HEADER IMMUNE SYSTEM 19-MAY-18 6DHB
TITLE CRYSTAL STRUCTURE OF THE HUMAN TIM-3 WITH BOUND CALCIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATITIS A VIRUS CELLULAR RECEPTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 24-130;
COMPND 5 SYNONYM: HAVCR-2,T-CELL IMMUNOGLOBULIN AND MUCIN DOMAIN-CONTAINING
COMPND 6 PROTEIN 3,TIMD-3,T-CELL IMMUNOGLOBULIN MUCIN RECEPTOR 3,TIM-3,T-CELL
COMPND 7 MEMBRANE PROTEIN 3;
COMPND 8 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: HAVCR2, TIM3, TIMD3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS T CELL IMMUNOGLOBULIN MUCIN-3 IMMUNOLOGICAL TOLERANCE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.GANDHI,W.M.KIM,Y.H.HUANG,D.BONSOR,E.SUNDBERG,Z.-Y.SUN,G.A.PETSKO,
AUTHOR 2 V.KUCHROO,R.S.BLUMBERG
REVDAT 4 11-OCT-23 6DHB 1 REMARK
REVDAT 3 18-DEC-19 6DHB 1 REMARK
REVDAT 2 19-DEC-18 6DHB 1 JRNL
REVDAT 1 12-DEC-18 6DHB 0
JRNL AUTH A.K.GANDHI,W.M.KIM,Z.J.SUN,Y.H.HUANG,D.A.BONSOR,
JRNL AUTH 2 E.J.SUNDBERG,Y.KONDO,G.WAGNER,V.K.KUCHROO,G.PETSKO,
JRNL AUTH 3 R.S.BLUMBERG
JRNL TITL HIGH RESOLUTION X-RAY AND NMR STRUCTURAL STUDY OF HUMAN
JRNL TITL 2 T-CELL IMMUNOGLOBULIN AND MUCIN DOMAIN CONTAINING PROTEIN-3.
JRNL REF SCI REP V. 8 17512 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 30504845
JRNL DOI 10.1038/S41598-018-35754-0
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 10256
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 528
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) : 684
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.1390
REMARK 3 BIN FREE R VALUE SET COUNT : 36
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 856
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : -0.50000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.097
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.665
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 898 ; 0.023 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 839 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1217 ; 2.056 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1923 ; 1.092 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 107 ; 6.682 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 41 ;26.986 ;23.902
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 140 ;13.584 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;23.637 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 129 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1014 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 212 ; 0.002 ; 0.020
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): 431 ; 1.391 ; 1.054
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 430 ; 1.327 ; 1.049
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 537 ; 2.073 ; 1.574
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 538 ; 2.072 ; 1.582
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 467 ; 2.865 ; 1.394
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 467 ; 2.866 ; 1.394
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 681 ; 4.481 ; 1.933
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1034 ; 6.200 ; 9.804
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 998 ; 6.066 ; 9.368
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6DHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234599.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10879
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 43.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.1000
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 (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.08500
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5F71, 2OYP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, PEG, PH 8.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.15500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.86000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.53000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.86000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.15500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.53000
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: MONOMERIC
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 320 O HOH A 337 4545 2.12
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 ARG A 47 NE - CZ - NH1 ANGL. DEV. = -3.6 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 GLU A 40 -166.02 68.30
REMARK 500 ASP A 49 -149.57 -127.98
REMARK 500 ARG A 51 -21.98 -140.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 92 O
REMARK 620 2 GLY A 94 O 100.9
REMARK 620 3 ASN A 97 OD1 85.7 81.9
REMARK 620 4 ASP A 98 OD1 92.3 166.7 101.2
REMARK 620 5 BEZ A 202 O2 167.5 87.3 86.1 80.0
REMARK 620 6 HOH A 387 O 89.1 86.0 165.7 92.4 100.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204
DBREF 6DHB A 2 108 UNP Q8TDQ0 HAVR2_HUMAN 24 130
SEQADV 6DHB MET A 1 UNP Q8TDQ0 INITIATING METHIONINE
SEQRES 1 A 108 MET VAL GLU TYR ARG ALA GLU VAL GLY GLN ASN ALA TYR
SEQRES 2 A 108 LEU PRO CYS PHE TYR THR PRO ALA ALA PRO GLY ASN LEU
SEQRES 3 A 108 VAL PRO VAL CYS TRP GLY LYS GLY ALA CYS PRO VAL PHE
SEQRES 4 A 108 GLU CYS GLY ASN VAL VAL LEU ARG THR ASP GLU ARG ASP
SEQRES 5 A 108 VAL ASN TYR TRP THR SER ARG TYR TRP LEU ASN GLY ASP
SEQRES 6 A 108 PHE ARG LYS GLY ASP VAL SER LEU THR ILE GLU ASN VAL
SEQRES 7 A 108 THR LEU ALA ASP SER GLY ILE TYR CYS CYS ARG ILE GLN
SEQRES 8 A 108 ILE PRO GLY ILE MET ASN ASP GLU LYS PHE ASN LEU LYS
SEQRES 9 A 108 LEU VAL ILE LYS
HET CA A 201 1
HET BEZ A 202 9
HET EDO A 203 4
HET EDO A 204 4
HETNAM CA CALCIUM ION
HETNAM BEZ BENZOIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CA CA 2+
FORMUL 3 BEZ C7 H6 O2
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 6 HOH *100(H2 O)
HELIX 1 AA1 ASP A 65 GLY A 69 5 5
HELIX 2 AA2 THR A 79 SER A 83 5 5
SHEET 1 AA1 6 VAL A 2 GLU A 7 0
SHEET 2 AA1 6 GLU A 99 LYS A 108 1 O LYS A 104 N TYR A 4
SHEET 3 AA1 6 GLY A 84 ILE A 90 -1 N GLY A 84 O LEU A 105
SHEET 4 AA1 6 VAL A 29 LYS A 33 -1 N CYS A 30 O ARG A 89
SHEET 5 AA1 6 VAL A 44 THR A 48 -1 O VAL A 45 N TRP A 31
SHEET 6 AA1 6 VAL A 53 TYR A 55 -1 O TYR A 55 N ARG A 47
SHEET 1 AA2 3 ALA A 12 LEU A 14 0
SHEET 2 AA2 3 LEU A 73 ILE A 75 -1 O ILE A 75 N ALA A 12
SHEET 3 AA2 3 TYR A 60 LEU A 62 -1 N TRP A 61 O THR A 74
SSBOND 1 CYS A 16 CYS A 88 1555 1555 2.03
SSBOND 2 CYS A 30 CYS A 41 1555 1555 2.12
SSBOND 3 CYS A 36 CYS A 87 1555 1555 2.07
LINK O ILE A 92 CA CA A 201 1555 1555 2.26
LINK O GLY A 94 CA CA A 201 1555 1555 2.33
LINK OD1 ASN A 97 CA CA A 201 1555 1555 2.28
LINK OD1 ASP A 98 CA CA A 201 1555 1555 2.30
LINK CA CA A 201 O2 BEZ A 202 1555 1555 2.31
LINK CA CA A 201 O HOH A 387 1555 1555 2.35
SITE 1 AC1 6 ILE A 92 GLY A 94 ASN A 97 ASP A 98
SITE 2 AC1 6 BEZ A 202 HOH A 387
SITE 1 AC2 10 TYR A 13 VAL A 38 PHE A 39 ARG A 89
SITE 2 AC2 10 GLY A 94 MET A 96 ASN A 97 ASP A 98
SITE 3 AC2 10 CA A 201 HOH A 331
SITE 1 AC3 5 GLY A 34 ALA A 81 SER A 83 ILE A 85
SITE 2 AC3 5 TYR A 86
SITE 1 AC4 5 GLU A 3 TRP A 56 LEU A 62 LYS A 104
SITE 2 AC4 5 HOH A 350
CRYST1 42.310 43.060 51.720 90.00 90.00 90.00 P 21 21 21 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 0.023635 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023223 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019335 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
