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Database: PDB
Entry: 4DM8
LinkDB: 4DM8
Original site: 4DM8 
HEADER    TRANSCRIPTION/PROTEIN BINDING           07-FEB-12   4DM8              
TITLE     CRYSTAL STRUCTURE OF RARB LBD IN COMPLEX WITH 9CIS RETINOIC ACID      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINOIC ACID RECEPTOR BETA;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 176-421;                                      
COMPND   5 SYNONYM: RAR-BETA, HBV-ACTIVATED PROTEIN, NUCLEAR RECEPTOR SUBFAMILY 
COMPND   6 1 GROUP B MEMBER 2, RAR-EPSILON;                                     
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 676-700;                                      
COMPND  12 SYNONYM: NCOA-1, CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74, BHLHE74, 
COMPND  13 PROTEIN HIN-2, RIP160, RENAL CARCINOMA ANTIGEN NY-REN-52, STEROID    
COMPND  14 RECEPTOR COACTIVATOR 1, SRC-1;                                       
COMPND  15 EC: 2.3.1.48;                                                        
COMPND  16 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: RARB, HAP, NR1B2;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    NUCLEAR RECEPTOR, RARB, 9CIS RETINOIC ACID, ALPHA HELICAL SANDWICH,   
KEYWDS   2 TRANSCRIPTION FACTOR, RETINOIC ACID, TRANSCRIPTION-PROTEIN BINDING   
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.OSZ,Y.BR LIVET,C.PELUSO-ILTIS,V.CURA,S.EILER,M.RUFF,W.BOURGUET,     
AUTHOR   2 N.ROCHEL,D.MORAS                                                     
REVDAT   3   16-NOV-16 4DM8    1       HETATM                                   
REVDAT   2   16-MAY-12 4DM8    1       JRNL                                     
REVDAT   1   07-MAR-12 4DM8    0                                                
JRNL        AUTH   J.OSZ,Y.BRELIVET,C.PELUSO-ILTIS,V.CURA,S.EILER,M.RUFF,       
JRNL        AUTH 2 W.BOURGUET,N.ROCHEL,D.MORAS                                  
JRNL        TITL   STRUCTURAL BASIS FOR A MOLECULAR ALLOSTERIC CONTROL          
JRNL        TITL 2 MECHANISM OF COFACTOR BINDING TO NUCLEAR RECEPTORS.          
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  E588 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22355136                                                     
JRNL        DOI    10.1073/PNAS.1118192109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
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             : 21814                          
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) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1094                            
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            : 3911                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.070                           
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 4DM8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070505.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0093                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21814                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% POLYETHYLENE GLYCOL 8000, 0.2 M       
REMARK 280  KCL, 0.01 M MGCL2 AND 0.05 M MES PH 5.6, VAPOR DIFFUSION, HANGING   
REMARK 280  DROP, TEMPERATURE 290K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.24100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.38950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.81100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.38950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.24100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.81100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     SER A   159                                                      
REMARK 465     SER 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     HIS A   166                                                      
REMARK 465     SER A   167                                                      
REMARK 465     SER A   168                                                      
REMARK 465     GLY A   169                                                      
REMARK 465     LEU A   170                                                      
REMARK 465     VAL A   171                                                      
REMARK 465     PRO A   172                                                      
REMARK 465     ARG A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     SER A   175                                                      
REMARK 465     HIS A   176                                                      
REMARK 465     MET A   177                                                      
REMARK 465     SER A   371                                                      
REMARK 465     LYS A   372                                                      
REMARK 465     ASN A   418                                                      
REMARK 465     SER A   419                                                      
REMARK 465     GLU A   420                                                      
REMARK 465     GLY A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     GLU A   423                                                      
REMARK 465     MET B  1157                                                      
REMARK 465     GLY B  1158                                                      
REMARK 465     SER B  1159                                                      
REMARK 465     SER B  1160                                                      
REMARK 465     HIS B  1161                                                      
REMARK 465     HIS B  1162                                                      
REMARK 465     HIS B  1163                                                      
REMARK 465     HIS B  1164                                                      
REMARK 465     HIS B  1165                                                      
REMARK 465     HIS B  1166                                                      
REMARK 465     SER B  1167                                                      
REMARK 465     SER B  1168                                                      
REMARK 465     GLY B  1169                                                      
REMARK 465     LEU B  1170                                                      
REMARK 465     VAL B  1171                                                      
REMARK 465     PRO B  1172                                                      
REMARK 465     ARG B  1173                                                      
REMARK 465     GLY B  1174                                                      
REMARK 465     SER B  1175                                                      
REMARK 465     HIS B  1176                                                      
REMARK 465     MET B  1177                                                      
REMARK 465     GLU B  1178                                                      
REMARK 465     SER B  1179                                                      
REMARK 465     SER B  1419                                                      
REMARK 465     GLU B  1420                                                      
REMARK 465     GLY B  1421                                                      
REMARK 465     HIS B  1422                                                      
REMARK 465     GLU B  1423                                                      
REMARK 465     CYS C   619                                                      
REMARK 465     PRO C   620                                                      
REMARK 465     SER C   621                                                      
REMARK 465     SER C   622                                                      
REMARK 465     HIS C   623                                                      
REMARK 465     SER C   624                                                      
REMARK 465     SER C   625                                                      
REMARK 465     LEU C   626                                                      
REMARK 465     THR C   627                                                      
REMARK 465     GLU C   628                                                      
REMARK 465     ARG C   629                                                      
REMARK 465     HIS C   630                                                      
REMARK 465     GLU C   639                                                      
REMARK 465     GLY C   640                                                      
REMARK 465     SER C   641                                                      
REMARK 465     PRO C   642                                                      
REMARK 465     SER C   643                                                      
REMARK 465     CYS D  1619                                                      
REMARK 465     PRO D  1620                                                      
REMARK 465     SER D  1621                                                      
REMARK 465     SER D  1622                                                      
REMARK 465     HIS D  1623                                                      
REMARK 465     SER D  1624                                                      
REMARK 465     SER D  1625                                                      
REMARK 465     LEU D  1626                                                      
REMARK 465     THR D  1627                                                      
REMARK 465     GLU D  1628                                                      
REMARK 465     ARG D  1629                                                      
REMARK 465     HIS D  1630                                                      
REMARK 465     GLU D  1639                                                      
REMARK 465     GLY D  1640                                                      
REMARK 465     SER D  1641                                                      
REMARK 465     PRO D  1642                                                      
REMARK 465     SER D  1643                                                      
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     GLU A 181    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 373    CG   CD                                             
REMARK 470     ASN B1418    CG   OD1  ND2                                       
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     SER A   215                                                      
REMARK 475     ARG A   369                                                      
REMARK 475     PRO A   370                                                      
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  178   OE1  OE2                                            
REMARK 480     GLN A  206   CG   CD   OE1  NE2                                  
REMARK 480     SER A  214   OG                                                  
REMARK 480     LYS A  264   NZ                                                  
REMARK 480     GLN A  342   CG   CD   OE1  NE2                                  
REMARK 480     GLU B 1395   OE1  OE2                                            
REMARK 480     GLN D 1638   CG   CD   OE1  NE2                                  
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    GLU A 181     -178.49    -65.06                                   
REMARK 500    GLN A 206       27.02    -79.83                                   
REMARK 500    THR A 212     -150.22   -124.30                                   
REMARK 500    ASN A 213       15.65    176.75                                   
REMARK 500    SER A 214      -29.02    -38.19                                   
REMARK 500    SER A 215       51.99    175.50                                   
REMARK 500    LEU A 222      119.28   -173.06                                   
REMARK 500    PRO A 306        7.53    -68.27                                   
REMARK 500    ASP A 343       -1.31     85.07                                   
REMARK 500    ARG A 368      -80.91    -72.82                                   
REMARK 500    HIS A 374       22.59   -153.30                                   
REMARK 500    PRO A 405      -81.94    -51.51                                   
REMARK 500    SER B1214      122.79    -39.34                                   
REMARK 500    SER B1215       74.74     19.63                                   
REMARK 500    ARG B1369       68.00   -117.07                                   
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 REA A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE REA B 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF NUCLEAR RECEPTOR       
REMARK 800  COACTIVATOR 1                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1XAP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DM6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DMA   RELATED DB: PDB                                   
DBREF  4DM8 A  178   423  UNP    P10826   RARB_HUMAN     176    421             
DBREF  4DM8 B 1178  1423  UNP    P10826   RARB_HUMAN     176    421             
DBREF  4DM8 C  619   643  UNP    Q15788   NCOA1_HUMAN    676    700             
DBREF  4DM8 D 1619  1643  UNP    Q15788   NCOA1_HUMAN    676    700             
SEQADV 4DM8 MET A  157  UNP  P10826              INITIATING METHIONINE          
SEQADV 4DM8 GLY A  158  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER A  159  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER A  160  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS A  161  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS A  162  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS A  163  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS A  164  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS A  165  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS A  166  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER A  167  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER A  168  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 GLY A  169  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 LEU A  170  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 VAL A  171  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 PRO A  172  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 ARG A  173  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 GLY A  174  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER A  175  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS A  176  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 MET A  177  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 MET B 1157  UNP  P10826              INITIATING METHIONINE          
SEQADV 4DM8 GLY B 1158  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER B 1159  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER B 1160  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS B 1161  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS B 1162  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS B 1163  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS B 1164  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS B 1165  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS B 1166  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER B 1167  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER B 1168  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 GLY B 1169  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 LEU B 1170  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 VAL B 1171  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 PRO B 1172  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 ARG B 1173  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 GLY B 1174  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 SER B 1175  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 HIS B 1176  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM8 MET B 1177  UNP  P10826              EXPRESSION TAG                 
SEQRES   1 A  267  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  267  LEU VAL PRO ARG GLY SER HIS MET GLU SER TYR GLU MET          
SEQRES   3 A  267  THR ALA GLU LEU ASP ASP LEU THR GLU LYS ILE ARG LYS          
SEQRES   4 A  267  ALA HIS GLN GLU THR PHE PRO SER LEU CYS GLN LEU GLY          
SEQRES   5 A  267  LYS TYR THR THR ASN SER SER ALA ASP HIS ARG VAL ARG          
SEQRES   6 A  267  LEU ASP LEU GLY LEU TRP ASP LYS PHE SER GLU LEU ALA          
SEQRES   7 A  267  THR LYS CYS ILE ILE LYS ILE VAL GLU PHE ALA LYS ARG          
SEQRES   8 A  267  LEU PRO GLY PHE THR GLY LEU THR ILE ALA ASP GLN ILE          
SEQRES   9 A  267  THR LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU          
SEQRES  10 A  267  ARG ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET          
SEQRES  11 A  267  THR PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET          
SEQRES  12 A  267  HIS ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE          
SEQRES  13 A  267  THR PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP          
SEQRES  14 A  267  THR GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS          
SEQRES  15 A  267  GLY ASP ARG GLN ASP LEU GLU GLU PRO THR LYS VAL ASP          
SEQRES  16 A  267  LYS LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS ILE TYR          
SEQRES  17 A  267  ILE ARG LYS ARG ARG PRO SER LYS PRO HIS MET PHE PRO          
SEQRES  18 A  267  LYS ILE LEU MET LYS ILE THR ASP LEU ARG SER ILE SER          
SEQRES  19 A  267  ALA LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU          
SEQRES  20 A  267  ILE PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU          
SEQRES  21 A  267  GLU ASN SER GLU GLY HIS GLU                                  
SEQRES   1 B  267  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  267  LEU VAL PRO ARG GLY SER HIS MET GLU SER TYR GLU MET          
SEQRES   3 B  267  THR ALA GLU LEU ASP ASP LEU THR GLU LYS ILE ARG LYS          
SEQRES   4 B  267  ALA HIS GLN GLU THR PHE PRO SER LEU CYS GLN LEU GLY          
SEQRES   5 B  267  LYS TYR THR THR ASN SER SER ALA ASP HIS ARG VAL ARG          
SEQRES   6 B  267  LEU ASP LEU GLY LEU TRP ASP LYS PHE SER GLU LEU ALA          
SEQRES   7 B  267  THR LYS CYS ILE ILE LYS ILE VAL GLU PHE ALA LYS ARG          
SEQRES   8 B  267  LEU PRO GLY PHE THR GLY LEU THR ILE ALA ASP GLN ILE          
SEQRES   9 B  267  THR LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU          
SEQRES  10 B  267  ARG ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET          
SEQRES  11 B  267  THR PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET          
SEQRES  12 B  267  HIS ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE          
SEQRES  13 B  267  THR PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP          
SEQRES  14 B  267  THR GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS          
SEQRES  15 B  267  GLY ASP ARG GLN ASP LEU GLU GLU PRO THR LYS VAL ASP          
SEQRES  16 B  267  LYS LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS ILE TYR          
SEQRES  17 B  267  ILE ARG LYS ARG ARG PRO SER LYS PRO HIS MET PHE PRO          
SEQRES  18 B  267  LYS ILE LEU MET LYS ILE THR ASP LEU ARG SER ILE SER          
SEQRES  19 B  267  ALA LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU          
SEQRES  20 B  267  ILE PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU          
SEQRES  21 B  267  GLU ASN SER GLU GLY HIS GLU                                  
SEQRES   1 C   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 C   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
SEQRES   1 D   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 D   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
HET    REA  A 501      22                                                       
HET    REA  B1501      22                                                       
HETNAM     REA RETINOIC ACID                                                    
FORMUL   5  REA    2(C20 H28 O2)                                                
FORMUL   7  HOH   *128(H2 O)                                                    
HELIX    1   1 THR A  183  GLU A  199  1                                  17    
HELIX    2   2 ASP A  223  ARG A  247  1                                  25    
HELIX    3   3 GLY A  250  LEU A  254  5                                   5    
HELIX    4   4 THR A  255  THR A  277  1                                  23    
HELIX    5   5 ARG A  296  GLY A  303  1                                   8    
HELIX    6   6 PHE A  304  PRO A  306  5                                   3    
HELIX    7   7 LEU A  307  LEU A  319  1                                  13    
HELIX    8   8 PRO A  320  GLU A  322  5                                   3    
HELIX    9   9 ASP A  324  ILE A  337  1                                  14    
HELIX   10  10 GLU A  346  ARG A  369  1                                  24    
HELIX   11  11 HIS A  374  ILE A  404  1                                  31    
HELIX   12  12 PRO A  409  LEU A  416  1                                   8    
HELIX   13  13 GLU B 1181  PHE B 1201  1                                  21    
HELIX   14  14 ASP B 1223  LEU B 1248  1                                  26    
HELIX   15  15 GLY B 1250  LEU B 1254  5                                   5    
HELIX   16  16 THR B 1255  THR B 1277  1                                  23    
HELIX   17  17 ARG B 1296  GLY B 1303  1                                   8    
HELIX   18  18 PHE B 1304  PRO B 1306  5                                   3    
HELIX   19  19 LEU B 1307  LEU B 1319  1                                  13    
HELIX   20  20 PRO B 1320  GLU B 1322  5                                   3    
HELIX   21  21 ASP B 1324  ILE B 1337  1                                  14    
HELIX   22  22 GLU B 1346  LYS B 1367  1                                  22    
HELIX   23  23 HIS B 1374  MET B 1381  1                                   8    
HELIX   24  24 MET B 1381  MET B 1402  1                                  22    
HELIX   25  25 PRO B 1409  LEU B 1416  1                                   8    
HELIX   26  26 ILE C  632  GLN C  638  1                                   7    
HELIX   27  27 ILE D 1632  GLN D 1638  1                                   7    
SHEET    1   A 3 TYR A 279  THR A 280  0                                        
SHEET    2   A 3 THR A 285  THR A 287 -1  O  THR A 285   N  THR A 280           
SHEET    3   A 3 THR A 293  ASN A 295 -1  O  LEU A 294   N  MET A 286           
SHEET    1   B 3 TYR B1279  THR B1280  0                                        
SHEET    2   B 3 THR B1285  THR B1287 -1  O  THR B1285   N  THR B1280           
SHEET    3   B 3 THR B1293  ASN B1295 -1  O  LEU B1294   N  MET B1286           
SITE     1 AC1 11 PHE A 201  PHE A 230  LEU A 233  ALA A 234                    
SITE     2 AC1 11 LEU A 271  ILE A 272  ARG A 278  PHE A 288                    
SITE     3 AC1 11 SER A 289  LEU A 400  HOH A 621                               
SITE     1 AC2 11 PHE B1201  PHE B1230  LEU B1233  ALA B1234                    
SITE     2 AC2 11 LEU B1271  ILE B1272  ARG B1278  PHE B1288                    
SITE     3 AC2 11 SER B1289  PHE B1304  HOH B1672                               
SITE     1 AC3 12 LYS A 246  ILE A 256  GLN A 259  ILE A 260                    
SITE     2 AC3 12 PRO A 410  LEU A 411  GLU A 414  HOH A 609                    
SITE     3 AC3 12 GLU B1181  GLU B1185  HOH C 701  HOH C 702                    
CRYST1   58.482   83.622  108.779  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017099  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011959  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009193        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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