HEADER HORMONE RECEPTOR 31-AUG-10 3OOK
TITLE CRYSTAL STRUCTURE OF HUMAN FXR IN COMPLEX WITH 4-({(2S)-2-[2-(4-
TITLE 2 CHLOROPHENYL)-5,6-DIFLUORO-1H-BENZIMIDAZOL-1-YL]-2-
TITLE 3 CYCLOHEXYLACETYL}AMINO)-3,5-DIFLUOROBENZOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE ACID RECEPTOR;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 258-486;
COMPND 5 SYNONYM: FXR, FARNESOID X-ACTIVATED RECEPTOR, FARNESOL RECEPTOR HRR-
COMPND 6 1, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H MEMBER 4, RETINOID X
COMPND 7 RECEPTOR-INTERACTING PROTEIN 14, RXR-INTERACTING PROTEIN 14;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: PEPTIDE OF NUCLEAR RECEPTOR COACTIVATOR 1;
COMPND 12 CHAIN: B, D;
COMPND 13 FRAGMENT: UNP RESIDUES 744-757;
COMPND 14 SYNONYM: NCOA-1, CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74, BHLHE74,
COMPND 15 PROTEIN HIN-2, RIP160, RENAL CARCINOMA ANTIGEN NY-REN-52, STEROID
COMPND 16 RECEPTOR COACTIVATOR 1, SRC-1;
COMPND 17 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: NR1H4, HCG_20893;
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: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS NUCLEAR RECEPTOR, CHOLESTEROL, BILE ACID, DNA-BINDING, NUCLEUS,
KEYWDS 2 RECEPTOR, TRANSCRIPTION, LIGAND BINDING DOMAIN TRANSCRIPTION
KEYWDS 3 REGULATION, COACTIVATOR, FXR ALTERNATIVE SPLICING, HORMONE RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.RUDOLPH
REVDAT 4 03-APR-24 3OOK 1 REMARK
REVDAT 3 20-MAR-24 3OOK 1 REMARK SEQADV
REVDAT 2 26-FEB-14 3OOK 1 JRNL VERSN
REVDAT 1 19-JAN-11 3OOK 0
JRNL AUTH H.G.F.RICHTER,G.M.BENSON,K.H.BLEICHER,D.BLUM,E.CHAPUT,
JRNL AUTH 2 N.CLEMANN,S.FENG,C.GARDES,U.GRETHER,P.HARTMAN,B.KUHN,
JRNL AUTH 3 R.E.MARTIN,J.M.PLANCHER,M.G.RUDOLPH,F.SCHULER,S.TAYLOR
JRNL TITL OPTIMIZATION OF A NOVEL CLASS OF BENZIMIDAZOLE-BASED
JRNL TITL 2 FARNESOID X RECEPTOR (FXR) AGONISTS TO IMPROVE
JRNL TITL 3 PHYSICOCHEMICAL AND ADME PROPERTIES
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 1134 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 21269824
JRNL DOI 10.1016/J.BMCL.2010.12.123
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.5
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) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 26269
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1337
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 : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2931
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.4050
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2765
REMARK 3 BIN R VALUE (WORKING SET) : 0.4025
REMARK 3 BIN FREE R VALUE : 0.4485
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.66
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 166
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 : 3968
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.01430
REMARK 3 B22 (A**2) : -6.49580
REMARK 3 B33 (A**2) : 4.48160
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) : 0.371
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.360
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.250
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.349
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.250
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 : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4136 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5593 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1485 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 119 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 573 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4136 ; 20.000 ; 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 : 529 ; 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 : 4983 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.09
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.37
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.21
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 3OOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061376.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-07
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26309
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 38.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.170
REMARK 200 R MERGE (I) : 0.06860
REMARK 200 R SYM (I) : 0.06860
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.26
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: INHOUSE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 20% PEG 5000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 95.00350
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 95.00350
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 36.23850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.64400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.23850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.64400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 95.00350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.23850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.64400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 95.00350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.23850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.64400
REMARK 290 SMTRY3 8 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 244
REMARK 465 SER A 245
REMARK 465 HIS A 246
REMARK 465 LYS B 744
REMARK 465 GLU B 757
REMARK 465 GLY C 244
REMARK 465 SER C 245
REMARK 465 HIS C 246
REMARK 465 LYS D 744
REMARK 465 ASP D 745
REMARK 465 GLU D 757
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 LYS A 266 6.36 -66.91
REMARK 500 LYS A 380 57.14 34.09
REMARK 500 LEU A 395 36.64 -87.17
REMARK 500 ASP A 398 45.74 -77.17
REMARK 500 TYR A 401 5.04 80.46
REMARK 500 GLN A 427 59.59 -141.23
REMARK 500 LEU C 395 52.77 -92.73
REMARK 500 TYR C 401 -5.52 81.71
REMARK 500 ILE C 402 109.92 -59.23
REMARK 500 ARG C 459 70.13 -67.54
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 OOK A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OOK C 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OKH RELATED DB: PDB
REMARK 900 RELATED ID: 3OKI RELATED DB: PDB
REMARK 900 RELATED ID: 3OLF RELATED DB: PDB
REMARK 900 RELATED ID: 3OMK RELATED DB: PDB
REMARK 900 RELATED ID: 3OMM RELATED DB: PDB
REMARK 900 RELATED ID: 3OOF RELATED DB: PDB
DBREF 3OOK A 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 3OOK B 744 757 UNP Q15788 NCOA1_HUMAN 744 757
DBREF 3OOK C 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 3OOK D 744 757 UNP Q15788 NCOA1_HUMAN 744 757
SEQADV 3OOK GLY A 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 3OOK SER A 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 3OOK HIS A 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 3OOK MET A 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 3OOK ALA A 281 UNP Q96RI1 GLU 291 ENGINEERED MUTATION
SEQADV 3OOK ALA A 354 UNP Q96RI1 GLU 364 ENGINEERED MUTATION
SEQADV 3OOK GLY C 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 3OOK SER C 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 3OOK HIS C 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 3OOK MET C 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 3OOK ALA C 281 UNP Q96RI1 GLU 291 ENGINEERED MUTATION
SEQADV 3OOK ALA C 354 UNP Q96RI1 GLU 364 ENGINEERED MUTATION
SEQRES 1 A 233 GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU
SEQRES 2 A 233 LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET
SEQRES 3 A 233 PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE
SEQRES 4 A 233 SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA
SEQRES 5 A 233 THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS
SEQRES 6 A 233 LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE
SEQRES 7 A 233 ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU
SEQRES 8 A 233 ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY
SEQRES 9 A 233 HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY
SEQRES 10 A 233 ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR
SEQRES 11 A 233 LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR
SEQRES 12 A 233 ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG
SEQRES 13 A 233 GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN
SEQRES 14 A 233 GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE
SEQRES 15 A 233 HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU
SEQRES 16 A 233 GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS
SEQRES 17 A 233 ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS
SEQRES 18 A 233 PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN
SEQRES 1 B 14 LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP
SEQRES 2 B 14 GLU
SEQRES 1 C 233 GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU
SEQRES 2 C 233 LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET
SEQRES 3 C 233 PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE
SEQRES 4 C 233 SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA
SEQRES 5 C 233 THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS
SEQRES 6 C 233 LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE
SEQRES 7 C 233 ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU
SEQRES 8 C 233 ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY
SEQRES 9 C 233 HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY
SEQRES 10 C 233 ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR
SEQRES 11 C 233 LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR
SEQRES 12 C 233 ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG
SEQRES 13 C 233 GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN
SEQRES 14 C 233 GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE
SEQRES 15 C 233 HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU
SEQRES 16 C 233 GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS
SEQRES 17 C 233 ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS
SEQRES 18 C 233 PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN
SEQRES 1 D 14 LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP
SEQRES 2 D 14 GLU
HET OOK A 1 39
HET OOK C 2 39
HETNAM OOK 4-({(2S)-2-[2-(4-CHLOROPHENYL)-5,6-DIFLUORO-1H-
HETNAM 2 OOK BENZIMIDAZOL-1-YL]-2-CYCLOHEXYLACETYL}AMINO)-3,5-
HETNAM 3 OOK DIFLUOROBENZOIC ACID
FORMUL 5 OOK 2(C28 H22 CL F4 N3 O3)
FORMUL 7 HOH *166(H2 O)
HELIX 1 1 THR A 250 LYS A 266 1 17
HELIX 2 2 MET A 269 GLU A 280 1 12
HELIX 3 3 SER A 283 LYS A 308 1 26
HELIX 4 4 GLY A 311 LEU A 315 5 5
HELIX 5 5 ASP A 316 ASN A 341 1 26
HELIX 6 6 GLY A 347 ASN A 358 1 12
HELIX 7 7 SER A 362 LEU A 379 1 18
HELIX 8 8 THR A 382 LEU A 395 1 14
HELIX 9 9 ASP A 404 HIS A 426 1 23
HELIX 10 10 GLN A 432 ARG A 445 1 14
HELIX 11 11 THR A 446 HIS A 449 5 4
HELIX 12 12 HIS A 450 SER A 457 1 8
HELIX 13 13 THR A 466 TRP A 473 1 8
HELIX 14 14 HIS B 746 LYS B 755 1 10
HELIX 15 15 THR C 250 LYS C 266 1 17
HELIX 16 16 MET C 269 GLU C 280 1 12
HELIX 17 17 SER C 283 LYS C 308 1 26
HELIX 18 18 GLY C 311 LEU C 315 5 5
HELIX 19 19 ASP C 316 ASN C 341 1 26
HELIX 20 20 GLY C 347 ASN C 358 1 12
HELIX 21 21 SER C 362 LEU C 379 1 18
HELIX 22 22 THR C 382 LEU C 395 1 14
HELIX 23 23 ASP C 404 GLN C 427 1 24
HELIX 24 24 GLN C 432 GLY C 439 1 8
HELIX 25 25 GLY C 439 HIS C 450 1 12
HELIX 26 26 HIS C 450 SER C 457 1 8
HELIX 27 27 THR C 466 ASP C 474 1 9
HELIX 28 28 HIS D 746 LYS D 755 1 10
SITE 1 AC1 17 HOH A 137 HOH A 138 ILE A 273 ILE A 277
SITE 2 AC1 17 ASN A 287 LEU A 291 MET A 294 ALA A 295
SITE 3 AC1 17 HIS A 298 MET A 332 ARG A 335 SER A 336
SITE 4 AC1 17 ILE A 339 PHE A 340 ILE A 356 MET A 369
SITE 5 AC1 17 TYR A 373
SITE 1 AC2 17 HOH C 136 ILE C 273 ILE C 277 ASN C 287
SITE 2 AC2 17 LEU C 291 MET C 294 ALA C 295 HIS C 298
SITE 3 AC2 17 MET C 332 PHE C 333 ARG C 335 SER C 336
SITE 4 AC2 17 ILE C 339 PHE C 340 ILE C 356 MET C 369
SITE 5 AC2 17 TYR C 373
CRYST1 72.477 83.288 190.007 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 0.013797 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012007 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005263 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
