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Database: PDB
Entry: 3BEJ
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Original site: 3BEJ 
HEADER    TRANSCRIPTION REGULATOR                 19-NOV-07   3BEJ              
TITLE     STRUCTURE OF HUMAN FXR IN COMPLEX WITH MFA-1 AND CO-ACTIVATOR PEPTIDE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BILE ACID RECEPTOR;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 249-486;                                          
COMPND   5 SYNONYM: FARNESOID X-ACTIVATED RECEPTOR, FARNESOL RECEPTOR HRR-1,    
COMPND   6 NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H MEMBER 4, RETINOID X RECEPTOR-  
COMPND   7 INTERACTING PROTEIN 14, RXR-INTERACTING PROTEIN 14;                  
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND  11 CHAIN: E, F;                                                         
COMPND  12 FRAGMENT: RESIDUES 676-700;                                          
COMPND  13 SYNONYM: NCOA-1, STEROID RECEPTOR COACTIVATOR 1, SRC-1, RIP160,      
COMPND  14 PROTEIN HIN-2, RENAL CARCINOMA ANTIGEN NY-REN-52;                    
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NR1H4, BAR, FXR, HRR1, RIP14;                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX-KG;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: NCOA1, SRC1;                                                   
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX-KG                               
KEYWDS    FXR, BAR, NR1H4, BILE ACID RECEPTOR, NHR, NUCLEAR RECEPTOR,           
KEYWDS   2 ACTIVATOR, ALTERNATIVE SPLICING, DNA-BINDING, METAL-BINDING,         
KEYWDS   3 NUCLEUS, REPRESSOR, TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC,   
KEYWDS   4 ZINC-FINGER, ACYLTRANSFERASE, CHROMOSOMAL REARRANGEMENT,             
KEYWDS   5 PHOSPHOPROTEIN, POLYMORPHISM, PROTO-ONCOGENE, TRANSFERASE, UBL       
KEYWDS   6 CONJUGATION, TRANSCRIPTION-TRANSFERASE COMPLEX, TRANSCRIPTION        
KEYWDS   7 REGULATOR                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.SOISSON,G.PARTHASARATHY,J.W.BECKER                                
REVDAT   6   31-JUL-19 3BEJ    1       COMPND REMARK                            
REVDAT   5   24-JAN-18 3BEJ    1       AUTHOR                                   
REVDAT   4   25-OCT-17 3BEJ    1       REMARK                                   
REVDAT   3   24-FEB-09 3BEJ    1       VERSN                                    
REVDAT   2   29-APR-08 3BEJ    1       JRNL                                     
REVDAT   1   18-MAR-08 3BEJ    0                                                
JRNL        AUTH   S.M.SOISSON,G.PARTHASARATHY,A.D.ADAMS,S.SAHOO,A.SITLANI,     
JRNL        AUTH 2 C.SPARROW,J.CUI,J.W.BECKER                                   
JRNL        TITL   IDENTIFICATION OF A POTENT SYNTHETIC FXR AGONIST WITH AN     
JRNL        TITL 2 UNEXPECTED MODE OF BINDING AND ACTIVATION.                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  5337 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18391212                                                     
JRNL        DOI    10.1073/PNAS.0710981105                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 41792                          
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)  : 0.203                          
REMARK   3   R VALUE            (WORKING SET)  : 0.200                          
REMARK   3   FREE R VALUE                      : 0.254                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.020                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1997                           
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               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.90                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.01                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.35                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 6106                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2240                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 5809                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2210                   
REMARK   3   BIN FREE R VALUE                        : 0.2840                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.86                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 297                      
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            : 3923                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 362                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.86200                                             
REMARK   3    B22 (A**2) : 1.68300                                              
REMARK   3    B33 (A**2) : 5.17900                                              
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) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4096   ; 2.000  ; NULL                
REMARK   3    BOND ANGLES               : 5522   ; 2.000  ; NULL                
REMARK   3    TORSION ANGLES            : 874    ; 0.000  ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : 129    ; 8.000  ; NULL                
REMARK   3    GENERAL PLANES            : 610    ; 8.000  ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : 4026   ; 20.000 ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : 169    ; 5.000  ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
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   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.011                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.27                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
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 3BEJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045420.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98793, 0.97931, 0.97907,         
REMARK 200                                   0.96863                            
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41792                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-22% PEG3350, 0.1M BIS-TRIS, 4 MM      
REMARK 280  YCL(3), 0.2M AMMONIUM ACETATE, 1 MM DTT. PROTEIN WAS                
REMARK 280  CARBOXYMETHYLATED WITH IODOACETIC ACID, PH 6.5, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.82100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.82550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.44450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.82550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.82100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.44450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     THR A   235                                                      
REMARK 465     THR A   236                                                      
REMARK 465     LYS A   237                                                      
REMARK 465     SER A   238                                                      
REMARK 465     CYS A   239                                                      
REMARK 465     ARG A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     LYS A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     PRO A   341                                                      
REMARK 465     SER A   342                                                      
REMARK 465     GLN A   472                                                      
REMARK 465     THR B   235                                                      
REMARK 465     THR B   236                                                      
REMARK 465     LYS B   237                                                      
REMARK 465     SER B   238                                                      
REMARK 465     CYS B   239                                                      
REMARK 465     ARG B   240                                                      
REMARK 465     GLU B   241                                                      
REMARK 465     LYS B   242                                                      
REMARK 465     THR B   243                                                      
REMARK 465     GLN B   472                                                      
REMARK 465     CYS E   676                                                      
REMARK 465     PRO E   677                                                      
REMARK 465     SER E   678                                                      
REMARK 465     SER E   679                                                      
REMARK 465     HIS E   680                                                      
REMARK 465     SER E   681                                                      
REMARK 465     SER E   682                                                      
REMARK 465     LEU E   683                                                      
REMARK 465     THR E   684                                                      
REMARK 465     GLU E   696                                                      
REMARK 465     GLY E   697                                                      
REMARK 465     SER E   698                                                      
REMARK 465     PRO E   699                                                      
REMARK 465     SER E   700                                                      
REMARK 465     CYS F   676                                                      
REMARK 465     PRO F   677                                                      
REMARK 465     SER F   678                                                      
REMARK 465     SER F   679                                                      
REMARK 465     HIS F   680                                                      
REMARK 465     SER F   681                                                      
REMARK 465     SER F   682                                                      
REMARK 465     LEU F   683                                                      
REMARK 465     GLU F   696                                                      
REMARK 465     GLY F   697                                                      
REMARK 465     SER F   698                                                      
REMARK 465     PRO F   699                                                      
REMARK 465     SER F   700                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   Y    YT3 A     1     O    HOH A   603              1.93            
REMARK 500   O    HOH B   590     O    HOH B   774              2.01            
REMARK 500   Y    YT3 B     2     O    HOH B   765              2.12            
REMARK 500   O    HOH A   514     O    HOH A   615              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLN A 309       27.97    -67.68                                   
REMARK 500    ASP A 312      105.56    -46.85                                   
REMARK 500    HIS A 313       51.47    -50.18                                   
REMARK 500    GLU A 314      -36.13   -171.94                                   
REMARK 500    HIS A 344      -52.07     66.20                                   
REMARK 500    LEU A 391       36.67    -83.34                                   
REMARK 500    TYR A 397       34.96    -90.70                                   
REMARK 500    GLN A 423       58.41   -146.89                                   
REMARK 500    PHE A 461      -79.12    -84.59                                   
REMARK 500    THR A 462      145.99    160.92                                   
REMARK 500    LEU B 391       41.73    -86.08                                   
REMARK 500    HIS B 422     -179.49    167.30                                   
REMARK 500    GLN B 423     -118.73    -78.44                                   
REMARK 500    GLU B 425      -71.02    132.12                                   
REMARK 500    ASN B 426       82.86     45.22                                   
REMARK 500    ASP B 470       56.72     35.76                                   
REMARK 500    ARG E 686      -49.06     93.04                                   
REMARK 500    ARG E 692      -91.13    -53.82                                   
REMARK 500    LEU E 693       -7.85    -44.45                                   
REMARK 500    GLU F 685      110.73    -33.13                                   
REMARK 500    ARG F 686      -35.22     68.44                                   
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 715        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH B 721        DISTANCE =  7.09 ANGSTROMS                       
REMARK 525    HOH B 730        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH B 756        DISTANCE =  9.19 ANGSTROMS                       
REMARK 525    HOH B 761        DISTANCE =  5.96 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MUF A 473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MUF B 1                   
DBREF  3BEJ A  235   472  UNP    Q96RI1   NR1H4_HUMAN    249    486             
DBREF  3BEJ B  235   472  UNP    Q96RI1   NR1H4_HUMAN    249    486             
DBREF  3BEJ E  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
DBREF  3BEJ F  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
SEQRES   1 A  238  THR THR LYS SER CYS ARG GLU LYS THR GLU LEU THR PRO          
SEQRES   2 A  238  ASP GLN GLN THR LEU LEU HIS PHE ILE MET ASP SER TYR          
SEQRES   3 A  238  ASN LYS GLN ARG MET PRO GLN GLU ILE THR ASN LYS ILE          
SEQRES   4 A  238  LEU LYS GLU GLU PHE SER ALA GLU GLU ASN PHE LEU ILE          
SEQRES   5 A  238  LEU THR GLU MET ALA THR ASN HIS VAL GLN VAL LEU VAL          
SEQRES   6 A  238  GLU PHE THR LYS LYS LEU PRO GLY PHE GLN THR LEU ASP          
SEQRES   7 A  238  HIS GLU ASP GLN ILE ALA LEU LEU LYS GLY SER ALA VAL          
SEQRES   8 A  238  GLU ALA MET PHE LEU ARG SER ALA GLU ILE PHE ASN LYS          
SEQRES   9 A  238  LYS LEU PRO SER GLY HIS SER ASP LEU LEU GLU GLU ARG          
SEQRES  10 A  238  ILE ARG ASN SER GLY ILE SER ASP GLU TYR ILE THR PRO          
SEQRES  11 A  238  MET PHE SER PHE TYR LYS SER ILE GLY GLU LEU LYS MET          
SEQRES  12 A  238  THR GLN GLU GLU TYR ALA LEU LEU THR ALA ILE VAL ILE          
SEQRES  13 A  238  LEU SER PRO ASP ARG GLN TYR ILE LYS ASP ARG GLU ALA          
SEQRES  14 A  238  VAL GLU LYS LEU GLN GLU PRO LEU LEU ASP VAL LEU GLN          
SEQRES  15 A  238  LYS LEU CYS LYS ILE HIS GLN PRO GLU ASN PRO GLN HIS          
SEQRES  16 A  238  PHE ALA CYS LEU LEU GLY ARG LEU THR GLU LEU ARG THR          
SEQRES  17 A  238  PHE ASN HIS HIS HIS ALA GLU MET LEU MET SER TRP ARG          
SEQRES  18 A  238  VAL ASN ASP HIS LYS PHE THR PRO LEU LEU CYS GLU ILE          
SEQRES  19 A  238  TRP ASP VAL GLN                                              
SEQRES   1 B  238  THR THR LYS SER CYS ARG GLU LYS THR GLU LEU THR PRO          
SEQRES   2 B  238  ASP GLN GLN THR LEU LEU HIS PHE ILE MET ASP SER TYR          
SEQRES   3 B  238  ASN LYS GLN ARG MET PRO GLN GLU ILE THR ASN LYS ILE          
SEQRES   4 B  238  LEU LYS GLU GLU PHE SER ALA GLU GLU ASN PHE LEU ILE          
SEQRES   5 B  238  LEU THR GLU MET ALA THR ASN HIS VAL GLN VAL LEU VAL          
SEQRES   6 B  238  GLU PHE THR LYS LYS LEU PRO GLY PHE GLN THR LEU ASP          
SEQRES   7 B  238  HIS GLU ASP GLN ILE ALA LEU LEU LYS GLY SER ALA VAL          
SEQRES   8 B  238  GLU ALA MET PHE LEU ARG SER ALA GLU ILE PHE ASN LYS          
SEQRES   9 B  238  LYS LEU PRO SER GLY HIS SER ASP LEU LEU GLU GLU ARG          
SEQRES  10 B  238  ILE ARG ASN SER GLY ILE SER ASP GLU TYR ILE THR PRO          
SEQRES  11 B  238  MET PHE SER PHE TYR LYS SER ILE GLY GLU LEU LYS MET          
SEQRES  12 B  238  THR GLN GLU GLU TYR ALA LEU LEU THR ALA ILE VAL ILE          
SEQRES  13 B  238  LEU SER PRO ASP ARG GLN TYR ILE LYS ASP ARG GLU ALA          
SEQRES  14 B  238  VAL GLU LYS LEU GLN GLU PRO LEU LEU ASP VAL LEU GLN          
SEQRES  15 B  238  LYS LEU CYS LYS ILE HIS GLN PRO GLU ASN PRO GLN HIS          
SEQRES  16 B  238  PHE ALA CYS LEU LEU GLY ARG LEU THR GLU LEU ARG THR          
SEQRES  17 B  238  PHE ASN HIS HIS HIS ALA GLU MET LEU MET SER TRP ARG          
SEQRES  18 B  238  VAL ASN ASP HIS LYS PHE THR PRO LEU LEU CYS GLU ILE          
SEQRES  19 B  238  TRP ASP VAL GLN                                              
SEQRES   1 E   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 E   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
SEQRES   1 F   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 F   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
HET    YT3  A   1       1                                                       
HET    MUF  A 473      31                                                       
HET    YT3  B   2       1                                                       
HET    MUF  B   1      31                                                       
HETNAM     YT3 YTTRIUM (III) ION                                                
HETNAM     MUF (8ALPHA,10ALPHA,13ALPHA,17BETA)-17-[(4-HYDROXYPHENYL)            
HETNAM   2 MUF  CARBONYL]ANDROSTA-3,5-DIENE-3-CARBOXYLIC ACID                   
FORMUL   5  YT3    2(Y 3+)                                                      
FORMUL   6  MUF    2(C27 H32 O4)                                                
FORMUL   9  HOH   *362(H2 O)                                                    
HELIX    1   1 THR A  246  ASN A  261  1                                  16    
HELIX    2   2 PRO A  266  GLU A  276  1                                  11    
HELIX    3   3 SER A  279  LEU A  305  1                                  27    
HELIX    4   4 GLY A  307  LEU A  311  5                                   5    
HELIX    5   5 GLU A  314  LYS A  339  1                                  26    
HELIX    6   6 HIS A  344  ARG A  353  1                                  10    
HELIX    7   7 SER A  358  GLU A  374  1                                  17    
HELIX    8   8 THR A  378  LEU A  391  1                                  14    
HELIX    9   9 ASP A  400  GLN A  423  1                                  24    
HELIX   10  10 GLN A  428  THR A  442  1                                  15    
HELIX   11  11 THR A  442  ASN A  457  1                                  16    
HELIX   12  12 THR A  462  ASP A  470  1                                   9    
HELIX   13  13 THR B  246  TYR B  260  1                                  15    
HELIX   14  14 PRO B  266  GLU B  276  1                                  11    
HELIX   15  15 SER B  279  LYS B  304  1                                  26    
HELIX   16  16 GLY B  307  LEU B  311  5                                   5    
HELIX   17  17 ASP B  312  ASN B  337  1                                  26    
HELIX   18  18 SER B  345  ARG B  353  1                                   9    
HELIX   19  19 SER B  358  LEU B  375  1                                  18    
HELIX   20  20 THR B  378  LEU B  391  1                                  14    
HELIX   21  21 ASP B  400  LYS B  420  1                                  21    
HELIX   22  22 GLN B  428  ASN B  457  1                                  30    
HELIX   23  23 THR B  462  TRP B  469  1                                   8    
HELIX   24  24 HIS E  687  LEU E  694  1                                   8    
HELIX   25  25 HIS F  687  GLN F  695  1                                   9    
CISPEP   1 LEU B  340    PRO B  341          0        -2.46                     
CISPEP   2 GLU E  685    ARG E  686          0         7.81                     
CISPEP   3 GLU F  685    ARG F  686          0        -2.18                     
SITE     1 AC1  8 ASP A 359  GLU A 360  HOH A 474  HOH A 475                    
SITE     2 AC1  8 HOH A 499  HOH A 514  HOH A 603  HOH B 734                    
SITE     1 AC2  8 HOH A 603  ASP B 359  GLU B 360  HOH B 569                    
SITE     2 AC2  8 HOH B 576  HOH B 590  HOH B 734  HOH B 765                    
SITE     1 AC3 17 MET A 265  PHE A 284  LEU A 287  THR A 288                    
SITE     2 AC3 17 MET A 290  MET A 328  ARG A 331  SER A 332                    
SITE     3 AC3 17 ILE A 335  LEU A 348  HIS A 447  TRP A 454                    
SITE     4 AC3 17 PHE A 461  TRP A 469  HOH A 485  HOH A 508                    
SITE     5 AC3 17 HOH A 570                                                     
SITE     1 AC4 17 MET B 265  PHE B 284  LEU B 287  THR B 288                    
SITE     2 AC4 17 MET B 328  PHE B 329  ARG B 331  SER B 332                    
SITE     3 AC4 17 ILE B 335  HIS B 447  MET B 450  TRP B 454                    
SITE     4 AC4 17 PHE B 461  TRP B 469  HOH B 595  HOH B 623                    
SITE     5 AC4 17 HOH B 733                                                     
CRYST1   41.642   90.889  129.651  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024014  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011002  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007713        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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