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Database: PDB
Entry: 4HEE
LinkDB: 4HEE
Original site: 4HEE 
HEADER    TRANSCRIPTION/TRANSCRIPTION INHIBITOR   03-OCT-12   4HEE              
TITLE     CRYSTAL STRUCTURE OF PPARGAMMA IN COMPLEX WITH COMPOUND 13            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;          
COMPND   3 CHAIN: X;                                                            
COMPND   4 FRAGMENT: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR-GAMMA (UNP      
COMPND   5 RESIDUES 235-505);                                                   
COMPND   6 SYNONYM: PPAR-GAMMA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;  
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND  10 CHAIN: Y;                                                            
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 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: PPARG, NR1C3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 OTHER_DETAILS: PEPTIDE SYNTHESIS                                     
KEYWDS    PPARGAMMA, TRANSCRIPTION-TRANSCRIPTION INHIBITOR COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HAN                                                                 
REVDAT   1   21-AUG-13 4HEE    0                                                
JRNL        AUTH   A.CASIMIRO-GARCIA,R.J.HEEMSTRA,C.F.BIGGE,J.CHEN,F.A.CISKE,   
JRNL        AUTH 2 J.A.DAVIS,T.ELLIS,N.ESMAEIL,D.FLYNN,S.HAN,M.JALAIE,          
JRNL        AUTH 3 J.F.OHREN,N.A.POWELL                                         
JRNL        TITL   DESIGN, SYNTHESIS, AND EVALUATION OF                         
JRNL        TITL 2 IMIDAZO[4,5-C]PYRIDIN-4-ONE DERIVATIVES WITH DUAL ACTIVITY   
JRNL        TITL 3 AT ANGIOTENSIN II TYPE 1 RECEPTOR AND PEROXISOME             
JRNL        TITL 4 PROLIFERATOR-ACTIVATED RECEPTOR-GAMMA                        
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23   767 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23265881                                                     
JRNL        DOI    10.1016/J.BMCL.2012.11.088                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 8619                           
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)  : 0.195                          
REMARK   3   R VALUE            (WORKING SET)  : 0.191                          
REMARK   3   FREE R VALUE                      : 0.258                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.160                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 445                            
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               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.79                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 84.19                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2234                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2106                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2123                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2064                   
REMARK   3   BIN FREE R VALUE                        : 0.2867                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.97                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 111                      
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            : 2143                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.45280                                              
REMARK   3    B22 (A**2) : -4.98920                                             
REMARK   3    B33 (A**2) : 2.53640                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.42                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2249   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3052   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 808    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 59     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 363    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2249   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 287    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2658   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.20                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.64                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.85                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { X|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.9361  -10.2645   17.7217           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1170 T22:   -0.0024                                    
REMARK   3     T33:   -0.1911 T12:    0.0079                                    
REMARK   3     T13:   -0.0477 T23:   -0.0005                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.4767 L22:    1.8408                                    
REMARK   3     L33:    4.2424 L12:    1.2128                                    
REMARK   3     L13:    2.9036 L23:    1.3073                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1158 S12:   -0.5242 S13:   -0.1854                     
REMARK   3     S21:   -0.1331 S22:   -0.0803 S23:   -0.0425                     
REMARK   3     S31:    0.0295 S32:   -0.7168 S33:   -0.0355                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { Y|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    1.9508   -8.6552   15.7078           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0085 T22:    0.0338                                    
REMARK   3     T33:    0.0418 T12:   -0.0506                                    
REMARK   3     T13:    0.0130 T23:   -0.1368                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9721 L22:    0.8695                                    
REMARK   3     L33:    1.4111 L12:   -0.1051                                    
REMARK   3     L13:   -0.9039 L23:    2.0460                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0193 S12:   -0.0212 S13:   -0.0267                     
REMARK   3     S21:   -0.0406 S22:    0.0154 S23:   -0.0518                     
REMARK   3     S31:   -0.0417 S32:    0.1250 S33:    0.0039                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075361.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8628                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.2                               
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM PIPES, 200MM SODIUM THIOCYANATE,   
REMARK 280  16% PEG4000, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.93400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.93400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       27.39350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       36.19100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       27.39350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.19100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.93400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       27.39350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       36.19100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       71.93400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       27.39350            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       36.19100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y                                  
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 X   196                                                      
REMARK 465     LYS X   197                                                      
REMARK 465     LYS X   198                                                      
REMARK 465     GLY X   199                                                      
REMARK 465     HIS X   200                                                      
REMARK 465     HIS X   201                                                      
REMARK 465     HIS X   202                                                      
REMARK 465     HIS X   203                                                      
REMARK 465     HIS X   204                                                      
REMARK 465     HIS X   205                                                      
REMARK 465     GLY X   206                                                      
REMARK 465     GLU X   207                                                      
REMARK 465     SER X   208                                                      
REMARK 465     THR X   241                                                      
REMARK 465     THR X   242                                                      
REMARK 465     ASP X   243                                                      
REMARK 465     ILE X   262                                                      
REMARK 465     LYS X   263                                                      
REMARK 465     PHE X   264                                                      
REMARK 465     LYS X   265                                                      
REMARK 465     HIS X   266                                                      
REMARK 465     ILE X   267                                                      
REMARK 465     THR X   268                                                      
REMARK 465     PRO X   269                                                      
REMARK 465     LEU X   270                                                      
REMARK 465     GLN X   271                                                      
REMARK 465     GLU X   272                                                      
REMARK 465     GLN X   273                                                      
REMARK 465     SER X   274                                                      
REMARK 465     LYS X   275                                                      
REMARK 465     TYR X   477                                                      
REMARK 465     CYS Y   676                                                      
REMARK 465     PRO Y   677                                                      
REMARK 465     SER Y   678                                                      
REMARK 465     SER Y   679                                                      
REMARK 465     HIS Y   680                                                      
REMARK 465     SER Y   681                                                      
REMARK 465     SER Y   682                                                      
REMARK 465     LEU Y   683                                                      
REMARK 465     SER Y   700                                                      
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    SER X 245      119.22   -178.76                                   
REMARK 500    ASP X 260       49.60    -97.49                                   
REMARK 500    LYS X 358      -81.00     20.07                                   
REMARK 500    THR X 461     -135.34    -92.58                                   
REMARK 500    ASP X 462       -1.66    -46.63                                   
REMARK 500    SER X 464      170.24     60.06                                   
REMARK 500    ASP X 475       78.19     57.40                                   
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    VAL X 307        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ASN X 308        24.2      L          L   OUTSIDE RANGE           
REMARK 500    ARG X 357        24.7      L          L   OUTSIDE RANGE           
REMARK 500    LYS X 358        23.1      L          L   OUTSIDE RANGE           
REMARK 500    GLU X 365        24.5      L          L   OUTSIDE RANGE           
REMARK 500    THR X 461        24.8      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 X 613        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH X 634        DISTANCE =  5.78 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 14R X 501                 
DBREF  4HEE X  207   477  UNP    P37231   PPARG_HUMAN    235    505             
DBREF  4HEE Y  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
SEQADV 4HEE MET X  196  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE LYS X  197  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE LYS X  198  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE GLY X  199  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE HIS X  200  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE HIS X  201  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE HIS X  202  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE HIS X  203  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE HIS X  204  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE HIS X  205  UNP  P37231              EXPRESSION TAG                 
SEQADV 4HEE GLY X  206  UNP  P37231              EXPRESSION TAG                 
SEQRES   1 X  282  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY GLU SER          
SEQRES   2 X  282  ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR ASP SER          
SEQRES   3 X  282  TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS ALA ARG          
SEQRES   4 X  282  ALA ILE LEU THR GLY LYS THR THR ASP LYS SER PRO PHE          
SEQRES   5 X  282  VAL ILE TYR ASP MET ASN SER LEU MET MET GLY GLU ASP          
SEQRES   6 X  282  LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN GLU GLN          
SEQRES   7 X  282  SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY CYS GLN          
SEQRES   8 X  282  PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR GLU TYR          
SEQRES   9 X  282  ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP LEU ASN          
SEQRES  10 X  282  ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS GLU ILE          
SEQRES  11 X  282  ILE TYR THR MET LEU ALA SER LEU MET ASN LYS ASP GLY          
SEQRES  12 X  282  VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR ARG GLU          
SEQRES  13 X  282  PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP PHE MET          
SEQRES  14 X  282  GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN ALA LEU          
SEQRES  15 X  282  GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE ALA VAL          
SEQRES  16 X  282  ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU ASN VAL          
SEQRES  17 X  282  LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU GLN ALA          
SEQRES  18 X  282  LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU SER SER          
SEQRES  19 X  282  GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR ASP LEU          
SEQRES  20 X  282  ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU GLN VAL          
SEQRES  21 X  282  ILE LYS LYS THR GLU THR ASP MET SER LEU HIS PRO LEU          
SEQRES  22 X  282  LEU GLN GLU ILE TYR LYS ASP LEU TYR                          
SEQRES   1 Y   25  CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS LYS          
SEQRES   2 Y   25  ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER              
HET    14R  X 501      66                                                       
HETNAM     14R 5-BENZYL-2-ETHYL-3-{(1S)-5-[2-(1H-TETRAZOL-5-YL)                 
HETNAM   2 14R  PHENYL]-2,3-DIHYDRO-1H-INDEN-1-YL}-3,5-DIHYDRO-4H-              
HETNAM   3 14R  IMIDAZO[4,5-C]PYRIDIN-4-ONE                                     
FORMUL   3  14R    C31 H27 N7 O                                                 
FORMUL   4  HOH   *51(H2 O)                                                     
HELIX    1   1 ALA X  209  PHE X  226  1                                  18    
HELIX    2   2 THR X  229  GLY X  239  1                                  11    
HELIX    3   3 ASP X  251  GLY X  258  1                                   8    
HELIX    4   4 VAL X  277  SER X  302  1                                  26    
HELIX    5   5 GLY X  305  LEU X  309  5                                   5    
HELIX    6   6 ASP X  310  ALA X  331  1                                  22    
HELIX    7   7 SER X  332  MET X  334  5                                   3    
HELIX    8   8 SER X  342  GLY X  344  5                                   3    
HELIX    9   9 ARG X  350  SER X  355  1                                   6    
HELIX   10  10 PRO X  359  PHE X  363  5                                   5    
HELIX   11  11 MET X  364  ALA X  376  1                                  13    
HELIX   12  12 ASP X  380  LEU X  393  1                                  14    
HELIX   13  13 ASN X  402  HIS X  425  1                                  24    
HELIX   14  14 GLN X  430  GLU X  460  1                                  31    
HELIX   15  15 HIS X  466  LYS X  474  1                                   9    
HELIX   16  16 HIS Y  687  GLY Y  697  1                                  11    
SHEET    1   A 3 PHE X 247  ILE X 249  0                                        
SHEET    2   A 3 GLY X 346  THR X 349  1  O  PHE X 347   N  ILE X 249           
SHEET    3   A 3 GLY X 338  ILE X 341 -1  N  ILE X 341   O  GLY X 346           
SITE     1 AC1 13 GLY X 284  CYS X 285  ARG X 288  SER X 289                    
SITE     2 AC1 13 HIS X 323  ILE X 326  TYR X 327  VAL X 339                    
SITE     3 AC1 13 LEU X 340  ILE X 341  SER X 342  LYS X 367                    
SITE     4 AC1 13 HIS X 449                                                     
CRYST1   54.787   72.382  143.868  90.00  90.00  90.00 C 2 2 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      0.018253  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013816  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006951        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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