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Database: PDB
Entry: 3A9E
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Original site: 3A9E 
HEADER    TRANSCRIPTION                           24-OCT-09   3A9E              
TITLE     CRYSTAL STRUCTURE OF A MIXED AGONIST-BOUND RAR-ALPHA AND ANTAGONIST-  
TITLE    2 BOUND RXR-ALPHA HETERODIMER LIGAND BINDING DOMAINS                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINOIC ACID RECEPTOR RXR-ALPHA;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN;                                     
COMPND   5 SYNONYM: RETINOID X RECEPTOR ALPHA, NUCLEAR RECEPTOR SUBFAMILY 2     
COMPND   6 GROUP B MEMBER 1;                                                    
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: RETINOIC ACID RECEPTOR ALPHA;                              
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: LIGAND BINDING DOMAIN;                                     
COMPND  12 SYNONYM: RAR-ALPHA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP B MEMBER 1;   
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: 13-MER (LXXLL MOTIF) FROM NUCLEAR RECEPTOR COACTIVATOR 2;  
COMPND  16 CHAIN: I;                                                            
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RXRA, NR2B1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RARA, NR1B1;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.               
KEYWDS    TRANSCRIPTION, NUCLEUS, RECEPTOR, TRANSCRIPTION REGULATION,           
KEYWDS   2 STRUCTURAL GENOMICS, SPINE2-COMPLEXES, STRUCTURAL PROTEOMICS IN      
KEYWDS   3 EUROPE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SATO,S.DUCLAUD,C.PELUSO-ILTIS,P.POUSSIN,D.MORAS,N.ROCHEL            
REVDAT   2   30-OCT-13 3A9E    1       JRNL   VERSN                             
REVDAT   1   06-OCT-10 3A9E    0                                                
JRNL        AUTH   Y.SATO,N.RAMALANJAONA,T.HUET,N.POTIER,J.OSZ,P.ANTONY,        
JRNL        AUTH 2 C.PELUSO-ILTIS,P.POUSSIN-COURMONTAGNE,E.ENNIFAR,Y.MELY,      
JRNL        AUTH 3 A.DEJAEGERE,D.MORAS,N.ROCHEL                                 
JRNL        TITL   THE PHANTOM EFFECT OF THE REXINOID LG100754: STRUCTURAL AND  
JRNL        TITL 2 FUNCTIONAL INSIGHTS                                          
JRNL        REF    PLOS ONE                      V.   5 15119 2010              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21152046                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0015119                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15179                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 737                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.8825 -  4.6862    0.98     3273   165  0.1877 0.2433        
REMARK   3     2  4.6862 -  3.7276    0.83     2665   121  0.1802 0.2250        
REMARK   3     3  3.7276 -  3.2587    0.72     2261   130  0.2251 0.2820        
REMARK   3     4  3.2587 -  2.9618    1.00     3118   170  0.2196 0.2985        
REMARK   3     5  2.9618 -  2.7501    1.00     3125   151  0.2276 0.3015        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.27                                          
REMARK   3   B_SOL              : 39.73                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.630            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.390           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.08600                                             
REMARK   3    B22 (A**2) : -1.08600                                             
REMARK   3    B33 (A**2) : 2.17210                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           3833                                  
REMARK   3   ANGLE     :  0.542           5188                                  
REMARK   3   CHIRALITY :  0.034            600                                  
REMARK   3   PLANARITY :  0.002            663                                  
REMARK   3   DIHEDRAL  : 12.291           1473                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1030  62.1620   7.2991              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1329 T22:   0.0319                                     
REMARK   3      T33:   0.1040 T12:   0.0226                                     
REMARK   3      T13:  -0.0205 T23:  -0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2469 L22:   1.4068                                     
REMARK   3      L33:   1.1789 L12:   0.5900                                     
REMARK   3      L13:  -0.1421 L23:  -0.3309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0839 S12:  -0.1236 S13:   0.0012                       
REMARK   3      S21:   0.0236 S22:  -0.0551 S23:  -0.1078                       
REMARK   3      S31:  -0.0510 S32:  -0.0769 S33:  -0.0318                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3A9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB028976.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07230                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1DKF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM POTASSIUM THIOCYANATE, 20% PEG     
REMARK 280  3350, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.66900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       52.65000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.65000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       83.50350            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.65000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.65000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       27.83450            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.65000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.65000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       83.50350            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.65000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.65000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       27.83450            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       55.66900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10900 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   228                                                      
REMARK 465     SER A   229                                                      
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     ALA A   462                                                      
REMARK 465     PRO A   463                                                      
REMARK 465     HIS A   464                                                      
REMARK 465     GLN A   465                                                      
REMARK 465     ALA A   466                                                      
REMARK 465     THR A   467                                                      
REMARK 465     MET B   153                                                      
REMARK 465     SER B   154                                                      
REMARK 465     LYS B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     SER B   157                                                      
REMARK 465     VAL B   158                                                      
REMARK 465     ARG B   159                                                      
REMARK 465     ASN B   160                                                      
REMARK 465     ASP B   161                                                      
REMARK 465     ARG B   162                                                      
REMARK 465     ASN B   163                                                      
REMARK 465     LYS B   164                                                      
REMARK 465     LYS B   165                                                      
REMARK 465     LYS B   166                                                      
REMARK 465     LYS B   167                                                      
REMARK 465     GLU B   168                                                      
REMARK 465     VAL B   169                                                      
REMARK 465     PRO B   170                                                      
REMARK 465     LYS B   171                                                      
REMARK 465     PRO B   172                                                      
REMARK 465     GLU B   173                                                      
REMARK 465     CYS B   174                                                      
REMARK 465     SER B   175                                                      
REMARK 465     GLU B   176                                                      
REMARK 465     ASN B   416                                                      
REMARK 465     SER B   417                                                      
REMARK 465     GLU B   418                                                      
REMARK 465     GLY B   419                                                      
REMARK 465     LEU B   420                                                      
REMARK 465     ASP B   421                                                      
REMARK 465     SER I  1482                                                      
REMARK 465     SER I  1483                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  233   CD   OE1  OE2                                       
REMARK 480     LYS A  239   CE   NZ                                             
REMARK 480     GLU A  248   CD   OE1  OE2                                       
REMARK 480     LYS A  250   CG   CD   CE   NZ                                   
REMARK 480     SER A  265   OG                                                  
REMARK 480     ASN A  267   CG   OD1  ND2                                       
REMARK 480     GLN A  275   CD   OE1  NE2                                       
REMARK 480     GLU A  286   CD   OE1  OE2                                       
REMARK 480     LYS A  289   CG   CD   CE   NZ                                   
REMARK 480     LEU A  299   CD1  CD2                                            
REMARK 480     ARG A  307   NE   CZ   NH1  NH2                                  
REMARK 480     LYS A  326   CG   CD   CE   NZ                                   
REMARK 480     LEU A  335   CD1  CD2                                            
REMARK 480     LYS A  369   NZ                                                  
REMARK 480     LYS A  386   CG   CD   CE   NZ                                   
REMARK 480     LYS A  410   CE   NZ                                             
REMARK 480     LYS A  412   CE   NZ                                             
REMARK 480     LYS A  422   CE   NZ                                             
REMARK 480     LYS A  436   CE   NZ                                             
REMARK 480     GLU A  439   CD   OE1  OE2                                       
REMARK 480     LYS A  445   CG   CD   CE   NZ                                   
REMARK 480     LEU A  446   CG   CD1  CD2                                       
REMARK 480     THR A  450   OG1  CG2                                            
REMARK 480     MET A  457   SD   CE                                             
REMARK 480     GLU A  458   CG   CD   OE1  OE2                                  
REMARK 480     GLU A  461   CD   OE1  OE2                                       
REMARK 480     THR B  179   OG1  CG2                                            
REMARK 480     GLU B  183   CD   OE1  OE2                                       
REMARK 480     LYS B  190   CD   CE   NZ                                        
REMARK 480     GLN B  204   CG   CD   OE1  NE2                                  
REMARK 480     GLU B  215   CG   CD   OE1  OE2                                  
REMARK 480     GLN B  216   CD   OE1  NE2                                       
REMARK 480     ASP B  223   OD1  OD2                                            
REMARK 480     LYS B  227   NZ                                                  
REMARK 480     LYS B  234   NZ                                                  
REMARK 480     GLU B  241   CD   OE1  OE2                                       
REMARK 480     GLU B  320   CD   OE1  OE2                                       
REMARK 480     LYS B  390   CD   CE   NZ                                        
REMARK 480     GLU B  393   CG   CD   OE1  OE2                                  
REMARK 480     LYS I 1471   CG   CD   CE   NZ                                   
REMARK 480     LYS I 1473   CG   CD   CE   NZ                                   
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    MET A 235       73.64   -156.45                                   
REMARK 500    LEU A 358      -70.30   -111.19                                   
REMARK 500    LEU A 441       42.57    -86.73                                   
REMARK 500    ASP A 449     -106.39   -116.77                                   
REMARK 500    THR A 450       95.20   -160.29                                   
REMARK 500    ILE A 452       18.27     54.84                                   
REMARK 500    PHE B 199       91.91   -160.22                                   
REMARK 500    GLN B 204       40.81    -77.41                                   
REMARK 500    GLU B 215      -72.13    -92.43                                   
REMARK 500    LEU B 220      131.90   -172.03                                   
REMARK 500    ASP B 338       40.27    -95.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A   9        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B 451        DISTANCE =  5.19 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 754 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE REA B 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DKF   RELATED DB: PDB                                   
REMARK 900 THE HOMAN RAR-ALPHA LIGAND-BINDING DOMAIN BOUND TO BMS614            
REMARK 900 AND MOUSE RXR-ALPHA LIGAND-BINDING DOMAIN BOUND (F318A)              
REMARK 900 BOUND TO OLEIC ACID.                                                 
REMARK 900 RELATED ID: 1XDK   RELATED DB: PDB                                   
REMARK 900 THE MOUSE RAR-BETA LIGAND-BINDING DOMAIN BOUND TO 9-CIS              
REMARK 900 RETINOIC ACID AND MOUSE RXR-ALPHA LIGAND-BINDING DOMAIN              
REMARK 900 BOUND BOUND TO 9-CIS RETINOIC ACID COMPLEXED WITH THE                
REMARK 900 PEPTIDES OF TRAP220.                                                 
DBREF  3A9E A  228   467  UNP    P28700   RXRA_MOUSE     228    467             
DBREF  3A9E B  153   421  UNP    P10276   RARA_HUMAN     153    421             
DBREF  3A9E I 1471  1483  UNP    Q15596   NCOA2_HUMAN    686    698             
SEQRES   1 A  240  THR SER SER ALA ASN GLU ASP MET PRO VAL GLU LYS ILE          
SEQRES   2 A  240  LEU GLU ALA GLU LEU ALA VAL GLU PRO LYS THR GLU THR          
SEQRES   3 A  240  TYR VAL GLU ALA ASN MET GLY LEU ASN PRO SER SER PRO          
SEQRES   4 A  240  ASN ASP PRO VAL THR ASN ILE CYS GLN ALA ALA ASP LYS          
SEQRES   5 A  240  GLN LEU PHE THR LEU VAL GLU TRP ALA LYS ARG ILE PRO          
SEQRES   6 A  240  HIS PHE SER GLU LEU PRO LEU ASP ASP GLN VAL ILE LEU          
SEQRES   7 A  240  LEU ARG ALA GLY TRP ASN GLU LEU LEU ILE ALA SER PHE          
SEQRES   8 A  240  SER HIS ARG SER ILE ALA VAL LYS ASP GLY ILE LEU LEU          
SEQRES   9 A  240  ALA THR GLY LEU HIS VAL HIS ARG ASN SER ALA HIS SER          
SEQRES  10 A  240  ALA GLY VAL GLY ALA ILE PHE ASP ARG VAL LEU THR GLU          
SEQRES  11 A  240  LEU VAL SER LYS MET ARG ASP MET GLN MET ASP LYS THR          
SEQRES  12 A  240  GLU LEU GLY CYS LEU ARG ALA ILE VAL LEU PHE ASN PRO          
SEQRES  13 A  240  ASP SER LYS GLY LEU SER ASN PRO ALA GLU VAL GLU ALA          
SEQRES  14 A  240  LEU ARG GLU LYS VAL TYR ALA SER LEU GLU ALA TYR CYS          
SEQRES  15 A  240  LYS HIS LYS TYR PRO GLU GLN PRO GLY ARG PHE ALA LYS          
SEQRES  16 A  240  LEU LEU LEU ARG LEU PRO ALA LEU ARG SER ILE GLY LEU          
SEQRES  17 A  240  LYS CYS LEU GLU HIS LEU PHE PHE PHE LYS LEU ILE GLY          
SEQRES  18 A  240  ASP THR PRO ILE ASP THR PHE LEU MET GLU MET LEU GLU          
SEQRES  19 A  240  ALA PRO HIS GLN ALA THR                                      
SEQRES   1 B  269  MET SER LYS GLU SER VAL ARG ASN ASP ARG ASN LYS LYS          
SEQRES   2 B  269  LYS LYS GLU VAL PRO LYS PRO GLU CYS SER GLU SER TYR          
SEQRES   3 B  269  THR LEU THR PRO GLU VAL GLY GLU LEU ILE GLU LYS VAL          
SEQRES   4 B  269  ARG LYS ALA HIS GLN GLU THR PHE PRO ALA LEU CYS GLN          
SEQRES   5 B  269  LEU GLY LYS TYR THR THR ASN ASN SER SER GLU GLN ARG          
SEQRES   6 B  269  VAL SER LEU ASP ILE ASP LEU TRP ASP LYS PHE SER GLU          
SEQRES   7 B  269  LEU SER THR LYS CYS ILE ILE LYS THR VAL GLU PHE ALA          
SEQRES   8 B  269  LYS GLN LEU PRO GLY PHE THR THR LEU THR ILE ALA ASP          
SEQRES   9 B  269  GLN ILE THR LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU          
SEQRES  10 B  269  ILE LEU ARG ILE CYS THR ARG TYR THR PRO GLU GLN ASP          
SEQRES  11 B  269  THR MET THR PHE SER ASP GLY LEU THR LEU ASN ARG THR          
SEQRES  12 B  269  GLN MET HIS ASN ALA GLY PHE GLY PRO LEU THR ASP LEU          
SEQRES  13 B  269  VAL PHE ALA PHE ALA ASN GLN LEU LEU PRO LEU GLU MET          
SEQRES  14 B  269  ASP ASP ALA GLU THR GLY LEU LEU SER ALA ILE CYS LEU          
SEQRES  15 B  269  ILE CYS GLY ASP ARG GLN ASP LEU GLU GLN PRO ASP ARG          
SEQRES  16 B  269  VAL ASP MET LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS          
SEQRES  17 B  269  VAL TYR VAL ARG LYS ARG ARG PRO SER ARG PRO HIS MET          
SEQRES  18 B  269  PHE PRO LYS MET LEU MET LYS ILE THR ASP LEU ARG SER          
SEQRES  19 B  269  ILE SER ALA LYS GLY ALA GLU ARG VAL ILE THR LEU LYS          
SEQRES  20 B  269  MET GLU ILE PRO GLY SER MET PRO PRO LEU ILE GLN GLU          
SEQRES  21 B  269  MET LEU GLU ASN SER GLU GLY LEU ASP                          
SEQRES   1 I   13  LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER SER          
HET    754  A   1      29                                                       
HET    REA  B   1      22                                                       
HETNAM     754 (2E,4E,6Z)-3-METHYL-7-(5,5,8,8-TETRAMETHYL-3-PROPOXY-5,          
HETNAM   2 754  6,7,8-TETRAHYDRONAPHTHALEN-2-YL)OCTA-2,4,6-TRIENOIC             
HETNAM   3 754  ACID                                                            
HETNAM     REA RETINOIC ACID                                                    
FORMUL   4  754    C26 H36 O3                                                   
FORMUL   5  REA    C20 H28 O2                                                   
FORMUL   6  HOH   *115(H2 O)                                                    
HELIX    1   1 PRO A  236  VAL A  247  1                                  12    
HELIX    2   2 ASP A  268  ARG A  290  1                                  23    
HELIX    3   3 PRO A  298  SER A  322  1                                  25    
HELIX    4   4 ARG A  339  ALA A  345  1                                   7    
HELIX    5   5 VAL A  347  LEU A  358  1                                  12    
HELIX    6   6 LEU A  358  MET A  365  1                                   8    
HELIX    7   7 ASP A  368  PHE A  381  1                                  14    
HELIX    8   8 ASN A  390  TYR A  413  1                                  24    
HELIX    9   9 GLY A  418  LEU A  425  1                                   8    
HELIX   10  10 ARG A  426  LEU A  441  1                                  16    
HELIX   11  11 LEU A  441  LEU A  446  1                                   6    
HELIX   12  12 THR A  450  ILE A  452  5                                   3    
HELIX   13  13 ASP A  453  GLU A  461  1                                   9    
HELIX   14  14 THR B  181  PHE B  199  1                                  19    
HELIX   15  15 ASP B  221  GLN B  245  1                                  25    
HELIX   16  16 THR B  253  CYS B  274  1                                  22    
HELIX   17  17 ARG B  294  GLY B  301  1                                   8    
HELIX   18  18 PHE B  302  PRO B  304  5                                   3    
HELIX   19  19 LEU B  305  LEU B  317  1                                  13    
HELIX   20  20 PRO B  318  GLU B  320  5                                   3    
HELIX   21  21 ASP B  322  ILE B  335  1                                  14    
HELIX   22  22 GLN B  344  ARG B  367  1                                  24    
HELIX   23  23 HIS B  372  ILE B  402  1                                  31    
HELIX   24  24 PRO B  407  GLU B  415  1                                   9    
HELIX   25  25 HIS I 1472  ASP I 1481  1                                  10    
SHEET    1   A 2 GLY A 328  LEU A 330  0                                        
SHEET    2   A 2 HIS A 336  HIS A 338 -1  O  VAL A 337   N  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 11 ILE A 273  ALA A 276  GLN A 280  TRP A 310                    
SITE     2 AC1 11 PHE A 318  ARG A 321  LEU A 331  ALA A 332                    
SITE     3 AC1 11 ILE A 350  CYS A 437  LEU A 441                               
SITE     1 AC2  9 HOH B  40  PHE B 228  CYS B 235  LEU B 269                    
SITE     2 AC2  9 ARG B 276  PHE B 286  SER B 287  VAL B 395                    
SITE     3 AC2  9 LEU B 398                                                     
CRYST1  105.300  105.300  111.338  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009497  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008982        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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