HEADER VIRAL PROTEIN 29-JUN-23 8PMY TITLE HEV GT3 P DOMAIN IN COMPLEX WITH GLYCAN-INSENSITIVE NAB P60.15 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SCFV_P60.15; COMPND 3 CHAIN: A, L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CAPSID PROTEIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER'S S2 CELLS; SOURCE 7 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1963; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMT; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: PASLAHEPEVIRUS BALAYANI; SOURCE 12 ORGANISM_TAXID: 1678143; SOURCE 13 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7227; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER'S S2 CELLS; SOURCE 16 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1963; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PMT KEYWDS HEV, P DOMAIN, NON-GLYCOSYLATED, GLYCAN-INSENSITIVE, NEUTRALIZING KEYWDS 2 ANTIBODY (NAB), VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.SSEBYATIKA,T.KREY JRNL AUTH G.SSEBYATIKA,K.DINKELBORG,L.J.STROEH,F.HINTE,L.CORNEILLIE, JRNL AUTH 2 L.HUEFFNER,E.M.GUZMAN,P.L.NANKYA,N.PLUECKEBAUM,S.PRALLET, JRNL AUTH 3 A.K.MEHNERT,L.VERHOYE,C.JUERGENS,E.STEINMANN,H.WEDEMEYER, JRNL AUTH 4 A.VIEJO-BORBOLLA,L.V.DAO THI,T.PIETSCHMANN,M.LUETGEHETMANN, JRNL AUTH 5 P.MEULEMAN,M.DANDRI,T.KREY,P.BEHRENDT JRNL TITL A NOVEL CLASS OF BROADLY NEUTRALIZING HEPATITIS E JRNL TITL 2 VIRUS-SPECIFIC HUMAN ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.41 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.4 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.65 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 21738 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.214 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1087 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.42 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.13 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3363 REMARK 3 BIN FREE R VALUE : 0.3985 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 21 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2888 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 3 REMARK 3 SOLVENT ATOMS : 107 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.19 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -13.46800 REMARK 3 B22 (A**2) : 24.31570 REMARK 3 B33 (A**2) : -10.84770 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.330 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.285 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.222 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.282 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.223 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 2962 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4036 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 964 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 491 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 2962 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 395 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 2507 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.96 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.43 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.21 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8PMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292131530. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JUN-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, DESY REMARK 200 BEAMLINE : P11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.99987 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : POINTLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21742 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.406 REMARK 200 RESOLUTION RANGE LOW (A) : 48.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 13.12 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.4300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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 (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 11% W/V PEG 8000, 0.1M ZINC ACETATE REMARK 280 AND 0.1M MES PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 79.33500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.33500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 28.09500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.47500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 28.09500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.47500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 79.33500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 28.09500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.47500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 79.33500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 28.09500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 61.47500 REMARK 290 SMTRY3 8 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3640 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15300 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 124 REMARK 465 GLY A 125 REMARK 465 THR A 126 REMARK 465 GLY A 127 REMARK 465 GLY A 128 REMARK 465 SER A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 GLY A 132 REMARK 465 GLY A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 GLY A 136 REMARK 465 GLY A 137 REMARK 465 GLY A 138 REMARK 465 SER A 139 REMARK 465 GLY A 140 REMARK 465 GLY A 141 REMARK 465 GLY A 142 REMARK 465 ALA A 143 REMARK 465 ILE A 144 REMARK 465 GLN A 145 REMARK 465 LEU A 146 REMARK 465 THR A 147 REMARK 465 GLN A 148 REMARK 465 SER A 149 REMARK 465 PRO A 150 REMARK 465 SER A 151 REMARK 465 SER A 152 REMARK 465 LEU A 153 REMARK 465 SER A 154 REMARK 465 ALA A 155 REMARK 465 SER A 156 REMARK 465 VAL A 157 REMARK 465 GLY A 158 REMARK 465 ASP A 159 REMARK 465 SER A 160 REMARK 465 VAL A 161 REMARK 465 THR A 162 REMARK 465 ILE A 163 REMARK 465 THR A 164 REMARK 465 CYS A 165 REMARK 465 ARG A 166 REMARK 465 ALA A 167 REMARK 465 SER A 168 REMARK 465 GLN A 169 REMARK 465 ASP A 170 REMARK 465 ILE A 171 REMARK 465 PHE A 172 REMARK 465 SER A 173 REMARK 465 TYR A 174 REMARK 465 LEU A 175 REMARK 465 ALA A 176 REMARK 465 TRP A 177 REMARK 465 TYR A 178 REMARK 465 GLN A 179 REMARK 465 GLN A 180 REMARK 465 LYS A 181 REMARK 465 PRO A 182 REMARK 465 GLY A 183 REMARK 465 LYS A 184 REMARK 465 ALA A 185 REMARK 465 PRO A 186 REMARK 465 LYS A 187 REMARK 465 LEU A 188 REMARK 465 LEU A 189 REMARK 465 ILE A 190 REMARK 465 TYR A 191 REMARK 465 ALA A 192 REMARK 465 ALA A 193 REMARK 465 SER A 194 REMARK 465 THR A 195 REMARK 465 LEU A 196 REMARK 465 GLN A 197 REMARK 465 SER A 198 REMARK 465 GLY A 199 REMARK 465 VAL A 200 REMARK 465 PRO A 201 REMARK 465 SER A 202 REMARK 465 ARG A 203 REMARK 465 PHE A 204 REMARK 465 SER A 205 REMARK 465 GLY A 206 REMARK 465 SER A 207 REMARK 465 GLY A 208 REMARK 465 SER A 209 REMARK 465 GLY A 210 REMARK 465 THR A 211 REMARK 465 ASP A 212 REMARK 465 PHE A 213 REMARK 465 THR A 214 REMARK 465 LEU A 215 REMARK 465 THR A 216 REMARK 465 ILE A 217 REMARK 465 SER A 218 REMARK 465 SER A 219 REMARK 465 LEU A 220 REMARK 465 GLN A 221 REMARK 465 PRO A 222 REMARK 465 GLU A 223 REMARK 465 ASP A 224 REMARK 465 PHE A 225 REMARK 465 ALA A 226 REMARK 465 THR A 227 REMARK 465 TYR A 228 REMARK 465 TYR A 229 REMARK 465 CYS A 230 REMARK 465 GLN A 231 REMARK 465 GLN A 232 REMARK 465 LEU A 233 REMARK 465 ASN A 234 REMARK 465 ARG A 235 REMARK 465 TYR A 236 REMARK 465 PRO A 237 REMARK 465 PHE A 238 REMARK 465 ALA A 239 REMARK 465 PHE A 240 REMARK 465 GLY A 241 REMARK 465 PRO A 242 REMARK 465 GLY A 243 REMARK 465 THR A 244 REMARK 465 LYS A 245 REMARK 465 VAL A 246 REMARK 465 ASP A 247 REMARK 465 ILE A 248 REMARK 465 LYS A 249 REMARK 465 ASP A 250 REMARK 465 ASP A 251 REMARK 465 ASP A 252 REMARK 465 ASP A 253 REMARK 465 LYS A 254 REMARK 465 GLY B 450 REMARK 465 ASP B 451 REMARK 465 ASP B 452 REMARK 465 ASP B 453 REMARK 465 ASP B 454 REMARK 465 LYS B 455 REMARK 465 PRO B 456 REMARK 465 ALA B 457 REMARK 465 PRO B 458 REMARK 465 SER B 605 REMARK 465 ALA B 606 REMARK 465 LEU B 607 REMARK 465 ALA B 608 REMARK 465 VAL B 609 REMARK 465 LEU B 610 REMARK 465 GLU B 611 REMARK 465 ASP B 612 REMARK 465 THR B 613 REMARK 465 THR B 614 REMARK 465 ASP B 615 REMARK 465 TYR B 616 REMARK 465 PRO B 617 REMARK 465 ALA B 618 REMARK 465 ARG B 619 REMARK 465 ALA B 620 REMARK 465 HIS B 621 REMARK 465 THR B 622 REMARK 465 PHE B 623 REMARK 465 ASP B 624 REMARK 465 ASP B 625 REMARK 465 PHE B 626 REMARK 465 CYS B 627 REMARK 465 PRO B 628 REMARK 465 GLU B 629 REMARK 465 CYS B 630 REMARK 465 ARG B 631 REMARK 465 THR B 632 REMARK 465 LEU B 633 REMARK 465 GLY B 634 REMARK 465 LEU B 635 REMARK 465 GLN B 636 REMARK 465 GLY B 637 REMARK 465 CYS B 638 REMARK 465 ALA B 639 REMARK 465 PHE B 640 REMARK 465 GLN B 641 REMARK 465 SER B 642 REMARK 465 THR B 643 REMARK 465 ILE B 644 REMARK 465 ALA B 645 REMARK 465 GLU B 646 REMARK 465 LEU B 647 REMARK 465 GLN B 648 REMARK 465 ARG B 649 REMARK 465 LEU B 650 REMARK 465 LYS B 651 REMARK 465 MET B 652 REMARK 465 LYS B 653 REMARK 465 VAL B 654 REMARK 465 GLY B 655 REMARK 465 LYS B 656 REMARK 465 THR B 657 REMARK 465 ARG B 658 REMARK 465 GLU B 659 REMARK 465 SER B 660 REMARK 465 GLU L -141 REMARK 465 VAL L -140 REMARK 465 GLN L -139 REMARK 465 LEU L -138 REMARK 465 VAL L -137 REMARK 465 GLN L -136 REMARK 465 SER L -135 REMARK 465 GLY L -134 REMARK 465 ALA L -133 REMARK 465 GLU L -132 REMARK 465 LEU L -131 REMARK 465 LYS L -130 REMARK 465 LYS L -129 REMARK 465 PRO L -128 REMARK 465 GLY L -127 REMARK 465 GLU L -126 REMARK 465 SER L -125 REMARK 465 LEU L -124 REMARK 465 ARG L -123 REMARK 465 ILE L -122 REMARK 465 SER L -121 REMARK 465 CYS L -120 REMARK 465 LYS L -119 REMARK 465 GLY L -118 REMARK 465 SER L -117 REMARK 465 GLY L -116 REMARK 465 TYR L -115 REMARK 465 ASP L -114 REMARK 465 PHE L -113 REMARK 465 ALA L -112 REMARK 465 ASN L -111 REMARK 465 TYR L -110 REMARK 465 TRP L -109 REMARK 465 ILE L -108 REMARK 465 GLY L -107 REMARK 465 TRP L -106 REMARK 465 VAL L -105 REMARK 465 ARG L -104 REMARK 465 GLN L -103 REMARK 465 MET L -102 REMARK 465 PRO L -101 REMARK 465 GLY L -100 REMARK 465 LYS L -99 REMARK 465 GLY L -98 REMARK 465 LEU L -97 REMARK 465 GLU L -96 REMARK 465 TRP L -95 REMARK 465 MET L -94 REMARK 465 GLY L -93 REMARK 465 ILE L -92 REMARK 465 ILE L -91 REMARK 465 TYR L -90 REMARK 465 PRO L -89 REMARK 465 ARG L -88 REMARK 465 ASP L -87 REMARK 465 SER L -86 REMARK 465 ASP L -85 REMARK 465 ILE L -84 REMARK 465 ARG L -83 REMARK 465 TYR L -82 REMARK 465 SER L -81 REMARK 465 PRO L -80 REMARK 465 SER L -79 REMARK 465 PHE L -78 REMARK 465 GLN L -77 REMARK 465 GLY L -76 REMARK 465 GLN L -75 REMARK 465 VAL L -74 REMARK 465 THR L -73 REMARK 465 ILE L -72 REMARK 465 SER L -71 REMARK 465 ALA L -70 REMARK 465 ASP L -69 REMARK 465 LYS L -68 REMARK 465 SER L -67 REMARK 465 ILE L -66 REMARK 465 SER L -65 REMARK 465 THR L -64 REMARK 465 ALA L -63 REMARK 465 TYR L -62 REMARK 465 LEU L -61 REMARK 465 GLN L -60 REMARK 465 LEU L -59 REMARK 465 SER L -58 REMARK 465 SER L -57 REMARK 465 LEU L -56 REMARK 465 LYS L -55 REMARK 465 ALA L -54 REMARK 465 SER L -53 REMARK 465 ASP L -52 REMARK 465 THR L -51 REMARK 465 ALA L -50 REMARK 465 MET L -49 REMARK 465 TYR L -48 REMARK 465 TYR L -47 REMARK 465 CYS L -46 REMARK 465 ALA L -45 REMARK 465 ARG L -44 REMARK 465 HIS L -43 REMARK 465 LEU L -42 REMARK 465 ARG L -41 REMARK 465 GLY L -40 REMARK 465 LEU L -39 REMARK 465 ARG L -38 REMARK 465 LEU L -37 REMARK 465 GLY L -36 REMARK 465 GLU L -35 REMARK 465 LEU L -34 REMARK 465 PHE L -33 REMARK 465 PRO L -32 REMARK 465 PHE L -31 REMARK 465 ASP L -30 REMARK 465 TYR L -29 REMARK 465 TRP L -28 REMARK 465 GLY L -27 REMARK 465 GLN L -26 REMARK 465 GLY L -25 REMARK 465 THR L -24 REMARK 465 LEU L -23 REMARK 465 VAL L -22 REMARK 465 THR L -21 REMARK 465 VAL L -20 REMARK 465 SER L -19 REMARK 465 SER L -18 REMARK 465 GLY L -17 REMARK 465 THR L -16 REMARK 465 GLY L -15 REMARK 465 GLY L -14 REMARK 465 SER L -13 REMARK 465 GLY L -12 REMARK 465 GLY L -11 REMARK 465 GLY L -10 REMARK 465 GLY L -9 REMARK 465 SER L -8 REMARK 465 GLY L -7 REMARK 465 GLY L -6 REMARK 465 GLY L -5 REMARK 465 GLY L -4 REMARK 465 SER L -3 REMARK 465 GLY L -2 REMARK 465 GLY L -1 REMARK 465 GLY L 0 REMARK 465 LYS L 107 REMARK 465 ASP L 108 REMARK 465 ASP L 109 REMARK 465 ASP L 110 REMARK 465 ASP L 111 REMARK 465 LYS L 112 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 LEU A 103 173.71 66.79 REMARK 500 LEU A 108 47.07 -87.40 REMARK 500 ASN B 468 17.02 84.65 REMARK 500 THR B 483 -42.19 -134.35 REMARK 500 ASN B 490 62.73 -164.88 REMARK 500 THR B 586 45.36 -78.67 REMARK 500 PHE L 30 -122.08 51.61 REMARK 500 ALA L 51 -41.99 69.18 REMARK 500 ALA L 84 171.27 178.35 REMARK 500 REMARK 500 REMARK: NULL DBREF 8PMY A 1 254 PDB 8PMY 8PMY 1 254 DBREF1 8PMY B 456 660 UNP A0A6C0PR31_HEV DBREF2 8PMY B A0A6C0PR31 44 248 DBREF 8PMY L -141 112 PDB 8PMY 8PMY -141 112 SEQADV 8PMY GLY B 450 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PMY ASP B 451 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PMY ASP B 452 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PMY ASP B 453 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PMY ASP B 454 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PMY LYS B 455 UNP A0A6C0PR3 EXPRESSION TAG SEQADV 8PMY PHE B 500 UNP A0A6C0PR3 LEU 88 CONFLICT SEQRES 1 A 254 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 A 254 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY SER GLY SEQRES 3 A 254 TYR ASP PHE ALA ASN TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4 A 254 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5 A 254 PRO ARG ASP SER ASP ILE ARG TYR SER PRO SER PHE GLN SEQRES 6 A 254 GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE SER THR SEQRES 7 A 254 ALA TYR LEU GLN LEU SER SER LEU LYS ALA SER ASP THR SEQRES 8 A 254 ALA MET TYR TYR CYS ALA ARG HIS LEU ARG GLY LEU ARG SEQRES 9 A 254 LEU GLY GLU LEU PHE PRO PHE ASP TYR TRP GLY GLN GLY SEQRES 10 A 254 THR LEU VAL THR VAL SER SER GLY THR GLY GLY SER GLY SEQRES 11 A 254 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY ALA SEQRES 12 A 254 ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SER SEQRES 13 A 254 VAL GLY ASP SER VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 14 A 254 ASP ILE PHE SER TYR LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 15 A 254 GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER THR SEQRES 16 A 254 LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 17 A 254 SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN SEQRES 18 A 254 PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN LEU ASN SEQRES 19 A 254 ARG TYR PRO PHE ALA PHE GLY PRO GLY THR LYS VAL ASP SEQRES 20 A 254 ILE LYS ASP ASP ASP ASP LYS SEQRES 1 B 211 GLY ASP ASP ASP ASP LYS PRO ALA PRO SER ARG PRO PHE SEQRES 2 B 211 SER VAL LEU ARG ALA ASN ASP VAL LEU TRP LEU SER LEU SEQRES 3 B 211 THR ALA ALA GLU TYR ASP GLN THR THR TYR GLY SER SER SEQRES 4 B 211 THR ASN PRO MET TYR VAL SER ASP THR VAL THR PHE VAL SEQRES 5 B 211 ASN VAL ALA THR GLY ALA GLN ALA VAL ALA ARG SER LEU SEQRES 6 B 211 ASP TRP SER LYS VAL THR LEU ASP GLY ARG PRO LEU THR SEQRES 7 B 211 THR ILE GLN GLN TYR SER LYS THR PHE TYR VAL LEU PRO SEQRES 8 B 211 LEU ARG GLY LYS LEU SER PHE TRP GLU ALA GLY THR THR SEQRES 9 B 211 LYS ALA GLY TYR PRO TYR ASN TYR ASN THR THR ALA SER SEQRES 10 B 211 ASP GLN ILE LEU ILE GLU ASN ALA ALA GLY HIS ARG VAL SEQRES 11 B 211 ALA ILE SER THR TYR THR THR SER LEU GLY ALA GLY PRO SEQRES 12 B 211 THR SER ILE SER ALA VAL GLY VAL LEU ALA PRO HIS SER SEQRES 13 B 211 ALA LEU ALA VAL LEU GLU ASP THR THR ASP TYR PRO ALA SEQRES 14 B 211 ARG ALA HIS THR PHE ASP ASP PHE CYS PRO GLU CYS ARG SEQRES 15 B 211 THR LEU GLY LEU GLN GLY CYS ALA PHE GLN SER THR ILE SEQRES 16 B 211 ALA GLU LEU GLN ARG LEU LYS MET LYS VAL GLY LYS THR SEQRES 17 B 211 ARG GLU SER SEQRES 1 L 254 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 L 254 PRO GLY GLU SER LEU ARG ILE SER CYS LYS GLY SER GLY SEQRES 3 L 254 TYR ASP PHE ALA ASN TYR TRP ILE GLY TRP VAL ARG GLN SEQRES 4 L 254 MET PRO GLY LYS GLY LEU GLU TRP MET GLY ILE ILE TYR SEQRES 5 L 254 PRO ARG ASP SER ASP ILE ARG TYR SER PRO SER PHE GLN SEQRES 6 L 254 GLY GLN VAL THR ILE SER ALA ASP LYS SER ILE SER THR SEQRES 7 L 254 ALA TYR LEU GLN LEU SER SER LEU LYS ALA SER ASP THR SEQRES 8 L 254 ALA MET TYR TYR CYS ALA ARG HIS LEU ARG GLY LEU ARG SEQRES 9 L 254 LEU GLY GLU LEU PHE PRO PHE ASP TYR TRP GLY GLN GLY SEQRES 10 L 254 THR LEU VAL THR VAL SER SER GLY THR GLY GLY SER GLY SEQRES 11 L 254 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY ALA SEQRES 12 L 254 ILE GLN LEU THR GLN SER PRO SER SER LEU SER ALA SER SEQRES 13 L 254 VAL GLY ASP SER VAL THR ILE THR CYS ARG ALA SER GLN SEQRES 14 L 254 ASP ILE PHE SER TYR LEU ALA TRP TYR GLN GLN LYS PRO SEQRES 15 L 254 GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER THR SEQRES 16 L 254 LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER GLY SEQRES 17 L 254 SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU GLN SEQRES 18 L 254 PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN LEU ASN SEQRES 19 L 254 ARG TYR PRO PHE ALA PHE GLY PRO GLY THR LYS VAL ASP SEQRES 20 L 254 ILE LYS ASP ASP ASP ASP LYS HET ZN A 301 1 HET ZN B 701 1 HET ZN B 702 1 HETNAM ZN ZINC ION FORMUL 4 ZN 3(ZN 2+) FORMUL 7 HOH *107(H2 O) HELIX 1 AA1 ASP A 28 TYR A 32 5 5 HELIX 2 AA2 LYS A 87 THR A 91 5 5 HELIX 3 AA3 LEU A 103 GLU A 107 5 5 HELIX 4 AA4 GLN L 79 PHE L 83 5 5 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 78 LEU A 83 -1 O LEU A 81 N ILE A 20 SHEET 4 AA1 4 VAL A 68 ASP A 73 -1 N ASP A 73 O THR A 78 SHEET 1 AA2 7 GLU A 10 LYS A 12 0 SHEET 2 AA2 7 ILE A 34 GLN A 39 0 SHEET 3 AA2 7 GLU A 46 TYR A 52 -1 O MET A 48 N TRP A 36 SHEET 4 AA2 7 ASP A 57 TYR A 60 -1 O ARG A 59 N ILE A 50 SHEET 5 AA2 7 ALA A 92 HIS A 99 -1 O TYR A 95 N VAL A 37 SHEET 6 AA2 7 PHE A 111 TRP A 114 -1 O TYR A 113 N ARG A 98 SHEET 7 AA2 7 THR A 118 VAL A 122 -1 O THR A 118 N TYR A 94 SHEET 1 AA3 3 VAL B 464 LEU B 465 0 SHEET 2 AA3 3 THR B 520 LEU B 521 1 O THR B 520 N LEU B 465 SHEET 3 AA3 3 ARG B 524 PRO B 525 -1 O ARG B 524 N LEU B 521 SHEET 1 AA410 VAL B 470 ASP B 481 0 SHEET 2 AA410 MET B 492 SER B 495 -1 O VAL B 494 N GLU B 479 SHEET 3 AA410 THR B 497 ASN B 502 -1 O THR B 497 N THR B 476 SHEET 4 AA410 GLN B 508 VAL B 510 -1 O ALA B 509 N PHE B 500 SHEET 5 AA410 THR B 527 GLN B 531 0 SHEET 6 AA410 LYS B 534 GLU B 549 -1 O VAL B 538 N THR B 527 SHEET 7 AA410 ALA B 555 GLY B 556 -1 O GLY B 556 N PHE B 547 SHEET 8 AA410 GLN B 568 GLU B 572 -1 O ILE B 571 N TYR B 537 SHEET 9 AA410 VAL B 579 SER B 582 -1 O ALA B 580 N LEU B 570 SHEET 10 AA410 THR B 593 LEU B 601 -1 O SER B 596 N TRP B 548 SHEET 1 AA5 4 LEU L 4 SER L 7 0 SHEET 2 AA5 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA5 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AA5 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AA6 6 SER L 10 SER L 12 0 SHEET 2 AA6 6 THR L 102 ASP L 105 1 O ASP L 105 N LEU L 11 SHEET 3 AA6 6 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA6 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA6 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA6 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.06 LINK OE1 GLU A 16 ZN ZN A 301 1555 1555 2.13 LINK NE2 HIS B 577 ZN ZN B 701 1555 1555 2.19 CISPEP 1 GLY B 591 PRO B 592 0 0.37 CISPEP 2 SER L 7 PRO L 8 0 -7.58 CISPEP 3 TYR L 94 PRO L 95 0 -6.81 CRYST1 56.190 122.950 158.670 90.00 90.00 90.00 C 2 2 21 16 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 0.017797 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008133 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006302 0.00000