HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-JUL-25 9PKF TITLE MUR35 FAB WITH HBV C18I 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: MUR35 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MUR35 LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: C18I 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 9PKF 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. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.42 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1 REMARK 3 NUMBER OF REFLECTIONS : 27937 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.250 REMARK 3 R VALUE (WORKING SET) : 0.247 REMARK 3 FREE R VALUE : 0.303 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 1387 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 45.4200 - 5.6000 0.93 2745 145 0.2358 0.2481 REMARK 3 2 5.6000 - 4.4500 0.91 2588 134 0.2095 0.2555 REMARK 3 3 4.4400 - 3.8800 0.93 2597 137 0.2087 0.2830 REMARK 3 4 3.8800 - 3.5300 0.93 2611 141 0.2377 0.2928 REMARK 3 5 3.5300 - 3.2800 0.96 2640 141 0.2595 0.3079 REMARK 3 6 3.2800 - 3.0800 0.96 2664 138 0.2981 0.4223 REMARK 3 7 3.0800 - 2.9300 0.97 2663 135 0.3175 0.4924 REMARK 3 8 2.9300 - 2.8000 0.98 2686 140 0.3335 0.3707 REMARK 3 9 2.8000 - 2.6900 0.98 2688 139 0.3256 0.3853 REMARK 3 10 2.6900 - 2.6000 0.97 2668 137 0.3103 0.3554 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) : 0.493 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.464 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 62.21 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.67 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 : 0.001 6074 REMARK 3 ANGLE : 0.412 8291 REMARK 3 CHIRALITY : 0.039 904 REMARK 3 PLANARITY : 0.003 1079 REMARK 3 DIHEDRAL : 11.572 2110 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): -42.5153 18.2544 -19.8502 REMARK 3 T TENSOR REMARK 3 T11: 0.4832 T22: 0.2534 REMARK 3 T33: 0.6254 T12: -0.0226 REMARK 3 T13: -0.0428 T23: -0.0099 REMARK 3 L TENSOR REMARK 3 L11: 1.0404 L22: 0.3492 REMARK 3 L33: 2.0528 L12: -0.4305 REMARK 3 L13: -0.4318 L23: 0.2854 REMARK 3 S TENSOR REMARK 3 S11: 0.0899 S12: 0.0894 S13: 0.0311 REMARK 3 S21: -0.0608 S22: 0.0347 S23: 0.0557 REMARK 3 S31: 0.0493 S32: 0.0625 S33: -0.1119 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 9PKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1000297997. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-FEB-22 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 : APS REMARK 200 BEAMLINE : 17-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28001 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 174.170 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7 REMARK 200 DATA REDUNDANCY : 4.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.15600 REMARK 200 FOR THE DATA SET : 7.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.45100 REMARK 200 FOR SHELL : 1.100 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 (%): 48.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40 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 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 87.08450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.50900 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 87.08450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.50900 REMARK 290 SMTRY3 4 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 ASP A 220 REMARK 465 GLY A 221 REMARK 465 GLU A 222 REMARK 465 ASP A 223 REMARK 465 GLN A 224 REMARK 465 THR A 225 REMARK 465 GLN A 226 REMARK 465 ASP A 227 REMARK 465 VAL A 249 REMARK 465 PRO A 250 REMARK 465 SER A 251 REMARK 465 GLY A 252 REMARK 465 GLN A 253 REMARK 465 GLU A 254 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 SER H 127 REMARK 465 SER H 128 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 THR H 135 REMARK 465 ALA H 136 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 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 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 MET B 0 REMARK 465 ILE B 1 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 121 CG CD CE NZ REMARK 470 GLU A 154 CG CD OE1 OE2 REMARK 470 LYS A 186 CG CD CE NZ REMARK 470 GLU A 198 CG CD OE1 OE2 REMARK 470 GLN A 218 CG CD OE1 NE2 REMARK 470 ARG A 219 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 229 CG CD OE1 OE2 REMARK 470 GLN A 255 CG CD OE1 NE2 REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2 REMARK 470 TYR A 257 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS A 260 CG ND1 CD2 CE1 NE2 REMARK 470 GLU A 275 CG CD OE1 OE2 REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 LYS H 117 CG CD CE NZ REMARK 470 LEU H 138 CG CD1 CD2 REMARK 470 THR H 151 OG1 CG2 REMARK 470 VAL H 152 CG1 CG2 REMARK 470 ASN H 155 CG OD1 ND2 REMARK 470 VAL H 163 CG1 CG2 REMARK 470 ILE H 195 CG1 CG2 CD1 REMARK 470 VAL H 198 CG1 CG2 REMARK 470 LYS H 201 CG CD CE NZ REMARK 470 LYS H 206 CG CD CE NZ REMARK 470 VAL H 207 CG1 CG2 REMARK 470 ARG H 210 CG CD NE CZ NH1 NH2 REMARK 470 VAL H 211 CG1 CG2 REMARK 470 GLU L 81 CG CD OE1 OE2 REMARK 470 LYS L 107 CG CD CE NZ REMARK 470 ARG L 108 CG CD NE CZ NH1 NH2 REMARK 470 VAL L 115 CG1 CG2 REMARK 470 PHE L 116 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE L 117 CG1 CG2 CD1 REMARK 470 PHE L 118 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU L 123 CG CD OE1 OE2 REMARK 470 GLU L 143 CG CD OE1 OE2 REMARK 470 LYS L 145 CG CD CE NZ REMARK 470 GLN L 147 CG CD OE1 NE2 REMARK 470 ASN L 152 CG OD1 ND2 REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 LEU L 179 CG CD1 CD2 REMARK 470 THR L 180 OG1 CG2 REMARK 470 LEU L 181 CG CD1 CD2 REMARK 470 LYS L 183 CG CD CE NZ REMARK 470 ASP L 185 CG OD1 OD2 REMARK 470 LYS L 188 CG CD CE NZ REMARK 470 HIS L 189 CG ND1 CD2 CE1 NE2 REMARK 470 LYS L 190 CG CD CE NZ REMARK 470 GLU L 195 CG CD OE1 OE2 REMARK 470 VAL L 205 CG1 CG2 REMARK 470 THR L 206 OG1 CG2 REMARK 470 LYS L 207 CG CD CE NZ REMARK 470 GLU B 44 CG CD OE1 OE2 REMARK 470 ARG B 45 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 48 CG CD CE NZ REMARK 470 LYS B 58 CG CD CE NZ REMARK 470 GLU B 69 CG CD OE1 OE2 REMARK 470 GLU B 74 CG CD OE1 OE2 REMARK 470 LYS B 75 CG CD CE NZ REMARK 470 ARG B 81 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 94 CG CD CE NZ 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 -132.15 59.18 REMARK 500 ASP A 30 38.04 -93.71 REMARK 500 LEU A 110 -53.93 -120.52 REMARK 500 TRP A 217 69.74 -117.59 REMARK 500 LYS A 243 148.20 -170.88 REMARK 500 SER H 100 169.78 67.27 REMARK 500 SER H 115 -63.07 -105.31 REMARK 500 ALA H 125 113.83 -161.41 REMARK 500 ASP H 144 69.96 61.44 REMARK 500 LEU H 159 87.93 -150.93 REMARK 500 SER H 187 48.63 -85.75 REMARK 500 GLN L 42 -168.08 -101.23 REMARK 500 ALA L 51 -21.98 66.34 REMARK 500 SER L 52 -21.99 -144.53 REMARK 500 ASP L 82 31.43 -79.95 REMARK 500 ARG L 108 -116.39 -127.97 REMARK 500 VAL L 110 90.94 -67.35 REMARK 500 GLU L 143 94.51 -66.93 REMARK 500 LYS L 169 -39.00 -140.03 REMARK 500 PRO L 204 109.90 -59.93 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9PIX RELATED DB: PDB REMARK 900 RELATED ID: 9PKC RELATED DB: PDB DBREF 9PKF A 1 276 UNP Q8WLS4 Q8WLS4_HUMAN 25 300 DBREF 9PKF H 1 232 PDB 9PKF 9PKF 1 232 DBREF 9PKF L 1 214 PDB 9PKF 9PKF 1 214 DBREF 9PKF P 1 10 UNP P69707 CAPSD_HBVB2 18 27 DBREF 9PKF B 1 99 UNP P61769 B2MG_HUMAN 21 119 SEQADV 9PKF MET A 0 UNP Q8WLS4 INITIATING METHIONINE SEQADV 9PKF GLY A 277 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF SER A 278 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLY A 279 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLY A 280 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF SER A 281 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLY A 282 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLY A 283 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF SER A 284 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF ALA A 285 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLY A 286 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLY A 287 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLY A 288 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF LEU A 289 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF ASN A 290 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF ASP A 291 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF ILE A 292 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF PHE A 293 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLU A 294 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF ALA A 295 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLN A 296 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF LYS A 297 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF ILE A 298 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF GLU A 299 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF TRP A 300 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKF 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 237 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS SEQRES 2 H 237 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 237 TYR THR PHE THR ASP HIS PHE MET ASN TRP VAL ARG GLN SEQRES 4 H 237 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ASP ILE ASN SEQRES 5 H 237 PRO ASN ASN GLY GLY THR SER TYR ASN GLN LYS PHE LYS SEQRES 6 H 237 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 H 237 ALA PHE MET GLU VAL ARG SER LEU THR SER ASP ASP SER SEQRES 8 H 237 ALA VAL TYR TYR CYS ALA ARG ARG GLY TYR TYR GLY SER SEQRES 9 H 237 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 H 237 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 237 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 237 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 237 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 237 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 237 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 237 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 237 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 18 H 237 HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR LYS ASP ASP SEQRES 19 H 237 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 GLY VAL SER SER SER TYR PHE SER TRP TYR GLN GLN SEQRES 4 L 215 THR PRO GLY GLN ALA PRO ARG LEU LEU ILE SER GLY ALA SEQRES 5 L 215 SER THR ARG ALA THR GLY ILE 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 GLN 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 ILE 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 *133(H2 O) HELIX 1 AA1 PRO A 50 GLU A 55 5 6 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 THR H 28 HIS H 32 5 5 HELIX 8 AA8 GLN H 61 LYS H 64 5 4 HELIX 9 AA9 THR H 83 SER H 87 5 5 HELIX 10 AB1 SER H 156 ALA H 158 5 3 HELIX 11 AB2 SER L 29 SER L 31 5 3 HELIX 12 AB3 GLN L 79 PHE L 83 5 5 HELIX 13 AB4 SER L 182 GLU L 187 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 GLN A 115 N MET A 98 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 THR A 200 N HIS A 192 SHEET 3 AA2 4 PHE A 241 VAL A 247 -1 O ALA A 245 N CYS A 203 SHEET 4 AA2 4 GLU A 229 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 THR A 200 N HIS A 192 SHEET 3 AA3 4 PHE A 241 VAL A 247 -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 3 THR A 214 THR A 216 0 SHEET 2 AA4 3 CYS A 259 GLN A 262 -1 O HIS A 260 N THR A 216 SHEET 3 AA4 3 LEU A 270 LEU A 272 -1 O LEU A 270 N VAL A 261 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 VAL 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 PHE 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 VAL H 89 ARG H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA6 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 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 VAL H 89 ARG H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA7 4 PHE H 100A TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA8 4 PHE H 122 LEU H 124 0 SHEET 2 AA8 4 GLY H 139 LEU H 141 -1 O LEU H 141 N PHE H 122 SHEET 3 AA8 4 SER H 179 VAL H 181 -1 O SER H 180 N CYS H 140 SHEET 4 AA8 4 HIS H 164 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA9 2 THR H 151 TRP H 154 0 SHEET 2 AA9 2 CYS H 196 ASN H 199 -1 O ASN H 197 N SER H 153 SHEET 1 AB1 2 VAL H 169 LEU H 170 0 SHEET 2 AB1 2 TYR H 176 SER H 177 -1 O SER H 177 N VAL H 169 SHEET 1 AB2 4 MET L 4 SER L 7 0 SHEET 2 AB2 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB2 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AB2 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 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 PHE L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AB3 6 ARG L 45 SER 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 SER L 49 SHEET 1 AB4 4 THR L 10 LEU L 13 0 SHEET 2 AB4 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB4 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB5 4 PHE L 116 PHE L 118 0 SHEET 2 AB5 4 VAL L 132 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB5 4 TYR L 173 LEU L 179 -1 O SER L 177 N CYS L 134 SHEET 4 AB5 4 SER L 159 GLN L 160 -1 N GLN L 160 O THR L 178 SHEET 1 AB6 2 VAL L 146 GLN L 147 0 SHEET 2 AB6 2 GLU L 195 VAL L 196 -1 O GLU L 195 N GLN L 147 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 PHE B 70 N ASN B 21 SHEET 4 AB7 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 AB8 4 LYS B 6 SER B 11 0 SHEET 2 AB8 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6 SHEET 3 AB8 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21 SHEET 4 AB8 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 AB9 4 GLU B 44 ARG B 45 0 SHEET 2 AB9 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 AB9 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38 SHEET 4 AB9 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82 SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.03 SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.03 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 2.03 SSBOND 7 CYS B 25 CYS B 80 1555 1555 2.03 CISPEP 1 TYR A 209 PRO A 210 0 0.66 CISPEP 2 PHE H 146 PRO H 147 0 -1.53 CISPEP 3 GLU H 148 PRO H 149 0 -3.49 CISPEP 4 SER L 7 PRO L 8 0 -2.87 CISPEP 5 LEU L 94 PRO L 95 0 -2.06 CISPEP 6 TYR L 140 PRO L 141 0 4.49 CISPEP 7 HIS B 31 PRO B 32 0 3.25 CRYST1 174.169 73.018 72.921 90.00 90.00 90.00 P 21 21 2 4 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 0.005742 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013695 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013713 0.00000