HEADER TRANSCRIPTION 09-SEP-10 3OSI
TITLE CRYSTAL STRUCTURE OF PPARGAMMA LIGAND BINDING DOMAIN IN COMPLEX WITH
TITLE 2 TETRACHLORO-BISPHENOL A (TCBPA)
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, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;
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);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS TRANSCRIPTION, LIGAND BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LE MAIRE,W.BOURGUET
REVDAT 4 21-FEB-24 3OSI 1 REMARK SEQADV
REVDAT 3 17-JUL-19 3OSI 1 REMARK
REVDAT 2 19-JUN-13 3OSI 1 JRNL VERSN
REVDAT 1 25-MAY-11 3OSI 0
JRNL AUTH A.RIU,M.GRIMALDI,A.LE MAIRE,G.BEY,K.PHILLIPS,A.BOULAHTOUF,
JRNL AUTH 2 E.PERDU,D.ZALKO,W.BOURGUET,P.BALAGUER
JRNL TITL PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA IS A TARGET
JRNL TITL 2 FOR HALOGENATED ANALOGS OF BISPHENOL A.
JRNL REF ENVIRON.HEALTH PERSPECT. V. 119 1227 2011
JRNL REFN ISSN 0091-6765
JRNL PMID 21561829
JRNL DOI 10.1289/EHP.1003328
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 17920
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 883
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 44.6818 - 4.9046 0.97 2887 134 0.1706 0.2243
REMARK 3 2 4.9046 - 3.8937 0.97 2782 188 0.1340 0.2246
REMARK 3 3 3.8937 - 3.4017 0.97 2791 147 0.1499 0.2220
REMARK 3 4 3.4017 - 3.0907 0.94 2665 156 0.1781 0.2957
REMARK 3 5 3.0907 - 2.8693 0.90 2606 128 0.2204 0.3232
REMARK 3 6 2.8693 - 2.7000 0.87 2490 130 0.2282 0.3343
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 56.44
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.55550
REMARK 3 B22 (A**2) : 9.88520
REMARK 3 B33 (A**2) : -12.44070
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.22800
REMARK 3 B23 (A**2) : 0.00000
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 4120
REMARK 3 ANGLE : 1.156 5564
REMARK 3 CHIRALITY : 0.069 651
REMARK 3 PLANARITY : 0.004 704
REMARK 3 DIHEDRAL : 19.466 1539
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 205:217)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2728 -4.4868 22.7531
REMARK 3 T TENSOR
REMARK 3 T11: 0.1966 T22: 0.2232
REMARK 3 T33: 0.4111 T12: 0.0056
REMARK 3 T13: 0.1512 T23: 0.0713
REMARK 3 L TENSOR
REMARK 3 L11: 0.7068 L22: 0.1718
REMARK 3 L33: 0.6813 L12: 0.1165
REMARK 3 L13: -0.1132 L23: 0.2978
REMARK 3 S TENSOR
REMARK 3 S11: -0.1822 S12: -0.3497 S13: -0.6299
REMARK 3 S21: -0.1176 S22: -0.5577 S23: -0.2295
REMARK 3 S31: 0.1398 S32: -0.1415 S33: 0.0052
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 218:233)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3877 10.0737 12.9968
REMARK 3 T TENSOR
REMARK 3 T11: 0.2358 T22: 0.0602
REMARK 3 T33: 0.1541 T12: 0.2017
REMARK 3 T13: 0.0632 T23: 0.1665
REMARK 3 L TENSOR
REMARK 3 L11: 2.5628 L22: 2.0524
REMARK 3 L33: 1.9581 L12: 1.5689
REMARK 3 L13: -0.3035 L23: 1.2562
REMARK 3 S TENSOR
REMARK 3 S11: 0.2868 S12: 0.5014 S13: 0.2808
REMARK 3 S21: -0.0443 S22: 0.3479 S23: 0.0657
REMARK 3 S31: -0.8730 S32: -0.5328 S33: 0.5662
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 234:250)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5631 13.5612 -3.2214
REMARK 3 T TENSOR
REMARK 3 T11: 0.2560 T22: 0.3934
REMARK 3 T33: 0.0786 T12: 0.0509
REMARK 3 T13: 0.0835 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 5.9326 L22: 2.7523
REMARK 3 L33: 0.4290 L12: 2.9348
REMARK 3 L13: 0.0653 L23: 0.3206
REMARK 3 S TENSOR
REMARK 3 S11: -0.6721 S12: 0.6955 S13: -0.5874
REMARK 3 S21: -1.0399 S22: 0.1597 S23: -0.4275
REMARK 3 S31: 0.0327 S32: 0.1411 S33: -0.0483
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 251:257)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6257 26.5053 -2.8013
REMARK 3 T TENSOR
REMARK 3 T11: 0.6603 T22: 0.2381
REMARK 3 T33: 0.2925 T12: -0.2418
REMARK 3 T13: 0.0163 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.2930 L22: 1.2024
REMARK 3 L33: 2.4714 L12: -0.4175
REMARK 3 L13: -0.6619 L23: 1.5523
REMARK 3 S TENSOR
REMARK 3 S11: 0.5773 S12: -0.0463 S13: 0.6644
REMARK 3 S21: -0.7265 S22: 0.7046 S23: -0.6504
REMARK 3 S31: -0.3861 S32: 0.6542 S33: 0.0489
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 258:279)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4370 29.5994 4.9977
REMARK 3 T TENSOR
REMARK 3 T11: 0.6259 T22: 0.3783
REMARK 3 T33: 0.4383 T12: 0.0344
REMARK 3 T13: 0.0848 T23: -0.1268
REMARK 3 L TENSOR
REMARK 3 L11: 1.3458 L22: 0.2593
REMARK 3 L33: 0.8194 L12: 0.3407
REMARK 3 L13: 0.6009 L23: -0.1620
REMARK 3 S TENSOR
REMARK 3 S11: 0.7758 S12: -1.2056 S13: 0.7178
REMARK 3 S21: -0.0286 S22: -0.6208 S23: 0.3810
REMARK 3 S31: -0.9158 S32: -0.8180 S33: 0.0166
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 280:288)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0255 23.8056 14.0747
REMARK 3 T TENSOR
REMARK 3 T11: 0.1718 T22: 0.6556
REMARK 3 T33: 0.3024 T12: -0.1337
REMARK 3 T13: -0.0916 T23: 0.1625
REMARK 3 L TENSOR
REMARK 3 L11: 0.2510 L22: 2.2767
REMARK 3 L33: 0.5346 L12: -0.2894
REMARK 3 L13: 0.3257 L23: -0.8290
REMARK 3 S TENSOR
REMARK 3 S11: 0.0332 S12: -1.0964 S13: -0.0865
REMARK 3 S21: 0.2125 S22: 0.9842 S23: 0.8043
REMARK 3 S31: -0.0967 S32: -1.0767 S33: 0.0554
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 289:304)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4988 15.5024 22.5458
REMARK 3 T TENSOR
REMARK 3 T11: 0.1949 T22: 0.1149
REMARK 3 T33: 0.2257 T12: 0.1530
REMARK 3 T13: -0.0107 T23: -0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 1.2442 L22: 0.8852
REMARK 3 L33: 0.8727 L12: 0.9246
REMARK 3 L13: 0.6894 L23: 0.2338
REMARK 3 S TENSOR
REMARK 3 S11: 0.2433 S12: 0.0144 S13: -0.1040
REMARK 3 S21: -0.2151 S22: -0.2411 S23: -0.1709
REMARK 3 S31: -0.0218 S32: -0.1567 S33: -0.0186
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 305:349)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0030 12.8091 18.9667
REMARK 3 T TENSOR
REMARK 3 T11: 0.0369 T22: 0.0951
REMARK 3 T33: 0.0613 T12: 0.0652
REMARK 3 T13: -0.0477 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.7845 L22: 0.7961
REMARK 3 L33: 0.3247 L12: 0.2040
REMARK 3 L13: -0.3090 L23: -0.1014
REMARK 3 S TENSOR
REMARK 3 S11: -0.1926 S12: 0.1795 S13: -0.2720
REMARK 3 S21: -0.0666 S22: 0.1041 S23: -0.1602
REMARK 3 S31: -0.0747 S32: -0.0023 S33: -0.0162
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 350:358)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0491 17.8633 6.1102
REMARK 3 T TENSOR
REMARK 3 T11: 0.2142 T22: 0.4060
REMARK 3 T33: 0.2322 T12: -0.0900
REMARK 3 T13: 0.0839 T23: -0.1157
REMARK 3 L TENSOR
REMARK 3 L11: 3.0929 L22: 0.1002
REMARK 3 L33: 0.9783 L12: -0.0196
REMARK 3 L13: 0.6212 L23: 0.2921
REMARK 3 S TENSOR
REMARK 3 S11: -0.6455 S12: 0.8106 S13: -0.7950
REMARK 3 S21: 0.3558 S22: -0.0429 S23: 0.3460
REMARK 3 S31: -0.1255 S32: 0.4103 S33: -0.0043
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 359:377)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6677 8.8544 11.5290
REMARK 3 T TENSOR
REMARK 3 T11: -0.0115 T22: 0.3217
REMARK 3 T33: 0.2737 T12: 0.0424
REMARK 3 T13: -0.0162 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 0.7986 L22: 0.9923
REMARK 3 L33: 2.0952 L12: 0.9131
REMARK 3 L13: -0.3964 L23: -0.5344
REMARK 3 S TENSOR
REMARK 3 S11: -0.2419 S12: 0.4595 S13: -0.2790
REMARK 3 S21: 0.0482 S22: 0.0188 S23: -0.9095
REMARK 3 S31: 0.2913 S32: 0.7902 S33: -0.1690
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 378:424)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4246 0.4403 25.7273
REMARK 3 T TENSOR
REMARK 3 T11: 0.0032 T22: 0.1441
REMARK 3 T33: 0.1743 T12: 0.2389
REMARK 3 T13: -0.0431 T23: 0.1177
REMARK 3 L TENSOR
REMARK 3 L11: 0.9023 L22: 0.6574
REMARK 3 L33: 0.7524 L12: -0.1112
REMARK 3 L13: 0.0940 L23: -0.4368
REMARK 3 S TENSOR
REMARK 3 S11: -0.4392 S12: 0.0915 S13: -0.2797
REMARK 3 S21: 0.0494 S22: 0.1341 S23: -0.0546
REMARK 3 S31: 0.3815 S32: 0.2146 S33: -0.1432
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 425:441)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2210 -6.2336 17.2577
REMARK 3 T TENSOR
REMARK 3 T11: 0.2669 T22: 0.1928
REMARK 3 T33: 0.2289 T12: 0.1434
REMARK 3 T13: -0.0508 T23: 0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 0.3435 L22: 0.3170
REMARK 3 L33: 0.2907 L12: -0.0617
REMARK 3 L13: 0.3167 L23: -0.1216
REMARK 3 S TENSOR
REMARK 3 S11: 0.1359 S12: -0.0200 S13: -0.3790
REMARK 3 S21: 0.2729 S22: 0.3294 S23: -0.4069
REMARK 3 S31: 0.0021 S32: -0.1705 S33: 0.0046
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN A AND RESID 442:458)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5997 15.3626 22.7462
REMARK 3 T TENSOR
REMARK 3 T11: 0.1366 T22: 0.2842
REMARK 3 T33: 0.3626 T12: 0.0733
REMARK 3 T13: -0.0624 T23: -0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 0.4227 L22: 1.2589
REMARK 3 L33: 0.2614 L12: 0.6594
REMARK 3 L13: 0.0568 L23: 0.3518
REMARK 3 S TENSOR
REMARK 3 S11: 0.1635 S12: -0.8367 S13: -0.1917
REMARK 3 S21: 0.6486 S22: -0.1922 S23: -0.2970
REMARK 3 S31: 0.3751 S32: 0.4756 S33: -0.0044
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN A AND RESID 459:467)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8755 29.0448 21.3595
REMARK 3 T TENSOR
REMARK 3 T11: 0.6671 T22: 0.1672
REMARK 3 T33: 0.4454 T12: 0.0534
REMARK 3 T13: -0.0665 T23: -0.1478
REMARK 3 L TENSOR
REMARK 3 L11: 2.7128 L22: 1.0817
REMARK 3 L33: 1.5080 L12: 1.3188
REMARK 3 L13: -1.5597 L23: -1.2066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0720 S12: 0.3716 S13: 0.4556
REMARK 3 S21: 1.1385 S22: 0.7150 S23: 0.3003
REMARK 3 S31: 0.4011 S32: 0.0863 S33: 0.0660
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN A AND RESID 468:476)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9453 20.0759 29.2738
REMARK 3 T TENSOR
REMARK 3 T11: 0.5736 T22: 0.4179
REMARK 3 T33: 0.2818 T12: -0.0440
REMARK 3 T13: 0.0435 T23: -0.1097
REMARK 3 L TENSOR
REMARK 3 L11: 0.0221 L22: 0.0777
REMARK 3 L33: 0.1241 L12: 0.0400
REMARK 3 L13: -0.0144 L23: -0.0585
REMARK 3 S TENSOR
REMARK 3 S11: 0.7281 S12: -0.5083 S13: -0.2352
REMARK 3 S21: 1.2838 S22: -0.0006 S23: 0.3929
REMARK 3 S31: -0.1594 S32: 0.8899 S33: -0.0018
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN B AND RESID 208:214)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9934 -27.1285 22.8884
REMARK 3 T TENSOR
REMARK 3 T11: 0.3652 T22: 0.1463
REMARK 3 T33: 0.4249 T12: 0.0854
REMARK 3 T13: 0.1026 T23: 0.1037
REMARK 3 L TENSOR
REMARK 3 L11: 1.5191 L22: 1.4287
REMARK 3 L33: 1.6196 L12: 1.2288
REMARK 3 L13: -0.6902 L23: -0.9650
REMARK 3 S TENSOR
REMARK 3 S11: 0.1430 S12: -0.9136 S13: -0.3609
REMARK 3 S21: 0.6531 S22: 0.1700 S23: 0.4671
REMARK 3 S31: 0.7403 S32: 0.3294 S33: 0.0809
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN B AND RESID 215:225)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0856 -26.0597 30.6775
REMARK 3 T TENSOR
REMARK 3 T11: 0.2499 T22: 0.0838
REMARK 3 T33: 0.3550 T12: 0.0456
REMARK 3 T13: -0.0079 T23: 0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 0.1162 L22: 0.0606
REMARK 3 L33: 0.3211 L12: -0.0712
REMARK 3 L13: -0.1116 L23: 0.0094
REMARK 3 S TENSOR
REMARK 3 S11: 0.4279 S12: -0.0775 S13: -0.4606
REMARK 3 S21: 0.0487 S22: -0.2038 S23: -0.2957
REMARK 3 S31: 0.4783 S32: 0.3801 S33: 0.0056
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN B AND RESID 226:244)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6367 -19.4249 45.1477
REMARK 3 T TENSOR
REMARK 3 T11: 0.4018 T22: 0.1907
REMARK 3 T33: 0.1732 T12: 0.1227
REMARK 3 T13: 0.0303 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 3.4117 L22: 1.9923
REMARK 3 L33: 0.6101 L12: -0.9780
REMARK 3 L13: 1.4344 L23: -0.5345
REMARK 3 S TENSOR
REMARK 3 S11: 0.1668 S12: -0.7004 S13: -0.6665
REMARK 3 S21: 0.7201 S22: 0.1970 S23: 0.7122
REMARK 3 S31: -0.2099 S32: -0.4044 S33: 0.0590
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN B AND RESID 245:250)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5613 -11.3525 55.3725
REMARK 3 T TENSOR
REMARK 3 T11: 0.5216 T22: 0.6906
REMARK 3 T33: 0.1081 T12: 0.0083
REMARK 3 T13: -0.0649 T23: 0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 2.0923 L22: 1.6731
REMARK 3 L33: 0.9930 L12: -1.0780
REMARK 3 L13: -0.8501 L23: 1.1172
REMARK 3 S TENSOR
REMARK 3 S11: 1.0596 S12: -0.7642 S13: -0.0719
REMARK 3 S21: -0.7112 S22: -0.1518 S23: 0.0136
REMARK 3 S31: 0.6924 S32: 0.6978 S33: 0.0596
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN B AND RESID 251:261)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0489 -8.7149 55.1066
REMARK 3 T TENSOR
REMARK 3 T11: 0.5135 T22: 0.9879
REMARK 3 T33: 0.3706 T12: -0.0391
REMARK 3 T13: 0.1102 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.0976 L22: 0.0062
REMARK 3 L33: 0.1020 L12: -0.0273
REMARK 3 L13: -0.0285 L23: 0.0020
REMARK 3 S TENSOR
REMARK 3 S11: 0.1669 S12: -0.4900 S13: 0.3083
REMARK 3 S21: -0.0696 S22: 0.1429 S23: -0.0950
REMARK 3 S31: -0.6740 S32: 1.3575 S33: -0.0044
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN B AND RESID 275:287)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8941 -4.9372 42.0692
REMARK 3 T TENSOR
REMARK 3 T11: 0.2860 T22: 0.4916
REMARK 3 T33: 0.2648 T12: -0.0189
REMARK 3 T13: -0.0761 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 0.1511 L22: 0.2838
REMARK 3 L33: 0.1526 L12: 0.0142
REMARK 3 L13: -0.0779 L23: -0.1870
REMARK 3 S TENSOR
REMARK 3 S11: 0.1049 S12: -0.3172 S13: -0.4171
REMARK 3 S21: -1.0039 S22: -0.0272 S23: -0.0319
REMARK 3 S31: 0.2656 S32: -0.0107 S33: -0.0006
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN B AND RESID 288:312)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1514 -19.2077 23.8166
REMARK 3 T TENSOR
REMARK 3 T11: 0.2066 T22: 0.1745
REMARK 3 T33: 0.3178 T12: 0.0914
REMARK 3 T13: 0.0143 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.7707 L22: 0.4283
REMARK 3 L33: 0.4772 L12: 0.3679
REMARK 3 L13: -0.2836 L23: 0.2073
REMARK 3 S TENSOR
REMARK 3 S11: -0.0495 S12: -0.0368 S13: -0.6433
REMARK 3 S21: 0.2133 S22: 0.2032 S23: 0.0455
REMARK 3 S31: 0.3011 S32: 0.3492 S33: 0.0002
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN B AND RESID 313:333)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7417 -10.8641 27.4442
REMARK 3 T TENSOR
REMARK 3 T11: 0.0810 T22: 0.0405
REMARK 3 T33: 0.0985 T12: 0.0688
REMARK 3 T13: 0.0140 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.7500 L22: 0.3723
REMARK 3 L33: 1.7364 L12: 0.4332
REMARK 3 L13: -0.7849 L23: -0.0877
REMARK 3 S TENSOR
REMARK 3 S11: -0.0616 S12: 0.1371 S13: -0.2141
REMARK 3 S21: 0.0675 S22: -0.2178 S23: -0.2175
REMARK 3 S31: -0.2087 S32: -0.1491 S33: -0.0786
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN B AND RESID 334:354)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8843 -7.6610 48.3568
REMARK 3 T TENSOR
REMARK 3 T11: 0.2868 T22: 0.2874
REMARK 3 T33: 0.1427 T12: 0.0990
REMARK 3 T13: 0.0027 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 2.2629 L22: 2.9179
REMARK 3 L33: 1.4980 L12: 0.2862
REMARK 3 L13: -0.8274 L23: -0.4591
REMARK 3 S TENSOR
REMARK 3 S11: 0.7918 S12: -0.5063 S13: -0.0655
REMARK 3 S21: -0.3793 S22: -0.6090 S23: 0.6344
REMARK 3 S31: -0.6567 S32: 0.1574 S33: 0.0593
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN B AND RESID 355:362)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5396 4.6092 44.0373
REMARK 3 T TENSOR
REMARK 3 T11: 0.7196 T22: 0.3512
REMARK 3 T33: 0.2110 T12: -0.0457
REMARK 3 T13: 0.1561 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 0.0876 L22: 0.0192
REMARK 3 L33: 0.1600 L12: 0.0234
REMARK 3 L13: -0.0222 L23: 0.0372
REMARK 3 S TENSOR
REMARK 3 S11: 0.4688 S12: -0.6207 S13: 1.1518
REMARK 3 S21: 0.5496 S22: 0.4144 S23: 0.2045
REMARK 3 S31: -1.0114 S32: -0.0542 S33: -0.0090
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN B AND RESID 363:378)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3523 -4.3710 39.7962
REMARK 3 T TENSOR
REMARK 3 T11: 0.3778 T22: 0.2013
REMARK 3 T33: 0.1709 T12: 0.1222
REMARK 3 T13: 0.0848 T23: 0.0482
REMARK 3 L TENSOR
REMARK 3 L11: 0.6450 L22: 1.0040
REMARK 3 L33: 0.4835 L12: 0.5871
REMARK 3 L13: 0.2096 L23: 0.2922
REMARK 3 S TENSOR
REMARK 3 S11: -0.0896 S12: -0.0165 S13: 0.4894
REMARK 3 S21: -0.3435 S22: -0.0131 S23: 0.5013
REMARK 3 S31: -0.3781 S32: -0.0916 S33: -0.0119
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN B AND RESID 379:422)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1396 -15.1465 21.7163
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.0645
REMARK 3 T33: 0.2150 T12: 0.1256
REMARK 3 T13: -0.0662 T23: 0.0712
REMARK 3 L TENSOR
REMARK 3 L11: 1.6851 L22: 0.4390
REMARK 3 L33: 2.6078 L12: 0.6969
REMARK 3 L13: -1.2641 L23: -1.0629
REMARK 3 S TENSOR
REMARK 3 S11: -0.1040 S12: 0.4844 S13: 0.1029
REMARK 3 S21: -0.2592 S22: 0.0047 S23: 0.0540
REMARK 3 S31: -0.1157 S32: -0.3485 S33: -0.1390
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN B AND RESID 423:438)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9101 -11.7556 31.6923
REMARK 3 T TENSOR
REMARK 3 T11: 0.2252 T22: 0.2631
REMARK 3 T33: 0.3304 T12: 0.0933
REMARK 3 T13: 0.0641 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.1419 L22: 0.2213
REMARK 3 L33: 0.0003 L12: -0.1829
REMARK 3 L13: -0.0087 L23: 0.0082
REMARK 3 S TENSOR
REMARK 3 S11: -0.1633 S12: 0.0182 S13: -0.5269
REMARK 3 S21: -0.0466 S22: 0.0625 S23: -0.0867
REMARK 3 S31: -0.1992 S32: -0.1877 S33: -0.0002
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN B AND RESID 439:453)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0082 0.0948 29.9329
REMARK 3 T TENSOR
REMARK 3 T11: 0.2809 T22: 0.3649
REMARK 3 T33: 0.3256 T12: 0.0651
REMARK 3 T13: 0.0957 T23: 0.0529
REMARK 3 L TENSOR
REMARK 3 L11: 0.4405 L22: 0.2144
REMARK 3 L33: 0.4160 L12: -0.0837
REMARK 3 L13: 0.0459 L23: -0.2902
REMARK 3 S TENSOR
REMARK 3 S11: 0.8066 S12: 0.6190 S13: 1.0568
REMARK 3 S21: 0.4020 S22: -0.3267 S23: 0.6288
REMARK 3 S31: -0.1557 S32: -0.0494 S33: -0.0002
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN B AND RESID 454:474)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5348 -2.5065 31.9353
REMARK 3 T TENSOR
REMARK 3 T11: 0.4225 T22: 0.2477
REMARK 3 T33: 0.2170 T12: 0.0631
REMARK 3 T13: -0.0618 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 0.2341 L22: 1.6457
REMARK 3 L33: 0.7410 L12: -0.6152
REMARK 3 L13: -0.1035 L23: 0.0746
REMARK 3 S TENSOR
REMARK 3 S11: 0.0711 S12: -0.1292 S13: -0.2513
REMARK 3 S21: -1.0002 S22: 0.2547 S23: -0.2387
REMARK 3 S31: 0.0789 S32: 1.0915 S33: 0.0444
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 3OSI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18014
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 44.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M TRI-SODIUM CITRATE, 100 MM HEPES,
REMARK 280 3% 1,2-PROPANEDIOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 46.46700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.87100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.46700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.87100
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 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 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 GLY A 192
REMARK 465 SER A 193
REMARK 465 HIS A 194
REMARK 465 MET 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 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 GLY B 192
REMARK 465 SER B 193
REMARK 465 HIS B 194
REMARK 465 MET B 195
REMARK 465 GLU B 196
REMARK 465 ILE B 197
REMARK 465 SER B 198
REMARK 465 SER B 199
REMARK 465 ASP B 200
REMARK 465 ILE B 201
REMARK 465 ASP B 202
REMARK 465 GLN B 203
REMARK 465 LEU B 204
REMARK 465 ASN B 205
REMARK 465 PRO B 206
REMARK 465 GLU B 207
REMARK 465 LYS B 240
REMARK 465 THR B 241
REMARK 465 THR B 242
REMARK 465 ASP B 243
REMARK 465 ILE B 262
REMARK 465 LYS B 263
REMARK 465 PHE B 264
REMARK 465 LYS B 265
REMARK 465 HIS B 266
REMARK 465 ILE B 267
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 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 MET A 256 CG SD CE
REMARK 470 LYS A 261 CG CD CE NZ
REMARK 470 ARG A 280 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 343 CG CD OE1 OE2
REMARK 470 GLN A 444 CG CD OE1 NE2
REMARK 470 LYS B 261 CG CD CE NZ
REMARK 470 LYS B 275 CG CD CE NZ
REMARK 470 GLN B 283 CG CD OE1 NE2
REMARK 470 GLU B 343 CG CD OE1 OE2
REMARK 470 LYS B 358 CG CD CE NZ
REMARK 470 LYS B 457 CG CD CE NZ
REMARK 470 LYS B 458 CG CD CE NZ
REMARK 470 LYS B 474 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 PRO A 246 C - N - CA ANGL. DEV. = 9.5 DEGREES
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 33.55 -68.51
REMARK 500 GLU A 276 -133.61 -92.83
REMARK 500 VAL A 277 -56.86 -130.32
REMARK 500 ASN A 402 83.54 -162.26
REMARK 500 HIS A 425 58.19 -142.23
REMARK 500 GLU A 460 69.20 -109.86
REMARK 500 THR B 238 -91.39 -128.25
REMARK 500 PRO B 304 111.07 -38.87
REMARK 500 LEU B 393 44.49 -88.12
REMARK 500 THR B 459 58.73 -160.10
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 XDH A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OSW RELATED DB: PDB
DBREF 3OSI A 196 476 UNP P37231 PPARG_HUMAN 224 504
DBREF 3OSI B 196 476 UNP P37231 PPARG_HUMAN 224 504
SEQADV 3OSI GLY A 192 UNP P37231 EXPRESSION TAG
SEQADV 3OSI SER A 193 UNP P37231 EXPRESSION TAG
SEQADV 3OSI HIS A 194 UNP P37231 EXPRESSION TAG
SEQADV 3OSI MET A 195 UNP P37231 EXPRESSION TAG
SEQADV 3OSI GLY B 192 UNP P37231 EXPRESSION TAG
SEQADV 3OSI SER B 193 UNP P37231 EXPRESSION TAG
SEQADV 3OSI HIS B 194 UNP P37231 EXPRESSION TAG
SEQADV 3OSI MET B 195 UNP P37231 EXPRESSION TAG
SEQRES 1 A 285 GLY SER HIS MET GLU ILE SER SER ASP ILE ASP GLN LEU
SEQRES 2 A 285 ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS HIS
SEQRES 3 A 285 LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR LYS
SEQRES 4 A 285 ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR ASP
SEQRES 5 A 285 LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU MET
SEQRES 6 A 285 MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR PRO
SEQRES 7 A 285 LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE PHE
SEQRES 8 A 285 GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN GLU
SEQRES 9 A 285 ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL ASN
SEQRES 10 A 285 LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY
SEQRES 11 A 285 VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU MET
SEQRES 12 A 285 ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY PHE
SEQRES 13 A 285 MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO PHE
SEQRES 14 A 285 GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL LYS
SEQRES 15 A 285 PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA ILE
SEQRES 16 A 285 PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO GLY
SEQRES 17 A 285 LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN
SEQRES 18 A 285 LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS
SEQRES 19 A 285 PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN LYS
SEQRES 20 A 285 MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL GLN
SEQRES 21 A 285 LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET SER
SEQRES 22 A 285 LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU
SEQRES 1 B 285 GLY SER HIS MET GLU ILE SER SER ASP ILE ASP GLN LEU
SEQRES 2 B 285 ASN PRO GLU SER ALA ASP LEU ARG ALA LEU ALA LYS HIS
SEQRES 3 B 285 LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU THR LYS
SEQRES 4 B 285 ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR THR ASP
SEQRES 5 B 285 LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER LEU MET
SEQRES 6 B 285 MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE THR PRO
SEQRES 7 B 285 LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG ILE PHE
SEQRES 8 B 285 GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL GLN GLU
SEQRES 9 B 285 ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE VAL ASN
SEQRES 10 B 285 LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS TYR GLY
SEQRES 11 B 285 VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER LEU MET
SEQRES 12 B 285 ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN GLY PHE
SEQRES 13 B 285 MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS PRO PHE
SEQRES 14 B 285 GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA VAL LYS
SEQRES 15 B 285 PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU ALA ILE
SEQRES 16 B 285 PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG PRO GLY
SEQRES 17 B 285 LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN ASP ASN
SEQRES 18 B 285 LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU ASN HIS
SEQRES 19 B 285 PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU GLN LYS
SEQRES 20 B 285 MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS VAL GLN
SEQRES 21 B 285 LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP MET SER
SEQRES 22 B 285 LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP LEU
HET XDH A 1 21
HET PGO A6128 5
HETNAM XDH 4,4'-PROPANE-2,2-DIYLBIS(2,6-DICHLOROPHENOL)
HETNAM PGO S-1,2-PROPANEDIOL
FORMUL 3 XDH C15 H12 CL4 O2
FORMUL 4 PGO C3 H8 O2
FORMUL 5 HOH *91(H2 O)
HELIX 1 1 ASN A 205 PHE A 226 1 22
HELIX 2 2 THR A 229 GLY A 239 1 11
HELIX 3 3 ASP A 251 LYS A 261 1 11
HELIX 4 4 VAL A 277 SER A 302 1 26
HELIX 5 5 GLY A 305 LEU A 309 5 5
HELIX 6 6 ASP A 310 ALA A 331 1 22
HELIX 7 7 SER A 342 GLY A 344 5 3
HELIX 8 8 ARG A 350 LEU A 356 1 7
HELIX 9 9 PRO A 359 PHE A 363 5 5
HELIX 10 10 MET A 364 ALA A 376 1 13
HELIX 11 11 ASP A 380 LEU A 393 1 14
HELIX 12 12 VAL A 403 HIS A 425 1 23
HELIX 13 13 GLN A 430 LYS A 438 1 9
HELIX 14 14 LYS A 438 GLU A 460 1 23
HELIX 15 15 HIS A 466 LYS A 474 1 9
HELIX 16 16 SER B 208 PHE B 226 1 19
HELIX 17 17 THR B 229 THR B 238 1 10
HELIX 18 18 ASP B 251 LYS B 261 1 11
HELIX 19 19 GLU B 276 LYS B 301 1 26
HELIX 20 20 GLY B 305 LEU B 309 5 5
HELIX 21 21 ASP B 310 ALA B 331 1 22
HELIX 22 22 ARG B 350 LEU B 356 1 7
HELIX 23 23 PRO B 359 PHE B 363 5 5
HELIX 24 24 MET B 364 ALA B 376 1 13
HELIX 25 25 ASP B 380 LEU B 393 1 14
HELIX 26 26 ASN B 402 HIS B 425 1 24
HELIX 27 27 GLN B 430 LYS B 458 1 29
HELIX 28 28 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 8.14
CISPEP 2 LYS B 358 PRO B 359 0 5.26
SITE 1 AC1 9 CYS A 285 ARG A 288 SER A 289 LEU A 330
SITE 2 AC1 9 VAL A 339 LEU A 340 ILE A 341 SER A 342
SITE 3 AC1 9 GLU A 343
CRYST1 92.934 61.742 118.644 90.00 102.79 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 0.010760 0.000000 0.002444 0.00000
SCALE2 0.000000 0.016196 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008643 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
