HEADER TRANSCRIPTION 31-MAY-17 5Q1H
TITLE LIGAND BINDING TO FARNESOID-X-RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILE ACID RECEPTOR;
COMPND 3 CHAIN: A, C, E, G;
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, F, H;
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 8 17-NOV-21 5Q1H 1 REMARK
REVDAT 7 10-FEB-21 5Q1H 1 AUTHOR JRNL
REVDAT 6 21-FEB-18 5Q1H 1 REMARK
REVDAT 5 31-JAN-18 5Q1H 1 JRNL
REVDAT 4 20-DEC-17 5Q1H 1 JRNL
REVDAT 3 04-OCT-17 5Q1H 1 REMARK
REVDAT 2 19-JUL-17 5Q1H 1 AUTHOR JRNL
REVDAT 1 05-JUL-17 5Q1H 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. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 55294
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2807
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.26
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.35
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3733
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2260
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3547
REMARK 3 BIN R VALUE (WORKING SET) : 0.2237
REMARK 3 BIN FREE R VALUE : 0.2718
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.98
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 186
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 : 7837
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 144
REMARK 3 SOLVENT ATOMS : 277
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28850
REMARK 3 B22 (A**2) : 0.99970
REMARK 3 B33 (A**2) : -1.28820
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.26580
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.270
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.232
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.180
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.242
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.186
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 : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8194 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11078 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2972 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 229 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1138 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8194 ; 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 : 1052 ; 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 : 9511 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.43
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.30
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4576 8.3633 4.1871
REMARK 3 T TENSOR
REMARK 3 T11: -0.2146 T22: -0.0513
REMARK 3 T33: -0.1491 T12: -0.0151
REMARK 3 T13: 0.0113 T23: -0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 1.6637 L22: 3.8219
REMARK 3 L33: 2.4520 L12: -0.4283
REMARK 3 L13: 0.4620 L23: -1.4976
REMARK 3 S TENSOR
REMARK 3 S11: -0.1287 S12: -0.0633 S13: -0.0134
REMARK 3 S21: 0.1255 S22: 0.2100 S23: -0.0536
REMARK 3 S31: -0.1419 S32: -0.1677 S33: -0.0813
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0873 48.3604 18.8921
REMARK 3 T TENSOR
REMARK 3 T11: -0.0697 T22: -0.1559
REMARK 3 T33: -0.2264 T12: -0.0403
REMARK 3 T13: -0.0413 T23: -0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 2.1006 L22: 2.1431
REMARK 3 L33: 3.8591 L12: -0.2723
REMARK 3 L13: -0.3670 L23: 0.3214
REMARK 3 S TENSOR
REMARK 3 S11: -0.1233 S12: -0.1911 S13: 0.1095
REMARK 3 S21: -0.1394 S22: 0.1347 S23: -0.0441
REMARK 3 S31: -0.1660 S32: 0.3216 S33: -0.0114
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1408 20.4977 32.1821
REMARK 3 T TENSOR
REMARK 3 T11: -0.1448 T22: -0.0671
REMARK 3 T33: -0.1975 T12: 0.0053
REMARK 3 T13: 0.0284 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 2.3264 L22: 4.0714
REMARK 3 L33: 2.1195 L12: 1.0369
REMARK 3 L13: 0.1524 L23: 0.9633
REMARK 3 S TENSOR
REMARK 3 S11: -0.0205 S12: 0.2606 S13: -0.0753
REMARK 3 S21: -0.0240 S22: 0.2552 S23: -0.2018
REMARK 3 S31: -0.1253 S32: 0.1040 S33: -0.2348
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { G|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1606 -19.8446 4.6162
REMARK 3 T TENSOR
REMARK 3 T11: -0.1883 T22: -0.1595
REMARK 3 T33: -0.1046 T12: 0.0410
REMARK 3 T13: -0.0611 T23: 0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 3.0421 L22: 2.5157
REMARK 3 L33: 2.8527 L12: 0.6337
REMARK 3 L13: -0.1456 L23: 0.7794
REMARK 3 S TENSOR
REMARK 3 S11: -0.0070 S12: -0.1729 S13: -0.2907
REMARK 3 S21: 0.1229 S22: 0.1919 S23: 0.0641
REMARK 3 S31: 0.3040 S32: 0.1286 S33: -0.1849
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5Q1H 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_1001401379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55434
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.66700
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 (%): 50.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 25%PEG3350,
REMARK 280 EVAPORATION, HANGING 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 91.93950
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, 3, 4
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: 1090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11990 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: 1130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 350
REMARK 350 BIOMOLECULE: 3
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: 1110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 4
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: 1070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 GLN A 476
REMARK 465 LYS B 744
REMARK 465 ASP B 756
REMARK 465 GLU B 757
REMARK 465 GLY C 244
REMARK 465 SER C 245
REMARK 465 HIS C 246
REMARK 465 VAL C 475
REMARK 465 GLN C 476
REMARK 465 LYS D 744
REMARK 465 ASP D 745
REMARK 465 ASP D 756
REMARK 465 GLU D 757
REMARK 465 GLY E 244
REMARK 465 SER E 245
REMARK 465 HIS E 246
REMARK 465 LYS F 744
REMARK 465 ASP F 745
REMARK 465 LYS F 755
REMARK 465 ASP F 756
REMARK 465 GLU F 757
REMARK 465 GLY G 244
REMARK 465 SER G 245
REMARK 465 HIS G 246
REMARK 465 GLN G 476
REMARK 465 LYS H 744
REMARK 465 ASP H 745
REMARK 465 ASP H 756
REMARK 465 GLU H 757
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 MET A 247 CG SD CE
REMARK 470 MET C 247 CG SD CE
REMARK 470 ASP E 462 CG OD1 OD2
REMARK 470 GLN E 476 CG CD OE1 NE2
REMARK 470 MET G 247 CG SD CE
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 SER A 346 122.57 -37.40
REMARK 500 LEU A 395 40.99 -82.11
REMARK 500 ASP A 398 47.32 -88.57
REMARK 500 TYR A 401 17.89 81.77
REMARK 500 LYS A 424 1.57 -69.73
REMARK 500 ILE A 425 -50.13 -122.27
REMARK 500 LEU C 395 57.79 -92.36
REMARK 500 ASP E 398 58.66 -94.12
REMARK 500 TYR E 401 2.72 80.56
REMARK 500 HIS G 348 16.06 -60.55
REMARK 500 LEU G 395 45.27 -92.53
REMARK 500 ASP G 398 31.78 -83.46
REMARK 500 GLN G 427 58.81 -140.65
REMARK 500 ASP G 474 67.43 61.00
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 A 668 DISTANCE = 5.98 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NP C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NP E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NP G 500
DBREF 5Q1H A 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 5Q1H B 744 757 UNP A8K1V4 A8K1V4_HUMAN 744 757
DBREF 5Q1H C 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 5Q1H D 744 757 UNP A8K1V4 A8K1V4_HUMAN 744 757
DBREF 5Q1H E 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 5Q1H F 744 757 UNP A8K1V4 A8K1V4_HUMAN 744 757
DBREF 5Q1H G 248 476 UNP Q96RI1 NR1H4_HUMAN 258 486
DBREF 5Q1H H 744 757 UNP A8K1V4 A8K1V4_HUMAN 744 757
SEQADV 5Q1H GLY A 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H SER A 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H HIS A 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H MET A 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H ALA A 281 UNP Q96RI1 GLU 291 CONFLICT
SEQADV 5Q1H ALA A 354 UNP Q96RI1 GLU 364 CONFLICT
SEQADV 5Q1H GLY C 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H SER C 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H HIS C 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H MET C 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H ALA C 281 UNP Q96RI1 GLU 291 CONFLICT
SEQADV 5Q1H ALA C 354 UNP Q96RI1 GLU 364 CONFLICT
SEQADV 5Q1H GLY E 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H SER E 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H HIS E 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H MET E 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H ALA E 281 UNP Q96RI1 GLU 291 CONFLICT
SEQADV 5Q1H ALA E 354 UNP Q96RI1 GLU 364 CONFLICT
SEQADV 5Q1H GLY G 244 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H SER G 245 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H HIS G 246 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H MET G 247 UNP Q96RI1 EXPRESSION TAG
SEQADV 5Q1H ALA G 281 UNP Q96RI1 GLU 291 CONFLICT
SEQADV 5Q1H ALA G 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
SEQRES 1 E 233 GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU
SEQRES 2 E 233 LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET
SEQRES 3 E 233 PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE
SEQRES 4 E 233 SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA
SEQRES 5 E 233 THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS
SEQRES 6 E 233 LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE
SEQRES 7 E 233 ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU
SEQRES 8 E 233 ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY
SEQRES 9 E 233 HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY
SEQRES 10 E 233 ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR
SEQRES 11 E 233 LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR
SEQRES 12 E 233 ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG
SEQRES 13 E 233 GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN
SEQRES 14 E 233 GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE
SEQRES 15 E 233 HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU
SEQRES 16 E 233 GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS
SEQRES 17 E 233 ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS
SEQRES 18 E 233 PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN
SEQRES 1 F 14 LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP
SEQRES 2 F 14 GLU
SEQRES 1 G 233 GLY SER HIS MET GLU LEU THR PRO ASP GLN GLN THR LEU
SEQRES 2 G 233 LEU HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET
SEQRES 3 G 233 PRO GLN GLU ILE THR ASN LYS ILE LEU LYS GLU ALA PHE
SEQRES 4 G 233 SER ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA
SEQRES 5 G 233 THR ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS
SEQRES 6 G 233 LEU PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE
SEQRES 7 G 233 ALA LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU
SEQRES 8 G 233 ARG SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY
SEQRES 9 G 233 HIS SER ASP LEU LEU GLU ALA ARG ILE ARG ASN SER GLY
SEQRES 10 G 233 ILE SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR
SEQRES 11 G 233 LYS SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR
SEQRES 12 G 233 ALA LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG
SEQRES 13 G 233 GLN TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN
SEQRES 14 G 233 GLU PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE
SEQRES 15 G 233 HIS GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU
SEQRES 16 G 233 GLY ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS
SEQRES 17 G 233 ALA GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS
SEQRES 18 G 233 PHE THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN
SEQRES 1 H 14 LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU ASP LYS ASP
SEQRES 2 H 14 GLU
HET 9NP A 500 36
HET 9NP C 500 36
HET 9NP E 500 36
HET 9NP G 500 36
HETNAM 9NP (2S)-N,2-DICYCLOHEXYL-2-{2-[4-(1H-TETRAZOL-5-YL)
HETNAM 2 9NP PHENYL]-1H-BENZIMIDAZOL-1-YL}ACETAMIDE
FORMUL 9 9NP 4(C28 H33 N7 O)
FORMUL 13 HOH *277(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 ASP A 474 1 9
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 LYS C 342 1 27
HELIX 19 AC1 GLY C 347 ASN C 358 1 12
HELIX 20 AC2 SER C 362 LEU C 379 1 18
HELIX 21 AC3 THR C 382 LEU C 395 1 14
HELIX 22 AC4 ASP C 404 GLN C 427 1 24
HELIX 23 AC5 GLN C 432 TRP C 458 1 27
HELIX 24 AC6 THR C 466 ASP C 474 1 9
HELIX 25 AC7 GLN D 747 ASP D 754 1 8
HELIX 26 AC8 THR E 250 ASN E 265 1 16
HELIX 27 AC9 MET E 269 GLU E 280 1 12
HELIX 28 AD1 SER E 283 LEU E 309 1 27
HELIX 29 AD2 GLY E 311 LEU E 315 5 5
HELIX 30 AD3 ASP E 316 ASN E 341 1 26
HELIX 31 AD4 GLY E 347 ASN E 358 1 12
HELIX 32 AD5 SER E 362 LEU E 379 1 18
HELIX 33 AD6 THR E 382 LEU E 395 1 14
HELIX 34 AD7 ASP E 404 GLN E 427 1 24
HELIX 35 AD8 GLN E 432 HIS E 450 1 19
HELIX 36 AD9 HIS E 450 SER E 457 1 8
HELIX 37 AE1 THR E 466 ASP E 474 1 9
HELIX 38 AE2 GLN F 747 ASP F 754 1 8
HELIX 39 AE3 THR G 250 ASN G 265 1 16
HELIX 40 AE4 MET G 269 GLU G 280 1 12
HELIX 41 AE5 SER G 283 LYS G 308 1 26
HELIX 42 AE6 GLY G 311 LEU G 315 5 5
HELIX 43 AE7 ASP G 316 ASN G 341 1 26
HELIX 44 AE8 HIS G 348 ASN G 358 1 11
HELIX 45 AE9 SER G 362 LEU G 379 1 18
HELIX 46 AF1 THR G 382 LEU G 395 1 14
HELIX 47 AF2 ASP G 404 GLN G 427 1 24
HELIX 48 AF3 GLN G 432 HIS G 450 1 19
HELIX 49 AF4 HIS G 450 SER G 457 1 8
HELIX 50 AF5 THR G 466 ASP G 474 1 9
HELIX 51 AF6 GLN H 747 LYS H 755 1 9
SSBOND 1 CYS A 436 CYS G 436 1555 1555 2.05
SITE 1 AC1 15 ILE A 277 ASN A 287 LEU A 291 MET A 294
SITE 2 AC1 15 HIS A 298 PHE A 333 SER A 336 ILE A 339
SITE 3 AC1 15 ILE A 356 ILE A 361 TYR A 373 HIS A 451
SITE 4 AC1 15 MET A 454 LEU A 455 TRP A 458
SITE 1 AC2 14 ILE C 277 ILE C 290 LEU C 291 MET C 294
SITE 2 AC2 14 HIS C 298 MET C 332 SER C 336 ILE C 356
SITE 3 AC2 14 ILE C 361 TYR C 373 HIS C 451 MET C 454
SITE 4 AC2 14 LEU C 455 TRP C 458
SITE 1 AC3 14 ILE E 277 LEU E 291 MET E 294 HIS E 298
SITE 2 AC3 14 PHE E 333 SER E 336 ILE E 356 SER E 359
SITE 3 AC3 14 ILE E 361 TYR E 373 HIS E 451 MET E 454
SITE 4 AC3 14 LEU E 455 TRP E 458
SITE 1 AC4 12 LEU G 291 MET G 294 HIS G 298 MET G 332
SITE 2 AC4 12 PHE G 333 SER G 336 ILE G 356 TYR G 373
SITE 3 AC4 12 HIS G 451 MET G 454 LEU G 455 TRP G 458
CRYST1 55.414 183.879 55.787 90.00 98.36 90.00 P 1 21 1 8
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 0.018046 0.000000 0.002652 0.00000
SCALE2 0.000000 0.005438 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018118 0.00000
(ATOM LINES ARE NOT SHOWN.)
END