HEADER VIRAL PROTEIN/IMMUNE SYSTEM 11-JUL-25 9PIX TITLE MUR14 FAB WITH HBV C18V PMHC COMPND MOL_ID: 1; COMPND 2 MOLECULE: MHC CLASS I ANTIGEN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MUR14 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MUR14 LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: C18V PEPTIDE; COMPND 15 CHAIN: P; COMPND 16 SYNONYM: CAPSID PROTEIN,CORE ANTIGEN,CORE PROTEIN; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 5; COMPND 19 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 20 CHAIN: B; COMPND 21 FRAGMENT: UNP RESIDUES 21-119; COMPND 22 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: HLA-A; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 18 ORGANISM_COMMON: MOUSE; SOURCE 19 ORGANISM_TAXID: 10090; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 24 MOL_ID: 4; SOURCE 25 SYNTHETIC: YES; SOURCE 26 ORGANISM_SCIENTIFIC: HEPATITIS B VIRUS; SOURCE 27 ORGANISM_TAXID: 10407; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_COMMON: HUMAN; SOURCE 31 ORGANISM_TAXID: 9606; SOURCE 32 GENE: B2M, CDABP0092, HDCMA22P; SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HBV, PMHC, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR D.E.MORTENSON REVDAT 1 01-OCT-25 9PIX 0 JRNL AUTH S.KHAN,J.LUM,H.STEPHENSON,P.B.KOHLI,D.MORTENSON, JRNL AUTH 2 D.RAMAKRISHNAN,M.HUNG,S.DING,E.SETO,S.LU,R.YEN,D.JIN,B.LEE, JRNL AUTH 3 S.CLANCY,N.S.OAKDALE,N.NOVIKOV,D.KANG,R.LI,D.PAN,R.DAVE, JRNL AUTH 4 E.LANSDON,S.P.FLETCHER,A.V.GARG,N.THOMSEN,S.BALSITIS JRNL TITL A HIGHLY SELECTIVE TCR-MIMIC ANTIBODY REVEALS UNEXPECTED JRNL TITL 2 MECHANISMS OF HBV PEPTIDE-MHC RECOGNITION AND PREVIOUSLY JRNL TITL 3 UNKNOWN TARGET BIOLOGY. JRNL REF MABS V. 17 62998 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40990156 JRNL DOI 10.1080/19420862.2025.2562998 REMARK 2 REMARK 2 RESOLUTION. 2.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21_5207 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.80 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 37959 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.188 REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1900 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 45.8000 - 5.6600 0.99 2639 140 0.1607 0.1853 REMARK 3 2 5.6600 - 4.4900 1.00 2606 137 0.1366 0.1587 REMARK 3 3 4.4900 - 3.9300 1.00 2585 132 0.1384 0.1702 REMARK 3 4 3.9300 - 3.5700 0.99 2578 134 0.1589 0.2088 REMARK 3 5 3.5700 - 3.3100 1.00 2553 139 0.1667 0.2237 REMARK 3 6 3.3100 - 3.1200 1.00 2556 137 0.1926 0.2505 REMARK 3 7 3.1200 - 2.9600 1.00 2594 132 0.2225 0.3127 REMARK 3 8 2.9600 - 2.8300 1.00 2551 145 0.2203 0.3006 REMARK 3 9 2.8300 - 2.7200 1.00 2567 127 0.2318 0.3115 REMARK 3 10 2.7200 - 2.6300 1.00 2566 138 0.2483 0.3615 REMARK 3 11 2.6300 - 2.5500 1.00 2556 135 0.2629 0.3754 REMARK 3 12 2.5500 - 2.4700 1.00 2567 129 0.2660 0.3298 REMARK 3 13 2.4700 - 2.4100 1.00 2557 138 0.2724 0.3083 REMARK 3 14 2.4100 - 2.3500 1.00 2584 137 0.2984 0.3597 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.381 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.925 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.96 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.91 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 6561 REMARK 3 ANGLE : 0.501 8949 REMARK 3 CHIRALITY : 0.040 968 REMARK 3 PLANARITY : 0.004 1159 REMARK 3 DIHEDRAL : 12.707 2347 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 20.3529 2.5885 -1.4580 REMARK 3 T TENSOR REMARK 3 T11: 0.3025 T22: 0.2293 REMARK 3 T33: 0.2836 T12: 0.0118 REMARK 3 T13: -0.0581 T23: -0.0217 REMARK 3 L TENSOR REMARK 3 L11: 1.4316 L22: 0.2290 REMARK 3 L33: 0.8231 L12: 0.3493 REMARK 3 L13: -0.7905 L23: -0.2441 REMARK 3 S TENSOR REMARK 3 S11: -0.0840 S12: 0.0025 S13: -0.0783 REMARK 3 S21: -0.0180 S22: 0.0192 S23: -0.0555 REMARK 3 S31: 0.0720 S32: 0.0631 S33: 0.0769 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9PIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1000297929. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-JUN-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37980 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350 REMARK 200 RESOLUTION RANGE LOW (A) : 49.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 4.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.19100 REMARK 200 FOR THE DATA SET : 7.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.26900 REMARK 200 FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NH4F, 20% PEG3350, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 300K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.68000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, P, B 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 MET A 0 REMARK 465 PRO A 276 REMARK 465 GLY A 277 REMARK 465 SER A 278 REMARK 465 GLY A 279 REMARK 465 GLY A 280 REMARK 465 SER A 281 REMARK 465 GLY A 282 REMARK 465 GLY A 283 REMARK 465 SER A 284 REMARK 465 ALA A 285 REMARK 465 GLY A 286 REMARK 465 GLY A 287 REMARK 465 GLY A 288 REMARK 465 LEU A 289 REMARK 465 ASN A 290 REMARK 465 ASP A 291 REMARK 465 ILE A 292 REMARK 465 PHE A 293 REMARK 465 GLU A 294 REMARK 465 ALA A 295 REMARK 465 GLN A 296 REMARK 465 LYS A 297 REMARK 465 ILE A 298 REMARK 465 GLU A 299 REMARK 465 TRP A 300 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 HIS H 217 REMARK 465 HIS H 218 REMARK 465 HIS H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 ASP H 225 REMARK 465 TYR H 226 REMARK 465 LYS H 227 REMARK 465 ASP H 228 REMARK 465 ASP H 229 REMARK 465 ASP H 230 REMARK 465 ASP H 231 REMARK 465 LYS H 232 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 MET B 0 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 58 CG CD OE1 OE2 REMARK 470 LYS A 121 CG CD CE NZ REMARK 470 GLU A 177 CG CD OE1 OE2 REMARK 470 ARG A 181 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 275 CG CD OE1 OE2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 GLU H 85 CG CD OE1 OE2 REMARK 470 LYS H 206 CG CD CE NZ REMARK 470 ARG H 210 CG CD NE CZ NH1 NH2 REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 ASP L 122 CG OD1 OD2 REMARK 470 LEU L 154 CG CD1 CD2 REMARK 470 LYS L 188 CG CD CE NZ REMARK 470 LYS L 190 CG CD CE NZ REMARK 470 GLU L 195 CG CD OE1 OE2 REMARK 470 GLU B 47 CG CD OE1 OE2 REMARK 470 LYS B 58 CG CD CE NZ REMARK 470 GLU B 74 CG CD OE1 OE2 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 ASP A 29 -118.11 51.75 REMARK 500 TRP A 107 19.15 59.83 REMARK 500 TYR A 123 -72.74 -115.52 REMARK 500 SER A 195 -161.89 -165.18 REMARK 500 ASP H 144 63.64 63.77 REMARK 500 ALA H 158 31.68 -86.49 REMARK 500 LEU H 159 98.64 -161.55 REMARK 500 SER L 26 3.29 -69.48 REMARK 500 ALA L 51 -27.65 68.32 REMARK 500 SER L 77 78.49 50.95 REMARK 500 ALA L 84 -157.48 -167.27 REMARK 500 ASN L 138 89.85 52.51 REMARK 500 LYS L 169 -70.94 -93.82 REMARK 500 TRP B 60 -1.97 77.34 REMARK 500 ASP B 98 65.73 -103.97 REMARK 500 REMARK 500 REMARK: NULL DBREF 9PIX A 1 276 UNP Q8WLS4 Q8WLS4_HUMAN 25 300 DBREF 9PIX H 1 232 PDB 9PIX 9PIX 1 232 DBREF 9PIX L 1 214 PDB 9PIX 9PIX 1 214 DBREF 9PIX P 1 10 UNP P17391 CAPSD_HBVB1 18 27 DBREF 9PIX B 1 99 UNP P61769 B2MG_HUMAN 21 119 SEQADV 9PIX MET A 0 UNP Q8WLS4 INITIATING METHIONINE SEQADV 9PIX GLY A 277 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX SER A 278 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLY A 279 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLY A 280 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX SER A 281 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLY A 282 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLY A 283 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX SER A 284 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX ALA A 285 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLY A 286 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLY A 287 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLY A 288 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX LEU A 289 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX ASN A 290 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX ASP A 291 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX ILE A 292 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX PHE A 293 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLU A 294 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX ALA A 295 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLN A 296 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX LYS A 297 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX ILE A 298 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX GLU A 299 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX TRP A 300 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PIX MET B 0 UNP P61769 INITIATING METHIONINE SEQRES 1 A 301 MET GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SEQRES 2 A 301 SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL SEQRES 3 A 301 GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER SEQRES 4 A 301 ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP SEQRES 5 A 301 ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR SEQRES 6 A 301 ARG LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP SEQRES 7 A 301 LEU GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA SEQRES 8 A 301 GLY SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL SEQRES 9 A 301 GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR SEQRES 10 A 301 ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP SEQRES 11 A 301 LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR SEQRES 12 A 301 THR LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN SEQRES 13 A 301 LEU ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU SEQRES 14 A 301 ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG SEQRES 15 A 301 THR ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SEQRES 16 A 301 SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER SEQRES 17 A 301 PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP SEQRES 18 A 301 GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR SEQRES 19 A 301 ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA SEQRES 20 A 301 VAL VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS SEQRES 21 A 301 HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU SEQRES 22 A 301 ARG TRP GLU PRO GLY SER GLY GLY SER GLY GLY SER ALA SEQRES 23 A 301 GLY GLY GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE SEQRES 24 A 301 GLU TRP SEQRES 1 H 240 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 240 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 240 TYR THR PHE THR ASP TYR PHE MET ASN TRP VAL LYS GLN SEQRES 4 H 240 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ASP ILE ASN SEQRES 5 H 240 PRO ASN ASN GLY GLY THR SER TYR ASN GLN LYS PHE LYS SEQRES 6 H 240 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 H 240 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 H 240 ALA VAL TYR TYR CYS ALA ARG GLY LEU TYR ASP GLY TYR SEQRES 9 H 240 TYR VAL GLY PHE ALA TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 240 THR VAL SER ALA ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 240 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 240 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 240 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 240 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 240 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 240 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 240 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 18 H 240 LYS SER CYS HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR SEQRES 19 H 240 LYS ASP ASP ASP ASP LYS SEQRES 1 L 215 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL SER SER SER TYR LEU SER TRP TYR GLN GLN SEQRES 4 L 215 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 215 SER THR ARG ALA THR GLY LEU PRO ALA ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 215 LEU GLN PRO GLU ASP PHE ALA VAL TYR TYR CYS HIS GLN SEQRES 8 L 215 ASP TYR ASN LEU PRO TYR THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 P 10 PHE LEU PRO SER ASP PHE PHE PRO SER VAL SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET FORMUL 6 HOH *374(H2 O) HELIX 1 AA1 ALA A 49 GLU A 55 5 7 HELIX 2 AA2 GLY A 56 TYR A 85 1 30 HELIX 3 AA3 ASP A 137 ALA A 150 1 14 HELIX 4 AA4 HIS A 151 GLY A 162 1 12 HELIX 5 AA5 GLY A 162 GLY A 175 1 14 HELIX 6 AA6 GLY A 175 GLN A 180 1 6 HELIX 7 AA7 GLN A 253 GLN A 255 5 3 HELIX 8 AA8 THR H 28 TYR H 32 5 5 HELIX 9 AA9 GLN H 61 LYS H 64 5 4 HELIX 10 AB1 THR H 83 SER H 87 5 5 HELIX 11 AB2 PRO H 185 GLY H 190 5 6 HELIX 12 AB3 LYS H 201 ASN H 204 5 4 HELIX 13 AB4 SER L 29 SER L 31 5 3 HELIX 14 AB5 GLN L 79 PHE L 83 5 5 HELIX 15 AB6 SER L 121 LYS L 126 1 6 HELIX 16 AB7 LYS L 183 LYS L 188 1 6 SHEET 1 AA1 8 GLU A 46 PRO A 47 0 SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46 SHEET 3 AA1 8 ARG A 21 VAL A 28 -1 N VAL A 28 O THR A 31 SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27 SHEET 5 AA1 8 THR A 94 VAL A 103 -1 O VAL A 103 N HIS A 3 SHEET 6 AA1 8 PHE A 109 TYR A 118 -1 O ARG A 111 N ASP A 102 SHEET 7 AA1 8 LYS A 121 LEU A 126 -1 O LEU A 126 N HIS A 114 SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125 SHEET 1 AA2 4 LYS A 186 ALA A 193 0 SHEET 2 AA2 4 ALA A 199 PHE A 208 -1 O LEU A 206 N LYS A 186 SHEET 3 AA2 4 PHE A 241 VAL A 249 -1 O ALA A 245 N CYS A 203 SHEET 4 AA2 4 THR A 228 LEU A 230 -1 N GLU A 229 O ALA A 246 SHEET 1 AA3 4 LYS A 186 ALA A 193 0 SHEET 2 AA3 4 ALA A 199 PHE A 208 -1 O LEU A 206 N LYS A 186 SHEET 3 AA3 4 PHE A 241 VAL A 249 -1 O ALA A 245 N CYS A 203 SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242 SHEET 1 AA4 4 GLU A 222 ASP A 223 0 SHEET 2 AA4 4 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222 SHEET 3 AA4 4 TYR A 257 GLN A 262 -1 O HIS A 260 N THR A 216 SHEET 4 AA4 4 LEU A 270 ARG A 273 -1 O LEU A 272 N CYS A 259 SHEET 1 AA5 4 GLN H 3 GLN H 6 0 SHEET 2 AA5 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA5 4 THR H 77 LEU H 82 -1 O MET H 80 N ILE H 20 SHEET 4 AA5 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA6 6 GLU H 10 VAL H 12 0 SHEET 2 AA6 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA6 6 ALA H 88 TYR H 97 -1 N ALA H 88 O VAL H 109 SHEET 4 AA6 6 MET H 34 GLN H 39 -1 N ASN H 35 O ALA H 93 SHEET 5 AA6 6 LEU H 45 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA6 6 THR H 57 TYR H 59 -1 O SER H 58 N ASP H 50 SHEET 1 AA7 4 GLU H 10 VAL H 12 0 SHEET 2 AA7 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA7 4 ALA H 88 TYR H 97 -1 N ALA H 88 O VAL H 109 SHEET 4 AA7 4 TYR H 100A TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA8 4 SER H 120 LEU H 124 0 SHEET 2 AA8 4 ALA H 136 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA8 4 TYR H 176 VAL H 184 -1 O VAL H 184 N ALA H 136 SHEET 4 AA8 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA9 4 SER H 120 LEU H 124 0 SHEET 2 AA9 4 ALA H 136 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA9 4 TYR H 176 VAL H 184 -1 O VAL H 184 N ALA H 136 SHEET 4 AA9 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB1 3 THR H 151 TRP H 154 0 SHEET 2 AB1 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB1 3 THR H 205 ARG H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AB2 3 MET L 4 SER L 7 0 SHEET 2 AB2 3 ALA L 19 VAL L 28 -1 O ARG L 24 N THR L 5 SHEET 3 AB2 3 PHE L 62 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 1 AB3 6 THR L 10 LEU L 13 0 SHEET 2 AB3 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB3 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AB3 6 ARG L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AB3 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AB4 4 SER L 114 PHE L 118 0 SHEET 2 AB4 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB4 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB4 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB5 4 LEU L 154 GLN L 155 0 SHEET 2 AB5 4 LYS L 145 VAL L 150 -1 N TRP L 148 O GLN L 155 SHEET 3 AB5 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB5 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB6 4 LYS B 6 SER B 11 0 SHEET 2 AB6 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6 SHEET 3 AB6 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25 SHEET 4 AB6 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 AB7 4 LYS B 6 SER B 11 0 SHEET 2 AB7 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6 SHEET 3 AB7 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25 SHEET 4 AB7 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 AB8 4 GLU B 44 ARG B 45 0 SHEET 2 AB8 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 AB8 4 TYR B 78 ASN B 83 -1 O ASN B 83 N GLU B 36 SHEET 4 AB8 4 LYS B 91 LYS B 94 -1 O VAL B 93 N CYS B 80 SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.04 SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 6 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 7 CYS B 25 CYS B 80 1555 1555 2.04 CISPEP 1 TYR A 209 PRO A 210 0 3.73 CISPEP 2 PHE H 146 PRO H 147 0 -3.88 CISPEP 3 GLU H 148 PRO H 149 0 2.10 CISPEP 4 SER L 7 PRO L 8 0 -2.47 CISPEP 5 LEU L 94 PRO L 95 0 1.67 CISPEP 6 TYR L 140 PRO L 141 0 3.72 CISPEP 7 HIS B 31 PRO B 32 0 1.80 CRYST1 71.599 73.360 93.889 90.00 111.03 90.00 P 1 21 1 2 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 0.013967 0.000000 0.005370 0.00000 SCALE2 0.000000 0.013631 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011411 0.00000