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Database: PDB
Entry: 5GTO
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Original site: 5GTO 
HEADER    TRANSCRIPTION                           22-AUG-16   5GTO              
TITLE     HUMAN PPARGAMMA LIGAND BINDING DMAIN COMPLEXED WITH S35               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-283;                                        
COMPND   5 SYNONYM: PPAR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND   9 CHAIN: B;                                                            
COMPND  10 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: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);                             
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    PPARGAMMA, AGONIST, TRANSCRIPTION                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.Y.JANG,S.W.SUH                                                      
REVDAT   3   08-NOV-23 5GTO    1       REMARK                                   
REVDAT   2   30-AUG-17 5GTO    1       REMARK                                   
REVDAT   1   05-JUL-17 5GTO    0                                                
JRNL        AUTH   J.Y.JANG,M.KOH,H.BAE,D.R.AN,H.N.IM,H.S.KIM,J.Y.YOON,         
JRNL        AUTH 2 H.J.YOON,B.W.HAN,S.B.PARK,S.W.SUH                            
JRNL        TITL   STRUCTURAL BASIS FOR DIFFERENTIAL ACTIVITIES OF ENANTIOMERIC 
JRNL        TITL 2 PPAR GAMMA AGONISTS: BINDING OF S35 TO THE ALTERNATE SITE.   
JRNL        REF    BIOCHIM. BIOPHYS. ACTA        V.1865   674 2017              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   28342850                                                     
JRNL        DOI    10.1016/J.BBAPAP.2017.03.008                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 21608                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1113                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1553                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 95                           
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2245                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 67                                      
REMARK   3   SOLVENT ATOMS            : 108                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.21000                                             
REMARK   3    B22 (A**2) : 0.60000                                              
REMARK   3    B33 (A**2) : 0.61000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.204         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.134         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.128         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2360 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2380 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3171 ; 1.482 ; 2.012       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5486 ; 1.233 ; 3.009       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   277 ; 4.855 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   102 ;31.378 ;24.804       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   454 ;13.878 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;19.429 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   361 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2544 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   509 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1111 ; 3.321 ; 5.095       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1110 ; 3.321 ; 5.091       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1384 ; 5.056 ; 7.614       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1385 ; 5.055 ; 7.618       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1248 ; 3.965 ; 5.850       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1249 ; 3.963 ; 5.851       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1786 ; 6.534 ; 8.524       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2794 ; 9.851 ;42.682       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2762 ; 9.809 ;42.545       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5GTO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300001426.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-NOV-13                          
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               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00002                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22810                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 41.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3VN2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M SODIUM MALONATE (PH 7.0), VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 296K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       65.91150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.64300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       65.91150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.64300            
REMARK 290   SMTRY3   4  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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A   195                                                      
REMARK 465     GLU A   196                                                      
REMARK 465     ILE A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     ILE A   201                                                      
REMARK 465     ASP A   202                                                      
REMARK 465     GLN A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     ASN A   205                                                      
REMARK 465     PRO A   206                                                      
REMARK 465     GLN A   271                                                      
REMARK 465     GLU A   272                                                      
REMARK 465     GLN A   273                                                      
REMARK 465     SER A   274                                                      
REMARK 465     GLU B   685                                                      
REMARK 465     GLY B   697                                                      
REMARK 465     SER B   698                                                      
REMARK 465     PRO B   699                                                      
REMARK 465     SER B   700                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NE2  GLN A   437     O    HOH A   601              2.15            
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    ASP A 243      158.41    -49.64                                   
REMARK 500    LEU A 393       49.67    -86.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue T35 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MYR A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5GTN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5GTP   RELATED DB: PDB                                   
DBREF  5GTO A  195   477  UNP    P37231   PPARG_HUMAN    223    505             
DBREF  5GTO B  685   700  PDB    5GTO     5GTO           685    700             
SEQRES   1 A  283  ALA GLU ILE SER SER ASP ILE ASP GLN LEU ASN PRO GLU          
SEQRES   2 A  283  SER ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR ASP          
SEQRES   3 A  283  SER TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS ALA          
SEQRES   4 A  283  ARG ALA ILE LEU THR GLY LYS THR THR ASP LYS SER PRO          
SEQRES   5 A  283  PHE VAL ILE TYR ASP MET ASN SER LEU MET MET GLY GLU          
SEQRES   6 A  283  ASP LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN GLU          
SEQRES   7 A  283  GLN SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY CYS          
SEQRES   8 A  283  GLN PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR GLU          
SEQRES   9 A  283  TYR ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP LEU          
SEQRES  10 A  283  ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS GLU          
SEQRES  11 A  283  ILE ILE TYR THR MET LEU ALA SER LEU MET ASN LYS ASP          
SEQRES  12 A  283  GLY VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR ARG          
SEQRES  13 A  283  GLU PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP PHE          
SEQRES  14 A  283  MET GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN ALA          
SEQRES  15 A  283  LEU GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE ALA          
SEQRES  16 A  283  VAL ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU ASN          
SEQRES  17 A  283  VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU GLN          
SEQRES  18 A  283  ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU SER          
SEQRES  19 A  283  SER GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR ASP          
SEQRES  20 A  283  LEU ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU GLN          
SEQRES  21 A  283  VAL ILE LYS LYS THR GLU THR ASP MET SER LEU HIS PRO          
SEQRES  22 A  283  LEU LEU GLN GLU ILE TYR LYS ASP LEU TYR                      
SEQRES   1 B   16  GLU ARG HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY          
SEQRES   2 B   16  SER PRO SER                                                  
HET    T35  A 501      45                                                       
HET    MYR  A 502      16                                                       
HET    GOL  A 503       6                                                       
HETNAM     T35 2-[4-[5-[(1~{S})-1-[(3,5-DIMETHOXYPHENYL)CARBAMOYL-              
HETNAM   2 T35  (PHENYLMETHYL)CARBAMOYL]OXYPROPYL]-1,2-OXAZOL-3-                
HETNAM   3 T35  YL]PHENOXY]-2-METHYL-PROPANOIC ACID                             
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  T35    C33 H35 N3 O9                                                
FORMUL   4  MYR    C14 H28 O2                                                   
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *108(H2 O)                                                    
HELIX    1 AA1 GLU A  207  PHE A  226  1                                  20    
HELIX    2 AA2 THR A  229  THR A  238  1                                  10    
HELIX    3 AA3 ASP A  251  LYS A  263  1                                  13    
HELIX    4 AA4 PHE A  264  ILE A  267  5                                   4    
HELIX    5 AA5 GLU A  276  SER A  302  1                                  27    
HELIX    6 AA6 ASP A  310  LEU A  333  1                                  24    
HELIX    7 AA7 ARG A  350  SER A  355  1                                   6    
HELIX    8 AA8 PRO A  359  PHE A  363  5                                   5    
HELIX    9 AA9 MET A  364  ALA A  376  1                                  13    
HELIX   10 AB1 ASP A  380  LEU A  393  1                                  14    
HELIX   11 AB2 ASN A  402  HIS A  425  1                                  24    
HELIX   12 AB3 GLN A  430  GLU A  460  1                                  31    
HELIX   13 AB4 HIS A  466  LYS A  474  1                                   9    
HELIX   14 AB5 HIS B  687  GLU B  696  1                                  10    
SHEET    1 AA1 4 PHE A 247  ILE A 249  0                                        
SHEET    2 AA1 4 GLY A 346  THR A 349  1  O  PHE A 347   N  ILE A 249           
SHEET    3 AA1 4 GLY A 338  ILE A 341 -1  N  VAL A 339   O  MET A 348           
SHEET    4 AA1 4 MET A 334  ASN A 335 -1  N  ASN A 335   O  GLY A 338           
CISPEP   1 LYS A  358    PRO A  359          0        -9.53                     
SITE     1 AC1 16 SER A 245  GLU A 259  ILE A 262  PHE A 264                    
SITE     2 AC1 16 ILE A 267  THR A 268  PRO A 269  LEU A 270                    
SITE     3 AC1 16 ARG A 280  ILE A 281  GLN A 283  GLY A 284                    
SITE     4 AC1 16 LEU A 340  ILE A 341  SER A 342  MYR A 502                    
SITE     1 AC2  8 LEU A 228  CYS A 285  SER A 289  MET A 329                    
SITE     2 AC2  8 LEU A 333  T35 A 501  GOL A 503  HOH A 610                    
SITE     1 AC3  8 PHE A 282  GLN A 286  SER A 289  HIS A 323                    
SITE     2 AC3  8 HIS A 449  LEU A 469  TYR A 473  MYR A 502                    
CRYST1  131.823   53.286   53.740  90.00  90.00  90.00 P 21 21 2     4          
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      0.007586  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018767  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018608        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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