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Entry: 4DQM
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HEADER    TRANSCRIPTION/TRANSFERASE               16-FEB-12   4DQM              
TITLE     REVEALING A MARINE NATURAL PRODUCT AS A NOVEL AGONIST FOR RETINOIC    
TITLE    2 ACID RECEPTORS WITH A UNIQUE BINDING MODE AND ANTITUMOR ACTIVITY     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINOIC ACID RECEPTOR ALPHA;                              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN, UNP RESIDUES 182-415;               
COMPND   5 SYNONYM: RAR-ALPHA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP B MEMBER 1;   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: LXXLL MOTIF 7, UNP RESIDUES 1432-1441;                     
COMPND  11 SYNONYM: NCOA-1, CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74, BHLHE74, 
COMPND  12 PROTEIN HIN-2, RIP160, RENAL CARCINOMA ANTIGEN NY-REN-52, STEROID    
COMPND  13 RECEPTOR COACTIVATOR 1, SRC-1;                                       
COMPND  14 EC: 2.3.1.48;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NR1B1, RARA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.               
KEYWDS    NUCLEAR RECEPTOR TRANSCRIPTION FACTOR, LIGAND BINDING DOMAIN,         
KEYWDS   2 TRANSCRIPTION REGULATION, NUCLEUS, TRANSCRIPTION-TRANSFERASE COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.WANG,Z.WANG,S.LIN,W.ZHENG,R.WANG,S.JIN,J.CHEN,L.JIN,Y.LI            
REVDAT   3   15-NOV-17 4DQM    1       REMARK                                   
REVDAT   2   16-APR-14 4DQM    1       REMARK                                   
REVDAT   1   03-OCT-12 4DQM    0                                                
JRNL        AUTH   S.WANG,Z.WANG,S.LIN,W.ZHENG,R.WANG,S.JIN,J.CHEN,L.JIN,Y.LI   
JRNL        TITL   REVEALING A NATURAL MARINE PRODUCT AS A NOVEL AGONIST FOR    
JRNL        TITL 2 RETINOIC ACID RECEPTORS WITH A UNIQUE BINDING MODE AND       
JRNL        TITL 3 INHIBITORY EFFECTS ON CANCER CELLS.                          
JRNL        REF    BIOCHEM.J.                    V. 446    79 2012              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   22642567                                                     
JRNL        DOI    10.1042/BJ20120726                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16995                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 922                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.62                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1139                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.3350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3855                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10000                                             
REMARK   3    B22 (A**2) : 0.15000                                              
REMARK   3    B33 (A**2) : -0.05000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.885         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.337         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.263         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.510        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3968 ; 0.014 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5360 ; 1.750 ; 2.018       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   484 ; 6.145 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   162 ;39.109 ;24.815       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   763 ;19.768 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;23.147 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   636 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2863 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4DQM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-FEB-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070660.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5619                             
REMARK 200  MONOCHROMATOR                  : DIAMOND [111]                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17478                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
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) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64800                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% V/V TACSIMATE PH7.0, 5% 2-PROPANOL,   
REMARK 280  0.1M IMADAZOLE , 8% PEG 3350, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.23000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.74000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.23000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.74000            
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: 950 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 900 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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     ASP C 282    N                                                   
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     CYS A  333   SG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    SER A   287     O3   LUF A   501              1.68            
REMARK 500   SG   CYS A   235     C23  LUF A   501              1.79            
REMARK 500   N    SER C   287     O3   LUF C   501              1.87            
REMARK 500   SG   CYS C   235     C23  LUF C   501              1.91            
REMARK 500   OE2  GLU C   412     O    SER D  1433              1.96            
REMARK 500   NH2  ARG C   364     O    HOH C   610              2.12            
REMARK 500   CA   PHE C   286     O3   LUF C   501              2.14            
REMARK 500   CA   PHE A   286     O3   LUF A   501              2.16            
REMARK 500   C    PHE A   286     O3   LUF A   501              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 333   CB    CYS A 333   SG     -0.344                       
REMARK 500    HIS A 372   CG    HIS A 372   CD2     0.054                       
REMARK 500    TRP C 225   CE2   TRP C 225   CD2     0.079                       
REMARK 500    HIS C 372   CG    HIS C 372   CD2     0.056                       
REMARK 500    GLU D1441   CD    GLU D1441   OE2     0.068                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 333   CA  -  CB  -  SG  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    LEU C 378   CB  -  CG  -  CD1 ANGL. DEV. = -10.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 208      126.90   -174.44                                   
REMARK 500    SER A 213       42.22     23.62                                   
REMARK 500    GLU A 215      -64.30    -99.12                                   
REMARK 500    ASP A 322     -165.84   -106.32                                   
REMARK 500    LYS A 390        6.73    -69.97                                   
REMARK 500    PRO A 403      -73.66    -75.75                                   
REMARK 500    LEU B1434      -53.40    -22.43                                   
REMARK 500    PHE C 199       86.37   -154.71                                   
REMARK 500    THR C 209     -151.51   -127.03                                   
REMARK 500    THR C 210      157.08    179.70                                   
REMARK 500    SER C 213       49.27     28.91                                   
REMARK 500    LEU C 220      112.86   -161.87                                   
REMARK 500    ASP C 341       18.69     86.53                                   
REMARK 500    PRO C 403      -81.80    -71.65                                   
REMARK 500    SER D1433        3.16    -53.47                                   
REMARK 500    LEU D1434      -53.64    107.17                                   
REMARK 500    THR D1440       44.80    -93.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     LUF C  501                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUF A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUF C 501                 
DBREF  4DQM A  182   415  UNP    P10276   RARA_HUMAN     182    415             
DBREF  4DQM B 1432  1441  UNP    Q15788   NCOA1_HUMAN   1432   1441             
DBREF  4DQM C  182   415  UNP    P10276   RARA_HUMAN     182    415             
DBREF  4DQM D 1432  1441  UNP    Q15788   NCOA1_HUMAN   1432   1441             
SEQRES   1 A  234  PRO GLU VAL GLY GLU LEU ILE GLU LYS VAL ARG LYS ALA          
SEQRES   2 A  234  HIS GLN GLU THR PHE PRO ALA LEU CYS GLN LEU GLY LYS          
SEQRES   3 A  234  TYR THR THR ASN ASN SER SER GLU GLN ARG VAL SER LEU          
SEQRES   4 A  234  ASP ILE ASP LEU TRP ASP LYS PHE SER GLU LEU SER THR          
SEQRES   5 A  234  LYS CYS ILE ILE LYS THR VAL GLU PHE ALA LYS GLN LEU          
SEQRES   6 A  234  PRO GLY PHE THR THR LEU THR ILE ALA ASP GLN ILE THR          
SEQRES   7 A  234  LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU ARG          
SEQRES   8 A  234  ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET THR          
SEQRES   9 A  234  PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET HIS          
SEQRES  10 A  234  ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE ALA          
SEQRES  11 A  234  PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP ALA          
SEQRES  12 A  234  GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS GLY          
SEQRES  13 A  234  ASP ARG GLN ASP LEU GLU GLN PRO ASP ARG VAL ASP MET          
SEQRES  14 A  234  LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS VAL TYR VAL          
SEQRES  15 A  234  ARG LYS ARG ARG PRO SER ARG PRO HIS MET PHE PRO LYS          
SEQRES  16 A  234  MET LEU MET LYS ILE THR ASP LEU ARG SER ILE SER ALA          
SEQRES  17 A  234  LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU ILE          
SEQRES  18 A  234  PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU GLU          
SEQRES   1 B   10  LYS SER LEU LEU GLN GLN LEU LEU THR GLU                      
SEQRES   1 C  234  PRO GLU VAL GLY GLU LEU ILE GLU LYS VAL ARG LYS ALA          
SEQRES   2 C  234  HIS GLN GLU THR PHE PRO ALA LEU CYS GLN LEU GLY LYS          
SEQRES   3 C  234  TYR THR THR ASN ASN SER SER GLU GLN ARG VAL SER LEU          
SEQRES   4 C  234  ASP ILE ASP LEU TRP ASP LYS PHE SER GLU LEU SER THR          
SEQRES   5 C  234  LYS CYS ILE ILE LYS THR VAL GLU PHE ALA LYS GLN LEU          
SEQRES   6 C  234  PRO GLY PHE THR THR LEU THR ILE ALA ASP GLN ILE THR          
SEQRES   7 C  234  LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU ARG          
SEQRES   8 C  234  ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET THR          
SEQRES   9 C  234  PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET HIS          
SEQRES  10 C  234  ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE ALA          
SEQRES  11 C  234  PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP ALA          
SEQRES  12 C  234  GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS GLY          
SEQRES  13 C  234  ASP ARG GLN ASP LEU GLU GLN PRO ASP ARG VAL ASP MET          
SEQRES  14 C  234  LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS VAL TYR VAL          
SEQRES  15 C  234  ARG LYS ARG ARG PRO SER ARG PRO HIS MET PHE PRO LYS          
SEQRES  16 C  234  MET LEU MET LYS ILE THR ASP LEU ARG SER ILE SER ALA          
SEQRES  17 C  234  LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU ILE          
SEQRES  18 C  234  PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU GLU          
SEQRES   1 D   10  LYS SER LEU LEU GLN GLN LEU LEU THR GLU                      
HET    LUF  A 501      28                                                       
HET    LUF  C 501      26                                                       
HETNAM     LUF (5S)-4-[(3E,7E)-4,8-DIMETHYL-10-(2,6,6-                          
HETNAM   2 LUF  TRIMETHYLCYCLOHEX-1-EN-1-YL)DECA-3,7-DIEN-1-YL]-5-              
HETNAM   3 LUF  HYDROXYFURAN-2(5H)-ONE                                          
HETSYN     LUF LUFFARIELLOLIDE                                                  
FORMUL   5  LUF    2(C25 H38 O3)                                                
FORMUL   7  HOH   *31(H2 O)                                                     
HELIX    1   1 PRO A  182  PHE A  199  1                                  18    
HELIX    2   2 ALA A  201  LEU A  205  5                                   5    
HELIX    3   3 ASP A  221  GLN A  245  1                                  25    
HELIX    4   4 GLY A  248  LEU A  252  5                                   5    
HELIX    5   5 THR A  253  THR A  275  1                                  23    
HELIX    6   6 ARG A  294  ALA A  300  1                                   7    
HELIX    7   7 GLY A  301  PRO A  304  5                                   4    
HELIX    8   8 LEU A  305  LEU A  317  1                                  13    
HELIX    9   9 PRO A  318  GLU A  320  5                                   3    
HELIX   10  10 ASP A  322  ILE A  335  1                                  14    
HELIX   11  11 GLN A  344  ARG A  367  1                                  24    
HELIX   12  12 HIS A  372  MET A  379  1                                   8    
HELIX   13  13 MET A  379  LYS A  390  1                                  12    
HELIX   14  14 LYS A  390  ILE A  402  1                                  13    
HELIX   15  15 PRO A  407  GLU A  415  1                                   9    
HELIX   16  16 SER B 1433  GLU B 1441  1                                   9    
HELIX   17  17 GLU C  183  PHE C  199  1                                  17    
HELIX   18  18 ALA C  201  LEU C  205  5                                   5    
HELIX   19  19 ASP C  221  GLN C  245  1                                  25    
HELIX   20  20 GLY C  248  LEU C  252  5                                   5    
HELIX   21  21 THR C  253  THR C  275  1                                  23    
HELIX   22  22 ARG C  294  ALA C  300  1                                   7    
HELIX   23  23 GLY C  301  GLY C  303  5                                   3    
HELIX   24  24 PRO C  304  LEU C  316  1                                  13    
HELIX   25  25 ASP C  322  ILE C  335  1                                  14    
HELIX   26  26 GLN C  344  ARG C  367  1                                  24    
HELIX   27  27 HIS C  372  LYS C  390  1                                  19    
HELIX   28  28 LYS C  390  MET C  400  1                                  11    
HELIX   29  29 PRO C  407  GLU C  415  1                                   9    
HELIX   30  30 LEU D 1435  THR D 1440  1                                   6    
SHEET    1   A 3 TYR A 277  THR A 278  0                                        
SHEET    2   A 3 THR A 283  THR A 285 -1  O  THR A 283   N  THR A 278           
SHEET    3   A 3 THR A 291  ASN A 293 -1  O  LEU A 292   N  MET A 284           
SHEET    1   B 3 TYR C 277  THR C 278  0                                        
SHEET    2   B 3 THR C 283  THR C 285 -1  O  THR C 283   N  THR C 278           
SHEET    3   B 3 THR C 291  ASN C 293 -1  O  LEU C 292   N  MET C 284           
LINK         SG  CYS A 235                 O2  LUF A 501     1555   1555  0.72  
LINK         SG  CYS C 235                 O2  LUF C 501     1555   1555  1.55  
SITE     1 AC1 13 PHE A 228  LEU A 231  SER A 232  CYS A 235                    
SITE     2 AC1 13 LEU A 266  LEU A 269  ILE A 273  ARG A 276                    
SITE     3 AC1 13 PHE A 286  SER A 287  GLY A 301  VAL A 395                    
SITE     4 AC1 13 LEU A 414                                                     
SITE     1 AC2 13 PHE C 228  LEU C 231  SER C 232  CYS C 235                    
SITE     2 AC2 13 LEU C 266  LEU C 269  ILE C 273  ARG C 276                    
SITE     3 AC2 13 PHE C 286  SER C 287  PHE C 302  VAL C 395                    
SITE     4 AC2 13 HOH C 605                                                     
CRYST1   54.120  104.460  113.480  90.00  90.00  90.00 P 2 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      0.018477  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009573  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008812        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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