HEADER IMMUNE SYSTEM 26-JAN-24 8VTD TITLE CO-STRUCTURE OF THE FAB OF THE ANTI-TIGIT VIBOSTOLIMAB ANTIBODY WITH TITLE 2 ITS ANTIGEN COMPND MOL_ID: 1; COMPND 2 MOLECULE: VIBOSTOLIMAB FAB LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VIBOSTOLIMAB FAB HEAVY CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: T-CELL IMMUNORECEPTOR WITH IG AND ITIM DOMAINS; COMPND 11 CHAIN: C; COMPND 12 SYNONYM: V-SET AND IMMUNOGLOBULIN DOMAIN-CONTAINING PROTEIN 9,V-SET COMPND 13 AND TRANSMEMBRANE DOMAIN-CONTAINING PROTEIN 3; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE 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: EXPI293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: TIGIT, VSIG9, VSTM3; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY TIGIT IMMUNOTHERAPY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.FISCHMANN REVDAT 1 02-JUL-25 8VTD 0 JRNL AUTH T.O.FISCHMANN,D.MALASHOCK,H.WANG,J.GREIN,S.BAHMANJAH,D.BAN, JRNL AUTH 2 E.CHIEN,M.HSIEH,T.MAYHOOD,J.YUAN,M.BEAUMONT,J.BAKER, JRNL AUTH 3 M.A.MCCOY,D.WILSON,S.M.G.WILLIAMS,W.BLUMENSCHEIN, JRNL AUTH 4 L.FAYADAT-DILMAN,W.SEGHEZZI,T.KEENAN,J.-H.HAN JRNL TITL PHARMACOLOGICAL AND STRUCTURAL CHARACTERIZATION OF JRNL TITL 2 VIBOSTOLIMAB, A NOVEL ANTI-HUMAN TIGIT BLOCKING ANTIBODY FOR JRNL TITL 3 CANCER IMMUNOTHERAPY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.23 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.7 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) : 1.23 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.14 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 67.8 REMARK 3 NUMBER OF REFLECTIONS : 117862 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) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 5944 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 : 50 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.23 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.32 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 6.95 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2358 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2139 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2226 REMARK 3 BIN R VALUE (WORKING SET) : 0.2136 REMARK 3 BIN FREE R VALUE : 0.2186 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.60 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 132 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 : 4106 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 12 REMARK 3 SOLVENT ATOMS : 588 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.10650 REMARK 3 B22 (A**2) : 0.27590 REMARK 3 B33 (A**2) : -0.38240 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.28830 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.170 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.059 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.059 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.062 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.057 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 : 0.959 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 8298 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 14956 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1756 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 1332 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 8298 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 568 ; 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 : 9075 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.11 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.82 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.14 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|1 - A|106 } REMARK 3 ORIGIN FOR THE GROUP (A): 2.8897 -26.9993 -15.9196 REMARK 3 T TENSOR REMARK 3 T11: -0.0315 T22: -0.0595 REMARK 3 T33: -0.0139 T12: 0.0124 REMARK 3 T13: -0.0062 T23: 0.0101 REMARK 3 L TENSOR REMARK 3 L11: 0.8418 L22: 0.9242 REMARK 3 L33: 1.1555 L12: -0.1903 REMARK 3 L13: 0.4259 L23: 0.2808 REMARK 3 S TENSOR REMARK 3 S11: 0.0714 S12: 0.0216 S13: -0.2186 REMARK 3 S21: -0.0208 S22: -0.0222 S23: 0.0556 REMARK 3 S31: 0.2173 S32: 0.0150 S33: -0.0492 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|107 - A|214 } REMARK 3 ORIGIN FOR THE GROUP (A): 1.4994 -33.9665 -51.6300 REMARK 3 T TENSOR REMARK 3 T11: -0.0556 T22: -0.0510 REMARK 3 T33: -0.0491 T12: 0.0166 REMARK 3 T13: -0.0030 T23: -0.0020 REMARK 3 L TENSOR REMARK 3 L11: 0.7936 L22: 1.2746 REMARK 3 L33: 1.8521 L12: -0.4275 REMARK 3 L13: -0.2158 L23: 0.2072 REMARK 3 S TENSOR REMARK 3 S11: 0.0827 S12: 0.0948 S13: 0.0107 REMARK 3 S21: -0.1020 S22: -0.0413 S23: -0.2025 REMARK 3 S31: 0.0315 S32: 0.2241 S33: -0.0414 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { B|1 - B|116 } REMARK 3 ORIGIN FOR THE GROUP (A): -7.2650 -7.9974 -21.6378 REMARK 3 T TENSOR REMARK 3 T11: -0.0276 T22: -0.0287 REMARK 3 T33: -0.0292 T12: 0.0060 REMARK 3 T13: -0.0097 T23: 0.0060 REMARK 3 L TENSOR REMARK 3 L11: 0.6104 L22: 0.7208 REMARK 3 L33: 0.9540 L12: 0.0646 REMARK 3 L13: 0.1790 L23: -0.0005 REMARK 3 S TENSOR REMARK 3 S11: -0.0179 S12: -0.0096 S13: -0.0019 REMARK 3 S21: -0.0876 S22: -0.0006 S23: 0.0661 REMARK 3 S31: -0.0491 S32: 0.0008 S33: 0.0185 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { B|117 - B|217 } REMARK 3 ORIGIN FOR THE GROUP (A): -13.3062 -28.0328 -48.6985 REMARK 3 T TENSOR REMARK 3 T11: -0.0138 T22: -0.0311 REMARK 3 T33: -0.0351 T12: 0.0045 REMARK 3 T13: -0.0160 T23: -0.0060 REMARK 3 L TENSOR REMARK 3 L11: 0.0695 L22: 2.9774 REMARK 3 L33: 0.5612 L12: 0.0393 REMARK 3 L13: -0.0506 L23: 0.6771 REMARK 3 S TENSOR REMARK 3 S11: 0.0319 S12: 0.0052 S13: -0.0506 REMARK 3 S21: -0.0786 S22: -0.0891 S23: 0.1374 REMARK 3 S31: -0.0630 S32: -0.0485 S33: 0.0572 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { C|* } REMARK 3 ORIGIN FOR THE GROUP (A): 1.4446 -7.0865 7.2254 REMARK 3 T TENSOR REMARK 3 T11: -0.0496 T22: 0.0070 REMARK 3 T33: -0.0746 T12: 0.0039 REMARK 3 T13: 0.0180 T23: 0.0140 REMARK 3 L TENSOR REMARK 3 L11: 0.6715 L22: 1.0575 REMARK 3 L33: 2.0140 L12: -0.5489 REMARK 3 L13: -0.5274 L23: 0.4656 REMARK 3 S TENSOR REMARK 3 S11: -0.0458 S12: -0.1337 S13: 0.0194 REMARK 3 S21: 0.1522 S22: 0.0849 S23: 0.0570 REMARK 3 S31: 0.0080 S32: 0.0082 S33: -0.0391 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8VTD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1000281103. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-NOV-18 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) : 1.000 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 20180409 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117862 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.230 REMARK 200 RESOLUTION RANGE LOW (A) : 42.144 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 67.7 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.04500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.23 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.36 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.65200 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 2.8.2 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.65 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% W/V PEG 20K, VAPOR DIFFUSION, REMARK 280 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 52.99800 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5700 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23970 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 C 22 REMARK 465 MET C 23 REMARK 465 THR C 24 REMARK 465 SER C 130 REMARK 465 VAL C 131 REMARK 465 ALA C 132 REMARK 465 GLU C 133 REMARK 465 HIS C 134 REMARK 465 GLY C 135 REMARK 465 ALA C 136 REMARK 465 ARG C 137 REMARK 465 HIS C 138 REMARK 465 HIS C 139 REMARK 465 HIS C 140 REMARK 465 HIS C 141 REMARK 465 HIS C 142 REMARK 465 HIS C 143 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 SER B 221 C O CB OG REMARK 470 SER C 129 C O CB OG 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 TYR A 30 -121.84 56.12 REMARK 500 ALA A 51 -34.60 68.65 REMARK 500 TRP B 104 56.91 -90.54 REMARK 500 GLN C 62 -124.05 56.20 REMARK 500 ASP C 115 26.73 -154.32 REMARK 500 REMARK 500 REMARK: NULL DBREF 8VTD A 1 214 PDB 8VTD 8VTD 1 214 DBREF 8VTD B 1 221 PDB 8VTD 8VTD 1 221 DBREF 8VTD C 22 137 UNP Q495A1 TIGIT_HUMAN 22 137 SEQADV 8VTD HIS C 138 UNP Q495A1 EXPRESSION TAG SEQADV 8VTD HIS C 139 UNP Q495A1 EXPRESSION TAG SEQADV 8VTD HIS C 140 UNP Q495A1 EXPRESSION TAG SEQADV 8VTD HIS C 141 UNP Q495A1 EXPRESSION TAG SEQADV 8VTD HIS C 142 UNP Q495A1 EXPRESSION TAG SEQADV 8VTD HIS C 143 UNP Q495A1 EXPRESSION TAG SEQRES 1 A 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 A 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 A 214 GLU HIS ILE TYR SER TYR LEU SER TRP TYR GLN GLN LYS SEQRES 4 A 214 PRO GLY LYS VAL PRO LYS LEU LEU ILE TYR ASN ALA LYS SEQRES 5 A 214 THR LEU ALA GLU GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 A 214 GLN PRO GLU ASP VAL ALA THR TYR TYR CYS GLN HIS HIS SEQRES 8 A 214 PHE GLY SER PRO LEU THR PHE GLY GLN GLY THR ARG LEU SEQRES 9 A 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 A 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 221 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 B 221 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 B 221 TYR THR PHE SER SER TYR VAL MET HIS TRP VAL ARG GLN SEQRES 4 B 221 ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASP SEQRES 5 B 221 PRO TYR ASN ASP GLY ALA LYS TYR ALA GLN LYS PHE GLN SEQRES 6 B 221 GLY ARG VAL THR LEU THR SER ASP LYS SER THR SER THR SEQRES 7 B 221 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 B 221 ALA VAL TYR TYR CYS ALA ARG GLY GLY PRO TYR GLY TRP SEQRES 9 B 221 TYR PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SEQRES 10 B 221 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 B 221 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 B 221 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 B 221 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 B 221 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 B 221 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 B 221 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 B 221 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 1 C 122 MET MET THR GLY THR ILE GLU THR THR GLY ASN ILE SER SEQRES 2 C 122 ALA GLU LYS GLY GLY SER ILE ILE LEU GLN CYS HIS LEU SEQRES 3 C 122 SER SER THR THR ALA GLN VAL THR GLN VAL ASN TRP GLU SEQRES 4 C 122 GLN GLN ASP GLN LEU LEU ALA ILE CYS ASN ALA ASP LEU SEQRES 5 C 122 GLY TRP HIS ILE SER PRO SER PHE LYS ASP ARG VAL ALA SEQRES 6 C 122 PRO GLY PRO GLY LEU GLY LEU THR LEU GLN SER LEU THR SEQRES 7 C 122 VAL ASN ASP THR GLY GLU TYR PHE CYS ILE TYR HIS THR SEQRES 8 C 122 TYR PRO ASP GLY THR TYR THR GLY ARG ILE PHE LEU GLU SEQRES 9 C 122 VAL LEU GLU SER SER VAL ALA GLU HIS GLY ALA ARG HIS SEQRES 10 C 122 HIS HIS HIS HIS HIS HET GOL A9901 6 HET GOL A9902 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 GOL 2(C3 H8 O3) FORMUL 6 HOH *588(H2 O) HELIX 1 AA1 GLN A 79 VAL A 83 5 5 HELIX 2 AA2 SER A 121 SER A 127 1 7 HELIX 3 AA3 LYS A 183 LYS A 188 1 6 HELIX 4 AA4 THR B 28 TYR B 32 5 5 HELIX 5 AA5 LYS B 74 THR B 76 5 3 HELIX 6 AA6 ARG B 87 THR B 91 5 5 HELIX 7 AA7 SER B 162 ALA B 164 5 3 HELIX 8 AA8 SER B 193 LEU B 195 5 3 HELIX 9 AA9 LYS B 207 ASN B 210 5 4 HELIX 10 AB1 PRO C 79 LYS C 82 5 4 HELIX 11 AB2 THR C 99 THR C 103 5 5 SHEET 1 AA1 4 MET A 4 SER A 7 0 SHEET 2 AA1 4 VAL A 19 ALA A 25 -1 O THR A 22 N SER A 7 SHEET 3 AA1 4 ASP A 70 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 4 AA1 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74 SHEET 1 AA2 6 SER A 10 ALA A 13 0 SHEET 2 AA2 6 THR A 102 ILE A 106 1 O ARG A 103 N LEU A 11 SHEET 3 AA2 6 THR A 85 HIS A 90 -1 N TYR A 86 O THR A 102 SHEET 4 AA2 6 LEU A 33 GLN A 38 -1 N GLN A 38 O THR A 85 SHEET 5 AA2 6 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 AA2 6 THR A 53 LEU A 54 -1 O THR A 53 N TYR A 49 SHEET 1 AA3 4 SER A 114 PHE A 118 0 SHEET 2 AA3 4 THR A 129 PHE A 139 -1 O ASN A 137 N SER A 114 SHEET 3 AA3 4 TYR A 173 SER A 182 -1 O LEU A 181 N ALA A 130 SHEET 4 AA3 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 AA4 4 ALA A 153 LEU A 154 0 SHEET 2 AA4 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 AA4 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 4 AA4 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196 SHEET 1 AA5 4 GLN B 3 GLN B 6 0 SHEET 2 AA5 4 VAL B 18 SER B 25 -1 O LYS B 23 N VAL B 5 SHEET 3 AA5 4 THR B 78 LEU B 83 -1 O ALA B 79 N CYS B 22 SHEET 4 AA5 4 VAL B 68 ASP B 73 -1 N THR B 69 O GLU B 82 SHEET 1 AA6 6 GLU B 10 LYS B 12 0 SHEET 2 AA6 6 THR B 113 VAL B 117 1 O THR B 116 N LYS B 12 SHEET 3 AA6 6 ALA B 92 GLY B 99 -1 N TYR B 94 O THR B 113 SHEET 4 AA6 6 MET B 34 GLN B 39 -1 N VAL B 37 O TYR B 95 SHEET 5 AA6 6 GLU B 46 ASP B 52 -1 O ILE B 48 N TRP B 36 SHEET 6 AA6 6 GLY B 57 TYR B 60 -1 O GLY B 57 N ASP B 52 SHEET 1 AA7 4 GLU B 10 LYS B 12 0 SHEET 2 AA7 4 THR B 113 VAL B 117 1 O THR B 116 N LYS B 12 SHEET 3 AA7 4 ALA B 92 GLY B 99 -1 N TYR B 94 O THR B 113 SHEET 4 AA7 4 PHE B 106 TRP B 109 -1 O VAL B 108 N ARG B 98 SHEET 1 AA8 4 SER B 126 LEU B 130 0 SHEET 2 AA8 4 THR B 141 TYR B 151 -1 O LEU B 147 N PHE B 128 SHEET 3 AA8 4 TYR B 182 PRO B 191 -1 O LEU B 184 N VAL B 148 SHEET 4 AA8 4 VAL B 169 THR B 171 -1 N HIS B 170 O VAL B 187 SHEET 1 AA9 4 THR B 137 SER B 138 0 SHEET 2 AA9 4 THR B 141 TYR B 151 -1 O THR B 141 N SER B 138 SHEET 3 AA9 4 TYR B 182 PRO B 191 -1 O LEU B 184 N VAL B 148 SHEET 4 AA9 4 VAL B 175 LEU B 176 -1 N VAL B 175 O SER B 183 SHEET 1 AB1 3 THR B 157 TRP B 160 0 SHEET 2 AB1 3 ILE B 201 HIS B 206 -1 O ASN B 203 N SER B 159 SHEET 3 AB1 3 THR B 211 LYS B 216 -1 O VAL B 213 N VAL B 204 SHEET 1 AB2 2 THR C 26 THR C 29 0 SHEET 2 AB2 2 CYS C 45 SER C 48 -1 O SER C 48 N THR C 26 SHEET 1 AB3 6 ASN C 32 GLU C 36 0 SHEET 2 AB3 6 GLY C 116 LEU C 127 1 O LEU C 127 N ALA C 35 SHEET 3 AB3 6 GLY C 104 THR C 112 -1 N TYR C 110 O TYR C 118 SHEET 4 AB3 6 VAL C 54 GLN C 61 -1 N GLN C 56 O HIS C 111 SHEET 5 AB3 6 GLN C 64 ASN C 70 -1 O CYS C 69 N VAL C 57 SHEET 6 AB3 6 GLY C 74 ILE C 77 -1 O GLY C 74 N ASN C 70 SHEET 1 AB4 3 ILE C 41 LEU C 43 0 SHEET 2 AB4 3 LEU C 93 LEU C 95 -1 O LEU C 93 N LEU C 43 SHEET 3 AB4 3 VAL C 85 PRO C 87 -1 N ALA C 86 O THR C 94 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.08 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.01 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.06 SSBOND 4 CYS B 146 CYS B 202 1555 1555 2.04 SSBOND 5 CYS C 45 CYS C 108 1555 1555 2.04 CISPEP 1 SER A 7 PRO A 8 0 -6.31 CISPEP 2 SER A 94 PRO A 95 0 1.85 CISPEP 3 TYR A 140 PRO A 141 0 3.41 CISPEP 4 PHE B 152 PRO B 153 0 -6.37 CISPEP 5 GLU B 154 PRO B 155 0 2.92 CISPEP 6 GLY C 88 PRO C 89 0 3.87 CISPEP 7 TYR C 113 PRO C 114 0 0.86 CRYST1 41.775 105.996 71.758 90.00 104.40 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 0.023938 0.000000 0.006146 0.00000 SCALE2 0.000000 0.009434 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014388 0.00000