HEADER IMMUNE SYSTEM 07-NOV-25 9Z3Q TITLE CRYO-EM STRUCTURE OF KSHV GLYCOPROTEIN GHGL IN COMPLEX WITH MLKH3 AND TITLE 2 MLKH10 FABS COMPND MOL_ID: 1; COMPND 2 MOLECULE: MLKH10 LIGHT CHAIN FV; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MLKH10 HEAVY CHAIN FV; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MLKH3 LIGHT CHAIN FV; COMPND 11 CHAIN: C; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: MLKH3 HEAVY CHAIN FV; COMPND 15 CHAIN: D; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: ENVELOPE GLYCOPROTEIN H; COMPND 19 CHAIN: E; COMPND 20 SYNONYM: GH; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 6; COMPND 23 MOLECULE: ENVELOPE GLYCOPROTEIN L; COMPND 24 CHAIN: F; COMPND 25 SYNONYM: GL; COMPND 26 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 10 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 11 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 12 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PTT3; SOURCE 15 MOL_ID: 2; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_COMMON: MOUSE; SOURCE 18 ORGANISM_TAXID: 10090; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 23 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 24 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 25 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 26 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PTT3; SOURCE 29 MOL_ID: 3; SOURCE 30 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 31 ORGANISM_COMMON: MOUSE; SOURCE 32 ORGANISM_TAXID: 10090; SOURCE 33 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 34 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 36 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 37 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 38 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 39 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 40 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 41 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 42 EXPRESSION_SYSTEM_PLASMID: PTT3; SOURCE 43 MOL_ID: 4; SOURCE 44 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 45 ORGANISM_COMMON: MOUSE; SOURCE 46 ORGANISM_TAXID: 10090; SOURCE 47 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 48 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 49 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 50 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 51 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 52 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 53 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 54 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 55 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 56 EXPRESSION_SYSTEM_PLASMID: PTT3; SOURCE 57 MOL_ID: 5; SOURCE 58 ORGANISM_SCIENTIFIC: HUMAN GAMMAHERPESVIRUS 8; SOURCE 59 ORGANISM_TAXID: 37296; SOURCE 60 STRAIN: GK18; SOURCE 61 GENE: GH, ORF22; SOURCE 62 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 63 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 64 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 65 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 66 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 67 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 68 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 69 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 70 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 71 EXPRESSION_SYSTEM_PLASMID: PTT3; SOURCE 72 MOL_ID: 6; SOURCE 73 ORGANISM_SCIENTIFIC: HUMAN GAMMAHERPESVIRUS 8; SOURCE 74 ORGANISM_TAXID: 37296; SOURCE 75 STRAIN: GK18; SOURCE 76 GENE: GL, 47; SOURCE 77 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 78 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 79 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 80 EXPRESSION_SYSTEM_CELL_LINE: HEK293S; SOURCE 81 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-3022; SOURCE 82 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 83 EXPRESSION_SYSTEM_TISSUE: KIDNEY; SOURCE 84 EXPRESSION_SYSTEM_CELL: EPITHELIAL-LIKE; SOURCE 85 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 86 EXPRESSION_SYSTEM_PLASMID: PTT3 KEYWDS KSHV, GLYCOPROTEIN, ANTIBODY, IMMUNE SYSTEM EXPDTA ELECTRON MICROSCOPY AUTHOR K.LANG,N.ALDRIDGE,M.PANCERA REVDAT 1 10-DEC-25 9Z3Q 0 JRNL AUTH Y.H.WAN,S.PERNIKOFF,N.ALDRIDGE,K.LANG,H.DUDLEY, JRNL AUTH 2 S.SCHARFFENBERGER,G.KHER,W.T.PHIPPS,M.PANCERA, JRNL AUTH 3 J.BOONYARATANAKORNKIT,A.T.MCGUIRE JRNL TITL MONOCLONAL NEUTRALIZING ANTIBODIES ELICITED BY INFECTION JRNL TITL 2 WITH KAPOSI SARCOMA-ASSOCIATED HERPESVIRUS REVEAL CRITICAL JRNL TITL 3 SITES OF VULNERABILITY ON GH/GL. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.51 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, UCSF CHIMERAX, CRYOSPARC, REMARK 3 PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 7CZF REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT 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) : 3.510 REMARK 3 NUMBER OF PARTICLES : 75257 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 9Z3Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-25. REMARK 100 THE DEPOSITION ID IS D_1000301919. 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 : KSHV GLYCOPROTEIN HETERODIMER REMARK 245 GHGL 1:1 MLKH3 AND MLKH10 FABS REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 9372 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 36000 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F 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 GLU D 1 REMARK 465 MET E -3 REMARK 465 ASP E -2 REMARK 465 ALA E -1 REMARK 465 MET E 0 REMARK 465 LYS E 1 REMARK 465 ARG E 2 REMARK 465 GLY E 3 REMARK 465 LEU E 4 REMARK 465 CYS E 5 REMARK 465 CYS E 6 REMARK 465 VAL E 7 REMARK 465 LEU E 8 REMARK 465 LEU E 9 REMARK 465 LEU E 10 REMARK 465 CYS E 11 REMARK 465 GLY E 12 REMARK 465 ALA E 13 REMARK 465 VAL E 14 REMARK 465 PHE E 15 REMARK 465 VAL E 16 REMARK 465 SER E 17 REMARK 465 PRO E 18 REMARK 465 SER E 19 REMARK 465 ALA E 20 REMARK 465 SER E 21 REMARK 465 ALA E 22 REMARK 465 THR E 23 REMARK 465 GLY E 24 REMARK 465 ALA E 25 REMARK 465 LEU E 26 REMARK 465 PRO E 27 REMARK 465 THR E 28 REMARK 465 THR E 29 REMARK 465 ALA E 30 REMARK 465 THR E 31 REMARK 465 THR E 32 REMARK 465 ILE E 33 REMARK 465 THR E 34 REMARK 465 ARG E 35 REMARK 465 PRO E 512 REMARK 465 ALA E 513 REMARK 465 LYS E 514 REMARK 465 LEU E 515 REMARK 465 ARG E 516 REMARK 465 ALA E 517 REMARK 465 GLU E 518 REMARK 465 ALA E 519 REMARK 465 PRO E 520 REMARK 465 GLN E 521 REMARK 465 SER E 522 REMARK 465 SER E 523 REMARK 465 ALA E 524 REMARK 465 LEU E 525 REMARK 465 THR E 526 REMARK 465 ARG E 527 REMARK 465 THR E 528 REMARK 465 ALA E 529 REMARK 465 VAL E 530 REMARK 465 ALA E 531 REMARK 465 ARG E 532 REMARK 465 GLY E 699 REMARK 465 SER E 700 REMARK 465 GLY E 701 REMARK 465 SER E 702 REMARK 465 GLY E 703 REMARK 465 HIS E 704 REMARK 465 HIS E 705 REMARK 465 HIS E 706 REMARK 465 HIS E 707 REMARK 465 HIS E 708 REMARK 465 HIS E 709 REMARK 465 GLY E 710 REMARK 465 LEU E 711 REMARK 465 ASN E 712 REMARK 465 ASP E 713 REMARK 465 ILE E 714 REMARK 465 PHE E 715 REMARK 465 GLU E 716 REMARK 465 ALA E 717 REMARK 465 GLN E 718 REMARK 465 LYS E 719 REMARK 465 ILE E 720 REMARK 465 GLU E 721 REMARK 465 TRP E 722 REMARK 465 HIS E 723 REMARK 465 GLU E 724 REMARK 465 MET F -8 REMARK 465 ASP F -7 REMARK 465 ALA F -6 REMARK 465 MET F -5 REMARK 465 LYS F -4 REMARK 465 ARG F -3 REMARK 465 GLY F -2 REMARK 465 LEU F -1 REMARK 465 CYS F 0 REMARK 465 CYS F 1 REMARK 465 VAL F 2 REMARK 465 LEU F 3 REMARK 465 LEU F 4 REMARK 465 LEU F 5 REMARK 465 CYS F 6 REMARK 465 GLY F 7 REMARK 465 ALA F 8 REMARK 465 VAL F 9 REMARK 465 PHE F 10 REMARK 465 VAL F 11 REMARK 465 SER F 12 REMARK 465 PRO F 13 REMARK 465 SER F 14 REMARK 465 ALA F 15 REMARK 465 SER F 16 REMARK 465 ASP F 17 REMARK 465 GLY F 18 REMARK 465 ILE F 131 REMARK 465 ILE F 132 REMARK 465 ILE F 133 REMARK 465 ILE F 134 REMARK 465 SER F 135 REMARK 465 VAL F 136 REMARK 465 GLY F 137 REMARK 465 LYS F 138 REMARK 465 ALA F 139 REMARK 465 MET F 140 REMARK 465 ASN F 141 REMARK 465 ARG F 142 REMARK 465 THR F 143 REMARK 465 GLY F 144 REMARK 465 SER F 145 REMARK 465 VAL F 146 REMARK 465 SER F 147 REMARK 465 GLY F 148 REMARK 465 SER F 149 REMARK 465 GLN F 150 REMARK 465 THR F 151 REMARK 465 ARG F 152 REMARK 465 ALA F 153 REMARK 465 LYS F 154 REMARK 465 SER F 155 REMARK 465 SER F 156 REMARK 465 SER F 157 REMARK 465 ARG F 158 REMARK 465 ARG F 159 REMARK 465 ALA F 160 REMARK 465 HIS F 161 REMARK 465 ALA F 162 REMARK 465 GLY F 163 REMARK 465 GLN F 164 REMARK 465 LYS F 165 REMARK 465 GLY F 166 REMARK 465 LYS F 167 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 CYS E 355 CA - CB - SG ANGL. DEV. = 9.5 DEGREES REMARK 500 LEU E 665 CA - CB - CG ANGL. DEV. = 15.2 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 51 -8.78 70.91 REMARK 500 ALA A 84 -174.54 -173.17 REMARK 500 LEU B 45 148.78 -173.12 REMARK 500 VAL B 48 -61.80 -122.18 REMARK 500 ASP B 61 -60.54 -92.80 REMARK 500 ASN B 100B -177.36 -174.03 REMARK 500 SER C 12 51.26 -96.85 REMARK 500 SER C 30 -124.03 57.54 REMARK 500 ALA C 51 -7.37 71.02 REMARK 500 ALA C 84 -175.21 -170.47 REMARK 500 PRO C 95 70.45 24.70 REMARK 500 GLN D 3 157.24 68.39 REMARK 500 SER D 84 -101.18 49.66 REMARK 500 ASP D 86 13.02 -141.90 REMARK 500 ASP E 109 -5.20 71.88 REMARK 500 LYS E 128 -55.80 -122.20 REMARK 500 PRO E 166 3.09 -69.83 REMARK 500 GLU E 189 -8.48 68.44 REMARK 500 SER E 211 -123.70 52.33 REMARK 500 ALA E 305 33.94 -98.92 REMARK 500 ARG E 390 49.52 -80.94 REMARK 500 ASP E 451 52.20 -92.82 REMARK 500 ASN E 550 -108.28 61.56 REMARK 500 HIS E 573 36.55 37.55 REMARK 500 ASN E 585 -40.05 -134.53 REMARK 500 ILE E 627 71.59 52.81 REMARK 500 SER E 628 -165.35 -78.15 REMARK 500 CYS E 634 67.00 -157.46 REMARK 500 ASN E 675 38.56 -98.11 REMARK 500 ASN E 688 15.01 -144.97 REMARK 500 TYR F 21 -120.78 31.86 REMARK 500 LEU F 39 156.83 67.50 REMARK 500 ALA F 60 -32.03 -130.69 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-73789 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF KSHV GLYCOPROTEIN GHGL IN COMPLEX WITH MLKH3 REMARK 900 AND MLKH10 FABS DBREF 9Z3Q A 1 107 PDB 9Z3Q 9Z3Q 1 107 DBREF 9Z3Q B 1 113 PDB 9Z3Q 9Z3Q 1 113 DBREF 9Z3Q C 1 107 PDB 9Z3Q 9Z3Q 1 107 DBREF 9Z3Q D 1 113 PDB 9Z3Q 9Z3Q 1 113 DBREF 9Z3Q E 23 698 UNP F5HAK9 GH_HHV8P 23 698 DBREF 9Z3Q F 21 167 UNP F5HDB7 GL_HHV8P 21 167 SEQADV 9Z3Q MET E -3 UNP F5HAK9 INITIATING METHIONINE SEQADV 9Z3Q ASP E -2 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ALA E -1 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q MET E 0 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q LYS E 1 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ARG E 2 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLY E 3 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q LEU E 4 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q CYS E 5 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q CYS E 6 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q VAL E 7 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q LEU E 8 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q LEU E 9 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q LEU E 10 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q CYS E 11 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLY E 12 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ALA E 13 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q VAL E 14 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q PHE E 15 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q VAL E 16 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q SER E 17 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q PRO E 18 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q SER E 19 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ALA E 20 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q SER E 21 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ALA E 22 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLY E 699 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q SER E 700 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLY E 701 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q SER E 702 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLY E 703 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q HIS E 704 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q HIS E 705 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q HIS E 706 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q HIS E 707 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q HIS E 708 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q HIS E 709 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLY E 710 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q LEU E 711 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ASN E 712 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ASP E 713 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ILE E 714 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q PHE E 715 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLU E 716 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ALA E 717 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLN E 718 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q LYS E 719 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q ILE E 720 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLU E 721 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q TRP E 722 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q HIS E 723 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q GLU E 724 UNP F5HAK9 EXPRESSION TAG SEQADV 9Z3Q MET F -8 UNP F5HDB7 INITIATING METHIONINE SEQADV 9Z3Q ASP F -7 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q ALA F -6 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q MET F -5 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q LYS F -4 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q ARG F -3 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q GLY F -2 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q LEU F -1 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q CYS F 0 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q CYS F 1 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q VAL F 2 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q LEU F 3 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q LEU F 4 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q LEU F 5 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q CYS F 6 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q GLY F 7 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q ALA F 8 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q VAL F 9 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q PHE F 10 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q VAL F 11 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q SER F 12 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q PRO F 13 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q SER F 14 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q ALA F 15 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q SER F 16 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q ASP F 17 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q GLY F 18 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q ILE F 19 UNP F5HDB7 EXPRESSION TAG SEQADV 9Z3Q GLN F 20 UNP F5HDB7 EXPRESSION TAG SEQRES 1 A 112 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU SER VAL SEQRES 2 A 112 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 A 112 GLN SER VAL LEU TYR SER SER ASN ASN LYS ASN TYR LEU SEQRES 4 A 112 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 A 112 LEU ILE TYR TRP ALA SER THR ARG GLY SER GLY VAL PRO SEQRES 6 A 112 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 A 112 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 A 112 TYR TYR CYS GLN GLN TYR TYR ASN SER PRO ARG PHE GLY SEQRES 9 A 112 GLY TRP THR LYS VAL GLU ILE LYS SEQRES 1 B 121 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY VAL VAL ARG SEQRES 2 B 121 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 121 PHE THR PHE ASP ASP TYR GLY MET SER TRP VAL ARG GLN SEQRES 4 B 121 SER PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE ASN SEQRES 5 B 121 TRP ASN GLY GLY SER LEU SER TYR ALA ASP SER ILE GLN SEQRES 6 B 121 GLY ARG PHE THR ILE SER ARG ASP ASN ALA GLU ASN SER SEQRES 7 B 121 LEU TYR LEU GLN MET HIS SER LEU ARG ALA GLU ASP THR SEQRES 8 B 121 ALA LEU TYR TYR CYS ALA ARG VAL GLN GLY SER GLY SER SEQRES 9 B 121 TYR ASN ASN PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 B 121 THR VAL SER SER SEQRES 1 C 107 ASP ILE GLN LEU THR GLN SER PRO SER SER VAL SER ALA SEQRES 2 C 107 SER VAL GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 C 107 GLN GLY ILE SER SER TRP LEU VAL TRP TYR GLN GLN LYS SEQRES 4 C 107 PRO GLY LYS ALA PRO LYS PRO LEU ILE TYR ALA ALA SER SEQRES 5 C 107 SER LEU GLN ASN GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 C 107 GLY SER GLY THR ASP PHE THR LEU THR ILE ASN SER LEU SEQRES 7 C 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ALA SEQRES 8 C 107 ASN SER PHE PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 C 107 GLU ILE LYS SEQRES 1 D 122 GLU VAL GLN LEU VAL GLN SER GLY PRO GLU VAL LYS LYS SEQRES 2 D 122 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 D 122 ASP SER PHE SER SER ASN THR ILE SER TRP VAL ARG GLN SEQRES 4 D 122 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ARG LEU ILE SEQRES 5 D 122 THR ILE LEU GLY THR ALA ASN TYR ALA GLN LYS PHE GLN SEQRES 6 D 122 GLY ARG VAL THR ILE THR ALA ASP GLU THR ALA THR THR SEQRES 7 D 122 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 D 122 ALA ILE TYR TYR CYS ALA ILE SER GLU GLY GLY TYR THR SEQRES 9 D 122 TYR ASP SER GLY SER TYR ILE TRP GLY GLN GLY THR LEU SEQRES 10 D 122 VAL THR VAL SER SER SEQRES 1 E 728 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 E 728 LEU CYS GLY ALA VAL PHE VAL SER PRO SER ALA SER ALA SEQRES 3 E 728 THR GLY ALA LEU PRO THR THR ALA THR THR ILE THR ARG SEQRES 4 E 728 SER ALA THR GLN LEU ILE ASN GLY ARG THR ASN LEU SER SEQRES 5 E 728 ILE GLU LEU GLU PHE ASN GLY THR SER PHE PHE LEU ASN SEQRES 6 E 728 TRP GLN ASN LEU LEU ASN VAL ILE THR GLU PRO ALA LEU SEQRES 7 E 728 THR GLU LEU TRP THR SER ALA GLU VAL ALA GLU ASP LEU SEQRES 8 E 728 ARG VAL THR LEU LYS LYS ARG GLN SER LEU PHE PHE PRO SEQRES 9 E 728 ASN LYS THR VAL VAL ILE SER GLY ASP GLY HIS ARG TYR SEQRES 10 E 728 THR CYS GLU VAL PRO THR SER SER GLN THR TYR ASN ILE SEQRES 11 E 728 THR LYS GLY PHE ASN TYR SER ALA LEU PRO GLY HIS LEU SEQRES 12 E 728 GLY GLY PHE GLY ILE ASN ALA ARG LEU VAL LEU GLY ASP SEQRES 13 E 728 ILE PHE ALA SER LYS TRP SER LEU PHE ALA ARG ASP THR SEQRES 14 E 728 PRO GLU TYR ARG VAL PHE TYR PRO MET ASN VAL MET ALA SEQRES 15 E 728 VAL LYS PHE SER ILE SER ILE GLY ASN ASN GLU SER GLY SEQRES 16 E 728 VAL ALA LEU TYR GLY VAL VAL SER GLU ASP PHE VAL VAL SEQRES 17 E 728 VAL THR LEU HIS ASN ARG SER LYS GLU ALA ASN GLU THR SEQRES 18 E 728 ALA SER HIS LEU LEU PHE GLY LEU PRO ASP SER LEU PRO SEQRES 19 E 728 SER LEU LYS GLY HIS ALA THR TYR ASP GLU LEU THR PHE SEQRES 20 E 728 ALA ARG ASN ALA LYS TYR ALA LEU VAL ALA ILE LEU PRO SEQRES 21 E 728 LYS ASP SER TYR GLN THR LEU LEU THR GLU ASN TYR THR SEQRES 22 E 728 ARG ILE PHE LEU ASN MET THR GLU SER THR PRO LEU GLU SEQRES 23 E 728 PHE THR ARG THR ILE GLN THR ARG ILE VAL SER ILE GLU SEQRES 24 E 728 ALA ARG ARG ALA CYS ALA ALA GLN GLU ALA ALA PRO ASP SEQRES 25 E 728 ILE PHE LEU VAL LEU PHE GLN MET LEU VAL ALA HIS PHE SEQRES 26 E 728 LEU VAL ALA ARG GLY ILE ALA GLU HIS ARG PHE VAL GLU SEQRES 27 E 728 VAL ASP CYS VAL CYS ARG GLN TYR ALA GLU LEU TYR PHE SEQRES 28 E 728 LEU ARG ARG ILE SER ARG LEU CYS MET PRO THR PHE THR SEQRES 29 E 728 THR VAL GLY TYR ASN HIS THR THR LEU GLY ALA VAL ALA SEQRES 30 E 728 ALA THR GLN ILE ALA ARG VAL SER ALA THR LYS LEU ALA SEQRES 31 E 728 SER LEU PRO ARG SER SER GLN GLU THR VAL LEU ALA MET SEQRES 32 E 728 VAL GLN LEU GLY ALA ARG ASP GLY ALA VAL PRO SER SER SEQRES 33 E 728 ILE LEU GLU GLY ILE ALA MET VAL VAL GLU HIS MET TYR SEQRES 34 E 728 THR ALA TYR THR TYR VAL TYR THR LEU GLY ASP THR GLU SEQRES 35 E 728 ARG LYS LEU MET LEU ASP ILE HIS THR VAL LEU THR ASP SEQRES 36 E 728 SER CYS PRO PRO LYS ASP SER GLY VAL SER GLU LYS LEU SEQRES 37 E 728 LEU ARG THR TYR LEU MET PHE THR SER MET CYS THR ASN SEQRES 38 E 728 ILE GLU LEU GLY GLU MET ILE ALA ARG PHE SER LYS PRO SEQRES 39 E 728 ASP SER LEU ASN ILE TYR ARG ALA PHE SER PRO CYS PHE SEQRES 40 E 728 LEU GLY LEU ARG TYR ASP LEU HIS PRO ALA LYS LEU ARG SEQRES 41 E 728 ALA GLU ALA PRO GLN SER SER ALA LEU THR ARG THR ALA SEQRES 42 E 728 VAL ALA ARG GLY THR SER GLY PHE ALA GLU LEU LEU HIS SEQRES 43 E 728 ALA LEU HIS LEU ASP SER LEU ASN LEU ILE PRO ALA ILE SEQRES 44 E 728 ASN CYS SER LYS ILE THR ALA ASP LYS ILE ILE ALA THR SEQRES 45 E 728 VAL PRO LEU PRO HIS VAL THR TYR ILE ILE SER SER GLU SEQRES 46 E 728 ALA LEU SER ASN ALA VAL VAL TYR GLU VAL SER GLU ILE SEQRES 47 E 728 PHE LEU LYS SER ALA MET PHE ILE SER ALA ILE LYS PRO SEQRES 48 E 728 ASP CYS SER GLY PHE ASN PHE SER GLN ILE ASP ARG HIS SEQRES 49 E 728 ILE PRO ILE VAL TYR ASN ILE SER THR PRO ARG ARG GLY SEQRES 50 E 728 CYS PRO LEU CYS ASP SER VAL ILE MET SER TYR ASP GLU SEQRES 51 E 728 SER ASP GLY LEU GLN SER LEU MET TYR VAL THR ASN GLU SEQRES 52 E 728 ARG VAL GLN THR ASN LEU PHE LEU ASP LYS SER PRO PHE SEQRES 53 E 728 PHE ASP ASN ASN ASN LEU HIS ILE HIS TYR LEU TRP LEU SEQRES 54 E 728 ARG ASP ASN GLY THR VAL VAL GLU ILE ARG GLY MET TYR SEQRES 55 E 728 GLY SER GLY SER GLY HIS HIS HIS HIS HIS HIS GLY LEU SEQRES 56 E 728 ASN ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU SEQRES 1 F 176 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 F 176 LEU CYS GLY ALA VAL PHE VAL SER PRO SER ALA SER ASP SEQRES 3 F 176 GLY ILE GLN TYR VAL ALA LEU PRO CYS CYS ALA ILE GLN SEQRES 4 F 176 ALA SER ALA ALA SER THR LEU PRO LEU PHE PHE ALA VAL SEQRES 5 F 176 HIS SER ILE HIS PHE ALA ASP PRO ASN HIS CYS ASN GLY SEQRES 6 F 176 VAL CYS ILE ALA LYS LEU ARG SER LYS THR GLY ASP ILE SEQRES 7 F 176 THR VAL GLU THR CYS VAL ASN GLY PHE ASN LEU ARG SER SEQRES 8 F 176 PHE LEU VAL ALA VAL VAL ARG ARG LEU GLY SER TRP ALA SEQRES 9 F 176 SER GLN GLU ASN LEU ARG LEU LEU TRP TYR LEU GLN ARG SEQRES 10 F 176 SER LEU THR ALA TYR THR VAL GLY PHE ASN ALA THR THR SEQRES 11 F 176 ALA ASP SER SER ILE HIS ASN VAL ASN ILE ILE ILE ILE SEQRES 12 F 176 SER VAL GLY LYS ALA MET ASN ARG THR GLY SER VAL SER SEQRES 13 F 176 GLY SER GLN THR ARG ALA LYS SER SER SER ARG ARG ALA SEQRES 14 F 176 HIS ALA GLY GLN LYS GLY LYS HELIX 1 AA1 GLN A 79 VAL A 83 5 5 HELIX 2 AA2 SER D 28 SER D 31 5 4 HELIX 3 AA3 TRP E 62 ILE E 69 1 8 HELIX 4 AA4 THR E 70 ALA E 81 1 12 HELIX 5 AA5 ASP E 86 LEU E 97 1 12 HELIX 6 AA6 ASN E 131 LEU E 135 5 5 HELIX 7 AA7 ALA E 146 PHE E 154 1 9 HELIX 8 AA8 PRO E 166 PHE E 171 1 6 HELIX 9 AA9 THR E 237 LEU E 241 1 5 HELIX 10 AB1 GLN E 261 THR E 265 5 5 HELIX 11 AB2 ASN E 267 GLU E 277 1 11 HELIX 12 AB3 THR E 279 ARG E 297 1 19 HELIX 13 AB4 ARG E 298 ALA E 301 5 4 HELIX 14 AB5 ALA E 305 HIS E 330 1 26 HELIX 15 AB6 VAL E 335 MET E 356 1 22 HELIX 16 AB7 THR E 367 ALA E 378 1 12 HELIX 17 AB8 SER E 381 LEU E 388 1 8 HELIX 18 AB9 SER E 392 ALA E 404 1 13 HELIX 19 AC1 PRO E 410 THR E 429 1 20 HELIX 20 AC2 ASP E 436 ASP E 451 1 16 HELIX 21 AC3 ASP E 457 CYS E 475 1 19 HELIX 22 AC4 THR E 476 PHE E 487 1 12 HELIX 23 AC5 SER E 500 LEU E 504 5 5 HELIX 24 AC6 GLY E 536 ASP E 547 1 12 HELIX 25 AC7 ASN E 658 PHE E 666 1 9 HELIX 26 AC8 LEU F 39 PHE F 41 5 3 HELIX 27 AC9 GLY F 77 LEU F 91 1 15 HELIX 28 AD1 GLY F 92 ALA F 95 5 4 HELIX 29 AD2 SER F 96 GLY F 116 1 21 HELIX 30 AD3 ASN F 118 ALA F 122 5 5 HELIX 31 AD4 ASP F 123 ASN F 128 5 6 SHEET 1 AA1 2 SER A 10 SER A 12 0 SHEET 2 AA1 2 LYS A 103 GLU A 105 1 O LYS A 103 N LEU A 11 SHEET 1 AA2 2 ASN A 22 CYS A 23 0 SHEET 2 AA2 2 PHE A 71 THR A 72 -1 O PHE A 71 N CYS A 23 SHEET 1 AA3 2 LEU A 27C TYR A 27D 0 SHEET 2 AA3 2 LYS A 30 ASN A 31 -1 O LYS A 30 N TYR A 27D SHEET 1 AA4 3 LYS A 45 ILE A 48 0 SHEET 2 AA4 3 LEU A 33 GLN A 38 -1 N TRP A 35 O LEU A 47 SHEET 3 AA4 3 VAL A 85 GLN A 90 -1 O VAL A 85 N GLN A 38 SHEET 1 AA5 2 PHE A 62 SER A 63 0 SHEET 2 AA5 2 THR A 74 ILE A 75 -1 O THR A 74 N SER A 63 SHEET 1 AA6 6 GLY B 10 VAL B 12 0 SHEET 2 AA6 6 THR B 107 VAL B 111 1 O THR B 110 N VAL B 12 SHEET 3 AA6 6 ALA B 88 VAL B 95 -1 N TYR B 90 O THR B 107 SHEET 4 AA6 6 MET B 34 ARG B 38 -1 N SER B 35 O ALA B 93 SHEET 5 AA6 6 GLU B 46 ILE B 51 -1 O VAL B 48 N TRP B 36 SHEET 6 AA6 6 LEU B 57 TYR B 59 -1 O SER B 58 N GLY B 50 SHEET 1 AA7 4 GLY B 10 VAL B 12 0 SHEET 2 AA7 4 THR B 107 VAL B 111 1 O THR B 110 N VAL B 12 SHEET 3 AA7 4 ALA B 88 VAL B 95 -1 N TYR B 90 O THR B 107 SHEET 4 AA7 4 PHE B 100D TRP B 103 -1 O TYR B 102 N ARG B 94 SHEET 1 AA8 3 SER B 17 CYS B 22 0 SHEET 2 AA8 3 SER B 77 HIS B 82A-1 O LEU B 80 N LEU B 20 SHEET 3 AA8 3 PHE B 67 ASP B 72 -1 N SER B 70 O TYR B 79 SHEET 1 AA9 4 THR C 5 SER C 7 0 SHEET 2 AA9 4 VAL C 19 ARG C 24 -1 O SER C 22 N SER C 7 SHEET 3 AA9 4 ASP C 70 ILE C 75 -1 O ILE C 75 N VAL C 19 SHEET 4 AA9 4 GLY C 64 SER C 67 -1 N SER C 65 O THR C 72 SHEET 1 AB1 3 SER C 10 VAL C 11 0 SHEET 2 AB1 3 THR C 102 LEU C 104 1 O LYS C 103 N VAL C 11 SHEET 3 AB1 3 THR C 85 TYR C 86 -1 N TYR C 86 O THR C 102 SHEET 1 AB2 2 LEU C 33 TRP C 35 0 SHEET 2 AB2 2 CYS C 88 GLN C 90 -1 O GLN C 89 N VAL C 34 SHEET 1 AB3 2 ILE C 48 TYR C 49 0 SHEET 2 AB3 2 SER C 53 LEU C 54 -1 O SER C 53 N TYR C 49 SHEET 1 AB4 4 VAL D 5 GLN D 6 0 SHEET 2 AB4 4 SER D 21 LYS D 23 -1 O LYS D 23 N VAL D 5 SHEET 3 AB4 4 THR D 77 LEU D 82 -1 O ALA D 78 N CYS D 22 SHEET 4 AB4 4 VAL D 67 ALA D 71 -1 N THR D 70 O TYR D 79 SHEET 1 AB5 6 GLU D 10 VAL D 11 0 SHEET 2 AB5 6 THR D 107 THR D 110 1 O THR D 110 N GLU D 10 SHEET 3 AB5 6 ALA D 88 SER D 95 -1 N ALA D 88 O VAL D 109 SHEET 4 AB5 6 THR D 33 ARG D 38 -1 N SER D 35 O ALA D 93 SHEET 5 AB5 6 GLU D 46 ILE D 52 -1 O GLY D 49 N TRP D 36 SHEET 6 AB5 6 THR D 56 TYR D 59 -1 O ASN D 58 N ARG D 50 SHEET 1 AB6 4 GLU D 10 VAL D 11 0 SHEET 2 AB6 4 THR D 107 THR D 110 1 O THR D 110 N GLU D 10 SHEET 3 AB6 4 ALA D 88 SER D 95 -1 N ALA D 88 O VAL D 109 SHEET 4 AB6 4 ILE D 102 TRP D 103 -1 O ILE D 102 N ILE D 94 SHEET 1 AB7 5 SER E 57 ASN E 61 0 SHEET 2 AB7 5 ASN E 46 LEU E 51 -1 N LEU E 47 O LEU E 60 SHEET 3 AB7 5 VAL F 43 PHE F 48 1 O ILE F 46 N GLU E 50 SHEET 4 AB7 5 LEU F 62 THR F 66 -1 O ARG F 63 N HIS F 44 SHEET 5 AB7 5 ILE F 69 THR F 73 -1 O ILE F 69 N THR F 66 SHEET 1 AB8 8 VAL E 104 VAL E 105 0 SHEET 2 AB8 8 THR E 242 ARG E 245 1 O ARG E 245 N VAL E 104 SHEET 3 AB8 8 ALA E 250 ILE E 254 -1 O LEU E 251 N ALA E 244 SHEET 4 AB8 8 HIS E 220 GLY E 224 -1 N LEU E 222 O VAL E 252 SHEET 5 AB8 8 PHE E 202 VAL E 205 -1 N VAL E 205 O LEU E 221 SHEET 6 AB8 8 VAL E 197 VAL E 198 -1 N VAL E 197 O VAL E 204 SHEET 7 AB8 8 VAL E 179 SER E 182 -1 N VAL E 179 O VAL E 198 SHEET 8 AB8 8 THR E 360 VAL E 362 -1 O VAL E 362 N LYS E 180 SHEET 1 AB9 2 GLY E 143 ASN E 145 0 SHEET 2 AB9 2 PHE E 332 GLU E 334 -1 O VAL E 333 N ILE E 144 SHEET 1 AC1 2 SER E 159 LEU E 160 0 SHEET 2 AC1 2 MET E 174 ASN E 175 -1 O MET E 174 N LEU E 160 SHEET 1 AC2 4 ILE E 565 LEU E 571 0 SHEET 2 AC2 4 VAL E 574 SER E 579 -1 O ILE E 578 N ALA E 567 SHEET 3 AC2 4 PHE E 601 ILE E 605 -1 O ILE E 605 N THR E 575 SHEET 4 AC2 4 TYR E 589 GLU E 590 -1 N TYR E 589 O ILE E 602 SHEET 1 AC3 4 GLY E 649 TYR E 655 0 SHEET 2 AC3 4 VAL E 640 ASP E 645 -1 N ASP E 645 O GLY E 649 SHEET 3 AC3 4 HIS E 681 LEU E 685 -1 O HIS E 681 N TYR E 644 SHEET 4 AC3 4 VAL E 691 ILE E 694 -1 O VAL E 692 N TRP E 684 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.03 SSBOND 2 CYS B 22 CYS B 92 1555 1555 2.03 SSBOND 3 CYS C 23 CYS C 88 1555 1555 2.03 SSBOND 4 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 5 CYS E 115 CYS E 337 1555 1555 2.03 SSBOND 6 CYS E 300 CYS E 355 1555 1555 2.04 SSBOND 7 CYS E 475 CYS E 502 1555 1555 2.03 SSBOND 8 CYS E 557 CYS E 609 1555 1555 2.03 SSBOND 9 CYS F 26 CYS F 54 1555 1555 2.03 SSBOND 10 CYS F 27 CYS F 74 1555 1555 2.03 CISPEP 1 SER A 7 PRO A 8 0 -3.82 CISPEP 2 SER C 7 PRO C 8 0 -2.93 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