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Database: PDB
Entry: 4DM6
LinkDB: 4DM6
Original site: 4DM6 
HEADER    TRANSCRIPTION/PROTEIN BINDING           07-FEB-12   4DM6              
TITLE     CRYSTAL STRUCTURE OF RARB LBD HOMODIMER IN COMPLEX WITH TTNPB         
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: E, F;                                                         
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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSCRIPTION, NUCLEAR RECEPTOR, RETINOIC ACID, ALPHA HELICAL         
KEYWDS   2 SANDWICH, TRANSCRIPTION REGULATOR, RETINOIC ACID BINDING, NUCLEUS -  
KEYWDS   3 CYTOPLASM, TRANSCRIPTION-PROTEIN BINDING COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.OSZ,Y.BRELIVET,C.PELUSO-ILTIS,V.CURA,S.EILER,M.RUFF,W.BOURGUET,     
AUTHOR   2 N.ROCHEL,D.MORAS                                                     
REVDAT   2   16-MAY-12 4DM6    1       JRNL                                     
REVDAT   1   07-MAR-12 4DM6    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
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             : 38045                          
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) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2003                            
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            : 3973                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 178                                     
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.08                            
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 4DM6 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 RCSB070503.                                      
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 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39762                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
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) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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   (%): 34.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89                     
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, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 290K, PH 5.6                                            
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       29.04500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.07000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.03000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.07000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.04500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.03000            
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: 1930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
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: 1900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
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     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 E   676                                                      
REMARK 465     PRO E   677                                                      
REMARK 465     SER E   678                                                      
REMARK 465     SER E   679                                                      
REMARK 465     HIS E   680                                                      
REMARK 465     SER E   681                                                      
REMARK 465     SER E   682                                                      
REMARK 465     LEU E   683                                                      
REMARK 465     THR E   684                                                      
REMARK 465     GLU E   685                                                      
REMARK 465     GLY E   697                                                      
REMARK 465     SER E   698                                                      
REMARK 465     PRO E   699                                                      
REMARK 465     SER E   700                                                      
REMARK 465     CYS F   776                                                      
REMARK 465     PRO F   777                                                      
REMARK 465     SER F   778                                                      
REMARK 465     SER F   779                                                      
REMARK 465     HIS F   780                                                      
REMARK 465     SER F   781                                                      
REMARK 465     SER F   782                                                      
REMARK 465     LEU F   783                                                      
REMARK 465     THR F   784                                                      
REMARK 465     GLU F   785                                                      
REMARK 465     SER F   798                                                      
REMARK 465     PRO F   799                                                      
REMARK 465     SER F   800                                                      
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 470     ARG E 686    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 696    CG   CD   OE1  OE2                                  
REMARK 470     ARG F 786    CB   CG   CD   NE   CZ   NH1  NH2                   
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     GLN A  206   CG   CD   OE1  NE2                                  
REMARK 480     LYS A  264   NZ                                                  
REMARK 480     GLU B 1395   OE1  OE2                                            
REMARK 480     LYS E  688   CE   NZ                                             
REMARK 480     GLN E  695   CD   OE1  NE2                                       
REMARK 480     LYS F  788   CE   NZ                                             
REMARK 480     GLU F  796   CG   CD   OE1  OE2                                  
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    ASN A 213   CB    ASN A 213   CG     -0.143                       
REMARK 500    SER A 214   CB    SER A 214   OG     -0.091                       
REMARK 500    SER A 214   C     SER A 214   O      -0.130                       
REMARK 500    ALA A 216   CA    ALA A 216   CB     -0.160                       
REMARK 500    SER B1214   C     SER B1214   O      -0.174                       
REMARK 500    SER B1215   CB    SER B1215   OG     -0.106                       
REMARK 500    SER B1215   C     SER B1215   O      -0.195                       
REMARK 500    ALA B1216   C     ALA B1216   O      -0.159                       
REMARK 500    LEU E 690   C     LEU E 690   O      -0.128                       
REMARK 500    HIS E 691   C     HIS E 691   O      -0.119                       
REMARK 500    LEU F 794   C     LEU F 794   O      -0.182                       
REMARK 500    GLN F 795   CD    GLN F 795   OE1    -0.136                       
REMARK 500    GLN F 795   C     GLN F 795   O      -0.148                       
REMARK 500    GLU F 796   CB    GLU F 796   CG     -0.213                       
REMARK 500    GLU F 796   C     GLU F 796   O      -0.143                       
REMARK 500    GLY F 797   CA    GLY F 797   C      -0.099                       
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    SER B1215   N   -  CA  -  C   ANGL. DEV. =  18.3 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    THR A 183       59.37   -145.04                                   
REMARK 500    PHE A 201       93.88   -166.96                                   
REMARK 500    SER A 215       47.18     27.76                                   
REMARK 500    ASP A 217      -65.00    -92.63                                   
REMARK 500    LEU A 222      128.49   -171.96                                   
REMARK 500    ASP A 343       32.89     72.73                                   
REMARK 500    SER B1215       43.93     27.94                                   
REMARK 500    GLU F 796      -88.84   -109.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER B1215        20.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 641        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A 645        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH A 660        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH B1677        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH B1685        DISTANCE =  6.54 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTB A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTB B 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E 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: 4DM8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DMA   RELATED DB: PDB                                   
DBREF  4DM6 A  178   423  UNP    P10826   RARB_HUMAN     176    421             
DBREF  4DM6 B 1178  1423  UNP    P10826   RARB_HUMAN     176    421             
DBREF  4DM6 E  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
DBREF  4DM6 F  776   800  UNP    Q15788   NCOA1_HUMAN    676    700             
SEQADV 4DM6 MET A  157  UNP  P10826              INITIATING METHIONINE          
SEQADV 4DM6 GLY A  158  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER A  159  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER A  160  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS A  161  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS A  162  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS A  163  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS A  164  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS A  165  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS A  166  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER A  167  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER A  168  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 GLY A  169  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 LEU A  170  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 VAL A  171  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 PRO A  172  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 ARG A  173  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 GLY A  174  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER A  175  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS A  176  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 MET A  177  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 MET B 1157  UNP  P10826              INITIATING METHIONINE          
SEQADV 4DM6 GLY B 1158  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER B 1159  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER B 1160  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS B 1161  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS B 1162  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS B 1163  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS B 1164  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS B 1165  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS B 1166  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER B 1167  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER B 1168  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 GLY B 1169  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 LEU B 1170  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 VAL B 1171  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 PRO B 1172  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 ARG B 1173  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 GLY B 1174  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 SER B 1175  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 HIS B 1176  UNP  P10826              EXPRESSION TAG                 
SEQADV 4DM6 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 E   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 E   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
SEQRES   1 F   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 F   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
HET    TTB  A 501      26                                                       
HET    TTB  B1501      26                                                       
HETNAM     TTB 4-[(1E)-2-(5,5,8,8-TETRAMETHYL-5,6,7,8-                          
HETNAM   2 TTB  TETRAHYDRONAPHTHALEN-2-YL)PROP-1-ENYL]BENZOIC ACID              
HETSYN     TTB TTNPB                                                            
FORMUL   5  TTB    2(C24 H28 O2)                                                
FORMUL   7  HOH   *178(H2 O)                                                    
HELIX    1   1 THR A  183  PHE A  201  1                                  19    
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  GLU A  417  1                                   9    
HELIX   13  13 GLU B 1181  GLU B 1199  1                                  19    
HELIX   14  14 SER B 1203  LEU B 1207  5                                   5    
HELIX   15  15 ASP B 1223  ARG B 1247  1                                  25    
HELIX   16  16 GLY B 1250  LEU B 1254  5                                   5    
HELIX   17  17 THR B 1255  THR B 1277  1                                  23    
HELIX   18  18 ARG B 1296  GLY B 1303  1                                   8    
HELIX   19  19 PHE B 1304  PRO B 1306  5                                   3    
HELIX   20  20 LEU B 1307  LEU B 1319  1                                  13    
HELIX   21  21 PRO B 1320  GLU B 1322  5                                   3    
HELIX   22  22 ASP B 1324  ILE B 1337  1                                  14    
HELIX   23  23 GLU B 1346  ARG B 1369  1                                  24    
HELIX   24  24 HIS B 1374  MET B 1381  1                                   8    
HELIX   25  25 MET B 1381  ILE B 1404  1                                  24    
HELIX   26  26 PRO B 1409  LEU B 1416  1                                   8    
HELIX   27  27 HIS E  687  GLU E  696  1                                  10    
HELIX   28  28 LYS F  788  GLU F  796  1                                   9    
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 14 PHE A 201  PHE A 230  LEU A 233  ALA A 234                    
SITE     2 AC1 14 LEU A 271  ILE A 272  ILE A 275  ARG A 278                    
SITE     3 AC1 14 PHE A 288  SER A 289  GLY A 393  VAL A 397                    
SITE     4 AC1 14 LEU A 416  HOH A 617                                          
SITE     1 AC2 18 PHE B1201  PHE B1230  LEU B1233  ALA B1234                    
SITE     2 AC2 18 CYS B1237  LEU B1271  ILE B1272  ILE B1275                    
SITE     3 AC2 18 ARG B1278  PHE B1288  SER B1289  GLY B1303                    
SITE     4 AC2 18 PHE B1304  GLY B1393  VAL B1397  LEU B1400                    
SITE     5 AC2 18 ILE B1412  HOH B1628                                          
SITE     1 AC3 12 LYS A 246  GLN A 259  ILE A 260  LYS A 264                    
SITE     2 AC3 12 PRO A 410  LEU A 411  GLU A 414  MET A 415                    
SITE     3 AC3 12 GLU A 417  HOH A 650  MET B1182  GLU B1185                    
CRYST1   58.090   84.060  102.140  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      0.017215  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011896  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009790        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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