HEADER IMMUNE SYSTEM 15-DEC-10 3Q0H
TITLE STRUCTURE OF T-CELL IMMUNORECEPTOR WITH IMMUNOGLOBULIN AND ITIM
TITLE 2 DOMAINS (TIGIT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T CELL IMMUNORECEPTOR WITH IG AND ITIM DOMAINS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: IG-LIKE V-TYPE DOMAIN RESIDUES 22-137;
COMPND 5 SYNONYM: V-SET AND IMMUNOGLOBULIN DOMAIN-CONTAINING PROTEIN 9, V-SET
COMPND 6 AND TRANSMEMBRANE DOMAIN-CONTAINING PROTEIN 3;
COMPND 7 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: TIGIT, VSIG9, VSTM3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS IMMUNE RECEPTOR, ADHESION, STRUCTURAL GENOMICS, NEW YORK STRUCTURAL
KEYWDS 2 GENOMICS RESEARCH CONSORTIUM, NYSGRC, PSI-BIOLOGY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR U.A.RAMAGOPAL,H.GUO,D.SAMANTA,S.G.NATHENSON,S.C.ALMO,NEW YORK
AUTHOR 2 STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NYSGRC)
REVDAT 4 13-SEP-23 3Q0H 1 SEQADV
REVDAT 3 08-NOV-17 3Q0H 1 REMARK
REVDAT 2 18-MAY-11 3Q0H 1 REMARK
REVDAT 1 16-FEB-11 3Q0H 0
JRNL AUTH U.A.RAMAGOPAL,H.GUO,D.SAMANTA,S.G.NATHENSON,S.C.ALMO
JRNL TITL STRUCTURE OF T-CELL IMMUNORECEPTOR WITH IMMUNOGLOBULIN AND
JRNL TITL 2 ITIM DOMAINS (TIGIT)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 27504
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1376
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1675
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1648
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.115
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.222
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1812 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2495 ; 1.678 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 242 ; 7.027 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 78 ;39.235 ;25.641
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 289 ;15.661 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;15.852 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 287 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1407 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1149 ; 0.939 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1883 ; 1.782 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 663 ; 2.799 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 612 ; 4.412 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8080 -13.6700 29.8070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0426 T22: 0.0666
REMARK 3 T33: 0.1015 T12: 0.0165
REMARK 3 T13: -0.0580 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 1.3745 L22: 2.3888
REMARK 3 L33: 1.0475 L12: -0.3686
REMARK 3 L13: -0.2802 L23: -0.7259
REMARK 3 S TENSOR
REMARK 3 S11: -0.0642 S12: -0.0097 S13: 0.0614
REMARK 3 S21: 0.1596 S22: 0.0046 S23: -0.1984
REMARK 3 S31: -0.0148 S32: 0.0352 S33: 0.0595
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6920 6.4450 19.5710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0658 T22: 0.0644
REMARK 3 T33: 0.0502 T12: 0.0152
REMARK 3 T13: 0.0325 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.5741 L22: 1.6573
REMARK 3 L33: 2.2492 L12: 0.5091
REMARK 3 L13: 0.4970 L23: -0.6509
REMARK 3 S TENSOR
REMARK 3 S11: 0.0047 S12: -0.0808 S13: -0.0448
REMARK 3 S21: -0.0503 S22: 0.0085 S23: 0.0143
REMARK 3 S31: 0.0421 S32: 0.0539 S33: -0.0132
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES :
REMARK 3 WITH TLS ADDED
REMARK 3
REMARK 3 UNKNOWN DENSITY NEAR CYS48: NOT MODELED
REMARK 4
REMARK 4 3Q0H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000063039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27916
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.53500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1IKF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M AMMONIUM SULFATE, 0.1M MES PH
REMARK 280 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 37.33550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 130
REMARK 465 VAL A 131
REMARK 465 ALA A 132
REMARK 465 GLU A 133
REMARK 465 HIS A 134
REMARK 465 GLY A 135
REMARK 465 ALA A 136
REMARK 465 ARG A 137
REMARK 465 MET B 21
REMARK 465 MET B 22
REMARK 465 MET B 23
REMARK 465 THR B 24
REMARK 465 ALA B 132
REMARK 465 GLU B 133
REMARK 465 HIS B 134
REMARK 465 GLY B 135
REMARK 465 ALA B 136
REMARK 465 ARG B 137
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 69 CB CYS A 69 SG 0.109
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 69 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 63 43.43 31.78
REMARK 500 ASP A 63 44.78 31.78
REMARK 500 ARG B 84 31.38 -140.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGRC-006165 RELATED DB: TARGETDB
DBREF 3Q0H A 22 137 UNP Q495A1 TIGIT_HUMAN 22 137
DBREF 3Q0H B 22 137 UNP Q495A1 TIGIT_HUMAN 22 137
SEQADV 3Q0H MET A 21 UNP Q495A1 EXPRESSION TAG
SEQADV 3Q0H MET B 21 UNP Q495A1 EXPRESSION TAG
SEQRES 1 A 117 MET MET MET THR GLY THR ILE GLU THR THR GLY ASN ILE
SEQRES 2 A 117 SER ALA GLU LYS GLY GLY SER ILE ILE LEU GLN CYS HIS
SEQRES 3 A 117 LEU SER SER THR THR ALA GLN VAL THR GLN VAL ASN TRP
SEQRES 4 A 117 GLU GLN GLN ASP GLN LEU LEU ALA ILE CYS ASN ALA ASP
SEQRES 5 A 117 LEU GLY TRP HIS ILE SER PRO SER PHE LYS ASP ARG VAL
SEQRES 6 A 117 ALA PRO GLY PRO GLY LEU GLY LEU THR LEU GLN SER LEU
SEQRES 7 A 117 THR VAL ASN ASP THR GLY GLU TYR PHE CYS ILE TYR HIS
SEQRES 8 A 117 THR TYR PRO ASP GLY THR TYR THR GLY ARG ILE PHE LEU
SEQRES 9 A 117 GLU VAL LEU GLU SER SER VAL ALA GLU HIS GLY ALA ARG
SEQRES 1 B 117 MET MET MET THR GLY THR ILE GLU THR THR GLY ASN ILE
SEQRES 2 B 117 SER ALA GLU LYS GLY GLY SER ILE ILE LEU GLN CYS HIS
SEQRES 3 B 117 LEU SER SER THR THR ALA GLN VAL THR GLN VAL ASN TRP
SEQRES 4 B 117 GLU GLN GLN ASP GLN LEU LEU ALA ILE CYS ASN ALA ASP
SEQRES 5 B 117 LEU GLY TRP HIS ILE SER PRO SER PHE LYS ASP ARG VAL
SEQRES 6 B 117 ALA PRO GLY PRO GLY LEU GLY LEU THR LEU GLN SER LEU
SEQRES 7 B 117 THR VAL ASN ASP THR GLY GLU TYR PHE CYS ILE TYR HIS
SEQRES 8 B 117 THR TYR PRO ASP GLY THR TYR THR GLY ARG ILE PHE LEU
SEQRES 9 B 117 GLU VAL LEU GLU SER SER VAL ALA GLU HIS GLY ALA ARG
FORMUL 3 HOH *120(H2 O)
HELIX 1 1 SER A 78 LYS A 82 5 5
HELIX 2 2 THR A 99 THR A 103 5 5
HELIX 3 3 PHE B 81 ASP B 83 5 3
HELIX 4 4 THR B 99 THR B 103 5 5
SHEET 1 A 2 THR A 26 THR A 29 0
SHEET 2 A 2 CYS A 45 SER A 48 -1 O HIS A 46 N GLU A 28
SHEET 1 B 6 ILE A 33 GLU A 36 0
SHEET 2 B 6 TYR A 118 LEU A 127 1 O GLU A 125 N ALA A 35
SHEET 3 B 6 GLY A 104 TYR A 113 -1 N TYR A 110 O TYR A 118
SHEET 4 B 6 GLN A 53 GLN A 61 -1 N GLU A 60 O PHE A 107
SHEET 5 B 6 GLN A 64 ASN A 70 -1 O LEU A 66 N TRP A 59
SHEET 6 B 6 GLY A 74 HIS A 76 -1 O HIS A 76 N ILE A 68
SHEET 1 C 3 ILE A 41 LEU A 43 0
SHEET 2 C 3 LEU A 93 LEU A 95 -1 O LEU A 93 N LEU A 43
SHEET 3 C 3 VAL A 85 PRO A 87 -1 N ALA A 86 O THR A 94
SHEET 1 D 2 THR B 26 THR B 29 0
SHEET 2 D 2 CYS B 45 SER B 48 -1 O HIS B 46 N GLU B 28
SHEET 1 E 6 ASN B 32 GLU B 36 0
SHEET 2 E 6 TYR B 118 LEU B 127 1 O LEU B 127 N ALA B 35
SHEET 3 E 6 GLY B 104 TYR B 113 -1 N TYR B 106 O ILE B 122
SHEET 4 E 6 GLN B 53 GLU B 60 -1 N ASN B 58 O ILE B 109
SHEET 5 E 6 LEU B 65 ASN B 70 -1 O LEU B 66 N TRP B 59
SHEET 6 E 6 GLY B 74 ILE B 77 -1 O HIS B 76 N ILE B 68
SHEET 1 F 3 ILE B 41 LEU B 43 0
SHEET 2 F 3 LEU B 93 LEU B 95 -1 O LEU B 93 N LEU B 43
SHEET 3 F 3 VAL B 85 PRO B 87 -1 N ALA B 86 O THR B 94
SSBOND 1 CYS A 45 CYS A 108 1555 1555 2.05
SSBOND 2 CYS B 45 CYS B 108 1555 1555 2.06
CISPEP 1 GLY A 88 PRO A 89 0 2.16
CISPEP 2 TYR A 113 PRO A 114 0 2.54
CISPEP 3 GLY B 88 PRO B 89 0 2.42
CISPEP 4 TYR B 113 PRO B 114 0 -1.38
CRYST1 39.951 74.671 43.346 90.00 92.39 90.00 P 1 21 1 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 0.025031 0.000000 0.001045 0.00000
SCALE2 0.000000 0.013392 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023090 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
