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Database: PDB
Entry: 3KMR
LinkDB: 3KMR
Original site: 3KMR 
HEADER    TRANSCRIPTION                           11-NOV-09   3KMR              
TITLE     CRYSTAL STRUCTURE OF RARALPHA LIGAND BINDING DOMAIN IN COMPLEX WITH AN
TITLE    2 AGONIST LIGAND (AM580) AND A COACTIVATOR FRAGMENT                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINOIC ACID RECEPTOR ALPHA;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUE 176-421);               
COMPND   5 SYNONYM: RAR-ALPHA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP B MEMBER 1;   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: NR INTERACTION MOTIF 2 (UNP RESIDUE 686-698);              
COMPND  11 SYNONYM: NCOA-1, STEROID RECEPTOR COACTIVATOR 1, SRC-1, RIP160,      
COMPND  12 PROTEIN HIN-2, RENAL CARCINOMA ANTIGEN NY-REN-52;                    
COMPND  13 EC: 2.3.1.48;                                                        
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NR1B1, RARA;                                                   
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: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHETIC                                             
KEYWDS    NUCLEAR RECEPTOR TRANSCRIPTION FACTOR LIGAND BINDING DOMAIN, DNA-     
KEYWDS   2 BINDING, METAL-BINDING, NUCLEUS, PHOSPHOPROTEIN, PROTO-ONCOGENE,     
KEYWDS   3 RECEPTOR, TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC-FINGER,      
KEYWDS   4 ACTIVATOR, ACYLTRANSFERASE, ISOPEPTIDE BOND, TRANSFERASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BOURGUET,C.TEYSSIER                                                 
REVDAT   3   14-JUL-10 3KMR    1       JRNL                                     
REVDAT   2   23-JUN-10 3KMR    1       JRNL                                     
REVDAT   1   02-JUN-10 3KMR    0                                                
JRNL        AUTH   A.LE MAIRE,C.TEYSSIER,C.ERB,M.GRIMALDI,S.ALVAREZ,            
JRNL        AUTH 2 A.R.DE LERA,P.BALAGUER,H.GRONEMEYER,C.A.ROYER,P.GERMAIN,     
JRNL        AUTH 3 W.BOURGUET                                                   
JRNL        TITL   A UNIQUE SECONDARY-STRUCTURE SWITCH CONTROLS CONSTITUTIVE    
JRNL        TITL 2 GENE REPRESSION BY RETINOIC ACID RECEPTOR.                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   801 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20543827                                                     
JRNL        DOI    10.1038/NSMB.1855                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0062                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 21452                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 720                             
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1205                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 40                           
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1937                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 121                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.43000                                             
REMARK   3    B22 (A**2) : 0.19000                                              
REMARK   3    B33 (A**2) : -0.21000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.84000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.147         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.423         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2000 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2707 ; 2.700 ; 2.014       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   244 ; 4.469 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    83 ;33.712 ;24.458       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   384 ;14.830 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;18.519 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   318 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1451 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1225 ; 0.490 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1994 ; 0.980 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   775 ; 1.750 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   712 ; 2.771 ; 4.500       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   182        A   415                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.2790  -0.2120 -13.8450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1174 T22:  -0.0273                                     
REMARK   3      T33:  -0.1778 T12:   0.0285                                     
REMARK   3      T13:   0.0157 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9204 L22:   1.1517                                     
REMARK   3      L33:   2.2730 L12:  -1.2056                                     
REMARK   3      L13:   1.1943 L23:  -0.4319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0076 S12:   0.2930 S13:   0.0291                       
REMARK   3      S21:  -0.0271 S22:  -0.0849 S23:   0.0439                       
REMARK   3      S31:  -0.2014 S32:   0.1784 S33:   0.0773                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   629        C   639                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.8070  -4.4300  -1.3720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0620 T22:   0.0799                                     
REMARK   3      T33:  -0.0381 T12:   0.0527                                     
REMARK   3      T13:   0.1129 T23:   0.0470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8708 L22:  24.5453                                     
REMARK   3      L33:  12.2324 L12:   1.4022                                     
REMARK   3      L13:  -1.8869 L23:  -3.2503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1747 S12:  -0.4924 S13:  -0.1438                       
REMARK   3      S21:   0.8383 S22:  -0.1424 S23:   1.0025                       
REMARK   3      S31:   0.0664 S32:  -0.2588 S33:  -0.0323                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B     1                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1520  -8.6170 -13.1240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1021 T22:   0.0012                                     
REMARK   3      T33:  -0.0488 T12:   0.0642                                     
REMARK   3      T13:   0.0133 T23:  -0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0348 L22:  12.2424                                     
REMARK   3      L33:  24.9241 L12:   8.7134                                     
REMARK   3      L13:  10.9931 L23:   9.9744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1863 S12:   0.1062 S13:  -0.2429                       
REMARK   3      S21:  -0.1156 S22:   0.0046 S23:   0.1717                       
REMARK   3      S31:   0.0905 S32:   0.1369 S33:  -0.1908                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D    85                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8540  -4.2810 -11.7050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0665 T22:   0.0127                                     
REMARK   3      T33:  -0.0934 T12:   0.0104                                     
REMARK   3      T13:   0.0104 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8425 L22:   0.6144                                     
REMARK   3      L33:   1.4532 L12:  -0.4892                                     
REMARK   3      L13:   0.7587 L23:  -0.3930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0249 S12:   0.1219 S13:  -0.1372                       
REMARK   3      S21:  -0.0359 S22:  -0.0553 S23:   0.0805                       
REMARK   3      S31:  -0.1313 S32:   0.1324 S33:   0.0304                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3KMR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056185.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9395                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22172                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : 0.04300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DKF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% (W/V) PEG 6000, 5% (W/V) GLYCEROL,   
REMARK 280  PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
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        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       44.15350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.60900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.15350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       30.60900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 990 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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     MET A   156                                                      
REMARK 465     GLY A   157                                                      
REMARK 465     SER A   158                                                      
REMARK 465     SER A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     HIS A   163                                                      
REMARK 465     HIS A   164                                                      
REMARK 465     HIS A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     SER A   167                                                      
REMARK 465     GLY A   168                                                      
REMARK 465     LEU A   169                                                      
REMARK 465     VAL A   170                                                      
REMARK 465     PRO A   171                                                      
REMARK 465     ARG A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     SER A   174                                                      
REMARK 465     HIS A   175                                                      
REMARK 465     GLU A   176                                                      
REMARK 465     SER A   177                                                      
REMARK 465     TYR A   178                                                      
REMARK 465     THR A   179                                                      
REMARK 465     LEU A   180                                                      
REMARK 465     THR A   181                                                      
REMARK 465     ASN A   416                                                      
REMARK 465     SER A   417                                                      
REMARK 465     GLU A   418                                                      
REMARK 465     GLY A   419                                                      
REMARK 465     LEU A   420                                                      
REMARK 465     ASP A   421                                                      
REMARK 465     ARG C   628                                                      
REMARK 465     GLY C   639                                                      
REMARK 465     SER C   640                                                      
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   OD1  ASP A   267     O    HOH A    46              1.97            
REMARK 500   OE2  GLU A   230     NZ   LYS A   234              2.13            
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    SER A 213       43.27     34.09                                   
REMARK 500    GLN C 637      -74.88    -86.19                                   
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 EQN A 1                   
DBREF  3KMR A  176   421  UNP    P10276   RARA_HUMAN     176    421             
DBREF  3KMR C  628   640  UNP    Q15788   NCOA1_HUMAN    686    698             
SEQADV 3KMR MET A  156  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR GLY A  157  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR SER A  158  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR SER A  159  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR HIS A  160  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR HIS A  161  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR HIS A  162  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR HIS A  163  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR HIS A  164  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR HIS A  165  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR SER A  166  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR SER A  167  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR GLY A  168  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR LEU A  169  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR VAL A  170  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR PRO A  171  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR ARG A  172  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR GLY A  173  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR SER A  174  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMR HIS A  175  UNP  P10276              EXPRESSION TAG                 
SEQRES   1 A  266  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  266  LEU VAL PRO ARG GLY SER HIS GLU SER TYR THR LEU THR          
SEQRES   3 A  266  PRO GLU VAL GLY GLU LEU ILE GLU LYS VAL ARG LYS ALA          
SEQRES   4 A  266  HIS GLN GLU THR PHE PRO ALA LEU CYS GLN LEU GLY LYS          
SEQRES   5 A  266  TYR THR THR ASN ASN SER SER GLU GLN ARG VAL SER LEU          
SEQRES   6 A  266  ASP ILE ASP LEU TRP ASP LYS PHE SER GLU LEU SER THR          
SEQRES   7 A  266  LYS CYS ILE ILE LYS THR VAL GLU PHE ALA LYS GLN LEU          
SEQRES   8 A  266  PRO GLY PHE THR THR LEU THR ILE ALA ASP GLN ILE THR          
SEQRES   9 A  266  LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU ARG          
SEQRES  10 A  266  ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET THR          
SEQRES  11 A  266  PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET HIS          
SEQRES  12 A  266  ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE ALA          
SEQRES  13 A  266  PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP ALA          
SEQRES  14 A  266  GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS GLY          
SEQRES  15 A  266  ASP ARG GLN ASP LEU GLU GLN PRO ASP ARG VAL ASP MET          
SEQRES  16 A  266  LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS VAL TYR VAL          
SEQRES  17 A  266  ARG LYS ARG ARG PRO SER ARG PRO HIS MET PHE PRO LYS          
SEQRES  18 A  266  MET LEU MET LYS ILE THR ASP LEU ARG SER ILE SER ALA          
SEQRES  19 A  266  LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU ILE          
SEQRES  20 A  266  PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU GLU          
SEQRES  21 A  266  ASN SER GLU GLY LEU ASP                                      
SEQRES   1 C   13  ARG HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY SER          
HET    EQN  A   1      26                                                       
HETNAM     EQN 4-{[(5,5,8,8-TETRAMETHYL-5,6,7,8-TETRAHYDRONAPHTHALEN-           
HETNAM   2 EQN  2-YL)CARBONYL]AMINO}BENZOIC ACID                                
FORMUL   3  EQN    C22 H25 N O3                                                 
FORMUL   4  HOH   *121(H2 O)                                                    
HELIX    1   1 PRO A  182  GLU A  197  1                                  16    
HELIX    2   2 ALA A  201  LEU A  205  5                                   5    
HELIX    3   3 ASP A  221  GLN A  245  1                                  25    
HELIX    4   4 GLY A  248  LEU A  252  5                                   5    
HELIX    5   5 THR A  253  ARG A  276  1                                  24    
HELIX    6   6 ARG A  294  GLY A  301  1                                   8    
HELIX    7   7 PHE A  302  PRO A  304  5                                   3    
HELIX    8   8 LEU A  305  LEU A  317  1                                  13    
HELIX    9   9 PRO A  318  GLU A  320  5                                   3    
HELIX   10  10 ASP A  322  ILE A  335  1                                  14    
HELIX   11  11 GLN A  344  ARG A  367  1                                  24    
HELIX   12  12 HIS A  372  ILE A  402  1                                  31    
HELIX   13  13 PRO A  407  GLU A  415  1                                   9    
HELIX   14  14 HIS C  629  GLU C  638  1                                  10    
SHEET    1   A 3 TYR A 277  THR A 278  0                                        
SHEET    2   A 3 THR A 283  THR A 285 -1  O  THR A 283   N  THR A 278           
SHEET    3   A 3 THR A 291  ASN A 293 -1  O  LEU A 292   N  MET A 284           
SITE     1 AC1 13 HOH A  14  HOH A  15  PHE A 228  LEU A 231                    
SITE     2 AC1 13 SER A 232  LEU A 269  ILE A 273  ARG A 276                    
SITE     3 AC1 13 PHE A 286  SER A 287  PHE A 302  GLY A 391                    
SITE     4 AC1 13 LEU A 398                                                     
CRYST1   88.307   61.218   49.444  90.00 105.38  90.00 C 1 2 1       4          
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      0.011324  0.000000  0.003115        0.00000                         
SCALE2      0.000000  0.016335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020976        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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