HEADER TRANSCRIPTION/TRANSCRIPTION INHIBITOR 18-JUN-13 4L98
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF F360L PPARGAMMA MUTANT WITH THE
TITLE 2 LIGAND LT175
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN (UNP RESIDUES 235-505);
COMPND 5 SYNONYM: PPAR-GAMMA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PPARG, NR1C3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS TRANSCRIPTION FACTOR, RXRALPHA, TRANSCRIPTION-TRANSCRIPTION INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.POCHETTI,R.MONTANARI,V.CONSALVI,R.CHIARALUCE,A.PASQUO,D.CAPELLI,
AUTHOR 2 F.LOIODICE,A.LAGHEZZA,C.LORI
REVDAT 5 20-SEP-23 4L98 1 REMARK
REVDAT 4 13-SEP-23 4L98 1 AUTHOR REMARK SEQADV
REVDAT 3 17-JUL-19 4L98 1 REMARK
REVDAT 2 23-NOV-16 4L98 1 JRNL
REVDAT 1 25-JUN-14 4L98 0
JRNL AUTH C.LORI,A.PASQUO,R.MONTANARI,D.CAPELLI,V.CONSALVI,
JRNL AUTH 2 R.CHIARALUCE,L.CERVONI,F.LOIODICE,A.LAGHEZZA,M.ASCHI,
JRNL AUTH 3 A.GIORGI,G.POCHETTI
JRNL TITL STRUCTURAL BASIS OF THE TRANSACTIVATION DEFICIENCY OF THE
JRNL TITL 2 HUMAN PPAR GAMMA F360L MUTANT ASSOCIATED WITH FAMILIAL
JRNL TITL 3 PARTIAL LIPODYSTROPHY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 1965 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 25004973
JRNL DOI 10.1107/S1399004714009638
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.MONTANARI,F.SACCOCCIA,E.SCOTTI,M.CRESTANI,C.GODIO,
REMARK 1 AUTH 2 F.GILARDI,F.LOIODICE,G.FRACCHIOLLA,A.LAGHEZZA,P.TORTORELLA,
REMARK 1 AUTH 3 A.LAVECCHIA,E.NOVELLINO,F.MAZZA,M.ASCHI,G.POCHETTI
REMARK 1 TITL CRYSTAL STRUCTURE OF THE PEROXISOME PROLIFERATOR-ACTIVATED
REMARK 1 TITL 2 RECEPTOR GAMMA (PPARGAMMA) LIGAND BINDING DOMAIN COMPLEXED
REMARK 1 TITL 3 WITH A NOVEL PARTIAL AGONIST: A NEW REGION OF THE
REMARK 1 TITL 4 HYDROPHOBIC POCKET COULD BE EXPLOITED FOR DRUG DESIGN.
REMARK 1 REF J.MED.CHEM. V. 51 7768 2008
REMARK 1 REFN ISSN 0022-2623
REMARK 1 PMID 19053776
REMARK 1 DOI 10.1021/JM800733H
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 117.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 37723
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1956
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) : 2.28
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2698
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 173
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4015
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 227
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.54000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : -2.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.242
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.210
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.851
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4467 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4456 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6020 ; 1.506 ; 2.004
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10287 ; 1.096 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 539 ; 6.348 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 193 ;38.558 ;25.440
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 868 ;17.650 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.814 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 695 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4909 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 959 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2162 ;10.933 ; 3.052
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2161 ;10.935 ; 3.052
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2699 ;16.914 ; 4.542
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2305 ;12.487 ; 3.578
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 208 476 B 208 476 16457 0.12 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 208 A 477
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4180 36.7570 44.0750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0513 T22: 0.0900
REMARK 3 T33: 0.0586 T12: 0.0205
REMARK 3 T13: -0.0121 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 2.0916 L22: 1.2455
REMARK 3 L33: 2.3632 L12: 0.3399
REMARK 3 L13: -0.6418 L23: -0.5588
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: -0.1558 S13: -0.3106
REMARK 3 S21: -0.0316 S22: -0.0214 S23: -0.1008
REMARK 3 S31: 0.3264 S32: 0.2203 S33: 0.0366
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 207 B 477
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5770 36.4530 13.8140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0693 T22: 0.1441
REMARK 3 T33: 0.0482 T12: 0.0205
REMARK 3 T13: -0.0298 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 2.1936 L22: 1.2021
REMARK 3 L33: 3.3256 L12: -0.4255
REMARK 3 L13: -0.4945 L23: 1.1690
REMARK 3 S TENSOR
REMARK 3 S11: 0.0382 S12: 0.2864 S13: -0.2810
REMARK 3 S21: -0.0302 S22: 0.0099 S23: 0.0570
REMARK 3 S31: 0.2598 S32: -0.1700 S33: -0.0480
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 : 1.00
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4L98 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080340.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.973
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39713
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 3B3K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.3 M SODIUM FORMATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 32.20500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.23000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.20500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.23000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A 203
REMARK 465 SER A 204
REMARK 465 HIS A 205
REMARK 465 MET A 206
REMARK 465 GLU A 207
REMARK 465 TYR A 250
REMARK 465 ASP A 251
REMARK 465 MET A 252
REMARK 465 ASN A 253
REMARK 465 SER A 254
REMARK 465 LEU A 255
REMARK 465 MET A 256
REMARK 465 MET A 257
REMARK 465 GLY A 258
REMARK 465 GLU A 259
REMARK 465 ASP A 260
REMARK 465 LYS A 261
REMARK 465 ILE A 262
REMARK 465 LYS A 263
REMARK 465 PHE A 264
REMARK 465 LYS A 265
REMARK 465 HIS A 266
REMARK 465 ILE A 267
REMARK 465 THR A 268
REMARK 465 PRO A 269
REMARK 465 LEU A 270
REMARK 465 GLN A 271
REMARK 465 GLU A 272
REMARK 465 GLN A 273
REMARK 465 SER A 274
REMARK 465 LYS A 275
REMARK 465 GLY B 203
REMARK 465 SER B 204
REMARK 465 HIS B 205
REMARK 465 MET B 206
REMARK 465 LYS B 240
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 GLN B 273
REMARK 465 SER B 274
REMARK 465 LYS B 275
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 ALA A 209 -110.71 83.56
REMARK 500 LYS A 244 91.78 96.11
REMARK 500 ARG A 357 162.07 -12.09
REMARK 500 LEU A 393 49.46 -84.05
REMARK 500 SER B 208 -68.32 -136.11
REMARK 500 ALA B 209 -70.19 -33.45
REMARK 500 LYS B 244 101.28 88.79
REMARK 500 ASP B 260 -53.22 -169.55
REMARK 500 LEU B 356 -174.20 -51.13
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 LRG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LRG B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3B3K RELATED DB: PDB
REMARK 900 PPARGAMMA WILD TYPE COMPLEXED WITH THE SAME LIGAND
REMARK 900 RELATED ID: 4L96 RELATED DB: PDB
DBREF 4L98 A 207 477 UNP P37231 PPARG_HUMAN 235 505
DBREF 4L98 B 207 477 UNP P37231 PPARG_HUMAN 235 505
SEQADV 4L98 GLY A 203 UNP P37231 EXPRESSION TAG
SEQADV 4L98 SER A 204 UNP P37231 EXPRESSION TAG
SEQADV 4L98 HIS A 205 UNP P37231 EXPRESSION TAG
SEQADV 4L98 MET A 206 UNP P37231 EXPRESSION TAG
SEQADV 4L98 LEU A 360 UNP P37231 PHE 388 ENGINEERED MUTATION
SEQADV 4L98 GLY B 203 UNP P37231 EXPRESSION TAG
SEQADV 4L98 SER B 204 UNP P37231 EXPRESSION TAG
SEQADV 4L98 HIS B 205 UNP P37231 EXPRESSION TAG
SEQADV 4L98 MET B 206 UNP P37231 EXPRESSION TAG
SEQADV 4L98 LEU B 360 UNP P37231 PHE 388 ENGINEERED MUTATION
SEQRES 1 A 275 GLY SER HIS MET GLU SER ALA ASP LEU ARG ALA LEU ALA
SEQRES 2 A 275 LYS HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU
SEQRES 3 A 275 THR LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR
SEQRES 4 A 275 THR ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER
SEQRES 5 A 275 LEU MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE
SEQRES 6 A 275 THR PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG
SEQRES 7 A 275 ILE PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL
SEQRES 8 A 275 GLN GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE
SEQRES 9 A 275 VAL ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS
SEQRES 10 A 275 TYR GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER
SEQRES 11 A 275 LEU MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN
SEQRES 12 A 275 GLY PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS
SEQRES 13 A 275 PRO LEU GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA
SEQRES 14 A 275 VAL LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU
SEQRES 15 A 275 ALA ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG
SEQRES 16 A 275 PRO GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN
SEQRES 17 A 275 ASP ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU
SEQRES 18 A 275 ASN HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU
SEQRES 19 A 275 GLN LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS
SEQRES 20 A 275 VAL GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP
SEQRES 21 A 275 MET SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP
SEQRES 22 A 275 LEU TYR
SEQRES 1 B 275 GLY SER HIS MET GLU SER ALA ASP LEU ARG ALA LEU ALA
SEQRES 2 B 275 LYS HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU
SEQRES 3 B 275 THR LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR
SEQRES 4 B 275 THR ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER
SEQRES 5 B 275 LEU MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE
SEQRES 6 B 275 THR PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG
SEQRES 7 B 275 ILE PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL
SEQRES 8 B 275 GLN GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE
SEQRES 9 B 275 VAL ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS
SEQRES 10 B 275 TYR GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER
SEQRES 11 B 275 LEU MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN
SEQRES 12 B 275 GLY PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS
SEQRES 13 B 275 PRO LEU GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA
SEQRES 14 B 275 VAL LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU
SEQRES 15 B 275 ALA ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG
SEQRES 16 B 275 PRO GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN
SEQRES 17 B 275 ASP ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU
SEQRES 18 B 275 ASN HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU
SEQRES 19 B 275 GLN LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS
SEQRES 20 B 275 VAL GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP
SEQRES 21 B 275 MET SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP
SEQRES 22 B 275 LEU TYR
HET LRG A 501 24
HET LRG B 501 24
HETNAM LRG (2S)-2-(BIPHENYL-4-YLOXY)-3-PHENYLPROPANOIC ACID
FORMUL 3 LRG 2(C21 H18 O3)
FORMUL 5 HOH *227(H2 O)
HELIX 1 1 ALA A 209 PHE A 226 1 18
HELIX 2 2 THR A 229 LEU A 237 1 9
HELIX 3 3 VAL A 277 ILE A 303 1 27
HELIX 4 4 GLY A 305 LEU A 309 5 5
HELIX 5 5 ASP A 310 SER A 332 1 23
HELIX 6 6 ARG A 350 LEU A 356 1 7
HELIX 7 7 PRO A 359 PHE A 363 5 5
HELIX 8 8 MET A 364 ALA A 376 1 13
HELIX 9 9 ASP A 380 LEU A 393 1 14
HELIX 10 10 ASN A 402 HIS A 425 1 24
HELIX 11 11 GLN A 430 GLU A 460 1 31
HELIX 12 12 ASP A 462 HIS A 466 5 5
HELIX 13 13 PRO A 467 TYR A 477 1 11
HELIX 14 14 SER B 208 PHE B 226 1 19
HELIX 15 15 THR B 229 THR B 238 1 10
HELIX 16 16 ASP B 251 GLY B 258 1 8
HELIX 17 17 VAL B 277 ILE B 303 1 27
HELIX 18 18 GLY B 305 LEU B 309 5 5
HELIX 19 19 ASP B 310 SER B 332 1 23
HELIX 20 20 ARG B 350 LEU B 356 1 7
HELIX 21 21 MET B 364 ALA B 376 1 13
HELIX 22 22 ASP B 380 LEU B 393 1 14
HELIX 23 23 ASN B 402 HIS B 425 1 24
HELIX 24 24 GLN B 430 GLU B 460 1 31
HELIX 25 25 ASP B 462 HIS B 466 5 5
HELIX 26 26 PRO B 467 TYR B 477 1 11
SHEET 1 A 4 PHE A 247 ILE A 249 0
SHEET 2 A 4 GLY A 346 THR A 349 1 O PHE A 347 N ILE A 249
SHEET 3 A 4 GLY A 338 ILE A 341 -1 N ILE A 341 O GLY A 346
SHEET 4 A 4 MET A 334 ASN A 335 -1 N ASN A 335 O GLY A 338
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 ILE B 341 O GLY B 346
SHEET 4 B 4 MET B 334 ASN B 335 -1 N ASN B 335 O GLY B 338
SITE 1 AC1 12 PHE A 282 CYS A 285 GLN A 286 SER A 289
SITE 2 AC1 12 HIS A 323 TYR A 327 HIS A 449 LEU A 465
SITE 3 AC1 12 HIS A 466 GLN A 470 TYR B 473 TYR B 477
SITE 1 AC2 14 TYR A 473 TYR A 477 PHE B 282 GLN B 283
SITE 2 AC2 14 CYS B 285 GLN B 286 SER B 289 HIS B 323
SITE 3 AC2 14 PHE B 363 HIS B 449 LEU B 465 HIS B 466
SITE 4 AC2 14 PRO B 467 GLN B 470
CRYST1 64.410 112.460 117.740 90.00 90.00 90.00 P 21 21 2 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 0.015526 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008493 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
