GenomeNet

Database: PDB
Entry: 2PRG
LinkDB: 2PRG
Original site: 2PRG 
HEADER    COMPLEX (THIAZOLIDINEDIONE/RECEPTOR)    14-AUG-98   2PRG              
TITLE     LIGAND-BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED  
TITLE    2 RECEPTOR GAMMA                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LBD (LIGAND BINDING DOMAIN), RESIDUES 207-477;             
COMPND   5 SYNONYM: E DOMAIN;                                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR SRC-1;                        
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: FRAGMENT CONTAINING HD1 & HD2 RESIDUES 628-703;            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: COMPLEX WITH ROSIGLITAZONE (BRL-49653) REGISTRY #     
COMPND  13 122320-73-4                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELLULAR_LOCATION: NUCLEUS;                                          
SOURCE   6 GENE: HUMAN PPAR GAMMA CDNA;                                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PRSET A;                                  
SOURCE  13 EXPRESSION_SYSTEM_GENE: HPPARGAMMA;                                  
SOURCE  14 MOL_ID: 2;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  16 ORGANISM_COMMON: HUMAN;                                              
SOURCE  17 ORGANISM_TAXID: 9606;                                                
SOURCE  18 CELLULAR_LOCATION: NUCLEUS;                                          
SOURCE  19 GENE: SRC-1 CDNA;                                                    
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  22 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  23 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  25 EXPRESSION_SYSTEM_PLASMID: PRSET A                                   
KEYWDS    COMPLEX (THIAZOLIDINEDIONE-RECEPTOR), LIGAND-BINDING DOMAIN, NUCLEAR  
KEYWDS   2 RECEPTOR, APO, TRANSCRIPTION FACTOR, ORPHAN RECEPTOR, COMPLEX        
KEYWDS   3 (THIAZOLIDINEDIONE-RECEPTOR) COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.T.NOLTE,G.B.WISELY,M.V.MILBURN                                      
REVDAT   3   15-JAN-20 2PRG    1       REMARK                                   
REVDAT   2   24-FEB-09 2PRG    1       VERSN                                    
REVDAT   1   19-JUL-99 2PRG    0                                                
JRNL        AUTH   R.T.NOLTE,G.B.WISELY,S.WESTIN,J.E.COBB,M.H.LAMBERT,          
JRNL        AUTH 2 R.KUROKAWA,M.G.ROSENFELD,T.M.WILLSON,C.K.GLASS,M.V.MILBURN   
JRNL        TITL   LIGAND BINDING AND CO-ACTIVATOR ASSEMBLY OF THE PEROXISOME   
JRNL        TITL 2 PROLIFERATOR-ACTIVATED RECEPTOR-GAMMA.                       
JRNL        REF    NATURE                        V. 395   137 1998              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   9744270                                                      
JRNL        DOI    10.1038/25931                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.3                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 26436                          
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 SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 653                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2745                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE                    : 0.2490                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 65                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.031                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4413                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 541                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.38000                                             
REMARK   3    B22 (A**2) : -4.56000                                             
REMARK   3    B33 (A**2) : 12.93000                                             
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.760                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.250 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.480 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.160 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.510 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : SHRINK MASK | SHELL MODEL                            
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 120.0                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : BSXPI_FIXDBLE.XPL                              
REMARK   3  PARAMETER FILE  4  : LOCALPARM.XPL                                  
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 2PRG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000178497.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : OCT-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26501                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY                : 3.420                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 58.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.14                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.18500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS 0.3, X-PLOR                                       
REMARK 200 STARTING MODEL: PDB ENTRY 1PRG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
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       26.10500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.98300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.53050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.98300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.10500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.53050            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 890 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: 2300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY B   239                                                      
REMARK 465     LYS B   240                                                      
REMARK 465     THR B   241                                                      
REMARK 465     THR B   242                                                      
REMARK 465     ASP B   243                                                      
REMARK 465     LYS B   244                                                      
REMARK 465     SER B   245                                                      
REMARK 465     PRO B   246                                                      
REMARK 465     PHE B   247                                                      
REMARK 465     MET B   257                                                      
REMARK 465     GLY B   258                                                      
REMARK 465     GLU B   259                                                      
REMARK 465     ASP B   260                                                      
REMARK 465     LYS B   261                                                      
REMARK 465     ILE B   262                                                      
REMARK 465     LYS B   263                                                      
REMARK 465     PHE B   264                                                      
REMARK 465     LYS B   265                                                      
REMARK 465     HIS B   266                                                      
REMARK 465     ILE B   267                                                      
REMARK 465     THR B   268                                                      
REMARK 465     PRO B   269                                                      
REMARK 465     LEU B   270                                                      
REMARK 465     GLN B   271                                                      
REMARK 465     GLU B   272                                                      
REMARK 465     ASP C   623                                                      
REMARK 465     SER C   624                                                      
REMARK 465     LYS C   625                                                      
REMARK 465     TYR C   626                                                      
REMARK 465     SER C   627                                                      
REMARK 465     ALA C   641                                                      
REMARK 465     GLU C   642                                                      
REMARK 465     GLN C   643                                                      
REMARK 465     GLN C   644                                                      
REMARK 465     LEU C   645                                                      
REMARK 465     ARG C   646                                                      
REMARK 465     HIS C   647                                                      
REMARK 465     ALA C   648                                                      
REMARK 465     ASP C   649                                                      
REMARK 465     ILE C   650                                                      
REMARK 465     ASP C   651                                                      
REMARK 465     THR C   652                                                      
REMARK 465     SER C   653                                                      
REMARK 465     CYS C   654                                                      
REMARK 465     LYS C   655                                                      
REMARK 465     ASP C   656                                                      
REMARK 465     VAL C   657                                                      
REMARK 465     LEU C   658                                                      
REMARK 465     SER C   659                                                      
REMARK 465     CYS C   660                                                      
REMARK 465     THR C   661                                                      
REMARK 465     GLY C   662                                                      
REMARK 465     THR C   663                                                      
REMARK 465     SER C   664                                                      
REMARK 465     ASN C   665                                                      
REMARK 465     SER C   666                                                      
REMARK 465     ALA C   667                                                      
REMARK 465     SER C   668                                                      
REMARK 465     ALA C   669                                                      
REMARK 465     ASN C   670                                                      
REMARK 465     SER C   671                                                      
REMARK 465     SER C   672                                                      
REMARK 465     GLY C   673                                                      
REMARK 465     GLY C   674                                                      
REMARK 465     SER C   675                                                      
REMARK 465     CYS C   676                                                      
REMARK 465     PRO C   677                                                      
REMARK 465     SER C   678                                                      
REMARK 465     SER C   679                                                      
REMARK 465     HIS C   680                                                      
REMARK 465     SER C   681                                                      
REMARK 465     SER C   682                                                      
REMARK 465     LEU C   683                                                      
REMARK 465     THR C   684                                                      
REMARK 465     THR C   704                                                      
REMARK 465     LEU C   705                                                      
REMARK 465     SER C   706                                                      
REMARK 465     VAL C   707                                                      
REMARK 465     GLU C   708                                                      
REMARK 465     PRO C   709                                                      
REMARK 465     ASP C   710                                                      
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    LYS A 240     -159.18    -65.26                                   
REMARK 500    THR A 241      100.99     40.72                                   
REMARK 500    ASP A 243      -15.48   -167.55                                   
REMARK 500    LYS A 244      144.60    175.83                                   
REMARK 500    HIS A 266      173.07    -55.86                                   
REMARK 500    PRO A 269       91.28    -55.59                                   
REMARK 500    LEU A 270     -128.15   -139.72                                   
REMARK 500    GLN A 273      171.96     34.51                                   
REMARK 500    SER A 274       -0.91    126.80                                   
REMARK 500    LYS A 358      -57.88     -6.11                                   
REMARK 500    SER A 464      107.35     77.84                                   
REMARK 500    ASP A 475       83.14     54.66                                   
REMARK 500    ASP B 251     -159.57   -139.90                                   
REMARK 500    LYS B 358      -79.30     10.75                                   
REMARK 500    THR C 629      -86.93     49.63                                   
REMARK 500    ARG C 686       14.79     53.98                                   
REMARK 500    GLU C 696     -133.85    -66.83                                   
REMARK 500    PRO C 699     -124.91    -60.75                                   
REMARK 500    SER C 700      125.38     85.17                                   
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 530        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH A 560        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH A 686        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A 728        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A 733        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 759        DISTANCE =  8.12 ANGSTROMS                       
REMARK 525    HOH A 767        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH B 565        DISTANCE =  7.34 ANGSTROMS                       
REMARK 525    HOH B 609        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH B 643        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH B 649        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH B 658        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH B 667        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH B 672        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH B 677        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH C 425        DISTANCE =  6.30 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: LB1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES ARE INVOLVED IN LIGAND BINDING.     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LB2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES ARE INVOLVED IN LIGAND BINDING.     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: RESIDUES INVOLVED IN BINDING THE LXXLL             
REMARK 800  COACTIVATOR HELIX.                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: RESIDUES INVOLVED IN BINDING THE COACTIVATOR       
REMARK 800  LXXLL HELIX.                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BRL A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BRL B 2                   
DBREF  2PRG A  207   477  UNP    P37231   PPARG_HUMAN    205    475             
DBREF  2PRG B  207   477  UNP    P37231   PPARG_HUMAN    205    475             
DBREF  2PRG C  623   710  UNP    O43792   O43792         623    710             
SEQRES   1 A  271  GLU SER ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR          
SEQRES   2 A  271  ASP SER TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS          
SEQRES   3 A  271  ALA ARG ALA ILE LEU THR GLY LYS THR THR ASP LYS SER          
SEQRES   4 A  271  PRO PHE VAL ILE TYR ASP MET ASN SER LEU MET MET GLY          
SEQRES   5 A  271  GLU ASP LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN          
SEQRES   6 A  271  GLU GLN SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY          
SEQRES   7 A  271  CYS GLN PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR          
SEQRES   8 A  271  GLU TYR ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP          
SEQRES   9 A  271  LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS          
SEQRES  10 A  271  GLU ILE ILE TYR THR MET LEU ALA SER LEU MET ASN LYS          
SEQRES  11 A  271  ASP GLY VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR          
SEQRES  12 A  271  ARG GLU PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP          
SEQRES  13 A  271  PHE MET GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN          
SEQRES  14 A  271  ALA LEU GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE          
SEQRES  15 A  271  ALA VAL ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU          
SEQRES  16 A  271  ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU          
SEQRES  17 A  271  GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU          
SEQRES  18 A  271  SER SER GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR          
SEQRES  19 A  271  ASP LEU ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU          
SEQRES  20 A  271  GLN VAL ILE LYS LYS THR GLU THR ASP MET SER LEU HIS          
SEQRES  21 A  271  PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU TYR                  
SEQRES   1 B  271  GLU SER ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR          
SEQRES   2 B  271  ASP SER TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS          
SEQRES   3 B  271  ALA ARG ALA ILE LEU THR GLY LYS THR THR ASP LYS SER          
SEQRES   4 B  271  PRO PHE VAL ILE TYR ASP MET ASN SER LEU MET MET GLY          
SEQRES   5 B  271  GLU ASP LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN          
SEQRES   6 B  271  GLU GLN SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY          
SEQRES   7 B  271  CYS GLN PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR          
SEQRES   8 B  271  GLU TYR ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP          
SEQRES   9 B  271  LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS          
SEQRES  10 B  271  GLU ILE ILE TYR THR MET LEU ALA SER LEU MET ASN LYS          
SEQRES  11 B  271  ASP GLY VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR          
SEQRES  12 B  271  ARG GLU PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP          
SEQRES  13 B  271  PHE MET GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN          
SEQRES  14 B  271  ALA LEU GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE          
SEQRES  15 B  271  ALA VAL ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU          
SEQRES  16 B  271  ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU          
SEQRES  17 B  271  GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU          
SEQRES  18 B  271  SER SER GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR          
SEQRES  19 B  271  ASP LEU ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU          
SEQRES  20 B  271  GLN VAL ILE LYS LYS THR GLU THR ASP MET SER LEU HIS          
SEQRES  21 B  271  PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU TYR                  
SEQRES   1 C   88  ASP SER LYS TYR SER GLN THR SER HIS LYS LEU VAL GLN          
SEQRES   2 C   88  LEU LEU THR THR THR ALA GLU GLN GLN LEU ARG HIS ALA          
SEQRES   3 C   88  ASP ILE ASP THR SER CYS LYS ASP VAL LEU SER CYS THR          
SEQRES   4 C   88  GLY THR SER ASN SER ALA SER ALA ASN SER SER GLY GLY          
SEQRES   5 C   88  SER CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS          
SEQRES   6 C   88  LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER          
SEQRES   7 C   88  ASP ILE THR THR LEU SER VAL GLU PRO ASP                      
HET    BRL  A   1      25                                                       
HET    BRL  B   2      25                                                       
HETNAM     BRL 2,4-THIAZOLIDIINEDIONE, 5-[[4-[2-(METHYL-2-                      
HETNAM   2 BRL  PYRIDINYLAMINO)ETHOXY]PHENYL]METHYL]-(9CL)                      
HETSYN     BRL BRL49653; ROSIGLITAZONE                                          
FORMUL   4  BRL    2(C18 H19 N3 O3 S)                                           
FORMUL   6  HOH   *541(H2 O)                                                    
HELIX    1   1 SER A  208  SER A  225  1                                  18    
HELIX    2   2 LYS A  230  THR A  238  1                                   9    
HELIX    3   3 MET A  252  PHE A  264  1                                  13    
HELIX    4   4 VAL A  277  SER A  302  1                                  26    
HELIX    5   5 PHE A  306  ASN A  308  5                                   3    
HELIX    6   6 LEU A  311  LEU A  333  1                                  23    
HELIX    7   7 ARG A  350  LEU A  353  1                                   4    
HELIX    8   8 LYS A  358  ASP A  362  1                                   5    
HELIX    9   9 GLU A  365  LEU A  377  1                                  13    
HELIX   10  10 ASP A  381  ILE A  392  1                                  12    
HELIX   11  11 VAL A  403  ASN A  424  1                                  22    
HELIX   12  12 LEU A  431  THR A  459  1                                  29    
HELIX   13  13 PRO A  467  TYR A  473  1                                   7    
HELIX   14  14 SER B  208  SER B  225  1                                  18    
HELIX   15  15 LYS B  230  LEU B  237  1                                   8    
HELIX   16  16 MET B  252  LEU B  255  1                                   4    
HELIX   17  17 SER B  274  SER B  302  1                                  29    
HELIX   18  18 PHE B  306  ASN B  308  5                                   3    
HELIX   19  19 LEU B  311  LEU B  333  1                                  23    
HELIX   20  20 SER B  342  GLY B  344  5                                   3    
HELIX   21  21 ARG B  350  SER B  355  1                                   6    
HELIX   22  22 PHE B  360  ASP B  362  5                                   3    
HELIX   23  23 GLU B  365  LEU B  377  1                                  13    
HELIX   24  24 ASP B  381  ILE B  392  1                                  12    
HELIX   25  25 VAL B  403  ASN B  424  1                                  22    
HELIX   26  26 LEU B  431  THR B  459  1                                  29    
HELIX   27  27 PRO B  467  TYR B  473  1                                   7    
HELIX   28  28 HIS C  631  THR C  638  1                                   8    
HELIX   29  29 LYS C  688  GLN C  695  1                                   8    
SHEET    1   A 3 PHE A 247  ILE A 249  0                                        
SHEET    2   A 3 GLY A 346  THR A 349  1  N  PHE A 347   O  PHE A 247           
SHEET    3   A 3 GLY A 338  ILE A 341 -1  N  ILE A 341   O  GLY A 346           
SHEET    1   B 2 GLY B 338  ILE B 341  0                                        
SHEET    2   B 2 GLY B 346  THR B 349 -1  N  MET B 348   O  VAL B 339           
SITE     1 LB1 11 HIS A 323  LEU A 469  HIS A 449  GLN A 286                    
SITE     2 LB1 11 TYR A 327  LEU A 330  PHE A 282  CYS A 285                    
SITE     3 LB1 11 ARG A 288  GLY A 338  ILE A 341                               
SITE     1 LB2 11 HIS B 323  LEU B 469  HIS B 449  GLN B 286                    
SITE     2 LB2 11 TYR B 327  LEU B 330  PHE B 282  CYS B 285                    
SITE     3 LB2 11 ARG B 288  GLY B 338  ILE B 341                               
SITE     1 CA1  8 GLU A 471  LYS A 301  THR A 297  GLN A 314                    
SITE     2 CA1  8 VAL A 315  LEU A 468  LEU A 318  LEU A 311                    
SITE     1 CA2  8 GLU B 471  LYS B 301  THR B 297  GLN B 314                    
SITE     2 CA2  8 VAL B 315  LEU B 468  LEU B 318  LEU B 311                    
SITE     1 AC1 11 PHE A 282  GLY A 284  CYS A 285  GLN A 286                    
SITE     2 AC1 11 SER A 289  HIS A 323  TYR A 327  ILE A 341                    
SITE     3 AC1 11 MET A 364  HIS A 449  TYR A 473                               
SITE     1 AC2 13 PHE B 282  CYS B 285  GLN B 286  SER B 289                    
SITE     2 AC2 13 HIS B 323  TYR B 327  LEU B 330  LEU B 340                    
SITE     3 AC2 13 ILE B 341  MET B 364  HIS B 449  LEU B 453                    
SITE     4 AC2 13 TYR B 473                                                     
CRYST1   52.210   69.061  177.966  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      0.019153  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014480  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005619        0.00000                         
MTRIX1   1 -0.696300 -0.444100  0.563900       68.34460    1                    
MTRIX2   1 -0.522900 -0.224400 -0.822300       24.76290    1                    
MTRIX3   1  0.491700 -0.867400 -0.076000      -15.42090    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system