HEADER LIGAND BINDING PROTEIN 04-JUN-07 2Q61
TITLE CRYSTAL STRUCTURE OF PPARGAMMA LIGAND BINDING DOMAIN BOUND TO PARTIAL
TITLE 2 AGONIST SR145
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 GENE: PPARG, NR1C3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS PROTEIN-LIGAND COMPLEX, LIGAND BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.BRUNING,K.W.NETTLES
REVDAT 5 30-AUG-23 2Q61 1 REMARK SEQADV
REVDAT 4 18-OCT-17 2Q61 1 REMARK
REVDAT 3 13-JUL-11 2Q61 1 VERSN
REVDAT 2 24-FEB-09 2Q61 1 VERSN
REVDAT 1 23-OCT-07 2Q61 0
JRNL AUTH J.B.BRUNING,M.J.CHALMERS,S.PRASAD,S.A.BUSBY,T.M.KAMENECKA,
JRNL AUTH 2 Y.HE,K.W.NETTLES,P.R.GRIFFIN
JRNL TITL PARTIAL AGONISTS ACTIVATE PPARGAMMA USING A HELIX 12
JRNL TITL 2 INDEPENDENT MECHANISM
JRNL REF STRUCTURE V. 15 1258 2007
JRNL REFN ISSN 0969-2126
JRNL PMID 17937915
JRNL DOI 10.1016/J.STR.2007.07.014
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 32379
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1650
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2067
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4075
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 33.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.243
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.194
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.133
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.152
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4308 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5836 ; 1.329 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 541 ; 5.057 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;37.107 ;24.892
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 815 ;17.104 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;18.870 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 676 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3171 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2034 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3001 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 220 ; 0.160 ; 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): 84 ; 0.181 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.146 ; 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): 2711 ; 0.692 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4235 ; 1.103 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1839 ; 1.917 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1585 ; 2.818 ; 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 : 10
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 209 A 230
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3734 7.6056 17.8312
REMARK 3 T TENSOR
REMARK 3 T11: 0.0306 T22: 0.0701
REMARK 3 T33: 0.1324 T12: -0.0055
REMARK 3 T13: -0.0291 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 3.8432 L22: 3.9225
REMARK 3 L33: 3.2358 L12: 0.5205
REMARK 3 L13: -1.2900 L23: 0.3547
REMARK 3 S TENSOR
REMARK 3 S11: -0.0907 S12: 0.1044 S13: -0.3212
REMARK 3 S21: 0.0455 S22: -0.0720 S23: 0.2010
REMARK 3 S31: -0.1081 S32: -0.3965 S33: 0.1628
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 : A 231 A 299
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2220 20.0405 6.3972
REMARK 3 T TENSOR
REMARK 3 T11: 0.1530 T22: 0.0641
REMARK 3 T33: 0.0775 T12: -0.0915
REMARK 3 T13: -0.0142 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 1.6939 L22: 0.7141
REMARK 3 L33: 3.2415 L12: 0.2985
REMARK 3 L13: -1.0300 L23: 0.0645
REMARK 3 S TENSOR
REMARK 3 S11: 0.0562 S12: 0.1247 S13: 0.1755
REMARK 3 S21: -0.0957 S22: 0.1141 S23: -0.0244
REMARK 3 S31: -0.6783 S32: 0.2416 S33: -0.1703
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 300 A 362
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4775 14.1022 16.6870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0789 T22: 0.0506
REMARK 3 T33: 0.1149 T12: -0.0408
REMARK 3 T13: -0.0383 T23: -0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 2.0866 L22: 0.5865
REMARK 3 L33: 4.2556 L12: 0.4648
REMARK 3 L13: -1.5497 L23: -0.7012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0048 S12: -0.1054 S13: -0.0857
REMARK 3 S21: -0.0161 S22: -0.0355 S23: -0.1253
REMARK 3 S31: -0.3268 S32: 0.3141 S33: 0.0307
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 363 A 461
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0558 3.9081 21.4466
REMARK 3 T TENSOR
REMARK 3 T11: 0.0502 T22: 0.0267
REMARK 3 T33: 0.1476 T12: -0.0010
REMARK 3 T13: -0.0179 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 2.0579 L22: 0.6614
REMARK 3 L33: 1.3007 L12: -0.1135
REMARK 3 L13: 0.0751 L23: -0.2267
REMARK 3 S TENSOR
REMARK 3 S11: -0.0537 S12: -0.1023 S13: -0.2598
REMARK 3 S21: 0.0108 S22: 0.0003 S23: -0.1307
REMARK 3 S31: 0.1161 S32: 0.1905 S33: 0.0534
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 462 A 475
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3917 24.2426 24.9234
REMARK 3 T TENSOR
REMARK 3 T11: 0.2604 T22: 0.0180
REMARK 3 T33: 0.1353 T12: -0.0718
REMARK 3 T13: -0.1311 T23: -0.1845
REMARK 3 L TENSOR
REMARK 3 L11: 12.5123 L22: 19.4895
REMARK 3 L33: 9.5786 L12: -2.2864
REMARK 3 L13: 8.4076 L23: -10.1928
REMARK 3 S TENSOR
REMARK 3 S11: -0.5999 S12: -0.6336 S13: 0.9460
REMARK 3 S21: -0.1044 S22: -0.6100 S23: -0.4765
REMARK 3 S31: -1.6315 S32: 0.1927 S33: 1.2099
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 207 B 241
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4221 -20.9946 36.9870
REMARK 3 T TENSOR
REMARK 3 T11: 0.1561 T22: 0.0149
REMARK 3 T33: 0.0651 T12: -0.0143
REMARK 3 T13: 0.0186 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 4.9944 L22: 4.2881
REMARK 3 L33: 3.8042 L12: 2.0481
REMARK 3 L13: -0.2591 L23: 2.2895
REMARK 3 S TENSOR
REMARK 3 S11: 0.2145 S12: -0.5713 S13: -0.4004
REMARK 3 S21: 0.4389 S22: -0.2729 S23: 0.0240
REMARK 3 S31: 0.7754 S32: 0.0623 S33: 0.0584
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 244 B 267
REMARK 3 ORIGIN FOR THE GROUP (A): 42.1209 -7.3448 52.7307
REMARK 3 T TENSOR
REMARK 3 T11: 0.0766 T22: 0.5501
REMARK 3 T33: 0.2837 T12: -0.3362
REMARK 3 T13: 0.1190 T23: -0.0872
REMARK 3 L TENSOR
REMARK 3 L11: 13.7474 L22: 0.9484
REMARK 3 L33: 16.4703 L12: 2.1908
REMARK 3 L13: -4.2546 L23: -3.6914
REMARK 3 S TENSOR
REMARK 3 S11: -0.0930 S12: -1.3441 S13: -1.3152
REMARK 3 S21: -0.0699 S22: -0.7062 S23: -0.8135
REMARK 3 S31: 0.7409 S32: 0.3958 S33: 0.7992
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 275 B 359
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8417 -8.6629 34.6819
REMARK 3 T TENSOR
REMARK 3 T11: 0.0779 T22: 0.0911
REMARK 3 T33: 0.0720 T12: -0.0179
REMARK 3 T13: 0.0299 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 2.9392 L22: 1.3479
REMARK 3 L33: 4.2257 L12: 0.9329
REMARK 3 L13: 0.0698 L23: 1.6323
REMARK 3 S TENSOR
REMARK 3 S11: 0.2300 S12: -0.3786 S13: 0.2308
REMARK 3 S21: 0.0203 S22: -0.0660 S23: -0.0182
REMARK 3 S31: -0.1106 S32: 0.3947 S33: -0.1640
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 360 B 452
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0199 -7.8003 29.2697
REMARK 3 T TENSOR
REMARK 3 T11: 0.0477 T22: 0.0277
REMARK 3 T33: 0.1168 T12: 0.0017
REMARK 3 T13: 0.0047 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 2.4895 L22: 1.7087
REMARK 3 L33: 1.8571 L12: 0.0413
REMARK 3 L13: -0.5879 L23: -0.1419
REMARK 3 S TENSOR
REMARK 3 S11: 0.0995 S12: -0.0550 S13: 0.3623
REMARK 3 S21: 0.0564 S22: -0.0747 S23: 0.1752
REMARK 3 S31: -0.0635 S32: -0.0056 S33: -0.0249
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 453 B 476
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3778 -1.0556 31.7117
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.2360
REMARK 3 T33: 0.1653 T12: -0.1251
REMARK 3 T13: -0.0320 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 2.6168 L22: 14.0310
REMARK 3 L33: 1.3013 L12: -1.2380
REMARK 3 L13: -1.1890 L23: 3.7614
REMARK 3 S TENSOR
REMARK 3 S11: -0.1874 S12: 0.2622 S13: 0.8922
REMARK 3 S21: -0.5248 S22: 0.0583 S23: -0.4487
REMARK 3 S31: 0.5111 S32: 0.0401 S33: 0.1291
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2Q61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32718
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.197
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : 0.42000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.047
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: PDB ENTRY 1KNU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM CITRATE, 0.125M TRIS 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, PH 8
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 45.06550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.19500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.06550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.19500
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 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 SER A 204
REMARK 465 ASN A 205
REMARK 465 PRO A 206
REMARK 465 GLU A 207
REMARK 465 SER A 208
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 SER 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 SER B 464
REMARK 465 LEU B 465
REMARK 465 TYR B 477
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 260 CG OD1 OD2
REMARK 470 LYS A 261 CG CD CE NZ
REMARK 470 LYS A 275 CD CE NZ
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 LYS A 457 CG CD CE NZ
REMARK 470 ASP A 475 CG OD1 OD2
REMARK 470 LYS B 244 CG CD CE NZ
REMARK 470 LYS B 263 CG CD CE NZ
REMARK 470 LYS B 265 CG CD CE NZ
REMARK 470 GLU B 351 CG CD OE1 OE2
REMARK 470 LYS B 354 CD CE NZ
REMARK 470 LYS B 358 CG CD CE NZ
REMARK 470 GLN B 454 CG CD OE1 NE2
REMARK 470 LYS B 457 CG CD CE NZ
REMARK 470 LYS B 458 CG CD CE NZ
REMARK 470 ASP B 475 CG OD1 OD2
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 O HOH A 7071 O HOH A 7078 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 462 CG ASP A 462 OD1 0.160
REMARK 500 ASP A 462 CG ASP A 462 OD2 0.171
REMARK 500 LYS B 244 N LYS B 244 CA 0.156
REMARK 500 LYS B 244 CA LYS B 244 CB 0.148
REMARK 500 GLU B 460 C THR B 461 N -0.190
REMARK 500 THR B 461 C ASP B 462 N -0.239
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 ASP A 210 69.31 37.24
REMARK 500 ARG A 357 140.04 -34.99
REMARK 500 THR A 461 -90.36 -104.36
REMARK 500 LYS B 240 67.31 -113.95
REMARK 500 PHE B 264 119.84 56.62
REMARK 500 SER B 342 66.98 35.67
REMARK 500 GLN B 454 31.67 -81.34
REMARK 500 VAL B 455 -45.48 -135.43
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 SF1 B 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF1 A 7001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q59 RELATED DB: PDB
REMARK 900 RELATED ID: 2Q5P RELATED DB: PDB
REMARK 900 RELATED ID: 2Q5S RELATED DB: PDB
REMARK 900 RELATED ID: 2Q6R RELATED DB: PDB
REMARK 900 RELATED ID: 2Q6S RELATED DB: PDB
DBREF 2Q61 A 205 477 UNP P37231 PPARG_HUMAN 233 505
DBREF 2Q61 B 205 477 UNP P37231 PPARG_HUMAN 233 505
SEQADV 2Q61 SER A 204 UNP P37231 EXPRESSION TAG
SEQADV 2Q61 SER B 204 UNP P37231 EXPRESSION TAG
SEQRES 1 A 274 SER ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS
SEQRES 2 A 274 HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR
SEQRES 3 A 274 LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR
SEQRES 4 A 274 ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU
SEQRES 5 A 274 MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR
SEQRES 6 A 274 PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE
SEQRES 7 A 274 PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN
SEQRES 8 A 274 GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL
SEQRES 9 A 274 ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR
SEQRES 10 A 274 GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU
SEQRES 11 A 274 MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY
SEQRES 12 A 274 PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO
SEQRES 13 A 274 PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL
SEQRES 14 A 274 LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA
SEQRES 15 A 274 ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO
SEQRES 16 A 274 GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP
SEQRES 17 A 274 ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN
SEQRES 18 A 274 HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN
SEQRES 19 A 274 LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL
SEQRES 20 A 274 GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET
SEQRES 21 A 274 SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU
SEQRES 22 A 274 TYR
SEQRES 1 B 274 SER ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS
SEQRES 2 B 274 HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR
SEQRES 3 B 274 LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR
SEQRES 4 B 274 ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU
SEQRES 5 B 274 MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR
SEQRES 6 B 274 PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE
SEQRES 7 B 274 PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN
SEQRES 8 B 274 GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL
SEQRES 9 B 274 ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR
SEQRES 10 B 274 GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU
SEQRES 11 B 274 MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY
SEQRES 12 B 274 PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO
SEQRES 13 B 274 PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL
SEQRES 14 B 274 LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA
SEQRES 15 B 274 ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO
SEQRES 16 B 274 GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP
SEQRES 17 B 274 ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN
SEQRES 18 B 274 HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN
SEQRES 19 B 274 LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL
SEQRES 20 B 274 GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET
SEQRES 21 B 274 SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU
SEQRES 22 B 274 TYR
HET SF1 A7001 27
HET SF1 B5001 27
HETNAM SF1 1-BENZYL-5-CHLORO-3-(PHENYLTHIO)-1H-INDOLE-2-CARBOXYLIC
HETNAM 2 SF1 ACID
HETSYN SF1 SR145
FORMUL 3 SF1 2(C22 H16 CL N O2 S)
FORMUL 5 HOH *156(H2 O)
HELIX 1 1 ASP A 210 PHE A 226 1 17
HELIX 2 2 THR A 229 THR A 238 1 10
HELIX 3 3 ASP A 251 LYS A 261 1 11
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 SER A 355 1 6
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 HIS A 466 LYS A 474 1 9
HELIX 13 13 GLU B 207 PHE B 226 1 20
HELIX 14 14 THR B 229 THR B 238 1 10
HELIX 15 15 ASP B 251 ILE B 262 1 12
HELIX 16 16 GLU B 276 SER B 302 1 27
HELIX 17 17 GLY B 305 LEU B 309 5 5
HELIX 18 18 ASP B 310 ALA B 331 1 22
HELIX 19 19 ARG B 350 SER B 355 1 6
HELIX 20 20 MET B 364 ALA B 376 1 13
HELIX 21 21 ASP B 380 LEU B 393 1 14
HELIX 22 22 ASN B 402 HIS B 425 1 24
HELIX 23 23 GLN B 430 GLU B 460 1 31
HELIX 24 24 HIS B 466 LYS B 474 1 9
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 VAL A 339 O MET A 348
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 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
CISPEP 1 LYS A 358 PRO A 359 0 8.76
CISPEP 2 LYS A 474 ASP A 475 0 -3.94
CISPEP 3 LYS B 358 PRO B 359 0 3.68
SITE 1 AC1 15 LEU B 255 PHE B 264 HIS B 266 ILE B 281
SITE 2 AC1 15 GLY B 284 CYS B 285 ARG B 288 LEU B 340
SITE 3 AC1 15 ILE B 341 SER B 342 MET B 348 LEU B 353
SITE 4 AC1 15 PHE B 363 HOH B5020 HOH B5056
SITE 1 AC2 14 LEU A 255 ILE A 281 GLY A 284 CYS A 285
SITE 2 AC2 14 ARG A 288 LEU A 330 LEU A 333 LEU A 340
SITE 3 AC2 14 ILE A 341 SER A 342 MET A 348 LEU A 353
SITE 4 AC2 14 PHE A 363 HOH A7026
CRYST1 90.131 62.390 117.930 90.00 100.98 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 0.011095 0.000000 0.002153 0.00000
SCALE2 0.000000 0.016028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008638 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
