HEADER TRANSCRIPTION 05-MAY-09 3HC5
TITLE FXR WITH SRC1 AND GSK826
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE ACID RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FXR;
COMPND 5 SYNONYM: FARNESOID X-ACTIVATED RECEPTOR, FARNESOL RECEPTOR HRR-1,
COMPND 6 NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H MEMBER 4, RETINOID X RECEPTOR-
COMPND 7 INTERACTING PROTEIN 14, RXR-INTERACTING PROTEIN 14;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: SRC1;
COMPND 13 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: BAR, FXR, HRR1, NR1H4, RIP14;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSETA;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS FXR, NUCLEAR RECEPTOR, GW4064, ALPHA-HELICAL SANDWICH, ACTIVATOR,
KEYWDS 2 ALTERNATIVE SPLICING, DNA-BINDING, METAL-BINDING, NUCLEUS, RECEPTOR,
KEYWDS 3 REPRESSOR, TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC, ZINC-
KEYWDS 4 FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR S.P.WILLIAMS,K.P.MADAUSS
REVDAT 4 06-SEP-23 3HC5 1 REMARK SEQADV
REVDAT 3 01-NOV-17 3HC5 1 REMARK
REVDAT 2 11-AUG-09 3HC5 1 JRNL
REVDAT 1 21-JUL-09 3HC5 0
JRNL AUTH A.AKWABI-AMEYAW,J.Y.BASS,R.D.CALDWELL,J.A.CARAVELLA,L.CHEN,
JRNL AUTH 2 K.L.CREECH,D.N.DEATON,K.P.MADAUSS,H.B.MARR,R.B.MCFADYEN,
JRNL AUTH 3 A.B.MILLER,F.NAVAS,D.J.PARKS,P.K.SPEARING,D.TODD,
JRNL AUTH 4 S.P.WILLIAMS,G.BRUCE WISELY
JRNL TITL FXR AGONIST ACTIVITY OF CONFORMATIONALLY CONSTRAINED ANALOGS
JRNL TITL 2 OF GW 4064.
JRNL REF BIOORG.MED.CHEM.LETT. V. 19 4733 2009
JRNL REFN ISSN 0960-894X
JRNL PMID 19586769
JRNL DOI 10.1016/J.BMCL.2009.06.062
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 10558
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 SET) : 0.220
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.900
REMARK 3 FREE R VALUE TEST SET COUNT : 727
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 (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 1864
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 38
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : 826.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000052953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.0
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11211
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.8900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3DCT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LI2SO4, 0.1M BIS-TRIS, 25%
REMARK 280 PEG3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z+1/2
REMARK 290 15555 -X,Y+1/2,-Z+1/2
REMARK 290 16555 X,-Y+1/2,-Z+1/2
REMARK 290 17555 Z,X+1/2,Y+1/2
REMARK 290 18555 Z,-X+1/2,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y+1/2
REMARK 290 20555 -Z,X+1/2,-Y+1/2
REMARK 290 21555 Y,Z+1/2,X+1/2
REMARK 290 22555 -Y,Z+1/2,-X+1/2
REMARK 290 23555 Y,-Z+1/2,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X+1/2
REMARK 290 25555 X+1/2,Y,Z+1/2
REMARK 290 26555 -X+1/2,-Y,Z+1/2
REMARK 290 27555 -X+1/2,Y,-Z+1/2
REMARK 290 28555 X+1/2,-Y,-Z+1/2
REMARK 290 29555 Z+1/2,X,Y+1/2
REMARK 290 30555 Z+1/2,-X,-Y+1/2
REMARK 290 31555 -Z+1/2,-X,Y+1/2
REMARK 290 32555 -Z+1/2,X,-Y+1/2
REMARK 290 33555 Y+1/2,Z,X+1/2
REMARK 290 34555 -Y+1/2,Z,-X+1/2
REMARK 290 35555 Y+1/2,-Z,-X+1/2
REMARK 290 36555 -Y+1/2,-Z,X+1/2
REMARK 290 37555 X+1/2,Y+1/2,Z
REMARK 290 38555 -X+1/2,-Y+1/2,Z
REMARK 290 39555 -X+1/2,Y+1/2,-Z
REMARK 290 40555 X+1/2,-Y+1/2,-Z
REMARK 290 41555 Z+1/2,X+1/2,Y
REMARK 290 42555 Z+1/2,-X+1/2,-Y
REMARK 290 43555 -Z+1/2,-X+1/2,Y
REMARK 290 44555 -Z+1/2,X+1/2,-Y
REMARK 290 45555 Y+1/2,Z+1/2,X
REMARK 290 46555 -Y+1/2,Z+1/2,-X
REMARK 290 47555 Y+1/2,-Z+1/2,-X
REMARK 290 48555 -Y+1/2,-Z+1/2,X
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY1 37 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY2 37 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY3 37 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 38 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY2 38 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY3 38 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 39 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY2 39 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY3 39 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 40 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY2 40 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY3 40 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 41 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY2 41 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY3 41 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 42 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY2 42 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY3 42 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 43 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY2 43 -1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY3 43 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 44 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY2 44 1.000000 0.000000 0.000000 79.94650
REMARK 290 SMTRY3 44 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 45 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY2 45 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY3 45 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 46 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY2 46 0.000000 0.000000 1.000000 79.94650
REMARK 290 SMTRY3 46 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 47 0.000000 1.000000 0.000000 79.94650
REMARK 290 SMTRY2 47 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY3 47 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 48 0.000000 -1.000000 0.000000 79.94650
REMARK 290 SMTRY2 48 0.000000 0.000000 -1.000000 79.94650
REMARK 290 SMTRY3 48 1.000000 0.000000 0.000000 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A 241
REMARK 465 SER A 242
REMARK 465 THR A 243
REMARK 465 LYS B 741
REMARK 465 GLU B 742
REMARK 465 SER B 743
REMARK 465 LYS B 744
REMARK 465 ASP B 756
REMARK 465 GLU B 757
REMARK 465 LYS B 758
REMARK 465 ASP B 759
REMARK 465 LEU B 760
REMARK 465 ARG B 761
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 GLU A 244 CG CD OE1 OE2
REMARK 470 GLN A 250 CG CD OE1 NE2
REMARK 470 PHE A 255 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 GLN A 263 CG CD OE1 NE2
REMARK 470 ARG A 264 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 268 CG CD OE1 OE2
REMARK 470 GLU A 277 CG CD OE1 OE2
REMARK 470 GLU A 281 CG CD OE1 OE2
REMARK 470 LYS A 303 CG CD CE NZ
REMARK 470 THR A 310 OG1 CG2
REMARK 470 GLU A 314 CG CD OE1 OE2
REMARK 470 LYS A 339 CG CD CE NZ
REMARK 470 SER A 342 OG
REMARK 470 LYS A 370 CG CD CE NZ
REMARK 470 LYS A 376 CG CD CE NZ
REMARK 470 LYS A 399 CG CD CE NZ
REMARK 470 GLU A 402 CG CD OE1 OE2
REMARK 470 GLU A 405 CG CD OE1 OE2
REMARK 470 LYS A 406 CG CD CE NZ
REMARK 470 GLU A 409 CG CD OE1 OE2
REMARK 470 LYS A 417 CG CD CE NZ
REMARK 470 LYS A 420 CG CD CE NZ
REMARK 470 ILE A 421 CG1 CG2 CD1
REMARK 470 LYS A 460 CG CD CE NZ
REMARK 470 VAL A 471 CG1 CG2
REMARK 470 GLN A 472 CG CD OE1 NE2
REMARK 470 ASP B 745 CG OD1 OD2
REMARK 470 ARG B 750 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 755 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 LEU A 245 80.30 66.18
REMARK 500 THR A 246 -162.98 -68.47
REMARK 500 SER A 345 -69.16 -29.68
REMARK 500 ASN A 354 57.33 -147.94
REMARK 500 LEU A 391 51.44 -90.49
REMARK 500 ARG A 395 135.56 -37.67
REMARK 500 ARG A 401 3.24 -58.42
REMARK 500 PHE A 461 -140.43 -109.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 82X A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DCT RELATED DB: PDB
REMARK 900 FXR WITH SRC1 AND GW4064
REMARK 900 RELATED ID: 3DCU RELATED DB: PDB
REMARK 900 FXR WITH SRC1 AND GSK8062
REMARK 900 RELATED ID: 3HC6 RELATED DB: PDB
DBREF 3HC5 A 243 472 UNP Q96RI1 NR1H4_HUMAN 257 486
DBREF 3HC5 B 741 761 UNP Q15788 NCOA1_HUMAN 741 761
SEQADV 3HC5 GLY A 241 UNP Q96RI1 EXPRESSION TAG
SEQADV 3HC5 SER A 242 UNP Q96RI1 EXPRESSION TAG
SEQRES 1 A 232 GLY SER THR GLU LEU THR PRO ASP GLN GLN THR LEU LEU
SEQRES 2 A 232 HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET PRO
SEQRES 3 A 232 GLN GLU ILE THR ASN LYS ILE LEU LYS GLU GLU PHE SER
SEQRES 4 A 232 ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA THR
SEQRES 5 A 232 ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS LEU
SEQRES 6 A 232 PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE ALA
SEQRES 7 A 232 LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU ARG
SEQRES 8 A 232 SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY HIS
SEQRES 9 A 232 SER ASP LEU LEU GLU GLU ARG ILE ARG ASN SER GLY ILE
SEQRES 10 A 232 SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR LYS
SEQRES 11 A 232 SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR ALA
SEQRES 12 A 232 LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG GLN
SEQRES 13 A 232 TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN GLU
SEQRES 14 A 232 PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE HIS
SEQRES 15 A 232 GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU GLY
SEQRES 16 A 232 ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS ALA
SEQRES 17 A 232 GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS PHE
SEQRES 18 A 232 THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN
SEQRES 1 B 21 LYS GLU SER LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU
SEQRES 2 B 21 ASP LYS ASP GLU LYS ASP LEU ARG
HET 82X A 1 36
HET SO4 A 473 5
HET SO4 A 2 5
HETNAM 82X 3-(6-{[3-(2,6-DICHLOROPHENYL)-5-(1-METHYLETHYL)
HETNAM 2 82X ISOXAZOL-4-YL]METHOXY}-1-BENZOTHIOPHEN-2-YL)BENZOIC
HETNAM 3 82X ACID
HETNAM SO4 SULFATE ION
FORMUL 3 82X C28 H21 CL2 N O4 S
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 HOH *38(H2 O)
HELIX 1 1 THR A 246 LYS A 262 1 17
HELIX 2 2 PRO A 266 ASN A 271 1 6
HELIX 3 3 ASN A 271 GLU A 276 1 6
HELIX 4 4 SER A 279 LYS A 303 1 25
HELIX 5 5 GLY A 307 LEU A 311 5 5
HELIX 6 6 ASP A 312 LYS A 338 1 27
HELIX 7 7 LEU A 340 GLY A 343 5 4
HELIX 8 8 HIS A 344 ARG A 353 1 10
HELIX 9 9 SER A 358 GLU A 374 1 17
HELIX 10 10 THR A 378 LEU A 391 1 14
HELIX 11 11 ASP A 400 GLN A 423 1 24
HELIX 12 12 GLN A 428 ASN A 457 1 30
HELIX 13 13 THR A 462 TRP A 469 1 8
HELIX 14 14 HIS B 746 LYS B 755 1 10
SITE 1 AC1 15 THR A 270 LEU A 287 THR A 288 MET A 290
SITE 2 AC1 15 ALA A 291 HIS A 294 MET A 328 PHE A 329
SITE 3 AC1 15 ARG A 331 SER A 342 GLY A 343 TYR A 369
SITE 4 AC1 15 HIS A 447 TRP A 454 TRP A 469
SITE 1 AC2 5 ASN A 271 LYS A 275 SER A 279 ALA A 280
SITE 2 AC2 5 ASN A 354
SITE 1 AC3 3 LYS A 338 THR A 378 GLN A 379
CRYST1 159.893 159.893 159.893 90.00 90.00 90.00 F 2 3 48
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 0.006254 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006254 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006254 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
