HEADER TRANSCRIPTION 31-MAY-17 5Q1B
TITLE LIGAND BINDING TO FARNESOID-X-RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE ACID RECEPTOR;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: FARNESOID X-ACTIVATED RECEPTOR,FARNESOL RECEPTOR HRR-1,
COMPND 5 NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H MEMBER 4,RETINOID X RECEPTOR-
COMPND 6 INTERACTING PROTEIN 14,RXR-INTERACTING PROTEIN 14;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: COACTIVATOR PEPTIDE SRC-1 HD3;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 744-757;
COMPND 12 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, BAR, FXR, HRR1, RIP14;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS D3R, FXR, DOCKING, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.RUDOLPH,J.BENZ,D.BURGER,R.THOMA,A.RUF,C.JOSEPH,B.KUHN,C.SHAO,
AUTHOR 2 H.YANG,S.K.BURLEY
REVDAT 7 17-NOV-21 5Q1B 1 REMARK
REVDAT 6 10-FEB-21 5Q1B 1 AUTHOR JRNL
REVDAT 5 21-FEB-18 5Q1B 1 REMARK
REVDAT 4 31-JAN-18 5Q1B 1 JRNL
REVDAT 3 20-DEC-17 5Q1B 1 JRNL
REVDAT 2 19-JUL-17 5Q1B 1 AUTHOR JRNL
REVDAT 1 05-JUL-17 5Q1B 0
JRNL AUTH Z.GAIEB,S.LIU,S.GATHIAKA,M.CHIU,H.YANG,C.SHAO,V.A.FEHER,
JRNL AUTH 2 W.P.WALTERS,B.KUHN,M.G.RUDOLPH,S.K.BURLEY,M.K.GILSON,
JRNL AUTH 3 R.E.AMARO
JRNL TITL D3R GRAND CHALLENGE 2: BLIND PREDICTION OF PROTEIN-LIGAND
JRNL TITL 2 POSES, AFFINITY RANKINGS, AND RELATIVE BINDING FREE
JRNL TITL 3 ENERGIES.
JRNL REF J. COMPUT. AIDED MOL. DES. V. 32 1 2018
JRNL REFN ESSN 1573-4951
JRNL PMID 29204945
JRNL DOI 10.1007/S10822-017-0088-4
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 25354
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1264
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.69
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2842
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.4638
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2706
REMARK 3 BIN R VALUE (WORKING SET) : 0.4641
REMARK 3 BIN FREE R VALUE : 0.4586
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.79
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
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 : 82
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.19480
REMARK 3 B22 (A**2) : -3.56570
REMARK 3 B33 (A**2) : -2.62910
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) : 0.360
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.333
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.216
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.337
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.219
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 : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4142 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5599 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1491 ; 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 : 4142 ; 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 : 4674 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.14
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.32
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6610 20.7121 -6.1534
REMARK 3 T TENSOR
REMARK 3 T11: -0.1217 T22: -0.2057
REMARK 3 T33: -0.0947 T12: -0.0531
REMARK 3 T13: -0.0019 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 2.5524 L22: 1.6293
REMARK 3 L33: 4.7126 L12: -0.1161
REMARK 3 L13: 1.0707 L23: 0.1413
REMARK 3 S TENSOR
REMARK 3 S11: -0.1522 S12: -0.0680 S13: 0.2644
REMARK 3 S21: -0.0013 S22: -0.0768 S23: -0.0391
REMARK 3 S31: -0.2151 S32: -0.1321 S33: 0.2290
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5248 1.0366 -5.6711
REMARK 3 T TENSOR
REMARK 3 T11: 0.1222 T22: -0.1257
REMARK 3 T33: -0.0227 T12: -0.0016
REMARK 3 T13: -0.0529 T23: 0.0669
REMARK 3 L TENSOR
REMARK 3 L11: 0.2252 L22: 1.2286
REMARK 3 L33: 1.1503 L12: -1.1263
REMARK 3 L13: 0.0827 L23: -0.0944
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: 0.0212 S13: -0.0069
REMARK 3 S21: -0.0068 S22: -0.0075 S23: -0.0473
REMARK 3 S31: 0.0175 S32: 0.0024 S33: 0.0039
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8462 52.5194 34.2591
REMARK 3 T TENSOR
REMARK 3 T11: -0.2092 T22: 0.0177
REMARK 3 T33: -0.2134 T12: 0.0968
REMARK 3 T13: -0.0163 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 2.9857 L22: 2.5199
REMARK 3 L33: 3.0213 L12: -0.9325
REMARK 3 L13: 0.0862 L23: 0.5738
REMARK 3 S TENSOR
REMARK 3 S11: 0.0817 S12: -0.1508 S13: -0.1564
REMARK 3 S21: -0.0312 S22: -0.1949 S23: 0.1911
REMARK 3 S31: 0.1302 S32: -0.0723 S33: 0.1132
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5Q1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1001401373.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-08
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 : X10SA
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 : 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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26246
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 38.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.670
REMARK 200 R MERGE (I) : 0.07750
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.66
REMARK 200 R MERGE FOR SHELL (I) : 0.65670
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 28% W/V PEG MME
REMARK 280 2000, EVAPORATION, HANGING 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 93.99500
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 93.99500
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 36.04500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.79000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.04500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.79000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 93.99500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.04500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.79000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.99500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.04500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.79000
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: 1160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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: 1140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 LEU A 395 42.89 -90.74
REMARK 500 ASP A 398 30.92 -69.87
REMARK 500 TYR A 401 10.51 84.88
REMARK 500 ARG A 459 61.52 -68.59
REMARK 500 TYR C 401 8.08 81.08
REMARK 500 ARG C 459 61.31 -68.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 634 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH C 635 DISTANCE = 7.09 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9N7 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9N7 C 501
DBREF 5Q1B A 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 5Q1B B 744 757 UNP A8K1V4 A8K1V4_HUMAN 744 757
DBREF 5Q1B C 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 5Q1B D 744 757 UNP A8K1V4 A8K1V4_HUMAN 744 757
SEQADV 5Q1B GLY A 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1B SER A 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1B HIS A 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1B MET A 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1B ALA A 281 UNP Q96RI1 GLU 291 CONFLICT
SEQADV 5Q1B ALA A 354 UNP Q96RI1 GLU 364 CONFLICT
SEQADV 5Q1B GLY C 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1B SER C 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1B HIS C 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1B MET C 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1B ALA C 281 UNP Q96RI1 GLU 291 CONFLICT
SEQADV 5Q1B ALA C 354 UNP Q96RI1 GLU 364 CONFLICT
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 9N7 A 501 41
HET 9N7 C 501 41
HETNAM 9N7 4-{[(2S)-2-CYCLOHEXYL-2-{5,6-DIFLUORO-2-[4-(1,3-
HETNAM 2 9N7 THIAZOL-2-YL)PHENYL]-1H-BENZIMIDAZOL-1-
HETNAM 3 9N7 YL}ACETYL]AMINO}BENZOIC ACID
FORMUL 5 9N7 2(C31 H26 F2 N4 O3 S)
FORMUL 7 HOH *81(H2 O)
HELIX 1 AA1 THR A 250 ASN A 265 1 16
HELIX 2 AA2 MET A 269 GLU A 280 1 12
HELIX 3 AA3 SER A 283 LYS A 308 1 26
HELIX 4 AA4 GLY A 311 LEU A 315 5 5
HELIX 5 AA5 ASP A 316 ASN A 341 1 26
HELIX 6 AA6 GLY A 347 ASN A 358 1 12
HELIX 7 AA7 SER A 362 LEU A 379 1 18
HELIX 8 AA8 THR A 382 LEU A 395 1 14
HELIX 9 AA9 ASP A 404 GLN A 427 1 24
HELIX 10 AB1 GLN A 432 HIS A 450 1 19
HELIX 11 AB2 HIS A 450 SER A 457 1 8
HELIX 12 AB3 THR A 466 TRP A 473 1 8
HELIX 13 AB4 HIS B 746 LYS B 755 1 10
HELIX 14 AB5 THR C 250 ASN C 265 1 16
HELIX 15 AB6 MET C 269 GLU C 280 1 12
HELIX 16 AB7 SER C 283 LYS C 308 1 26
HELIX 17 AB8 GLY C 311 LEU C 315 5 5
HELIX 18 AB9 ASP C 316 GLY C 326 1 11
HELIX 19 AC1 SER C 327 ASN C 341 1 15
HELIX 20 AC2 GLY C 347 ASN C 358 1 12
HELIX 21 AC3 SER C 362 LEU C 379 1 18
HELIX 22 AC4 THR C 382 LEU C 395 1 14
HELIX 23 AC5 ASP C 404 GLN C 427 1 24
HELIX 24 AC6 GLN C 432 HIS C 450 1 19
HELIX 25 AC7 HIS C 450 SER C 457 1 8
HELIX 26 AC8 THR C 466 TRP C 473 1 8
HELIX 27 AC9 GLN D 747 LYS D 755 1 9
SITE 1 AC1 16 ILE A 273 ILE A 277 ASN A 287 MET A 294
SITE 2 AC1 16 HIS A 298 MET A 332 PHE A 333 ARG A 335
SITE 3 AC1 16 SER A 336 ILE A 339 PHE A 340 LEU A 352
SITE 4 AC1 16 ILE A 356 TYR A 373 LEU A 455 HOH A 601
SITE 1 AC2 20 ARG C 268 ILE C 273 ILE C 277 ASN C 287
SITE 2 AC2 20 MET C 294 HIS C 298 MET C 332 PHE C 333
SITE 3 AC2 20 ARG C 335 SER C 336 ILE C 339 PHE C 340
SITE 4 AC2 20 ILE C 356 MET C 369 TYR C 373 HIS C 451
SITE 5 AC2 20 MET C 454 LEU C 455 HOH C 606 HOH C 609
CRYST1 72.090 83.580 187.990 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 0.013872 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011965 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005319 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
