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Database: PDB
Entry: 5HJS
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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   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                                                                             
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