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Database: PDB
Entry: 1DKF
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Original site: 1DKF 
HEADER    HORMONE/GROWTH FACTOR RECEPTOR          07-DEC-99   1DKF              
TITLE     CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR LIGAND-   
TITLE    2 BINDING DOMAINS                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (RETINOID X RECEPTOR-ALPHA);                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND-BINDING DOMAIN;                                     
COMPND   5 SYNONYM: RXR-ALPHA;                                                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTEIN (RETINOIC ACID RECEPTOR-ALPHA);                    
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: LIGAND-BINDING DOMAIN;                                     
COMPND  12 SYNONYM: RAR-ALPHA;                                                  
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    HELICAL SANDWICH, HETERODIMER, PROTEIN-LIGAND COMPLEX, HORMONE/GROWTH 
KEYWDS   2 FACTOR RECEPTOR, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL  
KEYWDS   3 GENOMICS, HORMONE-GROWTH FACTOR RECEPTOR COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BOURGUET,V.VIVAT,J.M.WURTZ,P.CHAMBON,H.GRONEMEYER,D.MORAS,          
AUTHOR   2 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)                              
REVDAT   6   11-APR-18 1DKF    1       REMARK                                   
REVDAT   5   04-APR-18 1DKF    1       REMARK                                   
REVDAT   4   04-OCT-17 1DKF    1       REMARK                                   
REVDAT   3   24-FEB-09 1DKF    1       VERSN                                    
REVDAT   2   26-APR-00 1DKF    1       REMARK SEQRES SEQADV                     
REVDAT   1   19-APR-00 1DKF    0                                                
JRNL        AUTH   W.BOURGUET,V.VIVAT,J.M.WURTZ,P.CHAMBON,H.GRONEMEYER,D.MORAS  
JRNL        TITL   CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR  
JRNL        TITL 2 LIGAND-BINDING DOMAINS.                                      
JRNL        REF    MOL.CELL                      V.   5   289 2000              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   10882070                                                     
JRNL        DOI    10.1016/S1097-2765(00)80424-4                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 26091                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1286                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3532                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 157                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.180                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000010158.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 120.0                              
REMARK 200  PH                             : 7.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SOFTWARE AT SYNCHROTRON            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29168                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000, PH 7.25                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.26667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      138.53333            
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      103.90000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      173.16667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       34.63333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.26667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      138.53333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      173.16667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      103.90000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       34.63333            
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 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     LYS A   250                                                      
REMARK 465     THR A   251                                                      
REMARK 465     GLU A   252                                                      
REMARK 465     THR A   253                                                      
REMARK 465     TYR A   254                                                      
REMARK 465     VAL A   255                                                      
REMARK 465     GLU A   256                                                      
REMARK 465     ALA A   257                                                      
REMARK 465     ASN A   258                                                      
REMARK 465     MET A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     ASN A   262                                                      
REMARK 465     PRO A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     SER A   265                                                      
REMARK 465     ASN B   211                                                      
REMARK 465     ASN B   212                                                      
REMARK 465     SER B   213                                                      
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     ASN B 416    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 236      106.06    -57.80                                   
REMARK 500    PRO A 292      127.06    -29.02                                   
REMARK 500    HIS A 293       -8.20     68.76                                   
REMARK 500    VAL A 325      174.78    -50.69                                   
REMARK 500    LEU A 358      -78.46   -119.00                                   
REMARK 500    LEU A 425       -0.33    -57.77                                   
REMARK 500    ILE A 447       50.85     34.25                                   
REMARK 500    ASP A 449       -2.81     59.88                                   
REMARK 500    PHE B 199       97.72   -160.59                                   
REMARK 500    THR B 251       32.49    -78.78                                   
REMARK 500    GLN B 344       74.18   -117.34                                   
REMARK 500    MET B 379        1.86    -66.48                                   
REMARK 500    MET B 406       74.46     68.95                                   
REMARK 500    LEU B 409      -22.71   -161.10                                   
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 BMS B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 700                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LBD   RELATED DB: PDB                                   
REMARK 900 1LBD CONTAINS THE UNLIGANDED RXR LIGAND-BINDING DOMAIN               
REMARK 900 RELATED ID: 2LBD   RELATED DB: PDB                                   
REMARK 900 2LBD CONTAINS THE RAR-GAMMA LIGAND-BINDING DOMAIN BOUND TO ALL-      
REMARK 900 TRANS RETINOIC ACID                                                  
REMARK 900 RELATED ID: IGBMC-0012-000   RELATED DB: TARGETDB                    
DBREF  1DKF A  230   462  UNP    P28700   RXRA_MOUSE     230    462             
DBREF  1DKF B  182   416  UNP    P10276   RARA_HUMAN     182    416             
SEQADV 1DKF ALA A  318  UNP  P28700    PHE   318 ENGINEERED                     
SEQRES   1 A  233  SER ALA ASN GLU ASP MET PRO VAL GLU LYS ILE LEU GLU          
SEQRES   2 A  233  ALA GLU LEU ALA VAL GLU PRO LYS THR GLU THR TYR VAL          
SEQRES   3 A  233  GLU ALA ASN MET GLY LEU ASN PRO SER SER PRO ASN ASP          
SEQRES   4 A  233  PRO VAL THR ASN ILE CYS GLN ALA ALA ASP LYS GLN LEU          
SEQRES   5 A  233  PHE THR LEU VAL GLU TRP ALA LYS ARG ILE PRO HIS PHE          
SEQRES   6 A  233  SER GLU LEU PRO LEU ASP ASP GLN VAL ILE LEU LEU ARG          
SEQRES   7 A  233  ALA GLY TRP ASN GLU LEU LEU ILE ALA SER ALA SER HIS          
SEQRES   8 A  233  ARG SER ILE ALA VAL LYS ASP GLY ILE LEU LEU ALA THR          
SEQRES   9 A  233  GLY LEU HIS VAL HIS ARG ASN SER ALA HIS SER ALA GLY          
SEQRES  10 A  233  VAL GLY ALA ILE PHE ASP ARG VAL LEU THR GLU LEU VAL          
SEQRES  11 A  233  SER LYS MET ARG ASP MET GLN MET ASP LYS THR GLU LEU          
SEQRES  12 A  233  GLY CYS LEU ARG ALA ILE VAL LEU PHE ASN PRO ASP SER          
SEQRES  13 A  233  LYS GLY LEU SER ASN PRO ALA GLU VAL GLU ALA LEU ARG          
SEQRES  14 A  233  GLU LYS VAL TYR ALA SER LEU GLU ALA TYR CYS LYS HIS          
SEQRES  15 A  233  LYS TYR PRO GLU GLN PRO GLY ARG PHE ALA LYS LEU LEU          
SEQRES  16 A  233  LEU ARG LEU PRO ALA LEU ARG SER ILE GLY LEU LYS CYS          
SEQRES  17 A  233  LEU GLU HIS LEU PHE PHE PHE LYS LEU ILE GLY ASP THR          
SEQRES  18 A  233  PRO ILE ASP THR PHE LEU MET GLU MET LEU GLU ALA              
SEQRES   1 B  235  PRO GLU VAL GLY GLU LEU ILE GLU LYS VAL ARG LYS ALA          
SEQRES   2 B  235  HIS GLN GLU THR PHE PRO ALA LEU CYS GLN LEU GLY LYS          
SEQRES   3 B  235  TYR THR THR ASN ASN SER SER GLU GLN ARG VAL SER LEU          
SEQRES   4 B  235  ASP ILE ASP LEU TRP ASP LYS PHE SER GLU LEU SER THR          
SEQRES   5 B  235  LYS CYS ILE ILE LYS THR VAL GLU PHE ALA LYS GLN LEU          
SEQRES   6 B  235  PRO GLY PHE THR THR LEU THR ILE ALA ASP GLN ILE THR          
SEQRES   7 B  235  LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU ARG          
SEQRES   8 B  235  ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET THR          
SEQRES   9 B  235  PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET HIS          
SEQRES  10 B  235  ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE ALA          
SEQRES  11 B  235  PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP ALA          
SEQRES  12 B  235  GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS GLY          
SEQRES  13 B  235  ASP ARG GLN ASP LEU GLU GLN PRO ASP ARG VAL ASP MET          
SEQRES  14 B  235  LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS VAL TYR VAL          
SEQRES  15 B  235  ARG LYS ARG ARG PRO SER ARG PRO HIS MET PHE PRO LYS          
SEQRES  16 B  235  MET LEU MET LYS ILE THR ASP LEU ARG SER ILE SER ALA          
SEQRES  17 B  235  LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU ILE          
SEQRES  18 B  235  PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU GLU          
SEQRES  19 B  235  ASN                                                          
HET    OLA  A 700      20                                                       
HET    BMS  B 600      34                                                       
HETNAM     OLA OLEIC ACID                                                       
HETNAM     BMS 4-[(4,4-DIMETHYL-1,2,3,4-TETRAHYDRO-[1,                          
HETNAM   2 BMS  2']BINAPTHALENYL-7-CARBONYL)-AMINO]-BENZOIC ACID                
FORMUL   3  OLA    C18 H34 O2                                                   
FORMUL   4  BMS    C29 H26 N2 O3                                                
FORMUL   5  HOH   *157(H2 O)                                                    
HELIX    1   1 SER A  230  MET A  235  1                                   6    
HELIX    2   2 PRO A  236  VAL A  247  1                                  12    
HELIX    3   3 ASP A  268  THR A  283  1                                  16    
HELIX    4   4 THR A  283  ARG A  290  1                                   8    
HELIX    5   5 PRO A  298  SER A  322  1                                  25    
HELIX    6   6 ARG A  339  ALA A  345  1                                   7    
HELIX    7   7 VAL A  347  LEU A  358  1                                  12    
HELIX    8   8 LEU A  358  MET A  365  1                                   8    
HELIX    9   9 ASP A  368  PHE A  381  1                                  14    
HELIX   10  10 ASN A  390  TYR A  413  1                                  24    
HELIX   11  11 GLY A  418  LEU A  425  1                                   8    
HELIX   12  12 LEU A  425  GLU A  439  1                                  15    
HELIX   13  13 LEU A  446  THR A  450  5                                   5    
HELIX   14  14 PRO A  451  ALA A  462  1                                  12    
HELIX   15  15 PRO B  182  PHE B  199  1                                  18    
HELIX   16  16 ALA B  201  LEU B  205  5                                   5    
HELIX   17  17 ASP B  221  LEU B  246  1                                  26    
HELIX   18  18 THR B  253  THR B  275  1                                  23    
HELIX   19  19 ARG B  294  GLY B  301  1                                   8    
HELIX   20  20 PHE B  302  PRO B  304  5                                   3    
HELIX   21  21 LEU B  305  LEU B  316  1                                  12    
HELIX   22  22 LEU B  317  GLU B  320  5                                   4    
HELIX   23  23 ASP B  322  ILE B  335  1                                  14    
HELIX   24  24 GLN B  344  ARG B  367  1                                  24    
HELIX   25  25 HIS B  372  MET B  379  1                                   8    
HELIX   26  26 MET B  379  ILE B  402  1                                  24    
HELIX   27  27 LEU B  409  ASN B  416  1                                   8    
SHEET    1   A 2 GLY A 328  LEU A 330  0                                        
SHEET    2   A 2 HIS A 336  HIS A 338 -1  N  VAL A 337   O  ILE A 329           
SHEET    1   B 3 TYR B 277  THR B 278  0                                        
SHEET    2   B 3 THR B 283  THR B 285 -1  O  THR B 283   N  THR B 278           
SHEET    3   B 3 THR B 291  ASN B 293 -1  O  LEU B 292   N  MET B 284           
SITE     1 AC1 18 HOH B  33  PHE B 199  PHE B 228  SER B 229                    
SITE     2 AC1 18 LEU B 231  SER B 232  THR B 233  CYS B 235                    
SITE     3 AC1 18 ILE B 236  LEU B 269  ILE B 270  ILE B 273                    
SITE     4 AC1 18 ARG B 276  PHE B 286  SER B 287  PHE B 302                    
SITE     5 AC1 18 GLY B 391  MET B 406                                          
SITE     1 AC2 11 HOH A   9  ALA A 276  ALA A 277  GLN A 280                    
SITE     2 AC2 11 ASN A 311  ALA A 318  ARG A 321  LEU A 331                    
SITE     3 AC2 11 ALA A 332  CYS A 437  PHE A 444                               
CRYST1  116.600  116.600  207.800  90.00  90.00 120.00 P 61 2 2     12          
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      0.008576  0.004952  0.000000        0.00000                         
SCALE2      0.000000  0.009903  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004812        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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