HEADER TRANSCRIPTION 26-AUG-14 4R6S
TITLE CRYSTAL STRUCTURE OF PPARGAMMMA IN COMPLEX WITH SR1663
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 231-505;
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: 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: PMCSG19
KEYWDS NUCLEAR RECEPTOR LIGAND BINDING DOMAIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.P.MARCIANO,P.R.GRIFFIN,J.B.BRUNING
REVDAT 3 20-SEP-23 4R6S 1 REMARK SEQADV
REVDAT 2 22-NOV-17 4R6S 1 REMARK
REVDAT 1 01-JUL-15 4R6S 0
JRNL AUTH D.P.MARCIANO,D.S.KURUVILLA,S.V.BOREGOWDA,A.ASTEIAN,
JRNL AUTH 2 T.S.HUGHES,R.GARCIA-ORDONEZ,C.A.CORZO,T.M.KHAN,S.J.NOVICK,
JRNL AUTH 3 H.PARK,D.J.KOJETIN,D.G.PHINNEY,J.B.BRUNING,T.M.KAMENECKA,
JRNL AUTH 4 P.R.GRIFFIN
JRNL TITL PHARMACOLOGICAL REPRESSION OF PPAR GAMMA PROMOTES
JRNL TITL 2 OSTEOGENESIS.
JRNL REF NAT COMMUN V. 6 7443 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26068133
JRNL DOI 10.1038/NCOMMS8443
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 28889
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1452
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 41.1309 - 4.9548 0.97 2838 137 0.1746 0.2285
REMARK 3 2 4.9548 - 3.9337 1.00 2811 159 0.1515 0.2142
REMARK 3 3 3.9337 - 3.4368 0.96 2689 133 0.1612 0.2147
REMARK 3 4 3.4368 - 3.1227 0.97 2706 157 0.1816 0.2505
REMARK 3 5 3.1227 - 2.8989 0.99 2788 153 0.1957 0.2845
REMARK 3 6 2.8989 - 2.7280 0.99 2770 160 0.1765 0.2459
REMARK 3 7 2.7280 - 2.5914 0.99 2772 144 0.1766 0.2290
REMARK 3 8 2.5914 - 2.4786 0.96 2686 139 0.1891 0.2477
REMARK 3 9 2.4786 - 2.3832 0.96 2674 141 0.1885 0.2603
REMARK 3 10 2.3832 - 2.3010 0.97 2703 129 0.2022 0.2792
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.57
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 : 0.009 4229
REMARK 3 ANGLE : 1.116 5741
REMARK 3 CHIRALITY : 0.069 663
REMARK 3 PLANARITY : 0.004 734
REMARK 3 DIHEDRAL : 14.659 1570
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 225 )
REMARK 3 ORIGIN FOR THE GROUP (A): 88.5733 46.0243 20.3033
REMARK 3 T TENSOR
REMARK 3 T11: 0.5772 T22: 0.7843
REMARK 3 T33: 0.6940 T12: 0.0687
REMARK 3 T13: 0.0812 T23: 0.0859
REMARK 3 L TENSOR
REMARK 3 L11: 0.4616 L22: 0.0593
REMARK 3 L33: 0.5961 L12: -0.1600
REMARK 3 L13: 0.2145 L23: 0.1030
REMARK 3 S TENSOR
REMARK 3 S11: -0.3421 S12: 0.0607 S13: -0.1258
REMARK 3 S21: 0.2307 S22: 0.3240 S23: 0.1440
REMARK 3 S31: 0.0087 S32: -0.8833 S33: 0.0003
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.0012 59.2531 1.2730
REMARK 3 T TENSOR
REMARK 3 T11: 0.5946 T22: 0.7420
REMARK 3 T33: 0.5594 T12: -0.0126
REMARK 3 T13: 0.0261 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 0.4095 L22: 0.1953
REMARK 3 L33: 0.3972 L12: -0.3494
REMARK 3 L13: 0.5202 L23: -0.2621
REMARK 3 S TENSOR
REMARK 3 S11: -0.3119 S12: 1.1234 S13: -0.5376
REMARK 3 S21: -0.0499 S22: 0.2388 S23: 0.1577
REMARK 3 S31: -0.2385 S32: -0.3048 S33: -0.0008
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 252 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 104.9761 64.1667 19.1130
REMARK 3 T TENSOR
REMARK 3 T11: 0.6609 T22: 0.6153
REMARK 3 T33: 0.6285 T12: 0.1060
REMARK 3 T13: -0.0847 T23: 0.0474
REMARK 3 L TENSOR
REMARK 3 L11: 0.3393 L22: 1.0897
REMARK 3 L33: 0.6359 L12: 1.3689
REMARK 3 L13: 0.1028 L23: 0.3039
REMARK 3 S TENSOR
REMARK 3 S11: -0.2673 S12: -0.1819 S13: 0.2241
REMARK 3 S21: -0.0187 S22: 0.2357 S23: 0.0338
REMARK 3 S31: -0.1655 S32: 0.2710 S33: 0.0004
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 334 THROUGH 377 )
REMARK 3 ORIGIN FOR THE GROUP (A): 115.0225 59.8172 7.6371
REMARK 3 T TENSOR
REMARK 3 T11: 0.6522 T22: 0.9478
REMARK 3 T33: 0.6151 T12: 0.0113
REMARK 3 T13: 0.0278 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.4108 L22: 0.8153
REMARK 3 L33: 0.9376 L12: 0.8013
REMARK 3 L13: -0.3622 L23: -0.4340
REMARK 3 S TENSOR
REMARK 3 S11: -0.0965 S12: 0.0071 S13: -0.1497
REMARK 3 S21: 0.0537 S22: 0.0046 S23: -0.1293
REMARK 3 S31: -0.3050 S32: 0.7373 S33: -0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 378 THROUGH 430 )
REMARK 3 ORIGIN FOR THE GROUP (A): 99.7649 45.5368 24.3184
REMARK 3 T TENSOR
REMARK 3 T11: 0.5628 T22: 0.6071
REMARK 3 T33: 0.6087 T12: 0.1945
REMARK 3 T13: -0.0224 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 0.7979 L22: 1.7356
REMARK 3 L33: 0.4785 L12: 0.7098
REMARK 3 L13: 0.4308 L23: -0.0920
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: -0.1649 S13: -0.3882
REMARK 3 S21: 0.0651 S22: 0.1488 S23: -0.0536
REMARK 3 S31: 0.4776 S32: 0.2329 S33: -0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 431 THROUGH 459 )
REMARK 3 ORIGIN FOR THE GROUP (A): 115.7560 53.8567 21.5969
REMARK 3 T TENSOR
REMARK 3 T11: 0.6910 T22: 0.7749
REMARK 3 T33: 0.8745 T12: 0.1789
REMARK 3 T13: -0.1011 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.5818 L22: -0.0237
REMARK 3 L33: -0.0686 L12: 0.4365
REMARK 3 L13: -0.3940 L23: -0.0895
REMARK 3 S TENSOR
REMARK 3 S11: 0.0480 S12: -0.5916 S13: -0.2604
REMARK 3 S21: 0.4610 S22: 0.0827 S23: -0.7016
REMARK 3 S31: 0.1971 S32: 0.4521 S33: 0.0007
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 460 THROUGH 476 )
REMARK 3 ORIGIN FOR THE GROUP (A): 114.1763 71.3358 25.6304
REMARK 3 T TENSOR
REMARK 3 T11: 1.0728 T22: 1.0421
REMARK 3 T33: 0.8078 T12: -0.0165
REMARK 3 T13: 0.0027 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 0.2452 L22: 0.0909
REMARK 3 L33: 0.0861 L12: 0.1707
REMARK 3 L13: 0.2096 L23: 0.0999
REMARK 3 S TENSOR
REMARK 3 S11: 0.8708 S12: -0.7853 S13: 1.3674
REMARK 3 S21: 1.0869 S22: -0.6327 S23: -0.3868
REMARK 3 S31: -1.2061 S32: 0.3957 S33: 0.0007
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 207 THROUGH 225 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.2504 19.8333 27.2607
REMARK 3 T TENSOR
REMARK 3 T11: 0.8142 T22: 0.4482
REMARK 3 T33: 0.8694 T12: 0.0984
REMARK 3 T13: -0.0082 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 0.0788 L22: 0.0048
REMARK 3 L33: 0.0635 L12: -0.0854
REMARK 3 L13: 0.0262 L23: -0.0242
REMARK 3 S TENSOR
REMARK 3 S11: 0.1474 S12: 0.6110 S13: -0.8639
REMARK 3 S21: -0.0834 S22: -0.2016 S23: 0.0525
REMARK 3 S31: 0.5385 S32: 0.3793 S33: -0.0010
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 226 THROUGH 251 )
REMARK 3 ORIGIN FOR THE GROUP (A): 122.2984 29.4012 48.5130
REMARK 3 T TENSOR
REMARK 3 T11: 0.9814 T22: 0.9572
REMARK 3 T33: 0.6433 T12: 0.1910
REMARK 3 T13: 0.0014 T23: 0.1381
REMARK 3 L TENSOR
REMARK 3 L11: 0.0408 L22: 0.0495
REMARK 3 L33: 0.1557 L12: -0.0185
REMARK 3 L13: 0.0271 L23: -0.1469
REMARK 3 S TENSOR
REMARK 3 S11: 0.4271 S12: -0.6884 S13: -0.7552
REMARK 3 S21: 0.0555 S22: -0.1112 S23: 0.0922
REMARK 3 S31: 0.6110 S32: 0.8354 S33: 0.0014
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 252 THROUGH 276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 139.0874 36.4255 52.1375
REMARK 3 T TENSOR
REMARK 3 T11: 0.9368 T22: 1.2794
REMARK 3 T33: 0.9110 T12: 0.0665
REMARK 3 T13: -0.0708 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: -0.0157 L22: 0.0011
REMARK 3 L33: 0.0201 L12: 0.0175
REMARK 3 L13: -0.0142 L23: 0.0245
REMARK 3 S TENSOR
REMARK 3 S11: 0.5296 S12: -1.9192 S13: 0.2930
REMARK 3 S21: 0.4577 S22: -0.1855 S23: 0.7836
REMARK 3 S31: 0.4047 S32: 0.4875 S33: -0.0023
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 277 THROUGH 302 )
REMARK 3 ORIGIN FOR THE GROUP (A): 133.1866 33.5528 35.3465
REMARK 3 T TENSOR
REMARK 3 T11: 0.6083 T22: 0.6479
REMARK 3 T33: 0.5331 T12: 0.1561
REMARK 3 T13: 0.0421 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 0.2589 L22: 0.0427
REMARK 3 L33: 0.1560 L12: -0.1264
REMARK 3 L13: -0.0869 L23: 0.2372
REMARK 3 S TENSOR
REMARK 3 S11: 0.0741 S12: -0.6042 S13: -0.2568
REMARK 3 S21: 0.0016 S22: -0.0861 S23: 0.0497
REMARK 3 S31: -0.0179 S32: -0.1567 S33: 0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 303 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 125.0300 32.4229 23.0643
REMARK 3 T TENSOR
REMARK 3 T11: 0.5834 T22: 0.5523
REMARK 3 T33: 0.6108 T12: 0.1096
REMARK 3 T13: 0.0479 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.1373 L22: 0.2042
REMARK 3 L33: 0.2277 L12: -0.3637
REMARK 3 L13: 0.3141 L23: 0.0729
REMARK 3 S TENSOR
REMARK 3 S11: -0.1230 S12: 0.2538 S13: -0.0130
REMARK 3 S21: 0.0611 S22: 0.1522 S23: -0.0120
REMARK 3 S31: 0.0075 S32: 0.2021 S33: -0.0004
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 334 THROUGH 377 )
REMARK 3 ORIGIN FOR THE GROUP (A): 124.1594 42.1281 44.7237
REMARK 3 T TENSOR
REMARK 3 T11: 0.9406 T22: 0.8015
REMARK 3 T33: 0.6088 T12: 0.1532
REMARK 3 T13: 0.0432 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 0.7884 L22: 0.2342
REMARK 3 L33: 0.4082 L12: 0.7698
REMARK 3 L13: 0.2379 L23: 0.0549
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: -0.6779 S13: 0.0568
REMARK 3 S21: 0.3841 S22: 0.1208 S23: 0.1265
REMARK 3 S31: -0.6802 S32: 0.0614 S33: -0.0005
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 378 THROUGH 453 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.8532 35.1806 25.7431
REMARK 3 T TENSOR
REMARK 3 T11: 0.5252 T22: 0.4971
REMARK 3 T33: 0.5968 T12: 0.1419
REMARK 3 T13: -0.0199 T23: 0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 1.9504 L22: 1.6366
REMARK 3 L33: 1.8484 L12: -0.6542
REMARK 3 L13: 0.3653 L23: 0.3145
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: -0.0672 S13: -0.0184
REMARK 3 S21: -0.0191 S22: 0.0078 S23: 0.3744
REMARK 3 S31: -0.2546 S32: -0.2262 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 454 THROUGH 474 )
REMARK 3 ORIGIN FOR THE GROUP (A): 142.8019 44.0885 32.9739
REMARK 3 T TENSOR
REMARK 3 T11: 0.9333 T22: 1.4210
REMARK 3 T33: 1.1489 T12: -0.1184
REMARK 3 T13: 0.1738 T23: 0.0679
REMARK 3 L TENSOR
REMARK 3 L11: 0.0884 L22: 0.1374
REMARK 3 L33: -0.0204 L12: 0.0578
REMARK 3 L13: -0.0799 L23: -0.1594
REMARK 3 S TENSOR
REMARK 3 S11: -0.2331 S12: 0.8672 S13: -0.3983
REMARK 3 S21: 0.3443 S22: -0.1403 S23: -0.3997
REMARK 3 S31: 0.7889 S32: 1.9313 S33: -0.0001
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 4R6S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000086970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-11
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) : 1.033
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, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28903
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.03200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.42600
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: 2Q59
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
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 46.62050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.97000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.62050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.97000
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -46.62050
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 30.97000
REMARK 350 BIOMT3 2 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 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 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 241
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 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 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 GLN A 203 CG CD OE1 NE2
REMARK 470 LEU A 204 CG CD1 CD2
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 LYS A 240 CG CD CE NZ
REMARK 470 LYS A 244 CG CD CE NZ
REMARK 470 MET A 256 CG SD CE
REMARK 470 MET A 257 CG SD CE
REMARK 470 LYS A 261 CG CD CE NZ
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 ARG A 280 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 282 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 LYS A 457 CG CD CE NZ
REMARK 470 GLU B 207 CG CD OE1 OE2
REMARK 470 LYS B 224 CG CD CE NZ
REMARK 470 LYS B 240 CG CD CE NZ
REMARK 470 LYS B 244 CG CD CE NZ
REMARK 470 GLU B 259 CG CD OE1 OE2
REMARK 470 ASP B 260 CG OD1 OD2
REMARK 470 LYS B 261 CG CD CE NZ
REMARK 470 ILE B 262 CB CG1 CG2 CD1
REMARK 470 LYS B 263 CG CD CE NZ
REMARK 470 PHE B 264 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 265 CG CD CE NZ
REMARK 470 ILE B 267 CG1 CG2 CD1
REMARK 470 LYS B 275 CG CD CE NZ
REMARK 470 LYS B 358 CG CD CE NZ
REMARK 470 GLU B 427 CG CD OE1 OE2
REMARK 470 GLN B 454 CG CD OE1 NE2
REMARK 470 LYS B 458 CG CD CE NZ
REMARK 470 GLU B 460 CG CD OE1 OE2
REMARK 470 GLN B 470 CG CD OE1 NE2
REMARK 470 LYS B 474 CG CD CE NZ
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 B 639 O HOH B 644 2.18
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 LEU A 393 54.64 -91.86
REMARK 500 GLU A 427 31.32 -93.75
REMARK 500 ASP B 251 -175.89 -174.46
REMARK 500 ILE B 262 -169.47 -111.06
REMARK 500 LYS B 263 61.72 -118.01
REMARK 500 HIS B 266 53.99 -109.46
REMARK 500 LYS B 457 10.02 -69.53
REMARK 500 LYS B 458 -118.74 -85.42
REMARK 500 THR B 459 95.02 24.36
REMARK 500 GLU B 460 23.90 -68.62
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 3K2 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3K2 B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4R2U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PPARGAMMA IN COMPLEX WITH SR1664
DBREF 4R6S A 203 477 UNP P37231 PPARG_HUMAN 231 505
DBREF 4R6S B 203 477 UNP P37231 PPARG_HUMAN 231 505
SEQADV 4R6S PHE A 447 UNP P37231 THR 475 ENGINEERED MUTATION
SEQADV 4R6S PHE B 447 UNP P37231 THR 475 ENGINEERED MUTATION
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 PHE 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 PHE 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 3K2 A 501 41
HET 3K2 B 501 41
HETNAM 3K2 4'-[(2,3-DIMETHYL-5-{[(1R)-1-(4-NITROPHENYL)
HETNAM 2 3K2 ETHYL]CARBAMOYL}-1H-INDOL-1-YL)METHYL]BIPHENYL-2-
HETNAM 3 3K2 CARBOXYLIC ACID
FORMUL 3 3K2 2(C33 H29 N3 O5)
FORMUL 5 HOH *116(H2 O)
HELIX 1 1 ASN A 205 PHE A 226 1 22
HELIX 2 2 THR A 229 THR A 238 1 10
HELIX 3 3 ASP A 251 ILE A 262 1 12
HELIX 4 4 VAL A 277 SER A 302 1 26
HELIX 5 5 ASP A 310 LEU A 333 1 24
HELIX 6 6 SER A 342 GLY A 344 5 3
HELIX 7 7 ARG A 350 SER A 355 1 6
HELIX 8 8 PRO A 359 PHE A 363 5 5
HELIX 9 9 MET A 364 ALA A 376 1 13
HELIX 10 10 ASP A 380 LEU A 393 1 14
HELIX 11 11 ASN A 402 HIS A 425 1 24
HELIX 12 12 GLN A 430 GLU A 460 1 31
HELIX 13 13 HIS A 466 LYS A 474 1 9
HELIX 14 14 SER B 208 PHE B 226 1 19
HELIX 15 15 THR B 229 GLY B 239 1 11
HELIX 16 16 ASP B 251 ILE B 262 1 12
HELIX 17 17 GLU B 276 SER B 302 1 27
HELIX 18 18 ASP B 310 SER B 332 1 23
HELIX 19 19 SER B 342 GLY B 344 5 3
HELIX 20 20 ARG B 350 SER B 355 1 6
HELIX 21 21 PRO B 359 PHE B 363 5 5
HELIX 22 22 MET B 364 ALA B 376 1 13
HELIX 23 23 ASP B 380 LEU B 393 1 14
HELIX 24 24 ASN B 402 HIS B 425 1 24
HELIX 25 25 GLN B 430 LYS B 457 1 28
HELIX 26 26 PRO B 467 TYR B 473 1 7
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 4.45
CISPEP 2 LYS B 358 PRO B 359 0 3.78
SITE 1 AC1 13 ILE A 281 PHE A 282 CYS A 285 GLN A 286
SITE 2 AC1 13 ARG A 288 SER A 289 TYR A 327 LEU A 330
SITE 3 AC1 13 ILE A 341 SER A 342 HIS A 449 LEU A 453
SITE 4 AC1 13 TYR A 473
SITE 1 AC2 14 PHE B 282 CYS B 285 GLN B 286 ARG B 288
SITE 2 AC2 14 SER B 289 HIS B 323 ILE B 326 TYR B 327
SITE 3 AC2 14 LEU B 330 ILE B 341 SER B 342 LYS B 367
SITE 4 AC2 14 HIS B 449 LEU B 453
CRYST1 93.241 61.940 119.226 90.00 103.44 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 0.010725 0.000000 0.002563 0.00000
SCALE2 0.000000 0.016145 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008624 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
