GenomeNet

Database: PDB
Entry: 5U3T
LinkDB: 5U3T
Original site: 5U3T 
HEADER    PROTEIN BINDING/ACTIVATOR               03-DEC-16   5U3T              
TITLE     HUMAN PPARDELTA LIGAND-BINDING DOMAIN IN COMPLEXED WITH SPECIFIC      
TITLE    2 AGONIST 4                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR DELTA;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PPAR-DELTA,NUCI,NUCLEAR HORMONE RECEPTOR 1,NUC1,NUCLEAR     
COMPND   5 RECEPTOR SUBFAMILY 1 GROUP C MEMBER 2,PEROXISOME PROLIFERATOR-       
COMPND   6 ACTIVATED RECEPTOR BETA,PPAR-BETA;                                   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: LIGAND-BINDING DOMAIN                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPARD, NR1C2, PPARB;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A(+)                                 
KEYWDS    PPARDELTA, LIGAND-BINDING DOMAIN, AGONIST, PROTEIN BINDING-ACTIVATOR  
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-C.WU,T.J.BAIGA,M.DOWNES,J.J.LA CLAIR,A.R.ATKINS,S.B.RICHARD,       
AUTHOR   2 T.A.STOCKLEY-NOEL,M.E.BOWMAN,R.M.EVANS,J.P.NOEL                      
REVDAT   5   04-OCT-23 5U3T    1       HETSYN                                   
REVDAT   4   29-JUL-20 5U3T    1       COMPND REMARK HETNAM SITE                
REVDAT   4 2                   1       ATOM                                     
REVDAT   3   05-APR-17 5U3T    1       JRNL                                     
REVDAT   2   29-MAR-17 5U3T    1       JRNL                                     
REVDAT   1   22-MAR-17 5U3T    0                                                
JRNL        AUTH   C.C.WU,T.J.BAIGA,M.DOWNES,J.J.LA CLAIR,A.R.ATKINS,           
JRNL        AUTH 2 S.B.RICHARD,W.FAN,T.A.STOCKLEY-NOEL,M.E.BOWMAN,J.P.NOEL,     
JRNL        AUTH 3 R.M.EVANS                                                    
JRNL        TITL   STRUCTURAL BASIS FOR SPECIFIC LIGATION OF THE PEROXISOME     
JRNL        TITL 2 PROLIFERATOR-ACTIVATED RECEPTOR DELTA.                       
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 114 E2563 2017              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   28320959                                                     
JRNL        DOI    10.1073/PNAS.1621513114                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9PRE_1665                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 72343                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.670                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1929                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.7658 -  4.0965    0.98     5409   137  0.1403 0.1596        
REMARK   3     2  4.0965 -  3.2517    1.00     5370   171  0.1471 0.1700        
REMARK   3     3  3.2517 -  2.8407    1.00     5383   122  0.1756 0.2535        
REMARK   3     4  2.8407 -  2.5810    1.00     5385   156  0.1752 0.2055        
REMARK   3     5  2.5810 -  2.3960    1.00     5383   148  0.1681 0.2394        
REMARK   3     6  2.3960 -  2.2548    0.99     5328   144  0.1675 0.2117        
REMARK   3     7  2.2548 -  2.1419    0.99     5341   141  0.1874 0.2388        
REMARK   3     8  2.1419 -  2.0486    0.99     5339   141  0.1942 0.2228        
REMARK   3     9  2.0486 -  1.9698    0.98     5249   157  0.2207 0.2917        
REMARK   3    10  1.9698 -  1.9018    0.97     5169   146  0.2639 0.2954        
REMARK   3    11  1.9018 -  1.8423    0.97     5268   133  0.2947 0.3655        
REMARK   3    12  1.8423 -  1.7896    0.95     5013   151  0.3226 0.3635        
REMARK   3    13  1.7896 -  1.7425    0.77     4163   104  0.3496 0.3902        
REMARK   3    14  1.7425 -  1.7000    0.49     2614    78  0.3616 0.3361        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.530           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           4944                                  
REMARK   3   ANGLE     :  1.448           6669                                  
REMARK   3   CHIRALITY :  0.054            742                                  
REMARK   3   PLANARITY :  0.006            841                                  
REMARK   3   DIHEDRAL  : 14.196           1847                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND ( RESID 170:440 OR RESID 501:508 ) )     
REMARK   3    ORIGIN FOR THE GROUP (A): -15.0022   5.1883 125.5684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0987 T22:   0.1098                                     
REMARK   3      T33:   0.1379 T12:   0.0109                                     
REMARK   3      T13:  -0.0236 T23:   0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2165 L22:   1.2663                                     
REMARK   3      L33:   2.3953 L12:   0.0836                                     
REMARK   3      L13:  -0.4176 L23:  -0.6234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0002 S12:  -0.0670 S13:  -0.0429                       
REMARK   3      S21:  -0.0759 S22:  -0.0400 S23:  -0.0709                       
REMARK   3      S31:   0.0058 S32:   0.1741 S33:   0.0072                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN B AND ( RESID 173:441 OR RESID 501:512 ) )     
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9911  43.2492 113.4946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1934 T22:   0.1673                                     
REMARK   3      T33:   0.1586 T12:  -0.0150                                     
REMARK   3      T13:   0.0049 T23:  -0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9708 L22:   0.8627                                     
REMARK   3      L33:   4.0101 L12:   0.1156                                     
REMARK   3      L13:  -0.2997 L23:  -0.8200                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0579 S12:   0.0280 S13:   0.0829                       
REMARK   3      S21:  -0.0379 S22:   0.0345 S23:  -0.0047                       
REMARK   3      S31:  -0.2044 S32:   0.3069 S33:  -0.0731                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5U3T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000225263.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5 - 8.8                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : 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   : 72951                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 94.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 48.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1GWZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BIS-TRIS PROPANE, POTASSIUM CHLORIDE,    
REMARK 280  PEG 8000, 1,2-PROPANDIOL, EDTA, DTT, PH 7.5, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 277.15K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       47.34500            
REMARK 290   SMTRY3   2  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 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     TYR A   441                                                      
REMARK 465     PRO B   170                                                      
REMARK 465     GLN B   171                                                      
REMARK 465     VAL B   172                                                      
REMARK 465     ALA B   205                                                      
REMARK 465     SER B   206                                                      
REMARK 465     HIS B   207                                                      
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   HE2  HIS A   413     O2   7UY A   501              1.57            
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 424       68.18   -118.28                                   
REMARK 500    ASN B 366       77.83   -101.48                                   
REMARK 500    GLU B 424       63.10   -101.58                                   
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 807        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH B 744        DISTANCE =  5.94 ANGSTROMS                       
DBREF  5U3T A  170   441  UNP    Q03181   PPARD_HUMAN     72    343             
DBREF  5U3T B  170   441  UNP    Q03181   PPARD_HUMAN     72    343             
SEQRES   1 A  272  PRO GLN VAL ALA ASP LEU LYS ALA PHE SER LYS HIS ILE          
SEQRES   2 A  272  TYR ASN ALA TYR LEU LYS ASN PHE ASN MET THR LYS LYS          
SEQRES   3 A  272  LYS ALA ARG SER ILE LEU THR GLY LYS ALA SER HIS THR          
SEQRES   4 A  272  ALA PRO PHE VAL ILE HIS ASP ILE GLU THR LEU TRP GLN          
SEQRES   5 A  272  ALA GLU LYS GLY LEU VAL TRP LYS GLN LEU VAL ASN GLY          
SEQRES   6 A  272  LEU PRO PRO TYR LYS GLU ILE SER VAL HIS VAL PHE TYR          
SEQRES   7 A  272  ARG CYS GLN CME THR THR VAL GLU THR VAL ARG GLU LEU          
SEQRES   8 A  272  THR GLU PHE ALA LYS SER ILE PRO SER PHE SER SER LEU          
SEQRES   9 A  272  PHE LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL          
SEQRES  10 A  272  HIS GLU ALA ILE PHE ALA MET LEU ALA SER ILE VAL ASN          
SEQRES  11 A  272  LYS ASP GLY LEU LEU VAL ALA ASN GLY SER GLY PHE VAL          
SEQRES  12 A  272  THR ARG GLU PHE LEU ARG SER LEU ARG LYS PRO PHE SER          
SEQRES  13 A  272  ASP ILE ILE GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE          
SEQRES  14 A  272  ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA LEU PHE          
SEQRES  15 A  272  ILE ALA ALA ILE ILE LEU CYS GLY ASP ARG PRO GLY LEU          
SEQRES  16 A  272  MET ASN VAL PRO ARG VAL GLU ALA ILE GLN ASP THR ILE          
SEQRES  17 A  272  LEU ARG ALA LEU GLU PHE HIS LEU GLN ALA ASN HIS PRO          
SEQRES  18 A  272  ASP ALA GLN TYR LEU PHE PRO LYS LEU LEU GLN LYS MET          
SEQRES  19 A  272  ALA ASP LEU ARG GLN LEU VAL THR GLU HIS ALA GLN MET          
SEQRES  20 A  272  MET GLN ARG ILE LYS LYS THR GLU THR GLU THR SER LEU          
SEQRES  21 A  272  HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP MET TYR              
SEQRES   1 B  272  PRO GLN VAL ALA ASP LEU LYS ALA PHE SER LYS HIS ILE          
SEQRES   2 B  272  TYR ASN ALA TYR LEU LYS ASN PHE ASN MET THR LYS LYS          
SEQRES   3 B  272  LYS ALA ARG SER ILE LEU THR GLY LYS ALA SER HIS THR          
SEQRES   4 B  272  ALA PRO PHE VAL ILE HIS ASP ILE GLU THR LEU TRP GLN          
SEQRES   5 B  272  ALA GLU LYS GLY LEU VAL TRP LYS GLN LEU VAL ASN GLY          
SEQRES   6 B  272  LEU PRO PRO TYR LYS GLU ILE SER VAL HIS VAL PHE TYR          
SEQRES   7 B  272  ARG CYS GLN CME THR THR VAL GLU THR VAL ARG GLU LEU          
SEQRES   8 B  272  THR GLU PHE ALA LYS SER ILE PRO SER PHE SER SER LEU          
SEQRES   9 B  272  PHE LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL          
SEQRES  10 B  272  HIS GLU ALA ILE PHE ALA MET LEU ALA SER ILE VAL ASN          
SEQRES  11 B  272  LYS ASP GLY LEU LEU VAL ALA ASN GLY SER GLY PHE VAL          
SEQRES  12 B  272  THR ARG GLU PHE LEU ARG SER LEU ARG LYS PRO PHE SER          
SEQRES  13 B  272  ASP ILE ILE GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE          
SEQRES  14 B  272  ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA LEU PHE          
SEQRES  15 B  272  ILE ALA ALA ILE ILE LEU CYS GLY ASP ARG PRO GLY LEU          
SEQRES  16 B  272  MET ASN VAL PRO ARG VAL GLU ALA ILE GLN ASP THR ILE          
SEQRES  17 B  272  LEU ARG ALA LEU GLU PHE HIS LEU GLN ALA ASN HIS PRO          
SEQRES  18 B  272  ASP ALA GLN TYR LEU PHE PRO LYS LEU LEU GLN LYS MET          
SEQRES  19 B  272  ALA ASP LEU ARG GLN LEU VAL THR GLU HIS ALA GLN MET          
SEQRES  20 B  272  MET GLN ARG ILE LYS LYS THR GLU THR GLU THR SER LEU          
SEQRES  21 B  272  HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP MET TYR              
MODRES 5U3T CME A  251  CYS  MODIFIED RESIDUE                                   
MODRES 5U3T CME B  251  CYS  MODIFIED RESIDUE                                   
HET    CME  A 251      18                                                       
HET    CME  B 251      18                                                       
HET    7UY  A 501     126                                                       
HET    B7G  A 502      45                                                       
HET    PGO  A 503      26                                                       
HET    PGO  A 504      26                                                       
HET    PGO  A 505      13                                                       
HET    PEG  A 506      17                                                       
HET    PGO  A 507      13                                                       
HET    PEG  A 508      17                                                       
HET    7UY  B 501     126                                                       
HET    B7G  B 502      45                                                       
HET    PGE  B 503      24                                                       
HET    PGO  B 504      26                                                       
HET    PEG  B 505      17                                                       
HET    PEG  B 506      17                                                       
HET    PEG  B 507      17                                                       
HET    PGO  B 508      13                                                       
HET    PGO  B 509      13                                                       
HET    PEG  B 510      17                                                       
HET    PGO  B 511      13                                                       
HET    PGO  B 512      13                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     7UY 6-[2-({(PROPAN-2-YL)[4-(THIOPHEN-3-YL)BENZENE-1-                 
HETNAM   2 7UY  CARBONYL]AMINO}METHYL)PHENOXY]HEXANOIC ACID                     
HETNAM     B7G HEPTYL BETA-D-GLUCOPYRANOSIDE                                    
HETNAM     PGO S-1,2-PROPANEDIOL                                                
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     B7G HEPTYL-BETA-D-GLUCOPYRANOSIDE; HEPTYL BETA-D-GLUCOSIDE;          
HETSYN   2 B7G  HEPTYL D-GLUCOSIDE; HEPTYL GLUCOSIDE                            
FORMUL   1  CME    2(C5 H11 N O3 S2)                                            
FORMUL   3  7UY    2(C27 H31 N O4 S)                                            
FORMUL   4  B7G    2(C13 H26 O6)                                                
FORMUL   5  PGO    9(C3 H8 O2)                                                  
FORMUL   8  PEG    6(C4 H10 O3)                                                 
FORMUL  13  PGE    C6 H14 O4                                                    
FORMUL  23  HOH   *351(H2 O)                                                    
HELIX    1 AA1 PRO A  170  PHE A  190  1                                  21    
HELIX    2 AA2 THR A  193  THR A  202  1                                  10    
HELIX    3 AA3 ASP A  215  LEU A  226  1                                  12    
HELIX    4 AA4 LEU A  231  LEU A  235  5                                   5    
HELIX    5 AA5 GLU A  240  SER A  266  1                                  27    
HELIX    6 AA6 ILE A  267  SER A  272  1                                   6    
HELIX    7 AA7 PHE A  274  ALA A  295  1                                  22    
HELIX    8 AA8 ARG A  314  SER A  319  1                                   6    
HELIX    9 AA9 PRO A  323  ALA A  340  1                                  18    
HELIX   10 AB1 ASP A  344  LEU A  357  1                                  14    
HELIX   11 AB2 ASN A  366  HIS A  389  1                                  24    
HELIX   12 AB3 TYR A  394  GLU A  424  1                                  31    
HELIX   13 AB4 HIS A  430  LYS A  438  1                                   9    
HELIX   14 AB5 ASP B  174  PHE B  190  1                                  17    
HELIX   15 AB6 THR B  193  THR B  202  1                                  10    
HELIX   16 AB7 ASP B  215  LEU B  226  1                                  12    
HELIX   17 AB8 LEU B  231  LEU B  235  5                                   5    
HELIX   18 AB9 GLU B  240  SER B  266  1                                  27    
HELIX   19 AC1 ILE B  267  SER B  272  1                                   6    
HELIX   20 AC2 PHE B  274  ALA B  295  1                                  22    
HELIX   21 AC3 ARG B  314  SER B  319  1                                   6    
HELIX   22 AC4 PRO B  323  ALA B  340  1                                  18    
HELIX   23 AC5 ASP B  344  LEU B  357  1                                  14    
HELIX   24 AC6 ASN B  366  HIS B  389  1                                  24    
HELIX   25 AC7 TYR B  394  GLU B  424  1                                  31    
HELIX   26 AC8 HIS B  430  LYS B  438  1                                   9    
SHEET    1 AA1 4 PHE A 211  ILE A 213  0                                        
SHEET    2 AA1 4 GLY A 310  THR A 313  1  O  PHE A 311   N  ILE A 213           
SHEET    3 AA1 4 GLY A 302  VAL A 305 -1  N  LEU A 303   O  VAL A 312           
SHEET    4 AA1 4 VAL A 298  ASN A 299 -1  N  ASN A 299   O  GLY A 302           
SHEET    1 AA2 4 PHE B 211  ILE B 213  0                                        
SHEET    2 AA2 4 GLY B 310  THR B 313  1  O  PHE B 311   N  ILE B 213           
SHEET    3 AA2 4 GLY B 302  VAL B 305 -1  N  LEU B 303   O  VAL B 312           
SHEET    4 AA2 4 VAL B 298  ASN B 299 -1  N  ASN B 299   O  GLY B 302           
LINK         C   GLN A 250                 N   CME A 251     1555   1555  1.33  
LINK         C   CME A 251                 N   THR A 252     1555   1555  1.33  
LINK         C   GLN B 250                 N   CME B 251     1555   1555  1.34  
LINK         C   CME B 251                 N   THR B 252     1555   1555  1.32  
CISPEP   1 LYS A  322    PRO A  323          0         5.33                     
CISPEP   2 LYS B  322    PRO B  323          0         4.47                     
CRYST1   39.640   94.690   96.430  90.00  97.99  90.00 P 1 21 1      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      0.025227  0.000000  0.003541        0.00000                         
SCALE2      0.000000  0.010561  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010472        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system