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Database: PDB
Entry: 5JI0
LinkDB: 5JI0
Original site: 5JI0 
HEADER    TRANSFERASE                             21-APR-16   5JI0              
TITLE     PPARGAMMA-RXRALPHA(S427F) HETERODIMER IN COMPLEX WITH SRC-1,          
TITLE    2 ROSIGLITAZONE, AND 9-CIS-RETANOIC ACID                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINOIC ACID RECEPTOR RXR-ALPHA;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NUCLEAR RECEPTOR SUBFAMILY 2 GROUP B MEMBER 1,RETINOID X    
COMPND   5 RECEPTOR ALPHA;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;          
COMPND  10 CHAIN: D;                                                            
COMPND  11 SYNONYM: PPAR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;   
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;                            
COMPND  15 CHAIN: E, F;                                                         
COMPND  16 SYNONYM: NCOA-1,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74,BHLHE74,   
COMPND  17 PROTEIN HIN-2,RIP160,RENAL CARCINOMA ANTIGEN NY-REN-52,STEROID       
COMPND  18 RECEPTOR COACTIVATOR 1,SRC-1;                                        
COMPND  19 EC: 2.3.1.48;                                                        
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 OTHER_DETAILS: AC-CPSSHSSLTERHKILHRLLQEGSPS-AMIDE                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RXRA, NR2B1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PPARG, NR1C3;                                                  
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606                                                 
KEYWDS    PPARG, RXRA, SRC1, AGONIST, NUCLEAR HORMONE RECEPTOR, HETERODIMER,    
KEYWDS   2 BLADDER CANCER, MUSCLE INVASIVE BLADDER CANCER, MIBC, TRANSFERASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.BLOUDOFF,N.A.LARSEN                                                 
REVDAT   1   26-APR-17 5JI0    0                                                
JRNL        AUTH   M.KORPAL,P.ZHU,K.BLOUDOFF,N.A.LARSEN,P.FEKKES                
JRNL        TITL   PPARGAMMA-RXRALPHA(S427F) HETERODIMER IN COMPLEX WITH SRC-1, 
JRNL        TITL 2 ROSIGLITAZONE, AND 9-CIS-RETANOIC ACID                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 40336                          
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) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2141                            
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) : 1.98                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2773                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 158                          
REMARK   3   BIN FREE R VALUE                    : 0.3000                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4087                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 231                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31000                                              
REMARK   3    B22 (A**2) : -2.94000                                             
REMARK   3    B33 (A**2) : 2.64000                                              
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): 0.169         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.163         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.132         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.780         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
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):  4214 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4186 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5687 ; 1.921 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9641 ; 1.168 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   508 ; 6.332 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   185 ;36.205 ;24.703       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   785 ;15.969 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;25.388 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   655 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4624 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   911 ; 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):  2047 ; 4.182 ; 4.456       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2046 ; 4.182 ; 4.454       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2547 ; 5.827 ; 6.644       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2548 ; 5.826 ; 6.647       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2167 ; 4.688 ; 4.920       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2168 ; 4.688 ; 4.922       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3140 ; 7.071 ; 7.219       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5123 ; 9.859 ;37.127       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5054 ; 9.888 ;37.086       
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 : NULL                                                 
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 5JI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220493.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GREW IN THE DARK AT ROOM        
REMARK 280  TEMPERATURE FROM 0.5 + 0.5 UL SITTING DROPS EQUILIBRATED OVER A     
REMARK 280  RESERVOIR CONTAINING 20-24% PEG3350 AND 0.02M NA CITRATE, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 296K                           
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       26.94000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.96350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.26350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.96350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.94000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.26350            
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, 3                                                 
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 970 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A   221                                                      
REMARK 465     MET A   222                                                      
REMARK 465     THR A   223                                                      
REMARK 465     SER A   224                                                      
REMARK 465     SER A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     ALA A   252                                                      
REMARK 465     ASN A   253                                                      
REMARK 465     MET A   254                                                      
REMARK 465     GLY A   255                                                      
REMARK 465     LEU A   256                                                      
REMARK 465     ASN A   257                                                      
REMARK 465     PRO A   258                                                      
REMARK 465     SER A   259                                                      
REMARK 465     SER A   260                                                      
REMARK 465     PRO A   261                                                      
REMARK 465     PRO A   446                                                      
REMARK 465     ILE A   447                                                      
REMARK 465     ASP A   448                                                      
REMARK 465     GLU A   456                                                      
REMARK 465     ALA A   457                                                      
REMARK 465     PRO A   458                                                      
REMARK 465     HIS A   459                                                      
REMARK 465     GLN A   460                                                      
REMARK 465     MET A   461                                                      
REMARK 465     THR A   462                                                      
REMARK 465     LYS D   263                                                      
REMARK 465     PHE D   264                                                      
REMARK 465     LYS D   265                                                      
REMARK 465     HIS D   266                                                      
REMARK 465     ACE E   675                                                      
REMARK 465     CYS E   676                                                      
REMARK 465     PRO E   677                                                      
REMARK 465     SER E   678                                                      
REMARK 465     SER E   679                                                      
REMARK 465     HIS E   680                                                      
REMARK 465     SER E   681                                                      
REMARK 465     NH2 E   701                                                      
REMARK 465     ACE F   675                                                      
REMARK 465     CYS F   676                                                      
REMARK 465     PRO F   677                                                      
REMARK 465     SER F   678                                                      
REMARK 465     SER F   679                                                      
REMARK 465     HIS F   680                                                      
REMARK 465     SER F   681                                                      
REMARK 465     SER F   682                                                      
REMARK 465     LEU F   683                                                      
REMARK 465     THR F   684                                                      
REMARK 465     GLU F   685                                                      
REMARK 465     ARG F   686                                                      
REMARK 465     HIS F   687                                                      
REMARK 465     GLY F   697                                                      
REMARK 465     SER F   698                                                      
REMARK 465     PRO F   699                                                      
REMARK 465     SER F   700                                                      
REMARK 465     NH2 F   701                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS D 244    CG   CD   CE   NZ                                   
REMARK 470     ARG E 692    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 688    CG   CD   CE   NZ                                   
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  HIS E   691     OE1  GLN E   695              2.07            
REMARK 500   O    HOH D   704     O    HOH D   732              2.11            
REMARK 500   O    HOH D   751     O    HOH D   756              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    THR D   238     OE1  GLN D   273     4447     1.52            
REMARK 500   CA   GLY D   239     OE1  GLN D   273     4447     1.57            
REMARK 500   O    GLY D   239     CG   GLN D   273     4447     1.73            
REMARK 500   N    GLY D   239     OE1  GLN D   273     4447     1.75            
REMARK 500   C    THR D   238     OE1  GLN D   273     4447     1.78            
REMARK 500   N    LYS D   240     NE2  GLN D   273     4447     1.78            
REMARK 500   C    GLY D   239     NE2  GLN D   273     4447     1.84            
REMARK 500   CA   GLY D   239     CD   GLN D   273     4447     1.87            
REMARK 500   C    GLY D   239     CG   GLN D   273     4447     2.06            
REMARK 500   O    GLY D   239     CD   GLN D   273     4447     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG D 212   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG D 234   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG D 234   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 228       52.83     37.69                                   
REMARK 500    MET A 230       77.53   -169.99                                   
REMARK 500    ALA A 241        4.80    -61.32                                   
REMARK 500    GLU A 243       83.35    113.96                                   
REMARK 500    THR A 248      -84.46    -82.12                                   
REMARK 500    HIS A 288       -4.95     71.60                                   
REMARK 500    GLU A 291        1.51    -62.38                                   
REMARK 500    LYS D 261       10.34    -62.87                                   
REMARK 500    SER D 274       -9.21     78.95                                   
REMARK 500    THR D 459       17.90   -152.26                                   
REMARK 500    THR D 461     -117.44     59.04                                   
REMARK 500    ASP D 475       30.54     72.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  228     ASP A  229                  146.26                    
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 9CR A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BRL D 501                 
DBREF  5JI0 A  223   462  UNP    P19793   RXRA_HUMAN     223    462             
DBREF  5JI0 D  206   477  UNP    P37231   PPARG_HUMAN    234    505             
DBREF  5JI0 E  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
DBREF  5JI0 F  676   700  UNP    Q15788   NCOA1_HUMAN    676    700             
SEQADV 5JI0 GLY A  221  UNP  P19793              EXPRESSION TAG                 
SEQADV 5JI0 MET A  222  UNP  P19793              EXPRESSION TAG                 
SEQADV 5JI0 PHE A  427  UNP  P19793    SER   427 ENGINEERED MUTATION            
SEQADV 5JI0 GLY D  205  UNP  P37231              EXPRESSION TAG                 
SEQADV 5JI0 ACE E  675  UNP  Q15788              ACETYLATION                    
SEQADV 5JI0 NH2 E  701  UNP  Q15788              AMIDATION                      
SEQADV 5JI0 ACE F  675  UNP  Q15788              ACETYLATION                    
SEQADV 5JI0 NH2 F  701  UNP  Q15788              AMIDATION                      
SEQRES   1 A  242  GLY MET THR SER SER ALA ASN GLU ASP MET PRO VAL GLU          
SEQRES   2 A  242  ARG ILE LEU GLU ALA GLU LEU ALA VAL GLU PRO LYS THR          
SEQRES   3 A  242  GLU THR TYR VAL GLU ALA ASN MET GLY LEU ASN PRO SER          
SEQRES   4 A  242  SER PRO ASN ASP PRO VAL THR ASN ILE CYS GLN ALA ALA          
SEQRES   5 A  242  ASP LYS GLN LEU PHE THR LEU VAL GLU TRP ALA LYS ARG          
SEQRES   6 A  242  ILE PRO HIS PHE SER GLU LEU PRO LEU ASP ASP GLN VAL          
SEQRES   7 A  242  ILE LEU LEU ARG ALA GLY TRP ASN GLU LEU LEU ILE ALA          
SEQRES   8 A  242  SER PHE SER HIS ARG SER ILE ALA VAL LYS ASP GLY ILE          
SEQRES   9 A  242  LEU LEU ALA THR GLY LEU HIS VAL HIS ARG ASN SER ALA          
SEQRES  10 A  242  HIS SER ALA GLY VAL GLY ALA ILE PHE ASP ARG VAL LEU          
SEQRES  11 A  242  THR GLU LEU VAL SER LYS MET ARG ASP MET GLN MET ASP          
SEQRES  12 A  242  LYS THR GLU LEU GLY CYS LEU ARG ALA ILE VAL LEU PHE          
SEQRES  13 A  242  ASN PRO ASP SER LYS GLY LEU SER ASN PRO ALA GLU VAL          
SEQRES  14 A  242  GLU ALA LEU ARG GLU LYS VAL TYR ALA SER LEU GLU ALA          
SEQRES  15 A  242  TYR CYS LYS HIS LYS TYR PRO GLU GLN PRO GLY ARG PHE          
SEQRES  16 A  242  ALA LYS LEU LEU LEU ARG LEU PRO ALA LEU ARG PHE ILE          
SEQRES  17 A  242  GLY LEU LYS CYS LEU GLU HIS LEU PHE PHE PHE LYS LEU          
SEQRES  18 A  242  ILE GLY ASP THR PRO ILE ASP THR PHE LEU MET GLU MET          
SEQRES  19 A  242  LEU GLU ALA PRO HIS GLN MET THR                              
SEQRES   1 D  273  GLY PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS HIS          
SEQRES   2 D  273  LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR LYS          
SEQRES   3 D  273  ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR ASP          
SEQRES   4 D  273  LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU MET          
SEQRES   5 D  273  MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR PRO          
SEQRES   6 D  273  LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE PHE          
SEQRES   7 D  273  GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN GLU          
SEQRES   8 D  273  ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL ASN          
SEQRES   9 D  273  LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY          
SEQRES  10 D  273  VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU MET          
SEQRES  11 D  273  ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY PHE          
SEQRES  12 D  273  MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO PHE          
SEQRES  13 D  273  GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL LYS          
SEQRES  14 D  273  PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA ILE          
SEQRES  15 D  273  PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO GLY          
SEQRES  16 D  273  LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN          
SEQRES  17 D  273  LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS          
SEQRES  18 D  273  PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN LYS          
SEQRES  19 D  273  MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL GLN          
SEQRES  20 D  273  LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET SER          
SEQRES  21 D  273  LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU TYR          
SEQRES   1 E   27  ACE CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS          
SEQRES   2 E   27  LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER          
SEQRES   3 E   27  NH2                                                          
SEQRES   1 F   27  ACE CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS          
SEQRES   2 F   27  LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER          
SEQRES   3 F   27  NH2                                                          
HET    9CR  A 501      22                                                       
HET    BRL  D 501      25                                                       
HETNAM     9CR (9CIS)-RETINOIC ACID                                             
HETNAM     BRL 2,4-THIAZOLIDIINEDIONE, 5-[[4-[2-(METHYL-2-                      
HETNAM   2 BRL  PYRIDINYLAMINO)ETHOXY]PHENYL]METHYL]-(9CL)                      
HETSYN     BRL BRL49653; ROSIGLITAZONE                                          
FORMUL   5  9CR    C20 H28 O2                                                   
FORMUL   6  BRL    C18 H19 N3 O3 S                                              
FORMUL   7  HOH   *231(H2 O)                                                    
HELIX    1 AA1 PRO A  231  ALA A  241  1                                  11    
HELIX    2 AA2 ASP A  263  ARG A  285  1                                  23    
HELIX    3 AA3 PRO A  293  SER A  317  1                                  25    
HELIX    4 AA4 ARG A  334  ALA A  340  1                                   7    
HELIX    5 AA5 VAL A  342  LEU A  353  1                                  12    
HELIX    6 AA6 LEU A  353  GLN A  361  1                                   9    
HELIX    7 AA7 ASP A  363  PHE A  376  1                                  14    
HELIX    8 AA8 ASN A  385  TYR A  408  1                                  24    
HELIX    9 AA9 GLY A  413  LEU A  420  1                                   8    
HELIX   10 AB1 ARG A  421  GLY A  443  1                                  23    
HELIX   11 AB2 PHE A  450  LEU A  455  1                                   6    
HELIX   12 AB3 GLU D  207  PHE D  226  1                                  20    
HELIX   13 AB4 THR D  229  THR D  238  1                                  10    
HELIX   14 AB5 ASP D  251  GLU D  259  1                                   9    
HELIX   15 AB6 GLU D  276  SER D  302  1                                  27    
HELIX   16 AB7 GLY D  305  LEU D  309  5                                   5    
HELIX   17 AB8 ASP D  310  LEU D  333  1                                  24    
HELIX   18 AB9 SER D  342  GLY D  344  5                                   3    
HELIX   19 AC1 ARG D  350  SER D  355  1                                   6    
HELIX   20 AC2 MET D  364  ALA D  376  1                                  13    
HELIX   21 AC3 ASP D  380  LEU D  393  1                                  14    
HELIX   22 AC4 ASN D  402  HIS D  425  1                                  24    
HELIX   23 AC5 GLN D  430  GLU D  460  1                                  31    
HELIX   24 AC6 HIS D  466  LYS D  474  1                                   9    
HELIX   25 AC7 THR E  684  ARG E  686  5                                   3    
HELIX   26 AC8 HIS E  687  GLY E  697  1                                  11    
HELIX   27 AC9 ILE F  689  GLU F  696  1                                   8    
SHEET    1 AA1 2 GLY A 323  LEU A 325  0                                        
SHEET    2 AA1 2 HIS A 331  HIS A 333 -1  O  VAL A 332   N  ILE A 324           
SHEET    1 AA2 4 PHE D 247  ILE D 249  0                                        
SHEET    2 AA2 4 GLY D 346  THR D 349  1  O  PHE D 347   N  ILE D 249           
SHEET    3 AA2 4 GLY D 338  ILE D 341 -1  N  ILE D 341   O  GLY D 346           
SHEET    4 AA2 4 MET D 334  ASN D 335 -1  N  ASN D 335   O  GLY D 338           
LINK         C   GLY D 239                 CD  GLN D 273     1555   4447  1.62  
CISPEP   1 LYS D  358    PRO D  359          0        -5.38                     
SITE     1 AC1  9 ILE A 268  GLN A 275  TRP A 305  PHE A 313                    
SITE     2 AC1  9 ARG A 316  LEU A 326  ALA A 327  CYS A 432                    
SITE     3 AC1  9 LEU A 436                                                     
SITE     1 AC2 12 PHE D 282  CYS D 285  GLN D 286  SER D 289                    
SITE     2 AC2 12 HIS D 323  TYR D 327  ILE D 341  MET D 364                    
SITE     3 AC2 12 HIS D 449  LEU D 453  TYR D 473  HOH D 768                    
CRYST1   53.880   66.527  165.927  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      0.018560  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015031  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006027        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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