HEADER COMPLEX (THIAZOLIDINEDIONE/RECEPTOR) 14-AUG-98 2PRG
TITLE LIGAND-BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED
TITLE 2 RECEPTOR GAMMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LBD (LIGAND BINDING DOMAIN), RESIDUES 207-477;
COMPND 5 SYNONYM: E DOMAIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR SRC-1;
COMPND 9 CHAIN: C;
COMPND 10 FRAGMENT: FRAGMENT CONTAINING HD1 & HD2 RESIDUES 628-703;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: COMPLEX WITH ROSIGLITAZONE (BRL-49653) REGISTRY #
COMPND 13 122320-73-4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: NUCLEUS;
SOURCE 6 GENE: HUMAN PPAR GAMMA CDNA;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PRSET A;
SOURCE 13 EXPRESSION_SYSTEM_GENE: HPPARGAMMA;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 CELLULAR_LOCATION: NUCLEUS;
SOURCE 19 GENE: SRC-1 CDNA;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 23 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 25 EXPRESSION_SYSTEM_PLASMID: PRSET A
KEYWDS COMPLEX (THIAZOLIDINEDIONE-RECEPTOR), LIGAND-BINDING DOMAIN, NUCLEAR
KEYWDS 2 RECEPTOR, APO, TRANSCRIPTION FACTOR, ORPHAN RECEPTOR, COMPLEX
KEYWDS 3 (THIAZOLIDINEDIONE-RECEPTOR) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.T.NOLTE,G.B.WISELY,M.V.MILBURN
REVDAT 4 09-AUG-23 2PRG 1 REMARK
REVDAT 3 15-JAN-20 2PRG 1 REMARK
REVDAT 2 24-FEB-09 2PRG 1 VERSN
REVDAT 1 19-JUL-99 2PRG 0
JRNL AUTH R.T.NOLTE,G.B.WISELY,S.WESTIN,J.E.COBB,M.H.LAMBERT,
JRNL AUTH 2 R.KUROKAWA,M.G.ROSENFELD,T.M.WILLSON,C.K.GLASS,M.V.MILBURN
JRNL TITL LIGAND BINDING AND CO-ACTIVATOR ASSEMBLY OF THE PEROXISOME
JRNL TITL 2 PROLIFERATOR-ACTIVATED RECEPTOR-GAMMA.
JRNL REF NATURE V. 395 137 1998
JRNL REFN ISSN 0028-0836
JRNL PMID 9744270
JRNL DOI 10.1038/25931
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.3
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 26436
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT : 653
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2745
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 65
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4413
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 541
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.38000
REMARK 3 B22 (A**2) : -4.56000
REMARK 3 B33 (A**2) : 12.93000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.250 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.480 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.160 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.510 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : SHRINK MASK | SHELL MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 120.0
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : BSXPI_FIXDBLE.XPL
REMARK 3 PARAMETER FILE 4 : LOCALPARM.XPL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2PRG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178497.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-97
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26501
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.7
REMARK 200 DATA REDUNDANCY : 3.420
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.14
REMARK 200 R MERGE FOR SHELL (I) : 0.18500
REMARK 200 R SYM FOR SHELL (I) : 0.18500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS 0.3, X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1PRG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.10500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.98300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.53050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.98300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.10500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.53050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY B 239
REMARK 465 LYS B 240
REMARK 465 THR B 241
REMARK 465 THR B 242
REMARK 465 ASP B 243
REMARK 465 LYS B 244
REMARK 465 SER B 245
REMARK 465 PRO B 246
REMARK 465 PHE B 247
REMARK 465 MET B 257
REMARK 465 GLY B 258
REMARK 465 GLU B 259
REMARK 465 ASP B 260
REMARK 465 LYS B 261
REMARK 465 ILE B 262
REMARK 465 LYS B 263
REMARK 465 PHE B 264
REMARK 465 LYS B 265
REMARK 465 HIS B 266
REMARK 465 ILE B 267
REMARK 465 THR B 268
REMARK 465 PRO B 269
REMARK 465 LEU B 270
REMARK 465 GLN B 271
REMARK 465 GLU B 272
REMARK 465 ASP C 623
REMARK 465 SER C 624
REMARK 465 LYS C 625
REMARK 465 TYR C 626
REMARK 465 SER C 627
REMARK 465 ALA C 641
REMARK 465 GLU C 642
REMARK 465 GLN C 643
REMARK 465 GLN C 644
REMARK 465 LEU C 645
REMARK 465 ARG C 646
REMARK 465 HIS C 647
REMARK 465 ALA C 648
REMARK 465 ASP C 649
REMARK 465 ILE C 650
REMARK 465 ASP C 651
REMARK 465 THR C 652
REMARK 465 SER C 653
REMARK 465 CYS C 654
REMARK 465 LYS C 655
REMARK 465 ASP C 656
REMARK 465 VAL C 657
REMARK 465 LEU C 658
REMARK 465 SER C 659
REMARK 465 CYS C 660
REMARK 465 THR C 661
REMARK 465 GLY C 662
REMARK 465 THR C 663
REMARK 465 SER C 664
REMARK 465 ASN C 665
REMARK 465 SER C 666
REMARK 465 ALA C 667
REMARK 465 SER C 668
REMARK 465 ALA C 669
REMARK 465 ASN C 670
REMARK 465 SER C 671
REMARK 465 SER C 672
REMARK 465 GLY C 673
REMARK 465 GLY C 674
REMARK 465 SER C 675
REMARK 465 CYS C 676
REMARK 465 PRO C 677
REMARK 465 SER C 678
REMARK 465 SER C 679
REMARK 465 HIS C 680
REMARK 465 SER C 681
REMARK 465 SER C 682
REMARK 465 LEU C 683
REMARK 465 THR C 684
REMARK 465 THR C 704
REMARK 465 LEU C 705
REMARK 465 SER C 706
REMARK 465 VAL C 707
REMARK 465 GLU C 708
REMARK 465 PRO C 709
REMARK 465 ASP C 710
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 240 -159.18 -65.26
REMARK 500 THR A 241 100.99 40.72
REMARK 500 ASP A 243 -15.48 -167.55
REMARK 500 LYS A 244 144.60 175.83
REMARK 500 HIS A 266 173.07 -55.86
REMARK 500 PRO A 269 91.28 -55.59
REMARK 500 LEU A 270 -128.15 -139.72
REMARK 500 GLN A 273 171.96 34.51
REMARK 500 SER A 274 -0.91 126.80
REMARK 500 LYS A 358 -57.88 -6.11
REMARK 500 SER A 464 107.35 77.84
REMARK 500 ASP A 475 83.14 54.66
REMARK 500 ASP B 251 -159.57 -139.90
REMARK 500 LYS B 358 -79.30 10.75
REMARK 500 THR C 629 -86.93 49.63
REMARK 500 ARG C 686 14.79 53.98
REMARK 500 GLU C 696 -133.85 -66.83
REMARK 500 PRO C 699 -124.91 -60.75
REMARK 500 SER C 700 125.38 85.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 530 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH A 560 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 686 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A 728 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 733 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 759 DISTANCE = 8.12 ANGSTROMS
REMARK 525 HOH A 767 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B 565 DISTANCE = 7.34 ANGSTROMS
REMARK 525 HOH B 609 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B 643 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH B 649 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 658 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH B 667 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH B 672 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH B 677 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH C 425 DISTANCE = 6.30 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: LB1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES ARE INVOLVED IN LIGAND BINDING.
REMARK 800
REMARK 800 SITE_IDENTIFIER: LB2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES ARE INVOLVED IN LIGAND BINDING.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: RESIDUES INVOLVED IN BINDING THE LXXLL
REMARK 800 COACTIVATOR HELIX.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: RESIDUES INVOLVED IN BINDING THE COACTIVATOR
REMARK 800 LXXLL HELIX.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BRL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BRL B 2
DBREF 2PRG A 207 477 UNP P37231 PPARG_HUMAN 205 475
DBREF 2PRG B 207 477 UNP P37231 PPARG_HUMAN 205 475
DBREF 2PRG C 623 710 UNP O43792 O43792 623 710
SEQRES 1 A 271 GLU SER ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR
SEQRES 2 A 271 ASP SER TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS
SEQRES 3 A 271 ALA ARG ALA ILE LEU THR GLY LYS THR THR ASP LYS SER
SEQRES 4 A 271 PRO PHE VAL ILE TYR ASP MET ASN SER LEU MET MET GLY
SEQRES 5 A 271 GLU ASP LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN
SEQRES 6 A 271 GLU GLN SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY
SEQRES 7 A 271 CYS GLN PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR
SEQRES 8 A 271 GLU TYR ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP
SEQRES 9 A 271 LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS
SEQRES 10 A 271 GLU ILE ILE TYR THR MET LEU ALA SER LEU MET ASN LYS
SEQRES 11 A 271 ASP GLY VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR
SEQRES 12 A 271 ARG GLU PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP
SEQRES 13 A 271 PHE MET GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN
SEQRES 14 A 271 ALA LEU GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE
SEQRES 15 A 271 ALA VAL ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU
SEQRES 16 A 271 ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU
SEQRES 17 A 271 GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU
SEQRES 18 A 271 SER SER GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR
SEQRES 19 A 271 ASP LEU ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU
SEQRES 20 A 271 GLN VAL ILE LYS LYS THR GLU THR ASP MET SER LEU HIS
SEQRES 21 A 271 PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU TYR
SEQRES 1 B 271 GLU SER ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR
SEQRES 2 B 271 ASP SER TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS
SEQRES 3 B 271 ALA ARG ALA ILE LEU THR GLY LYS THR THR ASP LYS SER
SEQRES 4 B 271 PRO PHE VAL ILE TYR ASP MET ASN SER LEU MET MET GLY
SEQRES 5 B 271 GLU ASP LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN
SEQRES 6 B 271 GLU GLN SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY
SEQRES 7 B 271 CYS GLN PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR
SEQRES 8 B 271 GLU TYR ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP
SEQRES 9 B 271 LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS
SEQRES 10 B 271 GLU ILE ILE TYR THR MET LEU ALA SER LEU MET ASN LYS
SEQRES 11 B 271 ASP GLY VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR
SEQRES 12 B 271 ARG GLU PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP
SEQRES 13 B 271 PHE MET GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN
SEQRES 14 B 271 ALA LEU GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE
SEQRES 15 B 271 ALA VAL ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU
SEQRES 16 B 271 ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU
SEQRES 17 B 271 GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU
SEQRES 18 B 271 SER SER GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR
SEQRES 19 B 271 ASP LEU ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU
SEQRES 20 B 271 GLN VAL ILE LYS LYS THR GLU THR ASP MET SER LEU HIS
SEQRES 21 B 271 PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU TYR
SEQRES 1 C 88 ASP SER LYS TYR SER GLN THR SER HIS LYS LEU VAL GLN
SEQRES 2 C 88 LEU LEU THR THR THR ALA GLU GLN GLN LEU ARG HIS ALA
SEQRES 3 C 88 ASP ILE ASP THR SER CYS LYS ASP VAL LEU SER CYS THR
SEQRES 4 C 88 GLY THR SER ASN SER ALA SER ALA ASN SER SER GLY GLY
SEQRES 5 C 88 SER CYS PRO SER SER HIS SER SER LEU THR GLU ARG HIS
SEQRES 6 C 88 LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY SER PRO SER
SEQRES 7 C 88 ASP ILE THR THR LEU SER VAL GLU PRO ASP
HET BRL A 1 25
HET BRL B 2 25
HETNAM BRL 2,4-THIAZOLIDIINEDIONE, 5-[[4-[2-(METHYL-2-
HETNAM 2 BRL PYRIDINYLAMINO)ETHOXY]PHENYL]METHYL]-(9CL)
HETSYN BRL BRL49653; ROSIGLITAZONE
FORMUL 4 BRL 2(C18 H19 N3 O3 S)
FORMUL 6 HOH *541(H2 O)
HELIX 1 1 SER A 208 SER A 225 1 18
HELIX 2 2 LYS A 230 THR A 238 1 9
HELIX 3 3 MET A 252 PHE A 264 1 13
HELIX 4 4 VAL A 277 SER A 302 1 26
HELIX 5 5 PHE A 306 ASN A 308 5 3
HELIX 6 6 LEU A 311 LEU A 333 1 23
HELIX 7 7 ARG A 350 LEU A 353 1 4
HELIX 8 8 LYS A 358 ASP A 362 1 5
HELIX 9 9 GLU A 365 LEU A 377 1 13
HELIX 10 10 ASP A 381 ILE A 392 1 12
HELIX 11 11 VAL A 403 ASN A 424 1 22
HELIX 12 12 LEU A 431 THR A 459 1 29
HELIX 13 13 PRO A 467 TYR A 473 1 7
HELIX 14 14 SER B 208 SER B 225 1 18
HELIX 15 15 LYS B 230 LEU B 237 1 8
HELIX 16 16 MET B 252 LEU B 255 1 4
HELIX 17 17 SER B 274 SER B 302 1 29
HELIX 18 18 PHE B 306 ASN B 308 5 3
HELIX 19 19 LEU B 311 LEU B 333 1 23
HELIX 20 20 SER B 342 GLY B 344 5 3
HELIX 21 21 ARG B 350 SER B 355 1 6
HELIX 22 22 PHE B 360 ASP B 362 5 3
HELIX 23 23 GLU B 365 LEU B 377 1 13
HELIX 24 24 ASP B 381 ILE B 392 1 12
HELIX 25 25 VAL B 403 ASN B 424 1 22
HELIX 26 26 LEU B 431 THR B 459 1 29
HELIX 27 27 PRO B 467 TYR B 473 1 7
HELIX 28 28 HIS C 631 THR C 638 1 8
HELIX 29 29 LYS C 688 GLN C 695 1 8
SHEET 1 A 3 PHE A 247 ILE A 249 0
SHEET 2 A 3 GLY A 346 THR A 349 1 N PHE A 347 O PHE A 247
SHEET 3 A 3 GLY A 338 ILE A 341 -1 N ILE A 341 O GLY A 346
SHEET 1 B 2 GLY B 338 ILE B 341 0
SHEET 2 B 2 GLY B 346 THR B 349 -1 N MET B 348 O VAL B 339
SITE 1 LB1 11 HIS A 323 LEU A 469 HIS A 449 GLN A 286
SITE 2 LB1 11 TYR A 327 LEU A 330 PHE A 282 CYS A 285
SITE 3 LB1 11 ARG A 288 GLY A 338 ILE A 341
SITE 1 LB2 11 HIS B 323 LEU B 469 HIS B 449 GLN B 286
SITE 2 LB2 11 TYR B 327 LEU B 330 PHE B 282 CYS B 285
SITE 3 LB2 11 ARG B 288 GLY B 338 ILE B 341
SITE 1 CA1 8 GLU A 471 LYS A 301 THR A 297 GLN A 314
SITE 2 CA1 8 VAL A 315 LEU A 468 LEU A 318 LEU A 311
SITE 1 CA2 8 GLU B 471 LYS B 301 THR B 297 GLN B 314
SITE 2 CA2 8 VAL B 315 LEU B 468 LEU B 318 LEU B 311
SITE 1 AC1 11 PHE A 282 GLY A 284 CYS A 285 GLN A 286
SITE 2 AC1 11 SER A 289 HIS A 323 TYR A 327 ILE A 341
SITE 3 AC1 11 MET A 364 HIS A 449 TYR A 473
SITE 1 AC2 13 PHE B 282 CYS B 285 GLN B 286 SER B 289
SITE 2 AC2 13 HIS B 323 TYR B 327 LEU B 330 LEU B 340
SITE 3 AC2 13 ILE B 341 MET B 364 HIS B 449 LEU B 453
SITE 4 AC2 13 TYR B 473
CRYST1 52.210 69.061 177.966 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019153 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014480 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005619 0.00000
MTRIX1 1 -0.696300 -0.444100 0.563900 68.34460 1
MTRIX2 1 -0.522900 -0.224400 -0.822300 24.76290 1
MTRIX3 1 0.491700 -0.867400 -0.076000 -15.42090 1
(ATOM LINES ARE NOT SHOWN.)
END