HEADER TRANSCRIPTION ACTIVATOR 23-NOV-05 2F4B
TITLE CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF HUMAN PPAR-GAMMA IN
TITLE 2 COMPLEX WITH AN AGONIST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN;
COMPND 5 SYNONYM: PPAR-GAMMA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1
KEYWDS PPAR, TRANSCRIPTION ACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR I.L.LU,Y.H.PENG,N.MAHINDROO,H.P.HSIEH,S.Y.WU
REVDAT 3 13-MAR-24 2F4B 1 REMARK
REVDAT 2 24-FEB-09 2F4B 1 VERSN
REVDAT 1 14-FEB-06 2F4B 0
JRNL AUTH N.MAHINDROO,C.C.WANG,C.C.LIAO,C.F.HUANG,I.L.LU,T.W.LIEN,
JRNL AUTH 2 Y.H.PENG,W.J.HUANG,Y.T.LIN,M.C.HSU,C.H.LIN,C.H.TSAI,J.T.HSU,
JRNL AUTH 3 X.CHEN,P.C.LYU,Y.S.CHAO,S.Y.WU,H.P.HSIEH
JRNL TITL INDOL-1-YL ACETIC ACIDS AS PEROXISOME PROLIFERATOR-ACTIVATED
JRNL TITL 2 RECEPTOR AGONISTS: DESIGN, SYNTHESIS, STRUCTURAL BIOLOGY,
JRNL TITL 3 AND MOLECULAR DOCKING STUDIES
JRNL REF J.MED.CHEM. V. 49 1212 2006
JRNL REFN ISSN 0022-2623
JRNL PMID 16451087
JRNL DOI 10.1021/JM0510373
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 31791
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1687
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2258
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4356
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.14000
REMARK 3 B22 (A**2) : -0.95000
REMARK 3 B33 (A**2) : -0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.65000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.268
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.232
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.157
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.562
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4475 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6033 ; 1.919 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 540 ; 7.022 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 196 ;39.615 ;25.408
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 868 ;18.428 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;18.918 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 692 ; 0.149 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3265 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2215 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3095 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 208 ; 0.194 ; 0.200
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): 76 ; 0.348 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.194 ; 0.200
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): 2827 ; 1.967 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1893 ; 3.830 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1632 ; 5.096 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F4B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL12B2
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 : MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34426
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
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: MOLECULAR REPLACEMENT
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 (%): 46.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2 SODIUM CITRATE, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 44.32100
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 300 REMARK: THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(A,B)
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 266 CG HIS A 266 CD2 0.058
REMARK 500 THR B 238 C THR B 238 O 0.116
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 HIS A 266 CA - C - O ANGL. DEV. = -13.2 DEGREES
REMARK 500 HIS A 266 O - C - N ANGL. DEV. = -11.9 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 244 96.61 -177.99
REMARK 500 ASP A 260 6.26 -54.08
REMARK 500 LYS A 261 -76.31 -62.13
REMARK 500 ILE A 262 70.74 7.96
REMARK 500 LYS A 263 -34.81 -131.81
REMARK 500 HIS A 266 -152.66 -106.61
REMARK 500 PRO A 269 19.58 -60.80
REMARK 500 GLN A 271 99.07 -48.71
REMARK 500 GLN A 273 127.64 176.74
REMARK 500 SER A 274 30.29 -154.47
REMARK 500 LYS A 358 -76.46 -29.58
REMARK 500 THR A 461 -148.88 -83.75
REMARK 500 SER A 464 94.10 64.89
REMARK 500 ASP A 475 50.73 37.01
REMARK 500 THR B 238 -100.05 -92.66
REMARK 500 THR B 241 54.48 33.37
REMARK 500 ASP B 243 -49.19 -164.18
REMARK 500 SER B 245 145.39 -39.46
REMARK 500 LYS B 263 16.72 -140.63
REMARK 500 HIS B 266 -144.09 155.42
REMARK 500 SER B 274 0.32 -152.07
REMARK 500 SER B 342 71.46 44.00
REMARK 500 LEU B 393 54.34 -91.72
REMARK 500 LEU B 468 -37.29 -146.42
REMARK 500 TYR B 473 92.74 -53.79
REMARK 500 ASP B 475 13.14 55.04
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 ARG A 357 LYS A 358 -146.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 HIS A 266 -28.78
REMARK 500 SER B 245 -17.27
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 EHA A 201
DBREF 2F4B A 207 477 UNP P37231 PPARG_HUMAN 235 505
DBREF 2F4B B 207 477 UNP P37231 PPARG_HUMAN 235 505
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
HET EHA A 201 39
HETNAM EHA (5-{3-[(6-BENZOYL-1-PROPYL-2-NAPHTHYL)OXY]PROPOXY}-1H-
HETNAM 2 EHA INDOL-1-YL)ACETIC ACID
HETSYN EHA 2-{5-[3-(6-BENZOYL-1-PROPYLNAPHTHALEN-2-YLOXY)
HETSYN 2 EHA PROPOXY]INDOL-1-YL}ETHANOIC ACID
FORMUL 3 EHA C33 H31 N O5
FORMUL 4 HOH *140(H2 O)
HELIX 1 1 GLU A 207 PHE A 226 1 20
HELIX 2 2 THR A 229 GLY A 239 1 11
HELIX 3 3 ASP A 251 ASP A 260 1 10
HELIX 4 4 GLU A 276 SER A 302 1 27
HELIX 5 5 GLY A 305 LEU A 309 5 5
HELIX 6 6 ASP A 310 SER A 332 1 23
HELIX 7 7 ARG A 350 LEU A 356 1 7
HELIX 8 8 ARG A 357 ASP A 362 1 6
HELIX 9 9 MET A 364 ALA A 376 1 13
HELIX 10 10 ASP A 380 LEU A 393 1 14
HELIX 11 11 ASN A 402 HIS A 425 1 24
HELIX 12 12 GLN A 430 GLU A 460 1 31
HELIX 13 13 HIS A 466 LYS A 474 1 9
HELIX 14 14 GLU B 207 PHE B 226 1 20
HELIX 15 15 THR B 229 THR B 238 1 10
HELIX 16 16 ASP B 251 ASP B 260 1 10
HELIX 17 17 GLU B 276 SER B 302 1 27
HELIX 18 18 GLY B 305 LEU B 309 5 5
HELIX 19 19 ASP B 310 ALA B 331 1 22
HELIX 20 20 ARG B 350 SER B 355 1 6
HELIX 21 21 ARG B 357 ASP B 362 1 6
HELIX 22 22 MET B 364 ALA B 376 1 13
HELIX 23 23 ASP B 380 LEU B 393 1 14
HELIX 24 24 ASN B 402 HIS B 425 1 24
HELIX 25 25 GLN B 430 GLU B 460 1 31
SHEET 1 A 3 PHE A 247 ILE A 249 0
SHEET 2 A 3 GLY A 346 THR A 349 1 O PHE A 347 N ILE A 249
SHEET 3 A 3 GLY A 338 ILE A 341 -1 N VAL A 339 O MET A 348
SHEET 1 B 4 PHE B 247 ILE B 249 0
SHEET 2 B 4 GLY B 346 THR B 349 1 O PHE B 347 N ILE B 249
SHEET 3 B 4 GLY B 338 ILE B 341 -1 N VAL B 339 O MET B 348
SHEET 4 B 4 MET B 334 ASN B 335 -1 N ASN B 335 O GLY B 338
SITE 1 AC1 17 LEU A 255 GLU A 259 ARG A 280 PHE A 282
SITE 2 AC1 17 GLY A 284 CYS A 285 GLN A 286 SER A 289
SITE 3 AC1 17 TYR A 327 LEU A 330 ILE A 341 MET A 348
SITE 4 AC1 17 PHE A 363 MET A 364 LYS A 367 HIS A 449
SITE 5 AC1 17 TYR A 473
CRYST1 55.967 88.642 57.878 90.00 90.01 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 0.017868 0.000000 0.000003 0.00000
SCALE2 0.000000 0.011281 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017278 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
