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Database: PDB
Entry: 3RVF
LinkDB: 3RVF
Original site: 3RVF 
HEADER    TRANSCRIPTION REGULATOR                 06-MAY-11   3RVF              
TITLE     FXR WITH SRC1 AND GSK2034                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BILE ACID RECEPTOR;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 257-486);              
COMPND   5 SYNONYM: FXR, FARNESOID X-ACTIVATED RECEPTOR, FARNESOL RECEPTOR HRR- 
COMPND   6 1, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP H MEMBER 4, RETINOID X         
COMPND   7 RECEPTOR-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: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 741-761;                                      
COMPND  13 SYNONYM: SRC1, NCOA-1, CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74,    
COMPND  14 BHLHE74, PROTEIN HIN-2, RIP160, RENAL CARCINOMA ANTIGEN NY-REN-52,   
COMPND  15 STEROID RECEPTOR COACTIVATOR 1;                                      
COMPND  16 EC: 2.3.1.48;                                                        
COMPND  17 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: BAR, FXR, HRR1, NR1H4, RIP14;                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSETA;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    NUCLEAR RECEPTOR, ALPHA-HELICAL SANDWICH, TRANSCRIPTION FACTOR, RXR,  
KEYWDS   2 TRANSCRIPTION CO-FACTORS, BILE ACID, FARNESOID, TRANSCRIPTION        
KEYWDS   3 REGULATOR                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.P.WILLIAMS,K.P.MADAUSS                                              
REVDAT   3   08-NOV-17 3RVF    1       REMARK                                   
REVDAT   2   05-OCT-11 3RVF    1       JRNL                                     
REVDAT   1   21-SEP-11 3RVF    0                                                
JRNL        AUTH   A.AKWABI-AMEYAW,J.A.CARAVELLA,L.CHEN,K.L.CREECH,D.N.DEATON,  
JRNL        AUTH 2 K.P.MADAUSS,H.B.MARR,A.B.MILLER,F.NAVAS,D.J.PARKS,           
JRNL        AUTH 3 P.K.SPEARING,D.TODD,S.P.WILLIAMS,G.B.WISELY                  
JRNL        TITL   CONFORMATIONALLY CONSTRAINED FARNESOID X RECEPTOR (FXR)      
JRNL        TITL 2 AGONISTS: ALTERNATIVE REPLACEMENTS OF THE STILBENE.          
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  21  6154 2011              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   21890356                                                     
JRNL        DOI    10.1016/J.BMCL.2011.08.034                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 6068                           
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 448                             
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 389                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 40                           
REMARK   3   BIN FREE R VALUE                    : 0.2520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1846                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.112         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.315         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.085        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.852                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1930 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1229 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2632 ; 1.084 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3008 ; 1.009 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   237 ; 4.448 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    82 ;37.845 ;24.390       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   304 ;20.843 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;18.488 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   304 ; 0.054 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2136 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   382 ; 0.002 ; 0.020       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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:                                           
REMARK   3  HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT                    
REMARK   3  U VALUES      : REFINED INDIVIDUALLY                                
REMARK   4                                                                      
REMARK   4 3RVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000065424.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-05                          
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) : 1.0                                
REMARK 200  MONOCHROMATOR                  : CRYSTAL                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6084                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.48900                            
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: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2 M LITHIUM SULFATE,      
REMARK 280  0.1 M BIS-TRIS, PH 6.5, HANGING DROP, TEMPERATURE 298K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3                            
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   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X,Y+1/2,Z+1/2                                           
REMARK 290      14555   -X,-Y+1/2,Z+1/2                                         
REMARK 290      15555   -X,Y+1/2,-Z+1/2                                         
REMARK 290      16555   X,-Y+1/2,-Z+1/2                                         
REMARK 290      17555   Z,X+1/2,Y+1/2                                           
REMARK 290      18555   Z,-X+1/2,-Y+1/2                                         
REMARK 290      19555   -Z,-X+1/2,Y+1/2                                         
REMARK 290      20555   -Z,X+1/2,-Y+1/2                                         
REMARK 290      21555   Y,Z+1/2,X+1/2                                           
REMARK 290      22555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      23555   Y,-Z+1/2,-X+1/2                                         
REMARK 290      24555   -Y,-Z+1/2,X+1/2                                         
REMARK 290      25555   X+1/2,Y,Z+1/2                                           
REMARK 290      26555   -X+1/2,-Y,Z+1/2                                         
REMARK 290      27555   -X+1/2,Y,-Z+1/2                                         
REMARK 290      28555   X+1/2,-Y,-Z+1/2                                         
REMARK 290      29555   Z+1/2,X,Y+1/2                                           
REMARK 290      30555   Z+1/2,-X,-Y+1/2                                         
REMARK 290      31555   -Z+1/2,-X,Y+1/2                                         
REMARK 290      32555   -Z+1/2,X,-Y+1/2                                         
REMARK 290      33555   Y+1/2,Z,X+1/2                                           
REMARK 290      34555   -Y+1/2,Z,-X+1/2                                         
REMARK 290      35555   Y+1/2,-Z,-X+1/2                                         
REMARK 290      36555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      37555   X+1/2,Y+1/2,Z                                           
REMARK 290      38555   -X+1/2,-Y+1/2,Z                                         
REMARK 290      39555   -X+1/2,Y+1/2,-Z                                         
REMARK 290      40555   X+1/2,-Y+1/2,-Z                                         
REMARK 290      41555   Z+1/2,X+1/2,Y                                           
REMARK 290      42555   Z+1/2,-X+1/2,-Y                                         
REMARK 290      43555   -Z+1/2,-X+1/2,Y                                         
REMARK 290      44555   -Z+1/2,X+1/2,-Y                                         
REMARK 290      45555   Y+1/2,Z+1/2,X                                           
REMARK 290      46555   -Y+1/2,Z+1/2,-X                                         
REMARK 290      47555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      48555   -Y+1/2,-Z+1/2,X                                         
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY1  25  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY2  25  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  25  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY1  26 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY2  26  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  26  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY1  27 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY2  27  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  27  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY1  28  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY2  28  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  28  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY1  29  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY2  29  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  29  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY1  30  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY2  30 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  30  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY1  31  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY2  31 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  31  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY1  32  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY2  32  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  32  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY1  33  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY2  33  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  33  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY1  34  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY2  34  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  34 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY1  35  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY2  35  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  35 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY1  36  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY2  36  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  36  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY1  37  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY2  37  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY3  37  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  38 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY2  38  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY3  38  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  39 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY2  39  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY3  39  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  40  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY2  40  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY3  40  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  41  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY2  41  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY3  41  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  42  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY2  42 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY3  42  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  43  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY2  43 -1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY3  43  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  44  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY2  44  1.000000  0.000000  0.000000       79.16550            
REMARK 290   SMTRY3  44  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  45  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY2  45  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY3  45  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  46  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY2  46  0.000000  0.000000  1.000000       79.16550            
REMARK 290   SMTRY3  46 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  47  0.000000  1.000000  0.000000       79.16550            
REMARK 290   SMTRY2  47  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY3  47 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  48  0.000000 -1.000000  0.000000       79.16550            
REMARK 290   SMTRY2  48  0.000000  0.000000 -1.000000       79.16550            
REMARK 290   SMTRY3  48  1.000000  0.000000  0.000000        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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   241                                                      
REMARK 465     SER A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     LYS B   741                                                      
REMARK 465     GLU B   742                                                      
REMARK 465     SER B   743                                                      
REMARK 465     LYS B   744                                                      
REMARK 465     ASP B   756                                                      
REMARK 465     GLU B   757                                                      
REMARK 465     LYS B   758                                                      
REMARK 465     ASP B   759                                                      
REMARK 465     LEU B   760                                                      
REMARK 465     ARG B   761                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A 245    CG   CD1  CD2                                       
REMARK 470     GLN A 249    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 250    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 255    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 258    CG   OD1  OD2                                       
REMARK 470     LYS A 262    CG   CD   CE   NZ                                   
REMARK 470     GLN A 263    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 268    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 277    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 281    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 303    CG   CD   CE   NZ                                   
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     LYS A 376    CG   CD   CE   NZ                                   
REMARK 470     ASP A 394    CG   OD1  OD2                                       
REMARK 470     LYS A 399    CG   CD   CE   NZ                                   
REMARK 470     GLU A 402    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 405    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 406    CG   CD   CE   NZ                                   
REMARK 470     GLU A 409    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 417    CG   CD   CE   NZ                                   
REMARK 470     LYS A 420    CG   CD   CE   NZ                                   
REMARK 470     ILE A 421    CG1  CG2  CD1                                       
REMARK 470     GLN A 423    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 425    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 460    CG   CD   CE   NZ                                   
REMARK 470     GLN A 472    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 745    CG   OD1  OD2                                       
REMARK 470     ARG B 750    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 755    CG   CD   CE   NZ                                   
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   NZ   LYS A   321     OD1  ASP A   470              2.14            
REMARK 500   O    LEU A   384     CD1  ILE A   388              2.17            
REMARK 500   NZ   LYS A   321     OD2  ASP A   470              2.18            
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    PHE A 461     -159.64    -97.19                                   
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 SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 034 A 473                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RUT   RELATED DB: PDB                                   
REMARK 900 FXR WITH SRC1 AND GSK359                                             
REMARK 900 RELATED ID: 3RUU   RELATED DB: PDB                                   
REMARK 900 FXR WITH SRC1 AND GSK237                                             
DBREF  3RVF A  243   472  UNP    Q96RI1   NR1H4_HUMAN    257    486             
DBREF  3RVF B  741   761  UNP    Q15788   NCOA1_HUMAN    741    761             
SEQADV 3RVF GLY A  241  UNP  Q96RI1              EXPRESSION TAG                 
SEQADV 3RVF SER A  242  UNP  Q96RI1              EXPRESSION TAG                 
SEQRES   1 A  232  GLY SER THR GLU LEU THR PRO ASP GLN GLN THR LEU LEU          
SEQRES   2 A  232  HIS PHE ILE MET ASP SER TYR ASN LYS GLN ARG MET PRO          
SEQRES   3 A  232  GLN GLU ILE THR ASN LYS ILE LEU LYS GLU GLU PHE SER          
SEQRES   4 A  232  ALA GLU GLU ASN PHE LEU ILE LEU THR GLU MET ALA THR          
SEQRES   5 A  232  ASN HIS VAL GLN VAL LEU VAL GLU PHE THR LYS LYS LEU          
SEQRES   6 A  232  PRO GLY PHE GLN THR LEU ASP HIS GLU ASP GLN ILE ALA          
SEQRES   7 A  232  LEU LEU LYS GLY SER ALA VAL GLU ALA MET PHE LEU ARG          
SEQRES   8 A  232  SER ALA GLU ILE PHE ASN LYS LYS LEU PRO SER GLY HIS          
SEQRES   9 A  232  SER ASP LEU LEU GLU GLU ARG ILE ARG ASN SER GLY ILE          
SEQRES  10 A  232  SER ASP GLU TYR ILE THR PRO MET PHE SER PHE TYR LYS          
SEQRES  11 A  232  SER ILE GLY GLU LEU LYS MET THR GLN GLU GLU TYR ALA          
SEQRES  12 A  232  LEU LEU THR ALA ILE VAL ILE LEU SER PRO ASP ARG GLN          
SEQRES  13 A  232  TYR ILE LYS ASP ARG GLU ALA VAL GLU LYS LEU GLN GLU          
SEQRES  14 A  232  PRO LEU LEU ASP VAL LEU GLN LYS LEU CYS LYS ILE HIS          
SEQRES  15 A  232  GLN PRO GLU ASN PRO GLN HIS PHE ALA CYS LEU LEU GLY          
SEQRES  16 A  232  ARG LEU THR GLU LEU ARG THR PHE ASN HIS HIS HIS ALA          
SEQRES  17 A  232  GLU MET LEU MET SER TRP ARG VAL ASN ASP HIS LYS PHE          
SEQRES  18 A  232  THR PRO LEU LEU CYS GLU ILE TRP ASP VAL GLN                  
SEQRES   1 B   21  LYS GLU SER LYS ASP HIS GLN LEU LEU ARG TYR LEU LEU          
SEQRES   2 B   21  ASP LYS ASP GLU LYS ASP LEU ARG                              
HET    SO4  A   1       5                                                       
HET    034  A 473      36                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     034 5-(4-{[3-(2,6-DICHLOROPHENYL)-5-(PROPAN-2-YL)-1,2-               
HETNAM   2 034  OXAZOL-4-YL]METHOXY}PHENYL)-1H-INDOLE-2-CARBOXYLIC              
HETNAM   3 034  ACID                                                            
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  034    C28 H22 CL2 N2 O4                                            
FORMUL   5  HOH   *2(H2 O)                                                      
HELIX    1   1 THR A  246  THR A  251  1                                   6    
HELIX    2   2 THR A  251  LYS A  262  1                                  12    
HELIX    3   3 PRO A  266  ASN A  271  1                                   6    
HELIX    4   4 ASN A  271  GLU A  276  1                                   6    
HELIX    5   5 SER A  279  LEU A  305  1                                  27    
HELIX    6   6 ASP A  312  LYS A  339  1                                  28    
HELIX    7   7 LEU A  340  GLY A  343  5                                   4    
HELIX    8   8 HIS A  344  ASN A  354  1                                  11    
HELIX    9   9 SER A  358  GLU A  374  1                                  17    
HELIX   10  10 THR A  378  LEU A  391  1                                  14    
HELIX   11  11 ASP A  400  GLN A  423  1                                  24    
HELIX   12  12 GLN A  428  ASN A  457  1                                  30    
HELIX   13  13 THR A  462  TRP A  469  1                                   8    
HELIX   14  14 HIS B  746  LYS B  755  1                                  10    
SITE     1 AC1  5 ASN A 271  LYS A 275  SER A 279  ALA A 280                    
SITE     2 AC1  5 ASN A 354                                                     
SITE     1 AC2 11 MET A 265  LEU A 287  THR A 288  ALA A 291                    
SITE     2 AC2 11 MET A 328  PHE A 329  ARG A 331  SER A 342                    
SITE     3 AC2 11 TYR A 369  HIS A 447  TRP A 454                               
CRYST1  158.331  158.331  158.331  90.00  90.00  90.00 F 2 3        48          
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      0.006316  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006316  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006316        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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