 456 MET TRP GLN GLU VAL GLY ARG ALA MET TYR ALA PRO PRO SEQRES 31 A 456 ILE ALA GLY ASN ILE THR CYS ILE SER ASN ILE THR GLY SEQRES 32 A 456 LEU LEU LEU THR ARG ASP TYR GLY LYS ASN ASN THR GLU SEQRES 33 A 456 THR PHE ARG PRO GLY GLY GLY ASN MET LYS ASP ASN TRP SEQRES 34 A 456 ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU SEQRES 35 A 456 PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL SEQRES 36 A 456 VAL SEQRES 1 B 126 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 2 B 126 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 3 B 126 LEU LEU SER GLY THR VAL TRP GLY ILE LYS GLN LEU GLN SEQRES 4 B 126 ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN SEQRES 5 B 126 GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE SEQRES 6 B 126 CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER ASN SEQRES 7 B 126 ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP LEU SEQRES 8 B 126 GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE ILE SEQRES 9 B 126 TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU LYS SEQRES 10 B 126 ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 C 122 GLN VAL ARG LEU ALA GLN TYR GLY GLY GLY VAL LYS ARG SEQRES 2 C 122 LEU GLY ALA THR MET THR LEU SER CYS VAL ALA SER GLY SEQRES 3 C 122 TYR THR PHE ASN ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 C 122 ALA PRO GLY GLN GLY PHE GLU LEU LEU GLY TYR ILE ASP SEQRES 5 C 122 PRO ALA ASN GLY ARG PRO ASP TYR ALA GLY ALA LEU ARG SEQRES 6 C 122 GLU ARG LEU SER PHE TYR ARG ASP LYS SER MET GLU THR SEQRES 7 C 122 LEU TYR MET ASP LEU ARG SER LEU ARG TYR ASP ASP THR SEQRES 8 C 122 ALA MET TYR TYR CYS VAL ARG ASN VAL GLY THR ALA GLY SEQRES 9 C 122 SER LEU LEU HIS TYR ASP HIS TRP GLY SER GLY SER PRO SEQRES 10 C 122 VAL ILE VAL SER SER SEQRES 1 D 105 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER ALA SEQRES 2 D 105 SER PRO GLY GLU ARG VAL THR LEU THR CYS ARG ALA SER SEQRES 3 D 105 ARG SER VAL ARG ASN ASN VAL ALA TRP TYR GLN HIS LYS SEQRES 4 D 105 GLY GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 D 105 THR ARG ALA ALA GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 D 105 ALA SER GLY THR GLU PHE THR LEU ALA ILE SER ASN LEU SEQRES 7 D 105 GLU SER GLU ASP PHE THR VAL TYR PHE CYS LEU GLN TYR SEQRES 8 D 105 ASN ASN TRP TRP THR PHE GLY GLN GLY THR ARG VAL ASP SEQRES 9 D 105 ILE SEQRES 1 E 456 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 E 456 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 E 456 ALA LYS ALA TYR GLU LYS GLU VAL HIS ASN ILE TRP ALA SEQRES 4 E 456 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 E 456 MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 E 456 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL ILE SEQRES 7 E 456 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 E 456 THR PRO LEU CYS CYS THR LEU ASN CYS THR ASN ALA THR SEQRES 9 E 456 ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN CYS SEQRES 10 E 456 SER PHE ASN ILE THR THR GLU LEU ARG CYS LYS ARG GLU SEQRES 11 E 456 LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL GLN SEQRES 12 E 456 LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN CYS SEQRES 13 E 456 ASP THR SER VAL ILE THR GLN VAL CYS PRO LYS LEU SER SEQRES 14 E 456 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 15 E 456 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR GLY SEQRES 16 E 456 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 17 E 456 HIS GLY ILE LYS PRO VAL LEU SER THR GLN LEU LEU LEU SEQRES 18 E 456 ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SER SEQRES 19 E 456 GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL HIS SEQRES 20 E 456 LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO ASN SEQRES 21 E 456 ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY GLN SEQRES 22 E 456 ALA PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE ARG SEQRES 23 E 456 GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN GLU SEQRES 24 E 456 THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR PHE SEQRES 25 E 456 PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY GLY SEQRES 26 E 456 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 27 E 456 GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN ARG SEQRES 28 E 456 THR TYR MET ALA ASN SER THR GLU THR ASN SER THR ARG SEQRES 29 E 456 THR ILE THR ILE HIS CYS ARG ILE LYS GLN ILE ILE ASN SEQRES 30 E 456 MET TRP GLN GLU VAL GLY ARG ALA MET TYR ALA PRO PRO SEQRES 31 E 456 ILE ALA GLY ASN ILE THR CYS ILE SER ASN ILE THR GLY SEQRES 32 E 456 LEU LEU LEU THR ARG ASP TYR GLY LYS ASN ASN THR GLU SEQRES 33 E 456 THR PHE ARG PRO GLY GLY GLY ASN MET LYS ASP ASN TRP SEQRES 34 E 456 ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU SEQRES 35 E 456 PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL SEQRES 36 E 456 VAL SEQRES 1 F 126 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 2 F 126 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 3 F 126 LEU LEU SER GLY THR VAL TRP GLY ILE LYS GLN LEU GLN SEQRES 4 F 126 ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN SEQRES 5 F 126 GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE SEQRES 6 F 126 CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER ASN SEQRES 7 F 126 ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP LEU SEQRES 8 F 126 GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE ILE SEQRES 9 F 126 TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU LYS SEQRES 10 F 126 ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 122 GLN VAL ARG LEU ALA GLN TYR GLY GLY GLY VAL LYS ARG SEQRES 2 G 122 LEU GLY ALA THR MET THR LEU SER CYS VAL ALA SER GLY SEQRES 3 G 122 TYR THR PHE ASN ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 G 122 ALA PRO GLY GLN GLY PHE GLU LEU LEU GLY TYR ILE ASP SEQRES 5 G 122 PRO ALA ASN GLY ARG PRO ASP TYR ALA GLY ALA LEU ARG SEQRES 6 G 122 GLU ARG LEU SER PHE TYR ARG ASP LYS SER MET GLU THR SEQRES 7 G 122 LEU TYR MET ASP LEU ARG SER LEU ARG TYR ASP ASP THR SEQRES 8 G 122 ALA MET TYR TYR CYS VAL ARG ASN VAL GLY THR ALA GLY SEQRES 9 G 122 SER LEU LEU HIS TYR ASP HIS TRP GLY SER GLY SER PRO SEQRES 10 G 122 VAL ILE VAL SER SER SEQRES 1 H 105 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER ALA SEQRES 2 H 105 SER PRO GLY GLU ARG VAL THR LEU THR CYS ARG ALA SER SEQRES 3 H 105 ARG SER VAL ARG ASN ASN VAL ALA TRP TYR GLN HIS LYS SEQRES 4 H 105 GLY GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 H 105 THR ARG ALA ALA GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 H 105 ALA SER GLY THR GLU PHE THR LEU ALA ILE SER ASN LEU SEQRES 7 H 105 GLU SER GLU ASP PHE THR VAL TYR PHE CYS LEU GLN TYR SEQRES 8 H 105 ASN ASN TRP TRP THR PHE GLY GLN GLY THR ARG VAL ASP SEQRES 9 H 105 ILE SEQRES 1 I 456 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 I 456 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 I 456 ALA LYS ALA TYR GLU LYS GLU VAL HIS ASN ILE TRP ALA SEQRES 4 I 456 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 I 456 MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 I 456 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL ILE SEQRES 7 I 456 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 I 456 THR PRO LEU CYS CYS THR LEU ASN CYS THR ASN ALA THR SEQRES 9 I 456 ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN CYS SEQRES 10 I 456 SER PHE ASN ILE THR THR GLU LEU ARG CYS LYS ARG GLU SEQRES 11 I 456 LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL GLN SEQRES 12 I 456 LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN CYS SEQRES 13 I 456 ASP THR SER VAL ILE THR GLN VAL CYS PRO LYS LEU SER SEQRES 14 I 456 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 15 I 456 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR GLY SEQRES 16 I 456 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 17 I 456 HIS GLY ILE LYS PRO VAL LEU SER THR GLN LEU LEU LEU SEQRES 18 I 456 ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SER SEQRES 19 I 456 GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL HIS SEQRES 20 I 456 LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO ASN SEQRES 21 I 456 ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY GLN SEQRES 22 I 456 ALA PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE ARG SEQRES 23 I 456 GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN GLU SEQRES 24 I 456 THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR PHE SEQRES 25 I 456 PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY GLY SEQRES 26 I 456 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 27 I 456 GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN ARG SEQRES 28 I 456 THR TYR MET ALA ASN SER THR GLU THR ASN SER THR ARG SEQRES 29 I 456 THR ILE THR ILE HIS CYS ARG ILE LYS GLN ILE ILE ASN SEQRES 30 I 456 MET TRP GLN GLU VAL GLY ARG ALA MET TYR ALA PRO PRO SEQRES 31 I 456 ILE ALA GLY ASN ILE THR CYS ILE SER ASN ILE THR GLY SEQRES 32 I 456 LEU LEU LEU THR ARG ASP TYR GLY LYS ASN ASN THR GLU SEQRES 33 I 456 THR PHE ARG PRO GLY GLY GLY ASN MET LYS ASP ASN TRP SEQRES 34 I 456 ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU SEQRES 35 I 456 PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL SEQRES 36 I 456 VAL SEQRES 1 J 126 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 2 J 126 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 3 J 126 LEU LEU SER GLY THR VAL TRP GLY ILE LYS GLN LEU GLN SEQRES 4 J 126 ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN SEQRES 5 J 126 GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE SEQRES 6 J 126 CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER ASN SEQRES 7 J 126 ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP LEU SEQRES 8 J 126 GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE ILE SEQRES 9 J 126 TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU LYS SEQRES 10 J 126 ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 K 122 GLN VAL ARG LEU ALA GLN TYR GLY GLY GLY VAL LYS ARG SEQRES 2 K 122 LEU GLY ALA THR MET THR LEU SER CYS VAL ALA SER GLY SEQRES 3 K 122 TYR THR PHE ASN ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 K 122 ALA PRO GLY GLN GLY PHE GLU LEU LEU GLY TYR ILE ASP SEQRES 5 K 122 PRO ALA ASN GLY ARG PRO ASP TYR ALA GLY ALA LEU ARG SEQRES 6 K 122 GLU ARG LEU SER PHE TYR ARG ASP LYS SER MET GLU THR SEQRES 7 K 122 LEU TYR MET ASP LEU ARG SER LEU ARG TYR ASP ASP THR SEQRES 8 K 122 ALA MET TYR TYR CYS VAL ARG ASN VAL GLY THR ALA GLY SEQRES 9 K 122 SER LEU LEU HIS TYR ASP HIS TRP GLY SER GLY SER PRO SEQRES 10 K 122 VAL ILE VAL SER SER SEQRES 1 L 105 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER ALA SEQRES 2 L 105 SER PRO GLY GLU ARG VAL THR LEU THR CYS ARG ALA SER SEQRES 3 L 105 ARG SER VAL ARG ASN ASN VAL ALA TRP TYR GLN HIS LYS SEQRES 4 L 105 GLY GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 105 THR ARG ALA ALA GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 L 105 ALA SER GLY THR GLU PHE THR LEU ALA ILE SER ASN LEU SEQRES 7 L 105 GLU SER GLU ASP PHE THR VAL TYR PHE CYS LEU GLN TYR SEQRES 8 L 105 ASN ASN TRP TRP THR PHE GLY GLN GLY THR ARG VAL ASP SEQRES 9 L 105 ILE HELIX 1 AA1 MET A 100 LYS A 117 1 18 HELIX 2 AA2 LEU A 122 CYS A 126 5 5 HELIX 3 AA3 ASN A 334 PHE A 353 1 20 HELIX 4 AA4 ASP A 368 THR A 373 1 6 HELIX 5 AA5 THR A 387 ASN A 392 1 6 HELIX 6 AA6 MET A 473 TYR A 482 1 10 HELIX 7 AA7 THR B 529 SER B 534 1 6 HELIX 8 AA8 THR B 536 ASN B 543 1 8 HELIX 9 AA9 LEU B 544 SER B 546 5 3 HELIX 10 AB1 GLY B 572 TRP B 596 1 25 HELIX 11 AB2 GLU B 621 ASN B 625 5 5 HELIX 12 AB3 THR B 627 SER B 636 1 10 HELIX 13 AB4 TYR B 638 ASP B 664 1 27 HELIX 14 AB5 LYS C 73 MET C 75 5 3 HELIX 15 AB6 ARG C 83 THR C 87 5 5 HELIX 16 AB7 MET E 100 LYS E 117 1 18 HELIX 17 AB8 LEU E 122 CYS E 126 5 5 HELIX 18 AB9 ASN E 334 PHE E 353 1 20 HELIX 19 AC1 ASP E 368 THR E 373 1 6 HELIX 20 AC2 THR E 387 ASN E 392 1 6 HELIX 21 AC3 MET E 473 TYR E 482 1 10 HELIX 22 AC4 THR F 529 SER F 534 1 6 HELIX 23 AC5 THR F 536 ASN F 543 1 8 HELIX 24 AC6 LEU F 544 SER F 546 5 3 HELIX 25 AC7 GLY F 572 TRP F 596 1 25 HELIX 26 AC8 GLU F 621 ASN F 625 5 5 HELIX 27 AC9 THR F 627 SER F 636 1 10 HELIX 28 AD1 TYR F 638 ASP F 664 1 27 HELIX 29 AD2 LYS G 73 MET G 75 5 3 HELIX 30 AD3 ARG G 83 THR G 87 5 5 HELIX 31 AD4 MET I 100 LYS I 117 1 18 HELIX 32 AD5 LEU I 122 CYS I 126 5 5 HELIX 33 AD6 ASN I 334 PHE I 353 1 20 HELIX 34 AD7 ASP I 368 THR I 373 1 6 HELIX 35 AD8 THR I 387 ASN I 392 1 6 HELIX 36 AD9 MET I 473 TYR I 482 1 10 HELIX 37 AE1 THR J 529 SER J 534 1 6 HELIX 38 AE2 THR J 536 ASN J 543 1 8 HELIX 39 AE3 LEU J 544 SER J 546 5 3 HELIX 40 AE4 GLY J 572 TRP J 596 1 25 HELIX 41 AE5 GLU J 621 ASN J 625 5 5 HELIX 42 AE6 THR J 627 SER J 636 1 10 HELIX 43 AE7 TYR J 638 ASP J 664 1 27 HELIX 44 AE8 LYS K 73 MET K 75 5 3 HELIX 45 AE9 ARG K 83 THR K 87 5 5 SHEET 1 AA1 3 GLY A 493 THR A 497 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N TYR A 39 O GLY A 493 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AA2 5 TRP A 45 GLU A 47 0 SHEET 2 AA2 5 LYS A 485 ILE A 489 -1 O LYS A 488 N LYS A 46 SHEET 3 AA2 5 TYR A 223 LEU A 226 -1 N LEU A 226 O LYS A 485 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O VAL A 245 N ILE A 225 SHEET 5 AA2 5 MET A 84 LEU A 86 -1 N LEU A 86 O VAL A 242 SHEET 1 AA3 2 PHE A 53 ALA A 55 0 SHEET 2 AA3 2 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 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 170 TYR A 177 0 SHEET 2 AA5 5 MET A 145 ILE A 161 -1 N CYS A 157 O ALA A 174 SHEET 3 AA5 5 LEU A 129 ASN A 133 -1 N ASN A 130 O SER A 158 SHEET 4 AA5 5 GLN A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA5 5 ILE A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA6 3 VAL A 200 GLN A 203 0 SHEET 2 AA6 3 ARG A 432 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 AA710 LEU A 259 LEU A 261 0 SHEET 2 AA710 ILE A 271 ARG A 273 0 SHEET 3 AA710 ILE A 284 ARG A 304 -1 O HIS A 287 N ILE A 271 SHEET 4 AA710 THR A 320 ILE A 323 -1 O ILE A 323 N ASN A 301 SHEET 5 AA710 ALA A 329 ILE A 333 -1 O ASN A 332 N GLU A 295 SHEET 6 AA710 HIS A 374 PHE A 376 0 SHEET 7 AA710 PHE A 382 CYS A 385 -1 O PHE A 383 N PHE A 376 SHEET 8 AA710 ILE A 414 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 9 AA710 GLY A 441 ARG A 456 -1 O ILE A 449 N VAL A 292 SHEET 10 AA710 PHE A 466 PRO A 468 -1 O ARG A 467 N THR A 455 SHEET 1 AA8 2 ILE A 307 ARG A 308 0 SHEET 2 AA8 2 ALA A 316 PHE A 317 -1 O PHE A 317 N ILE A 307 SHEET 1 AA9 2 ASN A 357 PHE A 361 0 SHEET 2 AA9 2 ARG A 393 MET A 396 -1 O TYR A 395 N ILE A 358 SHEET 1 AB1 4 ARG C 3 TYR C 7 0 SHEET 2 AB1 4 MET C 18 SER C 25 -1 O VAL C 23 N ALA C 5 SHEET 3 AB1 4 THR C 77 LEU C 82 -1 O LEU C 78 N CYS C 22 SHEET 4 AB1 4 LEU C 67 ASP C 72 -1 N TYR C 70 O TYR C 79 SHEET 1 AB2 7 GLY C 10 LYS C 12 0 SHEET 2 AB2 7 TYR C 33 GLN C 39 0 SHEET 3 AB2 7 GLU C 46 ILE C 51 -1 O LEU C 48 N TRP C 36 SHEET 4 AB2 7 PRO C 57 TYR C 59 -1 O ASP C 58 N TYR C 50 SHEET 5 AB2 7 ALA C 88 GLY C 97 -1 O TYR C 91 N VAL C 37 SHEET 6 AB2 7 LEU C 100B TRP C 103 -1 O LEU C 100C N VAL C 96 SHEET 7 AB2 7 SER C 107 VAL C 111 -1 O SER C 107 N TYR C 90 SHEET 1 AB3 4 LEU D 4 SER D 7 0 SHEET 2 AB3 4 VAL D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB3 4 GLU D 70 ILE D 75 -1 O PHE D 71 N CYS D 23 SHEET 4 AB3 4 PHE D 62 SER D 67 -1 N SER D 63 O ALA D 74 SHEET 1 AB4 7 THR D 10 SER D 12 0 SHEET 2 AB4 7 VAL D 33 HIS D 38 0 SHEET 3 AB4 7 ARG D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 4 AB4 7 THR D 53 ARG D 54 -1 O THR D 53 N TYR D 49 SHEET 5 AB4 7 VAL D 85 GLN D 90 -1 O VAL D 85 N HIS D 38 SHEET 6 AB4 7 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 7 AB4 7 THR D 102 ASP D 105 -1 O THR D 102 N TYR D 86 SHEET 1 AB5 3 GLY E 493 THR E 497 0 SHEET 2 AB5 3 TRP E 35 TYR E 39 -1 N TYR E 39 O GLY E 493 SHEET 3 AB5 3 ILE F 603 PRO F 609 -1 O VAL F 608 N VAL E 36 SHEET 1 AB6 5 TRP E 45 GLU E 47 0 SHEET 2 AB6 5 LYS E 485 ILE E 489 -1 O LYS E 488 N LYS E 46 SHEET 3 AB6 5 TYR E 223 LEU E 226 -1 N LEU E 226 O LYS E 485 SHEET 4 AB6 5 VAL E 242 VAL E 245 -1 O VAL E 245 N ILE E 225 SHEET 5 AB6 5 MET E 84 LEU E 86 -1 N LEU E 86 O VAL E 242 SHEET 1 AB7 2 PHE E 53 ALA E 55 0 SHEET 2 AB7 2 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AB8 2 GLU E 91 ASN E 94 0 SHEET 2 AB8 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AB9 5 ARG E 169 TYR E 177 0 SHEET 2 AB9 5 MET E 145 THR E 162 -1 N CYS E 157 O ALA E 174 SHEET 3 AB9 5 LEU E 129 THR E 132 -1 N THR E 132 O ASN E 147 SHEET 4 AB9 5 GLN E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AB9 5 ILE E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC1 3 VAL E 200 GLN E 203 0 SHEET 2 AC1 3 ARG E 432 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC1 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC210 LEU E 259 LEU E 261 0 SHEET 2 AC210 ILE E 271 ARG E 273 0 SHEET 3 AC210 ILE E 284 GLY E 312 -1 O HIS E 287 N ILE E 271 SHEET 4 AC210 GLN E 315 ILE E 323 -1 O PHE E 317 N ILE E 307 SHEET 5 AC210 ALA E 329 ILE E 333 -1 O ASN E 332 N GLU E 295 SHEET 6 AC210 HIS E 374 PHE E 376 0 SHEET 7 AC210 PHE E 382 CYS E 385 -1 O PHE E 383 N PHE E 376 SHEET 8 AC210 ILE E 414 LYS E 421 -1 O ARG E 419 N TYR E 384 SHEET 9 AC210 GLY E 441 ARG E 456 -1 O ILE E 449 N VAL E 292 SHEET 10 AC210 PHE E 466 PRO E 468 -1 O ARG E 467 N THR E 455 SHEET 1 AC3 2 ILE E 358 PHE E 361 0 SHEET 2 AC3 2 ARG E 393 TYR E 395 -1 O TYR E 395 N ILE E 358 SHEET 1 AC4 4 ARG G 3 TYR G 7 0 SHEET 2 AC4 4 MET G 18 SER G 25 -1 O VAL G 23 N ALA G 5 SHEET 3 AC4 4 THR G 77 LEU G 82 -1 O LEU G 78 N CYS G 22 SHEET 4 AC4 4 LEU G 67 ASP G 72 -1 N TYR G 70 O TYR G 79 SHEET 1 AC5 7 GLY G 10 LYS G 12 0 SHEET 2 AC5 7 TYR G 33 GLN G 39 0 SHEET 3 AC5 7 GLU G 46 ILE G 51 -1 O LEU G 48 N TRP G 36 SHEET 4 AC5 7 PRO G 57 TYR G 59 -1 O ASP G 58 N TYR G 50 SHEET 5 AC5 7 ALA G 88 GLY G 97 -1 O TYR G 91 N VAL G 37 SHEET 6 AC5 7 LEU G 100B TRP G 103 -1 O LEU G 100C N VAL G 96 SHEET 7 AC5 7 SER G 107 VAL G 111 -1 O SER G 107 N TYR G 90 SHEET 1 AC6 4 LEU H 4 SER H 7 0 SHEET 2 AC6 4 VAL H 19 ALA H 25 -1 O ARG H 24 N THR H 5 SHEET 3 AC6 4 GLU H 70 ILE H 75 -1 O PHE H 71 N CYS H 23 SHEET 4 AC6 4 PHE H 62 SER H 67 -1 N SER H 63 O ALA H 74 SHEET 1 AC7 7 THR H 10 SER H 12 0 SHEET 2 AC7 7 VAL H 33 HIS H 38 0 SHEET 3 AC7 7 ARG H 45 TYR H 49 -1 O LEU H 47 N TRP H 35 SHEET 4 AC7 7 THR H 53 ARG H 54 -1 O THR H 53 N TYR H 49 SHEET 5 AC7 7 VAL H 85 GLN H 90 -1 O VAL H 85 N HIS H 38 SHEET 6 AC7 7 THR H 97 PHE H 98 -1 O THR H 97 N GLN H 90 SHEET 7 AC7 7 THR H 102 ASP H 105 -1 O THR H 102 N TYR H 86 SHEET 1 AC8 3 GLY I 493 THR I 497 0 SHEET 2 AC8 3 TRP I 35 TYR I 39 -1 N TYR I 39 O GLY I 493 SHEET 3 AC8 3 ILE J 603 PRO J 609 -1 O VAL J 608 N VAL I 36 SHEET 1 AC9 5 TRP I 45 GLU I 47 0 SHEET 2 AC9 5 LYS I 485 ILE I 489 -1 O LYS I 488 N LYS I 46 SHEET 3 AC9 5 TYR I 223 LEU I 226 -1 N LEU I 226 O LYS I 485 SHEET 4 AC9 5 VAL I 242 VAL I 245 -1 O VAL I 245 N ILE I 225 SHEET 5 AC9 5 MET I 84 LEU I 86 -1 N LEU I 86 O VAL I 242 SHEET 1 AD1 2 PHE I 53 ALA I 55 0 SHEET 2 AD1 2 HIS I 216 CYS I 218 -1 O HIS I 216 N ALA I 55 SHEET 1 AD2 2 GLU I 91 ASN I 94 0 SHEET 2 AD2 2 THR I 236 CYS I 239 -1 O CYS I 239 N GLU I 91 SHEET 1 AD3 5 GLU I 170 TYR I 177 0 SHEET 2 AD3 5 MET I 145 ILE I 161 -1 N CYS I 157 O ALA I 174 SHEET 3 AD3 5 LEU I 129 THR I 132 -1 N THR I 132 O ASN I 147 SHEET 4 AD3 5 GLN I 190 LEU I 193 -1 O TYR I 191 N LEU I 129 SHEET 5 AD3 5 ILE I 181 GLN I 183 -1 N VAL I 182 O ARG I 192 SHEET 1 AD4 3 VAL I 200 GLN I 203 0 SHEET 2 AD4 3 ARG I 432 TYR I 435 1 O TYR I 435 N THR I 202 SHEET 3 AD4 3 ILE I 423 ILE I 424 -1 N ILE I 424 O MET I 434 SHEET 1 AD510 LEU I 259 LEU I 261 0 SHEET 2 AD510 ILE I 271 ARG I 273 0 SHEET 3 AD510 ILE I 284 ARG I 308 -1 O HIS I 287 N ILE I 271 SHEET 4 AD510 ALA I 316 ILE I 323 -1 O ILE I 323 N ASN I 301 SHEET 5 AD510 ALA I 329 ILE I 333 -1 O ASN I 332 N GLU I 295 SHEET 6 AD510 HIS I 374 PHE I 376 0 SHEET 7 AD510 PHE I 382 CYS I 385 -1 O PHE I 383 N PHE I 376 SHEET 8 AD510 ILE I 414 LYS I 421 -1 O ARG I 419 N TYR I 384 SHEET 9 AD510 GLY I 441 ARG I 456 -1 O ILE I 449 N VAL I 292 SHEET 10 AD510 PHE I 466 PRO I 468 -1 O ARG I 467 N THR I 455 SHEET 1 AD6 2 ILE I 358 PHE I 361 0 SHEET 2 AD6 2 ARG I 393 TYR I 395 -1 O TYR I 395 N ILE I 358 SHEET 1 AD7 4 ARG K 3 TYR K 7 0 SHEET 2 AD7 4 MET K 18 SER K 25 -1 O VAL K 23 N ALA K 5 SHEET 3 AD7 4 THR K 77 LEU K 82 -1 O LEU K 78 N CYS K 22 SHEET 4 AD7 4 LEU K 67 ASP K 72 -1 N SER K 68 O ASP K 81 SHEET 1 AD8 7 GLY K 10 LYS K 12 0 SHEET 2 AD8 7 TYR K 33 GLN K 39 0 SHEET 3 AD8 7 GLU K 46 ILE K 51 -1 O LEU K 48 N TRP K 36 SHEET 4 AD8 7 PRO K 57 TYR K 59 -1 O ASP K 58 N TYR K 50 SHEET 5 AD8 7 ALA K 88 GLY K 97 -1 O TYR K 91 N VAL K 37 SHEET 6 AD8 7 LEU K 100B TRP K 103 -1 O LEU K 100C N VAL K 96 SHEET 7 AD8 7 SER K 107 VAL K 111 -1 O SER K 107 N TYR K 90 SHEET 1 AD9 4 LEU L 4 SER L 7 0 SHEET 2 AD9 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AD9 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AD9 4 PHE L 62 SER L 67 -1 N SER L 63 O ALA L 74 SHEET 1 AE1 7 THR L 10 SER L 12 0 SHEET 2 AE1 7 VAL L 33 HIS L 38 0 SHEET 3 AE1 7 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 4 AE1 7 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 5 AE1 7 VAL L 85 GLN L 90 -1 O VAL L 85 N HIS L 38 SHEET 6 AE1 7 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 7 AE1 7 THR L 102 ASP L 105 -1 O THR L 102 N TYR L 86 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.04 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.04 SSBOND 4 CYS A 127 CYS I 167 1555 1555 2.02 SSBOND 5 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 6 CYS A 167 CYS E 127 1555 1555 2.04 SSBOND 7 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 8 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 9 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 10 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 11 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 12 CYS A 499 CYS B 605 1555 1555 2.04 SSBOND 13 CYS B 598 CYS B 604 1555 1555 2.04 SSBOND 14 CYS C 22 CYS C 92 1555 1555 2.03 SSBOND 15 CYS D 23 CYS D 88 1555 1555 2.05 SSBOND 16 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 17 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 18 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 19 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 20 CYS E 167 CYS I 127 1555 1555 2.04 SSBOND 21 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 22 CYS E 228 CYS E 239 1555 1555 2.04 SSBOND 23 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 24 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 25 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 26 CYS E 499 CYS F 605 1555 1555 2.04 SSBOND 27 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 28 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 29 CYS H 23 CYS H 88 1555 1555 2.05 SSBOND 30 CYS I 54 CYS I 74 1555 1555 2.04 SSBOND 31 CYS I 119 CYS I 205 1555 1555 2.03 SSBOND 32 CYS I 126 CYS I 196 1555 1555 2.04 SSBOND 33 CYS I 131 CYS I 157 1555 1555 2.03 SSBOND 34 CYS I 218 CYS I 247 1555 1555 2.03 SSBOND 35 CYS I 228 CYS I 239 1555 1555 2.03 SSBOND 36 CYS I 296 CYS I 331 1555 1555 2.03 SSBOND 37 CYS I 378 CYS I 445 1555 1555 2.03 SSBOND 38 CYS I 385 CYS I 418 1555 1555 2.03 SSBOND 39 CYS I 499 CYS J 605 1555 1555 2.04 SSBOND 40 CYS J 598 CYS J 604 1555 1555 2.04 SSBOND 41 CYS K 22 CYS K 92 1555 1555 2.03 SSBOND 42 CYS L 23 CYS L 88 1555 1555 2.05 CISPEP 1 ALA B 525 ALA B 526 0 11.21 CISPEP 2 GLY B 531 ALA B 532 0 -18.50 CISPEP 3 MET B 626 THR B 627 0 -19.83 CISPEP 4 SER D 7 PRO D 8 0 -10.47 CISPEP 5 ALA F 525 ALA F 526 0 11.12 CISPEP 6 GLY F 531 ALA F 532 0 -18.61 CISPEP 7 MET F 626 THR F 627 0 -20.03 CISPEP 8 SER H 7 PRO H 8 0 -10.08 CISPEP 9 ALA J 525 ALA J 526 0 11.13 CISPEP 10 GLY J 531 ALA J 532 0 -18.51 CISPEP 11 MET J 626 THR J 627 0 -19.75 CISPEP 12 SER L 7 PRO L 8 0 -10.41 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