HEADER TRANSCRIPTION/TRANSFERASE 21-SEP-15 5DVC
TITLE HUMAN PPARGAMMA LIGAND BINDING DMAIN COMPLEXED WITH SB1453 IN A
TITLE 2 COVALENT BONDED FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 223-505;
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 685-700;
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: PPARG, NR1C3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B(+);
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 PPARGAMMA, ANTAGONIST, TRANSCRIPTION-TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.Y.JANG
REVDAT 1 21-SEP-16 5DVC 0
JRNL AUTH J.Y.JANG
JRNL TITL HUMAN PPARGAMMA LIGAND BINDING DMAIN COMPLEXED WITH SB1453
JRNL TITL 2 IN A COVALENT BONDED FORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 16400
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 843
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1193
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2252
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : -4.33000
REMARK 3 B33 (A**2) : 4.49000
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): 0.271
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.215
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.171
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.235
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2340 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2344 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3150 ; 1.498 ; 2.009
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5406 ; 0.967 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 276 ; 5.223 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 101 ;35.126 ;24.950
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 451 ;13.981 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;20.246 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 358 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2536 ; 0.015 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 508 ; 0.024 ; 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): 1113 ; 3.205 ; 5.501
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1112 ; 3.205 ; 5.497
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1386 ; 5.036 ; 8.229
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1387 ; 5.035 ; 8.234
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1226 ; 3.756 ; 6.046
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1227 ; 3.755 ; 6.048
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1765 ; 6.160 ; 8.854
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2751 ; 9.421 ;43.957
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2727 ; 9.410 ;43.900
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5DVC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213864.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97935
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17551
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.9400
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) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 54.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M SODIUM MALONATE PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 297K
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 27.42900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.14050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.42900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.14050
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: 1080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 191
REMARK 465 SER A 192
REMARK 465 HIS A 193
REMARK 465 MET A 194
REMARK 465 ALA A 195
REMARK 465 GLU A 196
REMARK 465 ILE A 197
REMARK 465 SER A 198
REMARK 465 SER A 199
REMARK 465 ASP A 200
REMARK 465 ILE A 201
REMARK 465 ASP A 202
REMARK 465 GLN A 203
REMARK 465 LEU A 204
REMARK 465 ASN A 205
REMARK 465 GLN A 271
REMARK 465 GLU A 272
REMARK 465 GLN A 273
REMARK 465 SER A 274
REMARK 465 GLU B 685
REMARK 465 GLY B 697
REMARK 465 SER B 698
REMARK 465 PRO B 699
REMARK 465 SER B 700
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR A 473 OAE T53 A 501 2.14
REMARK 500 ND1 HIS A 323 O HOH A 601 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 418 OE2 GLU A 418 2655 2.19
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 240 51.44 -91.42
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 T53 A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DV3 RELATED DB: PDB
REMARK 900 RELATED ID: 5DV6 RELATED DB: PDB
REMARK 900 RELATED ID: 5DV8 RELATED DB: PDB
REMARK 900 RELATED ID: 5DWL RELATED DB: PDB
DBREF 5DVC A 195 477 UNP P37231 PPARG_HUMAN 223 505
DBREF 5DVC B 685 700 UNP Q15788 NCOA1_HUMAN 685 700
SEQADV 5DVC GLY A 191 UNP P37231 EXPRESSION TAG
SEQADV 5DVC SER A 192 UNP P37231 EXPRESSION TAG
SEQADV 5DVC HIS A 193 UNP P37231 EXPRESSION TAG
SEQADV 5DVC MET A 194 UNP P37231 EXPRESSION TAG
SEQRES 1 A 287 GLY SER HIS MET ALA GLU ILE SER SER ASP ILE ASP GLN
SEQRES 2 A 287 LEU ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS
SEQRES 3 A 287 HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR
SEQRES 4 A 287 LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR
SEQRES 5 A 287 ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU
SEQRES 6 A 287 MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR
SEQRES 7 A 287 PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE
SEQRES 8 A 287 PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN
SEQRES 9 A 287 GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL
SEQRES 10 A 287 ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR
SEQRES 11 A 287 GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU
SEQRES 12 A 287 MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY
SEQRES 13 A 287 PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO
SEQRES 14 A 287 PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL
SEQRES 15 A 287 LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA
SEQRES 16 A 287 ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO
SEQRES 17 A 287 GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP
SEQRES 18 A 287 ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN
SEQRES 19 A 287 HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN
SEQRES 20 A 287 LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL
SEQRES 21 A 287 GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET
SEQRES 22 A 287 SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU
SEQRES 23 A 287 TYR
SEQRES 1 B 16 GLU ARG HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU GLY
SEQRES 2 B 16 SER PRO SER
HET T53 A 501 44
HETNAM T53 N-[2-({3-[({4-[(4-METHYLPIPERAZIN-1-YL)
HETNAM 2 T53 METHYL]BENZOYL}AMINO)METHYL]BENZYL}OXY)PHENYL]-3-
HETNAM 3 T53 NITROBENZAMIDE
FORMUL 3 T53 C34 H35 N5 O5
FORMUL 4 HOH *87(H2 O)
HELIX 1 AA1 GLU A 207 PHE A 226 1 20
HELIX 2 AA2 THR A 229 GLY A 239 1 11
HELIX 3 AA3 ASP A 251 LYS A 263 1 13
HELIX 4 AA4 PHE A 264 ILE A 267 5 4
HELIX 5 AA5 GLU A 276 ILE A 303 1 28
HELIX 6 AA6 GLY A 305 LEU A 309 5 5
HELIX 7 AA7 ASP A 310 LEU A 333 1 24
HELIX 8 AA8 ARG A 350 SER A 355 1 6
HELIX 9 AA9 PRO A 359 PHE A 363 5 5
HELIX 10 AB1 MET A 364 ALA A 376 1 13
HELIX 11 AB2 ASP A 380 LEU A 393 1 14
HELIX 12 AB3 ASN A 402 HIS A 425 1 24
HELIX 13 AB4 GLN A 430 GLU A 460 1 31
HELIX 14 AB5 HIS A 466 LYS A 474 1 9
HELIX 15 AB6 HIS B 687 GLU B 696 1 10
SHEET 1 AA1 3 PHE A 247 ILE A 249 0
SHEET 2 AA1 3 GLY A 346 THR A 349 1 O PHE A 347 N ILE A 249
SHEET 3 AA1 3 GLY A 338 ILE A 341 -1 N VAL A 339 O MET A 348
LINK SG CYS A 285 CAL T53 A 501 1555 1555 1.67
CISPEP 1 LYS A 358 PRO A 359 0 -1.30
SITE 1 AC1 19 ILE A 262 PHE A 264 ILE A 267 PHE A 282
SITE 2 AC1 19 GLY A 284 CYS A 285 GLN A 286 ARG A 288
SITE 3 AC1 19 SER A 289 ILE A 326 ILE A 341 SER A 342
SITE 4 AC1 19 GLU A 343 PHE A 363 LEU A 453 LEU A 469
SITE 5 AC1 19 TYR A 473 HOH A 607 HOH A 665
CRYST1 54.858 130.281 52.249 90.00 90.00 90.00 P 21 21 2 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 0.018229 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007676 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019139 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
