HEADER SIGNALING PROTEIN 13-JAN-16 5HJS
TITLE IDENTIFICATION OF LXRBETA SELECTIVE AGONISTS FOR THE TREATMENT OF
TITLE 2 ALZHEIMER'S DISEASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXYSTEROLS RECEPTOR LXR-ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LIVER X RECEPTOR ALPHA,NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H
COMPND 5 MEMBER 3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;
COMPND 9 CHAIN: C, D;
COMPND 10 SYNONYM: NCOA-1,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74,BHLHE74,
COMPND 11 PROTEIN HIN-2,RIP160,RENAL CARCINOMA ANTIGEN NY-REN-52,STEROID
COMPND 12 RECEPTOR COACTIVATOR 1,SRC-1;
COMPND 13 EC: 2.3.1.48;
COMPND 14 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: NR1H3, LXRA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS AGONIST, ALZHEIMER'S, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PARTHASARATHY,D.KLEIN
REVDAT 4 06-MAR-24 5HJS 1 JRNL REMARK
REVDAT 3 27-APR-16 5HJS 1 JRNL
REVDAT 2 20-APR-16 5HJS 1 JRNL
REVDAT 1 06-APR-16 5HJS 0
JRNL AUTH S.J.STACHEL,C.ZERBINATTI,M.T.RUDD,M.COSDEN,S.SUON,K.K.NANDA,
JRNL AUTH 2 K.WESSNER,J.DIMUZIO,J.MAXWELL,Z.WU,J.M.USLANER,M.S.MICHENER,
JRNL AUTH 3 P.SZCZERBA,E.BRNARDIC,V.RADA,Y.KIM,R.MEISSNER,P.WUELFING,
JRNL AUTH 4 Y.YUAN,J.BALLARD,M.HOLAHAN,D.J.KLEIN,J.LU,X.FRADERA,
JRNL AUTH 5 G.PARTHASARATHY,V.N.UEBELE,Z.CHEN,Y.LI,J.LI,A.J.COOKE,
JRNL AUTH 6 D.J.BENNETT,M.T.BILODEAU,J.RENGER
JRNL TITL IDENTIFICATION AND IN VIVO EVALUATION OF LIVER X RECEPTOR
JRNL TITL 2 BETA-SELECTIVE AGONISTS FOR THE POTENTIAL TREATMENT OF
JRNL TITL 3 ALZHEIMER'S DISEASE.
JRNL REF J.MED.CHEM. V. 59 3489 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 27011007
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00176
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.11.5
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) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 78.4
REMARK 3 NUMBER OF REFLECTIONS : 61100
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 3104
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) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.43
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 715
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3588
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 681
REMARK 3 BIN R VALUE (WORKING SET) : 0.3596
REMARK 3 BIN FREE R VALUE : 0.3417
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.76
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 34
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 : 3950
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 328
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18900
REMARK 3 B22 (A**2) : -0.18900
REMARK 3 B33 (A**2) : 0.37800
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) : 0.234
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.126
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.120
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.123
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.119
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 : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4120 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5579 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1497 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 111 ; 8.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 601 ; 8.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4120 ; 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 : 519 ; 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 : 5030 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.96
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.14
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 5HJS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217149.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61151
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 63.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.6
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: NULL
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG MME 2000, 0.1M AMMONIUM
REMARK 280 SULFATE, 0.1M TRIS BUFFER PH 7.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
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 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 62.50350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.50350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.50350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.50350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.50350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.50350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.50350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.50350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 C 101 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 499 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 511 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 LYS A 2
REMARK 465 HIS A 3
REMARK 465 GLN A 4
REMARK 465 HIS A 5
REMARK 465 GLN A 6
REMARK 465 HIS A 7
REMARK 465 GLN A 8
REMARK 465 HIS A 9
REMARK 465 GLN A 10
REMARK 465 HIS A 11
REMARK 465 GLN A 12
REMARK 465 HIS A 13
REMARK 465 GLN A 14
REMARK 465 GLN A 15
REMARK 465 PRO A 16
REMARK 465 LEU A 17
REMARK 465 GLN A 18
REMARK 465 GLU A 19
REMARK 465 GLU A 20
REMARK 465 GLU A 21
REMARK 465 GLN A 22
REMARK 465 ALA A 23
REMARK 465 HIS A 24
REMARK 465 ALA A 25
REMARK 465 THR A 26
REMARK 465 SER A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 PRO A 30
REMARK 465 ARG A 31
REMARK 465 ALA A 32
REMARK 465 SER A 33
REMARK 465 SER A 34
REMARK 465 PRO A 35
REMARK 465 PRO A 36
REMARK 465 GLN A 37
REMARK 465 ILE A 38
REMARK 465 LEU A 39
REMARK 465 PRO A 40
REMARK 465 GLN A 59
REMARK 465 CYS A 60
REMARK 465 ASN A 61
REMARK 465 ARG A 62
REMARK 465 ARG A 63
REMARK 465 SER A 64
REMARK 465 PHE A 65
REMARK 465 SER A 66
REMARK 465 ASP A 67
REMARK 465 ARG A 68
REMARK 465 MET A 76
REMARK 465 ALA A 77
REMARK 465 PRO A 78
REMARK 465 ASP A 79
REMARK 465 PRO A 80
REMARK 465 HIS A 81
REMARK 465 GLU A 283
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 HIS B 3
REMARK 465 GLN B 4
REMARK 465 HIS B 5
REMARK 465 GLN B 6
REMARK 465 HIS B 7
REMARK 465 GLN B 8
REMARK 465 HIS B 9
REMARK 465 GLN B 10
REMARK 465 HIS B 11
REMARK 465 GLN B 12
REMARK 465 HIS B 13
REMARK 465 GLN B 14
REMARK 465 GLN B 15
REMARK 465 PRO B 16
REMARK 465 LEU B 17
REMARK 465 GLN B 18
REMARK 465 GLU B 19
REMARK 465 GLU B 20
REMARK 465 GLU B 21
REMARK 465 GLN B 22
REMARK 465 ALA B 23
REMARK 465 HIS B 24
REMARK 465 ALA B 25
REMARK 465 THR B 26
REMARK 465 SER B 27
REMARK 465 LEU B 28
REMARK 465 PRO B 29
REMARK 465 PRO B 30
REMARK 465 ARG B 31
REMARK 465 ALA B 32
REMARK 465 SER B 33
REMARK 465 SER B 34
REMARK 465 PRO B 35
REMARK 465 PRO B 36
REMARK 465 GLN B 37
REMARK 465 ILE B 38
REMARK 465 LEU B 39
REMARK 465 PRO B 40
REMARK 465 GLN B 59
REMARK 465 CYS B 60
REMARK 465 ASN B 61
REMARK 465 ARG B 62
REMARK 465 ARG B 63
REMARK 465 SER B 64
REMARK 465 PHE B 65
REMARK 465 SER B 66
REMARK 465 ASP B 67
REMARK 465 ARG B 68
REMARK 465 MET B 76
REMARK 465 ALA B 77
REMARK 465 PRO B 78
REMARK 465 ASP B 79
REMARK 465 PRO B 80
REMARK 465 HIS B 81
REMARK 465 GLU B 283
REMARK 465 CYS C -9
REMARK 465 PRO C -8
REMARK 465 SER C -7
REMARK 465 SER C -6
REMARK 465 HIS C -5
REMARK 465 SER C -4
REMARK 465 GLY C 12
REMARK 465 SER C 13
REMARK 465 PRO C 14
REMARK 465 SER C 15
REMARK 465 CYS D -9
REMARK 465 PRO D -8
REMARK 465 SER D -7
REMARK 465 SER D -6
REMARK 465 HIS D -5
REMARK 465 SER D -4
REMARK 465 GLY D 12
REMARK 465 SER D 13
REMARK 465 PRO D 14
REMARK 465 SER D 15
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 ARG A 70 73.62 -101.30
REMARK 500 LYS A 153 19.73 48.93
REMARK 500 ASP A 154 -62.76 -147.98
REMARK 500 PHE A 155 94.05 -60.78
REMARK 500 LYS B 153 -9.63 59.29
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 B 563 DISTANCE = 7.01 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 668 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 668 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HJP RELATED DB: PDB
DBREF 5HJS A 18 283 UNP Q13133 NR1H3_HUMAN 182 447
DBREF 5HJS B 18 283 UNP Q13133 NR1H3_HUMAN 182 447
DBREF 5HJS C -9 15 UNP Q15788 NCOA1_HUMAN 676 700
DBREF 5HJS D -9 15 UNP Q15788 NCOA1_HUMAN 676 700
SEQADV 5HJS MET A 1 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS LYS A 2 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS A 3 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN A 4 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS A 5 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN A 6 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS A 7 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN A 8 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS A 9 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN A 10 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS A 11 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN A 12 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS A 13 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN A 14 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN A 15 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS PRO A 16 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS LEU A 17 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS MET B 1 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS LYS B 2 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS B 3 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN B 4 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS B 5 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN B 6 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS B 7 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN B 8 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS B 9 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN B 10 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS B 11 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN B 12 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS HIS B 13 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN B 14 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS GLN B 15 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS PRO B 16 UNP Q13133 EXPRESSION TAG
SEQADV 5HJS LEU B 17 UNP Q13133 EXPRESSION TAG
SEQRES 1 A 283 MET LYS HIS GLN HIS GLN HIS GLN HIS GLN HIS GLN HIS
SEQRES 2 A 283 GLN GLN PRO LEU GLN GLU GLU GLU GLN ALA HIS ALA THR
SEQRES 3 A 283 SER LEU PRO PRO ARG ALA SER SER PRO PRO GLN ILE LEU
SEQRES 4 A 283 PRO GLN LEU SER PRO GLU GLN LEU GLY MET ILE GLU LYS
SEQRES 5 A 283 LEU VAL ALA ALA GLN GLN GLN CYS ASN ARG ARG SER PHE
SEQRES 6 A 283 SER ASP ARG LEU ARG VAL THR PRO TRP PRO MET ALA PRO
SEQRES 7 A 283 ASP PRO HIS SER ARG GLU ALA ARG GLN GLN ARG PHE ALA
SEQRES 8 A 283 HIS PHE THR GLU LEU ALA ILE VAL SER VAL GLN GLU ILE
SEQRES 9 A 283 VAL ASP PHE ALA LYS GLN LEU PRO GLY PHE LEU GLN LEU
SEQRES 10 A 283 SER ARG GLU ASP GLN ILE ALA LEU LEU LYS THR SER ALA
SEQRES 11 A 283 ILE GLU VAL MET LEU LEU GLU THR SER ARG ARG TYR ASN
SEQRES 12 A 283 PRO GLY SER GLU SER ILE THR PHE LEU LYS ASP PHE SER
SEQRES 13 A 283 TYR ASN ARG GLU ASP PHE ALA LYS ALA GLY LEU GLN VAL
SEQRES 14 A 283 GLU PHE ILE ASN PRO ILE PHE GLU PHE SER ARG ALA MET
SEQRES 15 A 283 ASN GLU LEU GLN LEU ASN ASP ALA GLU PHE ALA LEU LEU
SEQRES 16 A 283 ILE ALA ILE SER ILE PHE SER ALA ASP ARG PRO ASN VAL
SEQRES 17 A 283 GLN ASP GLN LEU GLN VAL GLU ARG LEU GLN HIS THR TYR
SEQRES 18 A 283 VAL GLU ALA LEU HIS ALA TYR VAL SER ILE HIS HIS PRO
SEQRES 19 A 283 HIS ASP ARG LEU MET PHE PRO ARG MET LEU MET LYS LEU
SEQRES 20 A 283 VAL SER LEU ARG THR LEU SER SER VAL HIS SER GLU GLN
SEQRES 21 A 283 VAL PHE ALA LEU ARG LEU GLN ASP LYS LYS LEU PRO PRO
SEQRES 22 A 283 LEU LEU SER GLU ILE TRP ASP VAL HIS GLU
SEQRES 1 B 283 MET LYS HIS GLN HIS GLN HIS GLN HIS GLN HIS GLN HIS
SEQRES 2 B 283 GLN GLN PRO LEU GLN GLU GLU GLU GLN ALA HIS ALA THR
SEQRES 3 B 283 SER LEU PRO PRO ARG ALA SER SER PRO PRO GLN ILE LEU
SEQRES 4 B 283 PRO GLN LEU SER PRO GLU GLN LEU GLY MET ILE GLU LYS
SEQRES 5 B 283 LEU VAL ALA ALA GLN GLN GLN CYS ASN ARG ARG SER PHE
SEQRES 6 B 283 SER ASP ARG LEU ARG VAL THR PRO TRP PRO MET ALA PRO
SEQRES 7 B 283 ASP PRO HIS SER ARG GLU ALA ARG GLN GLN ARG PHE ALA
SEQRES 8 B 283 HIS PHE THR GLU LEU ALA ILE VAL SER VAL GLN GLU ILE
SEQRES 9 B 283 VAL ASP PHE ALA LYS GLN LEU PRO GLY PHE LEU GLN LEU
SEQRES 10 B 283 SER ARG GLU ASP GLN ILE ALA LEU LEU LYS THR SER ALA
SEQRES 11 B 283 ILE GLU VAL MET LEU LEU GLU THR SER ARG ARG TYR ASN
SEQRES 12 B 283 PRO GLY SER GLU SER ILE THR PHE LEU LYS ASP PHE SER
SEQRES 13 B 283 TYR ASN ARG GLU ASP PHE ALA LYS ALA GLY LEU GLN VAL
SEQRES 14 B 283 GLU PHE ILE ASN PRO ILE PHE GLU PHE SER ARG ALA MET
SEQRES 15 B 283 ASN GLU LEU GLN LEU ASN ASP ALA GLU PHE ALA LEU LEU
SEQRES 16 B 283 ILE ALA ILE SER ILE PHE SER ALA ASP ARG PRO ASN VAL
SEQRES 17 B 283 GLN ASP GLN LEU GLN VAL GLU ARG LEU GLN HIS THR TYR
SEQRES 18 B 283 VAL GLU ALA LEU HIS ALA TYR VAL SER ILE HIS HIS PRO
SEQRES 19 B 283 HIS ASP ARG LEU MET PHE PRO ARG MET LEU MET LYS LEU
SEQRES 20 B 283 VAL SER LEU ARG THR LEU SER SER VAL HIS SER GLU GLN
SEQRES 21 B 283 VAL PHE ALA LEU ARG LEU GLN ASP LYS LYS LEU PRO PRO
SEQRES 22 B 283 LEU LEU SER GLU ILE TRP ASP VAL HIS GLU
SEQRES 1 C 25 CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS
SEQRES 2 C 25 ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER
SEQRES 1 D 25 CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS
SEQRES 2 D 25 ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER
HET 668 A 301 35
HET 668 B 301 35
HET SO4 C 101 5
HET SO4 D 101 5
HETNAM 668 2-CHLORO-4-{1'-[(2R)-2-HYDROXY-3-METHYL-2-
HETNAM 2 668 (TRIFLUOROMETHYL)BUTANOYL]-4,4'-BIPIPERIDIN-1-YL}-N,N-
HETNAM 3 668 DIMETHYLBENZAMIDE
HETNAM SO4 SULFATE ION
FORMUL 5 668 2(C25 H35 CL F3 N3 O3)
FORMUL 7 SO4 2(O4 S 2-)
FORMUL 9 HOH *328(H2 O)
HELIX 1 AA1 SER A 43 GLN A 57 1 15
HELIX 2 AA2 ARG A 83 LYS A 109 1 27
HELIX 3 AA3 GLY A 113 LEU A 117 5 5
HELIX 4 AA4 SER A 118 ARG A 141 1 24
HELIX 5 AA5 ASN A 158 ALA A 165 1 8
HELIX 6 AA6 GLN A 168 GLN A 186 1 19
HELIX 7 AA7 ASN A 188 PHE A 201 1 14
HELIX 8 AA8 ASP A 210 HIS A 233 1 24
HELIX 9 AA9 LEU A 238 GLN A 267 1 30
HELIX 10 AB1 PRO A 272 ASP A 280 1 9
HELIX 11 AB2 SER B 43 GLN B 58 1 16
HELIX 12 AB3 ARG B 83 GLN B 110 1 28
HELIX 13 AB4 SER B 118 ARG B 140 1 23
HELIX 14 AB5 ASN B 158 ALA B 165 1 8
HELIX 15 AB6 GLN B 168 GLN B 186 1 19
HELIX 16 AB7 ASN B 188 PHE B 201 1 14
HELIX 17 AB8 ASP B 210 HIS B 233 1 24
HELIX 18 AB9 LEU B 238 GLN B 267 1 30
HELIX 19 AC1 PRO B 272 ASP B 280 1 9
HELIX 20 AC2 LEU C -2 ARG C 1 5 4
HELIX 21 AC3 HIS C 2 GLU C 11 1 10
HELIX 22 AC4 LEU D -2 HIS D 2 1 5
HELIX 23 AC5 HIS D 2 GLU D 11 1 10
SHEET 1 AA1 3 TYR A 142 ASN A 143 0
SHEET 2 AA1 3 SER A 148 PHE A 151 -1 O SER A 148 N ASN A 143
SHEET 3 AA1 3 PHE A 155 TYR A 157 -1 O PHE A 155 N PHE A 151
SHEET 1 AA2 3 TYR B 142 ASN B 143 0
SHEET 2 AA2 3 SER B 148 PHE B 151 -1 O SER B 148 N ASN B 143
SHEET 3 AA2 3 PHE B 155 TYR B 157 -1 O TYR B 157 N ILE B 149
SITE 1 AC1 17 PHE A 93 THR A 94 LEU A 96 ALA A 97
SITE 2 AC1 17 GLU A 103 MET A 134 THR A 138 ARG A 141
SITE 3 AC1 17 PHE A 151 LEU A 152 LEU A 167 PHE A 171
SITE 4 AC1 17 HIS A 257 GLN A 260 LEU A 264 LEU A 271
SITE 5 AC1 17 TRP A 279
SITE 1 AC2 16 PHE B 90 THR B 94 LEU B 96 GLU B 103
SITE 2 AC2 16 ILE B 131 MET B 134 THR B 138 ARG B 141
SITE 3 AC2 16 PHE B 151 LEU B 152 LEU B 167 HIS B 257
SITE 4 AC2 16 GLN B 260 LEU B 264 LEU B 271 TRP B 279
SITE 1 AC3 4 ARG A 119 HIS C 6 GLN C 10 HOH C 202
SITE 1 AC4 4 ARG B 119 HIS D 6 GLN D 10 HOH D 201
CRYST1 125.007 125.007 92.339 90.00 90.00 90.00 P 4 21 2 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 0.008000 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010830 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
