HEADER TRANSCRIPTION/TRANSCRIPTION INHIBITOR 05-MAR-19 6O67
TITLE CRYSTAL STRUCTURE OF HUMAN PPARGAMMA LIGAND BINDING DOMAIN IN COMPLEX
TITLE 2 WITH MITOGLITAZONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PPAR-GAMMA,NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;
COMPND 5 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: PPARG, NR1C3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET46
KEYWDS NUCLEAR RECEPTORS, TZDS, DRUG DESIGN, THERAPEUTIC TARGETS,
KEYWDS 2 TRANSCRIPTION-TRANSCRIPTION INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SHANG,D.J.KOJETIN
REVDAT 3 11-OCT-23 6O67 1 REMARK
REVDAT 2 25-DEC-19 6O67 1 REMARK
REVDAT 1 06-NOV-19 6O67 0
JRNL AUTH J.SHANG,R.BRUST,P.R.GRIFFIN,T.M.KAMENECKA,D.J.KOJETIN
JRNL TITL QUANTITATIVE STRUCTURAL ASSESSMENT OF GRADED RECEPTOR
JRNL TITL 2 AGONISM.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 22179 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31611383
JRNL DOI 10.1073/PNAS.1909016116
REMARK 2
REMARK 2 RESOLUTION. 2.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 21737
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.190
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 50.2194 - 6.0703 1.00 1466 147 0.1771 0.2132
REMARK 3 2 6.0703 - 4.8194 1.00 1450 146 0.1944 0.2417
REMARK 3 3 4.8194 - 4.2106 1.00 1411 143 0.1511 0.1842
REMARK 3 4 4.2106 - 3.8258 1.00 1421 145 0.1546 0.2330
REMARK 3 5 3.8258 - 3.5516 1.00 1392 141 0.1626 0.2247
REMARK 3 6 3.5516 - 3.3423 1.00 1423 144 0.1802 0.2229
REMARK 3 7 3.3423 - 3.1749 1.00 1393 141 0.1905 0.2836
REMARK 3 8 3.1749 - 3.0367 1.00 1402 142 0.2050 0.2653
REMARK 3 9 3.0367 - 2.9198 1.00 1384 140 0.2007 0.2735
REMARK 3 10 2.9198 - 2.8191 1.00 1434 146 0.2048 0.2810
REMARK 3 11 2.8191 - 2.7310 1.00 1387 140 0.2139 0.2787
REMARK 3 12 2.7310 - 2.6529 1.00 1403 143 0.2307 0.2636
REMARK 3 13 2.6529 - 2.5831 1.00 1419 143 0.2330 0.2947
REMARK 3 14 2.5831 - 2.5200 1.00 1354 137 0.2579 0.3402
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.93
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 : 0.008 4202
REMARK 3 ANGLE : 0.994 5648
REMARK 3 CHIRALITY : 0.048 651
REMARK 3 PLANARITY : 0.005 708
REMARK 3 DIHEDRAL : 18.140 2605
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6O67 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240074.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97741
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21743
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 48.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.03612
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.30260
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.540
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: 1PRG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M SODIUM CITRATE, 100MM MOPS, PH
REMARK 280 7.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 46.46500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.17500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.46500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.17500
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 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 GLN A 203
REMARK 465 LEU A 204
REMARK 465 ASN A 205
REMARK 465 PRO A 206
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 ASP A 475
REMARK 465 LEU A 476
REMARK 465 TYR A 477
REMARK 465 GLN B 203
REMARK 465 LEU B 204
REMARK 465 ASN B 205
REMARK 465 PRO B 206
REMARK 465 THR B 242
REMARK 465 ASP B 243
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 THR B 461
REMARK 465 ASP B 462
REMARK 465 MET B 463
REMARK 465 SER B 464
REMARK 465 LEU B 465
REMARK 465 ASP B 475
REMARK 465 LEU B 476
REMARK 465 TYR B 477
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 ASP A 251 -175.09 -171.15
REMARK 500 PRO A 359 36.83 -94.26
REMARK 500 SER A 394 -71.22 -78.13
REMARK 500 LEU B 237 -103.43 -57.57
REMARK 500 LYS B 240 -78.55 -97.37
REMARK 500 LYS B 261 -78.87 -76.14
REMARK 500 GLU B 276 137.06 78.45
REMARK 500 LYS B 358 -65.56 -6.67
REMARK 500 LEU B 393 49.01 -92.45
REMARK 500 LYS B 458 40.66 -98.00
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 LO7 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KNA A 502
DBREF 6O67 A 203 477 UNP P37231 PPARG_HUMAN 231 505
DBREF 6O67 B 203 477 UNP P37231 PPARG_HUMAN 231 505
SEQRES 1 A 275 GLN LEU ASN PRO 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 PHE 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 GLN LEU ASN PRO 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 PHE 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 LO7 A 501 26
HET KNA A 502 11
HETNAM LO7 MITOGLITAZONE
HETNAM KNA NONANOIC ACID
HETSYN LO7 (5S)-5-({4-[2-(5-ETHYLPYRIDIN-2-YL)-2-
HETSYN 2 LO7 OXOETHOXY]PHENYL}METHYL)-1,3-THIAZOLIDINE-2,4-DIONE
FORMUL 3 LO7 C19 H18 N2 O4 S
FORMUL 4 KNA C9 H18 O2
FORMUL 5 HOH *158(H2 O)
HELIX 1 AA1 GLU A 207 PHE A 226 1 20
HELIX 2 AA2 THR A 229 THR A 238 1 10
HELIX 3 AA3 ASP A 251 GLY A 258 1 8
HELIX 4 AA4 GLU A 259 LYS A 261 5 3
HELIX 5 AA5 GLU A 276 SER A 302 1 27
HELIX 6 AA6 ASP A 310 ALA A 331 1 22
HELIX 7 AA7 ARG A 350 SER A 355 1 6
HELIX 8 AA8 MET A 364 ALA A 376 1 13
HELIX 9 AA9 ASP A 380 LEU A 393 1 14
HELIX 10 AB1 ASN A 402 HIS A 425 1 24
HELIX 11 AB2 GLN A 430 GLU A 460 1 31
HELIX 12 AB3 HIS A 466 TYR A 473 1 8
HELIX 13 AB4 SER B 208 PHE B 226 1 19
HELIX 14 AB5 THR B 229 LEU B 237 1 9
HELIX 15 AB6 ASP B 251 ILE B 262 1 12
HELIX 16 AB7 GLU B 276 SER B 302 1 27
HELIX 17 AB8 GLY B 305 LEU B 309 5 5
HELIX 18 AB9 ASP B 310 SER B 332 1 23
HELIX 19 AC1 ARG B 350 SER B 355 1 6
HELIX 20 AC2 PRO B 359 PHE B 363 5 5
HELIX 21 AC3 MET B 364 LEU B 377 1 14
HELIX 22 AC4 ASP B 380 LEU B 393 1 14
HELIX 23 AC5 ASN B 402 HIS B 425 1 24
HELIX 24 AC6 GLN B 430 ILE B 456 1 27
HELIX 25 AC7 PRO B 467 TYR B 473 1 7
SHEET 1 AA1 4 PHE A 247 ILE A 249 0
SHEET 2 AA1 4 GLY A 346 THR A 349 1 O PHE A 347 N ILE A 249
SHEET 3 AA1 4 GLY A 338 ILE A 341 -1 N VAL A 339 O MET A 348
SHEET 4 AA1 4 MET A 334 ASN A 335 -1 N ASN A 335 O GLY A 338
SHEET 1 AA2 4 PHE B 247 ILE B 249 0
SHEET 2 AA2 4 GLY B 346 THR B 349 1 O PHE B 347 N ILE B 249
SHEET 3 AA2 4 GLY B 338 ILE B 341 -1 N ILE B 341 O GLY B 346
SHEET 4 AA2 4 MET B 334 ASN B 335 -1 N ASN B 335 O GLY B 338
CISPEP 1 LYS A 358 PRO A 359 0 2.19
SITE 1 AC1 6 CYS A 285 PHE A 287 ILE A 341 SER A 342
SITE 2 AC1 6 MET A 364 KNA A 502
SITE 1 AC2 5 ILE A 262 LYS A 263 ILE A 341 LO7 A 501
SITE 2 AC2 5 HOH A 609
CRYST1 92.930 60.350 118.110 90.00 103.14 90.00 C 1 2 1 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 0.010761 0.000000 0.002512 0.00000
SCALE2 0.000000 0.016570 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008694 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
