HEADER PROTEIN BINDING/ACTIVATOR 03-DEC-16 5U3Z
TITLE HUMAN PPARDELTA LIGAND-BINDING DOMAIN IN COMPLEXED WITH SPECIFIC
TITLE 2 AGONIST 10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR DELTA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN;
COMPND 5 SYNONYM: PPAR-DELTA,NUCI,NUCLEAR HORMONE RECEPTOR 1,NUC1,NUCLEAR
COMPND 6 RECEPTOR SUBFAMILY 1 GROUP C MEMBER 2,PEROXISOME PROLIFERATOR-
COMPND 7 ACTIVATED RECEPTOR BETA,PPAR-BETA;
COMPND 8 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: PPARD, NR1C2, PPARB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
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 5U3Z 1 HETSYN
REVDAT 4 29-JUL-20 5U3Z 1 COMPND REMARK HETNAM SITE
REVDAT 4 2 1 ATOM
REVDAT 3 05-APR-17 5U3Z 1 JRNL
REVDAT 2 29-MAR-17 5U3Z 1 JRNL
REVDAT 1 22-MAR-17 5U3Z 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. 1.72 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) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 70701
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.730
REMARK 3 FREE R VALUE TEST SET COUNT : 1931
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 42.5431 - 4.1443 0.97 5125 137 0.1387 0.1812
REMARK 3 2 4.1443 - 3.2898 0.99 5077 166 0.1382 0.1851
REMARK 3 3 3.2898 - 2.8741 0.99 5161 122 0.1669 0.2179
REMARK 3 4 2.8741 - 2.6113 0.99 5075 151 0.1667 0.1922
REMARK 3 5 2.6113 - 2.4242 0.99 5103 134 0.1660 0.2228
REMARK 3 6 2.4242 - 2.2813 0.98 5026 144 0.1595 0.2210
REMARK 3 7 2.2813 - 2.1670 0.98 5066 143 0.1713 0.2112
REMARK 3 8 2.1670 - 2.0727 0.98 5017 138 0.1835 0.1791
REMARK 3 9 2.0727 - 1.9929 0.98 5033 137 0.2120 0.2264
REMARK 3 10 1.9929 - 1.9241 0.97 5029 148 0.2404 0.2667
REMARK 3 11 1.9241 - 1.8640 0.88 4527 127 0.2824 0.3266
REMARK 3 12 1.8640 - 1.8107 0.88 4509 128 0.3145 0.3470
REMARK 3 13 1.8107 - 1.7630 0.89 4556 131 0.3459 0.4180
REMARK 3 14 1.7630 - 1.7200 0.87 4466 125 0.3781 0.3916
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.680
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 : 0.011 4671
REMARK 3 ANGLE : 1.397 6309
REMARK 3 CHIRALITY : 0.058 716
REMARK 3 PLANARITY : 0.007 791
REMARK 3 DIHEDRAL : 14.335 1743
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 172:439 OR RESID 501:507 ) )
REMARK 3 OR ( CHAIN B AND RESID 501:501 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7086 0.6456 125.4855
REMARK 3 T TENSOR
REMARK 3 T11: 0.1173 T22: 0.1484
REMARK 3 T33: 0.1705 T12: 0.0196
REMARK 3 T13: -0.0207 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 1.4960 L22: 1.6675
REMARK 3 L33: 2.6705 L12: -0.1585
REMARK 3 L13: -0.4163 L23: -0.6712
REMARK 3 S TENSOR
REMARK 3 S11: 0.0074 S12: -0.0649 S13: -0.0637
REMARK 3 S21: -0.0881 S22: -0.0828 S23: -0.0675
REMARK 3 S31: 0.0449 S32: 0.1936 S33: 0.0330
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 508:509 ) OR ( CHAIN B AND (
REMARK 3 RESID 174:439 OR RESID 502:506 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8304 38.4721 113.3302
REMARK 3 T TENSOR
REMARK 3 T11: 0.2198 T22: 0.2021
REMARK 3 T33: 0.1981 T12: -0.0283
REMARK 3 T13: 0.0187 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.9679 L22: 1.0097
REMARK 3 L33: 4.2595 L12: 0.1793
REMARK 3 L13: -0.2381 L23: -0.3843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0554 S12: 0.0022 S13: 0.0893
REMARK 3 S21: -0.0396 S22: 0.0524 S23: 0.0044
REMARK 3 S31: -0.3799 S32: 0.3230 S33: -0.0796
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 5U3Z 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_1000225269.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-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 : 8.2.1
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 : 70808
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 47.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
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 (%): 56.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
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 47.37500
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 PRO A 170
REMARK 465 GLN A 171
REMARK 465 MET A 440
REMARK 465 TYR A 441
REMARK 465 PRO B 170
REMARK 465 GLN B 171
REMARK 465 VAL B 172
REMARK 465 ALA B 173
REMARK 465 LYS B 204
REMARK 465 ALA B 205
REMARK 465 SER B 206
REMARK 465 HIS B 207
REMARK 465 THR B 208
REMARK 465 MET B 440
REMARK 465 TYR B 441
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 HH22 ARG B 198 O VAL B 298 1.58
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 OE1 GLU A 382 OH TYR B 238 2547 2.13
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 LEU B 303 CA - CB - CG ANGL. DEV. = 17.3 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 LYS A 239 -54.59 -122.59
REMARK 500 GLU A 424 66.90 -109.31
REMARK 500 TYR A 437 30.98 -92.58
REMARK 500 LYS A 438 23.97 -73.80
REMARK 500 LYS B 239 -59.18 -120.76
REMARK 500 ASN B 366 73.38 -102.20
REMARK 500 GLU B 424 72.26 -116.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5U3Q RELATED DB: PDB
REMARK 900 RELATED ID: 5U3R RELATED DB: PDB
REMARK 900 RELATED ID: 5U3S RELATED DB: PDB
REMARK 900 RELATED ID: 5U3T RELATED DB: PDB
REMARK 900 RELATED ID: 5U3U RELATED DB: PDB
REMARK 900 RELATED ID: 5U3V RELATED DB: PDB
REMARK 900 RELATED ID: 5U3W RELATED DB: PDB
REMARK 900 RELATED ID: 5U3X RELATED DB: PDB
REMARK 900 RELATED ID: 5U3Y RELATED DB: PDB
REMARK 900 RELATED ID: 5U40 RELATED DB: PDB
REMARK 900 RELATED ID: 5U41 RELATED DB: PDB
REMARK 900 RELATED ID: 5U42 RELATED DB: PDB
REMARK 900 RELATED ID: 5U44 RELATED DB: PDB
REMARK 900 RELATED ID: 5U45 RELATED DB: PDB
REMARK 900 RELATED ID: 5U46 RELATED DB: PDB
DBREF 5U3Z A 170 441 UNP Q03181 PPARD_HUMAN 131 402
DBREF 5U3Z B 170 441 UNP Q03181 PPARD_HUMAN 131 402
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 CYS 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 CYS 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
HET 7UA A 501 61
HET PGO A 502 13
HET PEG A 503 17
HET PGO A 504 13
HET B7G A 505 45
HET PEG A 506 17
HET PGO A 507 13
HET B7G A 508 45
HET PGO A 509 26
HET B7G B 501 45
HET 7UA B 502 61
HET PEG B 503 17
HET PEG B 504 17
HET PGO B 505 13
HET PEG B 506 17
HETNAM 7UA 6-[2-({CYCLOPROPYL[4-(FURAN-3-YL)BENZENE-1-
HETNAM 2 7UA CARBONYL]AMINO}METHYL)PHENOXY]HEXANOIC ACID
HETNAM PGO S-1,2-PROPANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM B7G HEPTYL BETA-D-GLUCOPYRANOSIDE
HETSYN B7G HEPTYL-BETA-D-GLUCOPYRANOSIDE; HEPTYL BETA-D-GLUCOSIDE;
HETSYN 2 B7G HEPTYL D-GLUCOSIDE; HEPTYL GLUCOSIDE
FORMUL 3 7UA 2(C27 H29 N O5)
FORMUL 4 PGO 5(C3 H8 O2)
FORMUL 5 PEG 5(C4 H10 O3)
FORMUL 7 B7G 3(C13 H26 O6)
FORMUL 18 HOH *219(H2 O)
HELIX 1 AA1 VAL A 172 PHE A 190 1 19
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 ALA A 306 GLY A 308 5 3
HELIX 9 AA9 ARG A 314 SER A 319 1 6
HELIX 10 AB1 PRO A 323 ALA A 340 1 18
HELIX 11 AB2 ASP A 344 LEU A 357 1 14
HELIX 12 AB3 ASN A 366 HIS A 389 1 24
HELIX 13 AB4 TYR A 394 GLU A 424 1 31
HELIX 14 AB5 HIS A 430 TYR A 437 1 8
HELIX 15 AB6 LEU B 175 PHE B 190 1 16
HELIX 16 AB7 THR B 193 GLY B 203 1 11
HELIX 17 AB8 ASP B 215 LEU B 226 1 12
HELIX 18 AB9 LEU B 231 LEU B 235 5 5
HELIX 19 AC1 GLU B 240 SER B 266 1 27
HELIX 20 AC2 ILE B 267 SER B 272 1 6
HELIX 21 AC3 PHE B 274 ALA B 295 1 22
HELIX 22 AC4 ALA B 306 GLY B 308 5 3
HELIX 23 AC5 ARG B 314 SER B 319 1 6
HELIX 24 AC6 PRO B 323 ALA B 340 1 18
HELIX 25 AC7 ASP B 344 LEU B 357 1 14
HELIX 26 AC8 ASN B 366 HIS B 389 1 24
HELIX 27 AC9 TYR B 394 GLU B 424 1 31
HELIX 28 AD1 HIS B 430 TYR B 437 1 8
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
CISPEP 1 LYS A 322 PRO A 323 0 5.55
CISPEP 2 LYS B 322 PRO B 323 0 3.06
CRYST1 39.430 94.750 96.050 90.00 97.68 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 0.025361 0.000000 0.003420 0.00000
SCALE2 0.000000 0.010554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010505 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
