HEADER TRANSCRIPTION/TRANSFERASE/ANTIBIOTIC 05-JUN-12 4FGY
TITLE IDENTIFICATION OF A UNIQUE PPAR LIGAND WITH AN UNEXPECTED BINDING MODE
TITLE 2 AND ANTIBETIC ACTIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN, UNP RESIDUES 235-504;
COMPND 5 SYNONYM: PPAR-GAMMA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 686-696;
COMPND 11 SYNONYM: NCOA-1, CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 74, BHLHE74,
COMPND 12 PROTEIN HIN-2, RIP160, RENAL CARCINOMA ANTIGEN NY-REN-52, STEROID
COMPND 13 RECEPTOR COACTIVATOR 1, SRC-1;
COMPND 14 EC: 2.3.1.48;
COMPND 15 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: NR1C3, PPARG;
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: PET24A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS PPAR LBD, NUCLEAR RECEPTOR FOLD, LIGAND BINDING, GENE TRANSCRIPTION,
KEYWDS 2 TRANSCRIPTION-TRANSFERASE-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.WANG,Y.LI
REVDAT 3 28-FEB-24 4FGY 1 REMARK
REVDAT 2 02-MAY-18 4FGY 1 REMARK
REVDAT 1 20-MAR-13 4FGY 0
JRNL AUTH W.ZHENG,X.FENG,L.QIU,Z.PAN,R.WANG,S.LIN,D.HOU,L.JIN,Y.LI
JRNL TITL IDENTIFICATION OF THE ANTIBIOTIC IONOMYCIN AS AN UNEXPECTED
JRNL TITL 2 PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA
JRNL TITL 3 (PPAR-GAMMA) LIGAND WITH A UNIQUE BINDING MODE AND EFFECTIVE
JRNL TITL 4 GLUCOSE-LOWERING ACTIVITY IN A MOUSE MODEL OF DIABETES.
JRNL REF DIABETOLOGIA V. 56 401 2013
JRNL REFN
JRNL PMID 23178929
JRNL DOI 10.1007/S00125-012-2777-9
REMARK 2
REMARK 2 RESOLUTION. 2.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 6706
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 : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 344
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) : 2.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 449
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 27
REMARK 3 BIN FREE R VALUE : 0.4770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2219
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 18
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.23000
REMARK 3 B22 (A**2) : 0.07000
REMARK 3 B33 (A**2) : 0.16000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.493
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.396
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.407
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2315 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3122 ; 1.697 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 275 ; 6.928 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 102 ;39.777 ;25.196
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 446 ;22.049 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;20.932 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 369 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1658 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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 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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4FGY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000072887.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-11
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5862
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9605
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 61.345
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 5% ETHYLENE
REMARK 280 GLYCOL, 20% PEG 3350, PH 7.0, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 61.34550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.34550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 28.68000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.26350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 28.68000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.26350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.34550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 28.68000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.26350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.34550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 28.68000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.26350
REMARK 290 SMTRY3 8 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: 1190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 ILE A 290
REMARK 465 LYS A 291
REMARK 465 PHE A 292
REMARK 465 LYS A 293
REMARK 465 HIS A 294
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 SER A 236 26.21 -73.41
REMARK 500 LYS A 272 46.93 -142.05
REMARK 500 ASP A 288 94.96 -62.10
REMARK 500 THR A 296 70.52 46.84
REMARK 500 PRO A 297 -150.34 -65.83
REMARK 500 GLN A 299 -2.99 -39.13
REMARK 500 GLU A 300 -86.46 -60.57
REMARK 500 GLN A 301 108.93 48.60
REMARK 500 LYS A 303 -155.01 -107.29
REMARK 500 LYS A 386 -133.22 52.33
REMARK 500 PHE A 398 -30.47 98.54
REMARK 500 GLU A 406 46.93 35.12
REMARK 500 SER A 457 -75.50 47.14
REMARK 500 LYS A 486 -72.78 -77.23
REMARK 500 GLU A 488 61.64 64.96
REMARK 500 THR A 489 162.28 -47.12
REMARK 500 ASP A 490 -14.13 83.26
REMARK 500 LYS A 502 117.17 -174.49
REMARK 500 HIS B 691 -65.52 122.57
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 LEU A 298 GLN A 299 149.27
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 0W3 A 601
DBREF 4FGY A 235 504 UNP P37231 PPARG_HUMAN 235 504
DBREF 4FGY B 686 696 UNP Q15788 NCOA1_HUMAN 686 696
SEQRES 1 A 270 GLU SER ALA ASP LEU ARG ALA LEU ALA LYS HIS LEU TYR
SEQRES 2 A 270 ASP SER TYR ILE LYS SER PHE PRO LEU THR LYS ALA LYS
SEQRES 3 A 270 ALA ARG ALA ILE LEU THR GLY LYS THR THR ASP LYS SER
SEQRES 4 A 270 PRO PHE VAL ILE TYR ASP MET ASN SER LEU MET MET GLY
SEQRES 5 A 270 GLU ASP LYS ILE LYS PHE LYS HIS ILE THR PRO LEU GLN
SEQRES 6 A 270 GLU GLN SER LYS GLU VAL ALA ILE ARG ILE PHE GLN GLY
SEQRES 7 A 270 CYS GLN PHE ARG SER VAL GLU ALA VAL GLN GLU ILE THR
SEQRES 8 A 270 GLU TYR ALA LYS SER ILE PRO GLY PHE VAL ASN LEU ASP
SEQRES 9 A 270 LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY VAL HIS
SEQRES 10 A 270 GLU ILE ILE TYR THR MET LEU ALA SER LEU MET ASN LYS
SEQRES 11 A 270 ASP GLY VAL LEU ILE SER GLU GLY GLN GLY PHE MET THR
SEQRES 12 A 270 ARG GLU PHE LEU LYS SER LEU ARG LYS PRO PHE GLY ASP
SEQRES 13 A 270 PHE MET GLU PRO LYS PHE GLU PHE ALA VAL LYS PHE ASN
SEQRES 14 A 270 ALA LEU GLU LEU ASP ASP SER ASP LEU ALA ILE PHE ILE
SEQRES 15 A 270 ALA VAL ILE ILE LEU SER GLY ASP ARG PRO GLY LEU LEU
SEQRES 16 A 270 ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN LEU LEU
SEQRES 17 A 270 GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS PRO GLU
SEQRES 18 A 270 SER SER GLN LEU PHE ALA LYS LEU LEU GLN LYS MET THR
SEQRES 19 A 270 ASP LEU ARG GLN ILE VAL THR GLU HIS VAL GLN LEU LEU
SEQRES 20 A 270 GLN VAL ILE LYS LYS THR GLU THR ASP MET SER LEU HIS
SEQRES 21 A 270 PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU
SEQRES 1 B 11 ARG HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU
HET 0W3 A 601 50
HETNAM 0W3 (4R,6S,8S,12R,14R,16Z,18R,19R,20S,21S)-19,21-DIHYDROXY-
HETNAM 2 0W3 22-{(2S,2'R,5S,5'S)-5'-[(1R)-1-HYDROXYETHYL]-2,5'-
HETNAM 3 0W3 DIMETHYLOCTAHYDRO-2,2'-BIFURAN-5-YL}-4,6,8,12,14,18,
HETNAM 4 0W3 20-HEPTAMETHYL-9,11-DIOXODOCOS-16-ENOIC ACID
HETSYN 0W3 IONOMYCIN
FORMUL 3 0W3 C41 H72 O9
FORMUL 4 HOH *18(H2 O)
HELIX 1 1 ALA A 237 PHE A 254 1 18
HELIX 2 2 THR A 257 THR A 266 1 10
HELIX 3 3 THR A 269 SER A 273 5 5
HELIX 4 4 ASP A 279 ASP A 288 1 10
HELIX 5 5 GLU A 304 LYS A 329 1 26
HELIX 6 6 GLY A 333 LEU A 337 5 5
HELIX 7 7 ASP A 338 SER A 360 1 23
HELIX 8 8 SER A 370 GLY A 372 5 3
HELIX 9 9 ARG A 378 SER A 383 1 6
HELIX 10 10 MET A 392 GLU A 397 1 6
HELIX 11 11 PHE A 398 ALA A 404 1 7
HELIX 12 12 ASP A 408 LEU A 421 1 14
HELIX 13 13 ASN A 430 HIS A 453 1 24
HELIX 14 14 GLN A 458 THR A 487 1 30
HELIX 15 15 HIS A 494 TYR A 501 1 8
HELIX 16 16 LYS B 688 GLU B 696 1 9
SHEET 1 A 4 PHE A 275 ILE A 277 0
SHEET 2 A 4 GLY A 374 THR A 377 1 O THR A 377 N ILE A 277
SHEET 3 A 4 GLY A 366 ILE A 369 -1 N VAL A 367 O MET A 376
SHEET 4 A 4 MET A 362 ASN A 363 -1 N ASN A 363 O GLY A 366
CISPEP 1 ARG B 686 HIS B 687 0 -3.44
SITE 1 AC1 18 ALA A 306 ILE A 309 PHE A 310 CYS A 313
SITE 2 AC1 18 GLN A 314 ARG A 316 SER A 317 ILE A 354
SITE 3 AC1 18 TYR A 355 MET A 357 LEU A 358 LEU A 361
SITE 4 AC1 18 ILE A 369 LEU A 381 PHE A 391 MET A 392
SITE 5 AC1 18 HIS A 477 HOH A 710
CRYST1 57.360 86.527 122.691 90.00 90.00 90.00 C 2 2 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 0.017434 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011557 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
