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Database: PDB
Entry: 5AVL
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Original site: 5AVL 
HEADER    TRANSCRIPTION                           17-JUN-15   5AVL              
TITLE     CRYSTAL STRUCTURE OF LXRALPHA IN COMPLEX WITH TERT-BUTYL BENZOATE     
TITLE    2 ANALOG, COMPOUND 32B                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OXYSTEROLS RECEPTOR LXR-ALPHA;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN, UNP RESIDUES 182-447;               
COMPND   5 SYNONYM: LIVER X RECEPTOR ALPHA,NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H 
COMPND   6 MEMBER 3;                                                            
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 676-700;                                      
COMPND  12 SYNONYM: NCOA-1,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74,BHLHE74,   
COMPND  13 PROTEIN HIN-2,RIP160,RENAL CARCINOMA ANTIGEN NY-REN-52,STEROID       
COMPND  14 RECEPTOR COACTIVATOR 1,SRC-1;                                        
COMPND  15 EC: 2.3.1.48;                                                        
COMPND  16 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
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    AGONIST, COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.MATSUI,H.HANZAWA,K.TAMAKI                                           
REVDAT   1   26-AUG-15 5AVL    0                                                
JRNL        AUTH   Y.MATSUI,T.YAMAGUCHI,T.YAMAZAKI,M.YOSHIDA,M.ARAI,N.TERASAKA, 
JRNL        AUTH 2 S.HONZUMI,K.WAKABAYASHI,S.HAYASHI,D.NAKAI,H.HANZAWA,K.TAMAKI 
JRNL        TITL   DISCOVERY AND STRUCTURE-GUIDED OPTIMIZATION OF TERT-BUTYL    
JRNL        TITL 2 6-(PHENOXYMETHYL)-3-(TRIFLUOROMETHYL)BENZOATES AS LIVER X    
JRNL        TITL 3 RECEPTOR AGONISTS                                            
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  25  3914 2015              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   26238323                                                     
JRNL        DOI    10.1016/J.BMCL.2015.07.047                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 8192                           
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.500                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 958                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 586                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1959                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 46                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31000                                              
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -0.63000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 4.786         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.353         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.245         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.657        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2036 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2754 ; 1.808 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   235 ; 5.379 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   102 ;40.965 ;23.922       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   365 ;19.283 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;19.686 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   306 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1570 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   204        A   447                          
REMARK   3    RESIDUE RANGE :   B   682        B   696                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.1546  23.6046   0.5354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2337 T22:   0.0505                                     
REMARK   3      T33:   0.0341 T12:  -0.0119                                     
REMARK   3      T13:   0.0052 T23:  -0.0324                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0719 L22:   1.6413                                     
REMARK   3      L33:   3.7629 L12:  -0.1529                                     
REMARK   3      L13:   0.1838 L23:  -1.2911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1094 S12:   0.2600 S13:  -0.1678                       
REMARK   3      S21:  -0.3478 S22:  -0.0264 S23:   0.0151                       
REMARK   3      S31:   0.7915 S32:  -0.0675 S33:  -0.0831                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5AVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1300000049.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5-8.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9195                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29500                            
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: CNS                                                   
REMARK 200 STARTING MODEL: 5AVI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG2000MME, AMMONIUM SULFATE, TRIS       
REMARK 280  -HCL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
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   SMTRY1   9  1.000000  0.000000  0.000000       62.45450            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       62.45450            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       45.96000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       62.45450            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       62.45450            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       45.96000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       62.45450            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       62.45450            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       45.96000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       62.45450            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       62.45450            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       45.96000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       62.45450            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       62.45450            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       45.96000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       62.45450            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       62.45450            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       45.96000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       62.45450            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       62.45450            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       45.96000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       62.45450            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       62.45450            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       45.96000            
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: 4980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     MET A   165                                                      
REMARK 465     LYS A   166                                                      
REMARK 465     HIS A   167                                                      
REMARK 465     GLN A   168                                                      
REMARK 465     HIS A   169                                                      
REMARK 465     GLN A   170                                                      
REMARK 465     HIS A   171                                                      
REMARK 465     GLN A   172                                                      
REMARK 465     HIS A   173                                                      
REMARK 465     GLN A   174                                                      
REMARK 465     HIS A   175                                                      
REMARK 465     GLN A   176                                                      
REMARK 465     HIS A   177                                                      
REMARK 465     GLN A   178                                                      
REMARK 465     GLN A   179                                                      
REMARK 465     PRO A   180                                                      
REMARK 465     LEU A   181                                                      
REMARK 465     GLN A   182                                                      
REMARK 465     GLU A   183                                                      
REMARK 465     GLU A   184                                                      
REMARK 465     GLU A   185                                                      
REMARK 465     GLN A   186                                                      
REMARK 465     ALA A   187                                                      
REMARK 465     HIS A   188                                                      
REMARK 465     ALA A   189                                                      
REMARK 465     THR A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     PRO A   193                                                      
REMARK 465     PRO A   194                                                      
REMARK 465     ARG A   195                                                      
REMARK 465     ALA A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     PRO A   199                                                      
REMARK 465     PRO A   200                                                      
REMARK 465     GLN A   201                                                      
REMARK 465     ILE A   202                                                      
REMARK 465     LEU A   203                                                      
REMARK 465     GLN A   223                                                      
REMARK 465     CYS A   224                                                      
REMARK 465     ASN A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     ARG A   227                                                      
REMARK 465     SER A   228                                                      
REMARK 465     PHE A   229                                                      
REMARK 465     SER A   230                                                      
REMARK 465     ASP A   231                                                      
REMARK 465     ARG A   232                                                      
REMARK 465     LEU A   233                                                      
REMARK 465     ARG A   234                                                      
REMARK 465     PRO A   239                                                      
REMARK 465     MET A   240                                                      
REMARK 465     ALA A   241                                                      
REMARK 465     PRO A   242                                                      
REMARK 465     ASP A   243                                                      
REMARK 465     PRO A   244                                                      
REMARK 465     HIS A   245                                                      
REMARK 465     SER A   246                                                      
REMARK 465     CYS B   676                                                      
REMARK 465     PRO B   677                                                      
REMARK 465     SER B   678                                                      
REMARK 465     SER B   679                                                      
REMARK 465     HIS B   680                                                      
REMARK 465     SER B   681                                                      
REMARK 465     GLY B   697                                                      
REMARK 465     SER B   698                                                      
REMARK 465     PRO B   699                                                      
REMARK 465     SER B   700                                                      
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    PRO A 237      173.12    -41.54                                   
REMARK 500    LYS A 317      -67.21     53.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4KQ A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5AVI   RELATED DB: PDB                                   
DBREF  5AVL A  182   447  UNP    Q13133   NR1H3_HUMAN    182    447             
DBREF  5AVL B  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
SEQADV 5AVL MET A  165  UNP  Q13133              INITIATING METHIONINE          
SEQADV 5AVL LYS A  166  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL HIS A  167  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL GLN A  168  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL HIS A  169  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL GLN A  170  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL HIS A  171  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL GLN A  172  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL HIS A  173  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL GLN A  174  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL HIS A  175  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL GLN A  176  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL HIS A  177  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL GLN A  178  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL GLN A  179  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL PRO A  180  UNP  Q13133              EXPRESSION TAG                 
SEQADV 5AVL LEU A  181  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   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 B   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
HET    4KQ  A 501      36                                                       
HETNAM     4KQ 2-[4-[4-[[2-[(2-METHYLPROPAN-2-YL)OXYCARBONYL]-3-                
HETNAM   2 4KQ  OXIDANYL-4-(TRIFLUOROMETHYL)                                    
HETNAM   3 4KQ  PHENYL]METHOXY]PHENYL]PHENYL]ETHANOIC ACID                      
FORMUL   3  4KQ    C27 H25 F3 O6                                                
FORMUL   4  HOH   *46(H2 O)                                                     
HELIX    1 AA1 SER A  207  GLN A  221  1                                  15    
HELIX    2 AA2 GLU A  248  GLN A  274  1                                  27    
HELIX    3 AA3 GLY A  277  LEU A  281  5                                   5    
HELIX    4 AA4 SER A  282  ARG A  305  1                                  24    
HELIX    5 AA5 ARG A  323  ALA A  329  1                                   7    
HELIX    6 AA6 GLN A  332  LEU A  349  1                                  18    
HELIX    7 AA7 ASN A  352  PHE A  365  1                                  14    
HELIX    8 AA8 ASP A  374  HIS A  397  1                                  24    
HELIX    9 AA9 LEU A  402  GLN A  431  1                                  30    
HELIX   10 AB1 PRO A  436  ASP A  444  1                                   9    
HELIX   11 AB2 LEU B  683  HIS B  687  1                                   5    
HELIX   12 AB3 HIS B  687  GLU B  696  1                                  10    
SHEET    1 AA1 3 TYR A 306  ASN A 307  0                                        
SHEET    2 AA1 3 SER A 312  THR A 314 -1  O  SER A 312   N  ASN A 307           
SHEET    3 AA1 3 SER A 320  ASN A 322 -1  O  TYR A 321   N  ILE A 313           
SITE     1 AC1 19 PHE A 254  PHE A 257  LEU A 260  ALA A 261                    
SITE     2 AC1 19 SER A 264  ILE A 295  LEU A 299  THR A 302                    
SITE     3 AC1 19 ARG A 305  PHE A 315  LEU A 316  LEU A 331                    
SITE     4 AC1 19 PHE A 335  ILE A 339  HIS A 421  GLN A 424                    
SITE     5 AC1 19 LEU A 428  LEU A 435  TRP A 443                               
CRYST1  124.909  124.909   91.920  90.00  90.00  90.00 I 4 2 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      0.008006  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008006  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010879        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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