HEADER OXIDOREDUCTASE 01-MAY-12 4EYU
TITLE THE FREE STRUCTURE OF THE MOUSE C-TERMINAL DOMAIN OF KDM6B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 6B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1155-1641;
COMPND 5 SYNONYM: JMJC DOMAIN-CONTAINING PROTEIN 3, JUMONJI DOMAIN-CONTAINING
COMPND 6 PROTEIN 3;
COMPND 7 EC: 1.14.11.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: KDM6B, JMJD3, KIAA0346;
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: PET28 SUMO
KEYWDS JMJC DOMAIN, HISTONE K27 TRIMETHYL AND DIMETHYL DEMETHYLASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.J.CHENG,D.J.PATEL
REVDAT 5 28-FEB-24 4EYU 1 REMARK LINK
REVDAT 4 09-AUG-17 4EYU 1 SOURCE AUTHOR REMARK
REVDAT 3 29-AUG-12 4EYU 1 JRNL
REVDAT 2 15-AUG-12 4EYU 1 JRNL
REVDAT 1 08-AUG-12 4EYU 0
JRNL AUTH L.KRUIDENIER,C.W.CHUNG,Z.CHENG,J.LIDDLE,K.CHE,G.JOBERTY,
JRNL AUTH 2 M.BANTSCHEFF,C.BOUNTRA,A.BRIDGES,H.DIALLO,D.EBERHARD,
JRNL AUTH 3 S.HUTCHINSON,E.JONES,R.KATSO,M.LEVERIDGE,P.K.MANDER,
JRNL AUTH 4 J.MOSLEY,C.RAMIREZ-MOLINA,P.ROWLAND,C.J.SCHOFIELD,
JRNL AUTH 5 R.J.SHEPPARD,J.E.SMITH,C.SWALES,R.TANNER,P.THOMAS,A.TUMBER,
JRNL AUTH 6 G.DREWES,U.OPPERMANN,D.J.PATEL,K.LEE,D.M.WILSON
JRNL TITL A SELECTIVE JUMONJI H3K27 DEMETHYLASE INHIBITOR MODULATES
JRNL TITL 2 THE PROINFLAMMATORY MACROPHAGE RESPONSE.
JRNL REF NATURE V. 488 404 2012
JRNL REFN ISSN 0028-0836
JRNL PMID 22842901
JRNL DOI 10.1038/NATURE11262
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 38.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 54823
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2767
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 38.4515 - 6.2268 0.99 2816 155 0.1904 0.2026
REMARK 3 2 6.2268 - 4.9457 1.00 2723 146 0.2059 0.2104
REMARK 3 3 4.9457 - 4.3215 1.00 2687 138 0.1598 0.1937
REMARK 3 4 4.3215 - 3.9268 1.00 2655 138 0.1732 0.2399
REMARK 3 5 3.9268 - 3.6456 1.00 2672 124 0.1981 0.2282
REMARK 3 6 3.6456 - 3.4308 0.99 2635 160 0.2143 0.2475
REMARK 3 7 3.4308 - 3.2591 1.00 2666 117 0.2151 0.2656
REMARK 3 8 3.2591 - 3.1173 1.00 2633 127 0.2325 0.2548
REMARK 3 9 3.1173 - 2.9973 1.00 2628 134 0.2354 0.2828
REMARK 3 10 2.9973 - 2.8939 0.99 2630 146 0.2393 0.2989
REMARK 3 11 2.8939 - 2.8035 1.00 2613 144 0.2540 0.2681
REMARK 3 12 2.8035 - 2.7234 0.99 2603 147 0.2723 0.3997
REMARK 3 13 2.7234 - 2.6517 0.99 2601 147 0.2821 0.3459
REMARK 3 14 2.6517 - 2.5870 1.00 2588 154 0.2918 0.3234
REMARK 3 15 2.5870 - 2.5282 0.99 2588 139 0.3193 0.3696
REMARK 3 16 2.5282 - 2.4744 0.97 2568 139 0.3435 0.3768
REMARK 3 17 2.4744 - 2.4249 0.97 2525 127 0.3498 0.4257
REMARK 3 18 2.4249 - 2.3792 0.97 2543 145 0.3748 0.3484
REMARK 3 19 2.3792 - 2.3367 0.96 2523 120 0.3859 0.4770
REMARK 3 20 2.3367 - 2.2971 0.83 2159 120 0.3890 0.4204
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 : 0.30
REMARK 3 B_SOL : 43.41
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.650
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.640
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) : -19.28970
REMARK 3 B22 (A**2) : 36.00110
REMARK 3 B33 (A**2) : -16.71140
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 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 : 0.012 7518
REMARK 3 ANGLE : 1.145 10240
REMARK 3 CHIRALITY : 0.068 1118
REMARK 3 PLANARITY : 0.006 1310
REMARK 3 DIHEDRAL : 15.258 2722
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 1157:1203 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3459 -16.3905 -38.2808
REMARK 3 T TENSOR
REMARK 3 T11: 0.5305 T22: 0.6287
REMARK 3 T33: 0.4653 T12: -0.1472
REMARK 3 T13: -0.0267 T23: -0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 2.3550 L22: 1.3153
REMARK 3 L33: 0.6983 L12: -1.0111
REMARK 3 L13: 0.1951 L23: -0.5610
REMARK 3 S TENSOR
REMARK 3 S11: -0.1159 S12: 0.0221 S13: -0.5512
REMARK 3 S21: -0.1336 S22: 0.2621 S23: 0.1790
REMARK 3 S31: 0.5292 S32: 0.0340 S33: -0.1611
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 1204:1239 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1403 3.3830 -45.0236
REMARK 3 T TENSOR
REMARK 3 T11: 0.3752 T22: 0.6543
REMARK 3 T33: 0.2649 T12: -0.1292
REMARK 3 T13: 0.0269 T23: 0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 2.8198 L22: 2.3912
REMARK 3 L33: 3.4527 L12: -1.3714
REMARK 3 L13: 0.3558 L23: -1.3028
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: 0.0762 S13: -0.0523
REMARK 3 S21: -0.2032 S22: 0.1466 S23: 0.1402
REMARK 3 S31: -0.2268 S32: -0.5851 S33: -0.1786
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 1240:1268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8460 2.9059 -49.6284
REMARK 3 T TENSOR
REMARK 3 T11: 0.4038 T22: 0.7796
REMARK 3 T33: 0.3855 T12: -0.2218
REMARK 3 T13: 0.0397 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 2.2516 L22: 1.5777
REMARK 3 L33: 1.8471 L12: -1.5776
REMARK 3 L13: 0.3692 L23: -0.9977
REMARK 3 S TENSOR
REMARK 3 S11: 0.1738 S12: 0.2066 S13: 0.4868
REMARK 3 S21: -0.2852 S22: -0.1589 S23: -0.4517
REMARK 3 S31: -0.2193 S32: 0.8054 S33: 0.0537
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 1269:1298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8518 15.8470 -57.6518
REMARK 3 T TENSOR
REMARK 3 T11: 0.6960 T22: 0.0458
REMARK 3 T33: 0.4532 T12: -0.4175
REMARK 3 T13: 0.0469 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 1.3450 L22: 1.8283
REMARK 3 L33: 0.6140 L12: 0.7084
REMARK 3 L13: 0.1782 L23: -0.0965
REMARK 3 S TENSOR
REMARK 3 S11: -0.0801 S12: 0.3362 S13: 0.2094
REMARK 3 S21: -0.2933 S22: 0.2595 S23: 0.0221
REMARK 3 S31: -0.3699 S32: 0.2194 S33: 0.1502
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 1299:1374 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0373 7.2739 -36.8056
REMARK 3 T TENSOR
REMARK 3 T11: 0.3411 T22: 0.4115
REMARK 3 T33: 0.2908 T12: -0.0627
REMARK 3 T13: 0.0221 T23: -0.0621
REMARK 3 L TENSOR
REMARK 3 L11: 0.6243 L22: 0.7565
REMARK 3 L33: 4.3045 L12: -0.4738
REMARK 3 L13: 0.3161 L23: -0.8331
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: -0.4383 S13: 0.0293
REMARK 3 S21: 0.1337 S22: -0.0438 S23: 0.0394
REMARK 3 S31: -0.5177 S32: -0.0488 S33: -0.0712
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 1375:1503 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5085 -4.8284 -40.0428
REMARK 3 T TENSOR
REMARK 3 T11: 0.2795 T22: 0.3571
REMARK 3 T33: 0.2711 T12: -0.1466
REMARK 3 T13: -0.0122 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 2.0340 L22: 1.0145
REMARK 3 L33: 2.5577 L12: -1.0416
REMARK 3 L13: -0.0509 L23: -0.6487
REMARK 3 S TENSOR
REMARK 3 S11: -0.0504 S12: -0.1442 S13: 0.0083
REMARK 3 S21: 0.0397 S22: 0.0218 S23: -0.0350
REMARK 3 S31: 0.0800 S32: 0.1725 S33: -0.0375
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 1504:1636 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5763 -0.6588 -9.4340
REMARK 3 T TENSOR
REMARK 3 T11: 0.3356 T22: 0.8343
REMARK 3 T33: 0.3521 T12: -0.1539
REMARK 3 T13: -0.0127 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 2.2478 L22: 1.7319
REMARK 3 L33: 4.9719 L12: 0.4497
REMARK 3 L13: 0.4120 L23: 1.2671
REMARK 3 S TENSOR
REMARK 3 S11: 0.0856 S12: -0.4459 S13: 0.2302
REMARK 3 S21: 0.1037 S22: -0.1567 S23: -0.0537
REMARK 3 S31: -0.0886 S32: 0.3566 S33: 0.0438
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 1157:1196 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.0078 16.2392 -25.9582
REMARK 3 T TENSOR
REMARK 3 T11: 0.5059 T22: 0.8726
REMARK 3 T33: 0.4900 T12: -0.2240
REMARK 3 T13: 0.0230 T23: -0.1468
REMARK 3 L TENSOR
REMARK 3 L11: 1.2567 L22: 1.9580
REMARK 3 L33: 2.1970 L12: -0.7169
REMARK 3 L13: -0.1078 L23: -0.9856
REMARK 3 S TENSOR
REMARK 3 S11: -0.0653 S12: -0.1381 S13: 0.3474
REMARK 3 S21: 0.1697 S22: 0.2432 S23: -0.1290
REMARK 3 S31: -0.3963 S32: -0.0546 S33: -0.2020
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 1197:1228 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.3608 6.0706 -21.3539
REMARK 3 T TENSOR
REMARK 3 T11: 0.3906 T22: 1.0435
REMARK 3 T33: 0.3614 T12: -0.1045
REMARK 3 T13: 0.0481 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 1.7584 L22: 3.9350
REMARK 3 L33: 1.7330 L12: -0.0780
REMARK 3 L13: 0.0000 L23: -1.5368
REMARK 3 S TENSOR
REMARK 3 S11: 0.0681 S12: -0.1750 S13: 0.1883
REMARK 3 S21: 0.3132 S22: 0.2603 S23: 0.2217
REMARK 3 S31: -0.0823 S32: -0.7608 S33: -0.4359
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 1229:1257 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.5985 -10.4239 -15.8928
REMARK 3 T TENSOR
REMARK 3 T11: 0.3807 T22: 0.8189
REMARK 3 T33: 0.3502 T12: -0.0667
REMARK 3 T13: 0.0293 T23: -0.0692
REMARK 3 L TENSOR
REMARK 3 L11: 3.4689 L22: 2.4183
REMARK 3 L33: 2.6138 L12: 0.9932
REMARK 3 L13: 0.6500 L23: -0.9013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0723 S12: -0.1643 S13: -0.3400
REMARK 3 S21: -0.0113 S22: 0.0928 S23: -0.0918
REMARK 3 S31: 0.3057 S32: 0.0538 S33: -0.2055
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 1258:1297 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.8327 -11.1757 -10.0358
REMARK 3 T TENSOR
REMARK 3 T11: 0.3566 T22: 0.8297
REMARK 3 T33: 0.3350 T12: -0.0590
REMARK 3 T13: 0.0243 T23: -0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 2.2741 L22: 3.3678
REMARK 3 L33: 1.7183 L12: 0.7987
REMARK 3 L13: 0.3059 L23: -1.3767
REMARK 3 S TENSOR
REMARK 3 S11: -0.0289 S12: -0.2509 S13: -0.1292
REMARK 3 S21: 0.2230 S22: 0.2295 S23: -0.1683
REMARK 3 S31: -0.0183 S32: 0.2401 S33: -0.1082
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 1298:1374 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.5031 -7.4093 -27.4982
REMARK 3 T TENSOR
REMARK 3 T11: 0.4392 T22: 0.8998
REMARK 3 T33: 0.4244 T12: -0.2864
REMARK 3 T13: 0.0083 T23: -0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 1.3706 L22: 2.0998
REMARK 3 L33: 4.2343 L12: -0.9401
REMARK 3 L13: -0.4475 L23: -1.6409
REMARK 3 S TENSOR
REMARK 3 S11: -0.1282 S12: 0.1625 S13: -0.0618
REMARK 3 S21: -0.0172 S22: 0.1457 S23: 0.1344
REMARK 3 S31: 0.4510 S32: -0.2663 S33: 0.0003
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 1375:1503 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0149 4.7673 -24.3472
REMARK 3 T TENSOR
REMARK 3 T11: 0.3581 T22: 0.8227
REMARK 3 T33: 0.3876 T12: -0.1530
REMARK 3 T13: 0.0264 T23: -0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 1.4263 L22: 0.9361
REMARK 3 L33: 2.5560 L12: -0.1338
REMARK 3 L13: 0.6189 L23: -0.5783
REMARK 3 S TENSOR
REMARK 3 S11: -0.0448 S12: -0.0878 S13: 0.1230
REMARK 3 S21: -0.0153 S22: 0.1189 S23: -0.0672
REMARK 3 S31: -0.1524 S32: -0.0874 S33: -0.0345
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 1504:1589 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.3205 1.7006 -53.2272
REMARK 3 T TENSOR
REMARK 3 T11: 0.3128 T22: 0.7277
REMARK 3 T33: 0.3697 T12: -0.1538
REMARK 3 T13: -0.0007 T23: 0.0770
REMARK 3 L TENSOR
REMARK 3 L11: 1.7458 L22: 1.5981
REMARK 3 L33: 4.4083 L12: -1.4751
REMARK 3 L13: -0.6595 L23: 1.4412
REMARK 3 S TENSOR
REMARK 3 S11: 0.1155 S12: 0.3008 S13: -0.0876
REMARK 3 S21: -0.0500 S22: -0.1470 S23: -0.0444
REMARK 3 S31: -0.0968 S32: 0.2662 S33: 0.0750
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN B AND RESID 1594:1638 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.3771 -1.5586 -58.1316
REMARK 3 T TENSOR
REMARK 3 T11: 0.3410 T22: 0.8857
REMARK 3 T33: 0.3445 T12: -0.0692
REMARK 3 T13: 0.0290 T23: 0.1039
REMARK 3 L TENSOR
REMARK 3 L11: 0.3106 L22: 1.0323
REMARK 3 L33: 3.5064 L12: 0.4680
REMARK 3 L13: 0.2550 L23: 0.2976
REMARK 3 S TENSOR
REMARK 3 S11: -0.0966 S12: 0.1133 S13: -0.2100
REMARK 3 S21: 0.0809 S22: -0.0090 S23: -0.0683
REMARK 3 S31: 0.3729 S32: 0.2921 S33: 0.0052
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1155:1168 OR RESSEQ
REMARK 3 1321:1565 OR RESSEQ 1567:1589 OR RESSEQ
REMARK 3 1596:1636 ) AND (NOT ELEMENT H)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 1155:1168 OR RESSEQ
REMARK 3 1321:1565 OR RESSEQ 1567:1589 OR RESSEQ
REMARK 3 1596:1636 ) AND (NOT ELEMENT H)
REMARK 3 ATOM PAIRS NUMBER : 2609
REMARK 3 RMSD : 0.064
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4EYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072240.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SI MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55090
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.297
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07200
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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% METHANOL, 6% MPD, 5% PEG 4K, 5%
REMARK 280 GLYCEROL, HEPES PH 8.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 41.48850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.65100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.14200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.65100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.48850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.14200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1303
REMARK 465 PRO A 1304
REMARK 465 THR A 1305
REMARK 465 LYS A 1306
REMARK 465 ALA A 1307
REMARK 465 ALA A 1308
REMARK 465 ARG A 1309
REMARK 465 LYS A 1310
REMARK 465 SER A 1311
REMARK 465 ALA A 1312
REMARK 465 PRO A 1313
REMARK 465 ALA A 1314
REMARK 465 THR A 1315
REMARK 465 GLY A 1316
REMARK 465 GLY A 1317
REMARK 465 GLY A 1318
REMARK 465 SER A 1319
REMARK 465 SER A 1320
REMARK 465 GLY A 1321
REMARK 465 SER A 1322
REMARK 465 ASN A 1592
REMARK 465 GLY A 1593
REMARK 465 SER A 1594
REMARK 465 ARG A 1595
REMARK 465 ASN A 1596
REMARK 465 ALA A 1639
REMARK 465 SER A 1640
REMARK 465 THR A 1641
REMARK 465 SER A 1642
REMARK 465 ARG A 1643
REMARK 465 THR B 1172
REMARK 465 GLU B 1173
REMARK 465 GLN B 1302
REMARK 465 GLY B 1303
REMARK 465 PRO B 1304
REMARK 465 THR B 1305
REMARK 465 LYS B 1306
REMARK 465 ALA B 1307
REMARK 465 ALA B 1308
REMARK 465 ARG B 1309
REMARK 465 LYS B 1310
REMARK 465 SER B 1311
REMARK 465 ALA B 1312
REMARK 465 PRO B 1313
REMARK 465 ALA B 1314
REMARK 465 THR B 1315
REMARK 465 GLY B 1316
REMARK 465 GLY B 1317
REMARK 465 GLY B 1318
REMARK 465 SER B 1319
REMARK 465 SER B 1320
REMARK 465 GLY B 1321
REMARK 465 SER B 1322
REMARK 465 ASN B 1592
REMARK 465 GLY B 1593
REMARK 465 SER B 1594
REMARK 465 ARG B 1595
REMARK 465 ASN B 1596
REMARK 465 ALA B 1639
REMARK 465 SER B 1640
REMARK 465 THR B 1641
REMARK 465 SER B 1642
REMARK 465 ARG B 1643
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 GLU B1294 CG CD OE1 OE2
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 NH1 ARG A 1194 O ASN B 1576 2.14
REMARK 500 NH2 ARG B 1566 O GLU B 1570 2.16
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 PRO A1252 175.08 -55.97
REMARK 500 MET A1373 -66.90 -106.57
REMARK 500 ASN A1394 28.60 49.39
REMARK 500 ARG A1556 50.37 -95.03
REMARK 500 ALA A1572 175.64 -58.18
REMARK 500 ASN A1584 -57.23 74.27
REMARK 500 THR A1624 -38.28 -37.56
REMARK 500 ASN B1182 74.57 -116.84
REMARK 500 PRO B1252 173.84 -57.36
REMARK 500 ASP B1258 -175.23 -68.68
REMARK 500 MET B1373 -67.10 -106.24
REMARK 500 ASN B1394 28.44 49.80
REMARK 500 ARG B1556 49.41 -93.84
REMARK 500 ASN B1584 -124.78 62.20
REMARK 500 LEU B1613 4.78 87.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A1701 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A1390 NE2
REMARK 620 2 GLU A1392 OE2 108.2
REMARK 620 3 HIS A1470 NE2 104.6 85.4
REMARK 620 4 OGA A1700 O2 162.4 82.4 90.1
REMARK 620 5 OGA A1700 O2' 87.0 158.8 105.6 79.6
REMARK 620 6 HOH A1827 O 88.3 88.4 166.9 77.6 77.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1575 SG
REMARK 620 2 CYS A1578 SG 112.2
REMARK 620 3 CYS A1602 SG 124.2 107.3
REMARK 620 4 CYS A1605 SG 97.8 111.7 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B1701 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B1390 NE2
REMARK 620 2 GLU B1392 OE2 107.3
REMARK 620 3 HIS B1470 NE2 104.3 80.5
REMARK 620 4 OGA B1700 O2 156.0 82.2 98.9
REMARK 620 5 OGA B1700 O2' 85.2 160.7 111.3 80.9
REMARK 620 6 HOH B1832 O 80.1 94.9 174.4 77.2 72.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1575 SG
REMARK 620 2 CYS B1578 SG 110.6
REMARK 620 3 CYS B1602 SG 122.1 106.4
REMARK 620 4 CYS B1605 SG 99.4 114.9 103.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OGA A 1700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OGA B 1700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ASK RELATED DB: PDB
REMARK 900 KDM6B STRUCTURE BOUND WITH A HIGHLY SPECIFIC INHIBITOR
REMARK 900 RELATED ID: 4EZ4 RELATED DB: PDB
REMARK 900 RELATED ID: 4EZH RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 REPLACEMENT OF THE ORIGINAL LOOP SEQUENCE OF
REMARK 999 ESEDEESEEPDSTTGTSPSSAPDPKN(RESIDUES 1296-1322) WITH RESIDUES OF
REMARK 999 LEVLFQGPTKAARKSAPATGGGSSGS.
DBREF 4EYU A 1157 1295 UNP Q5NCY0 KDM6B_MOUSE 1155 1293
DBREF 4EYU A 1323 1643 UNP Q5NCY0 KDM6B_MOUSE 1321 1641
DBREF 4EYU B 1157 1295 UNP Q5NCY0 KDM6B_MOUSE 1155 1293
DBREF 4EYU B 1323 1643 UNP Q5NCY0 KDM6B_MOUSE 1321 1641
SEQADV 4EYU LEU A 1296 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLU A 1297 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU VAL A 1298 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU LEU A 1299 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU PHE A 1300 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLN A 1301 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY A 1303 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU PRO A 1304 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU THR A 1305 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU LYS A 1306 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ALA A 1307 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ALA A 1308 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ARG A 1309 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU LYS A 1310 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU SER A 1311 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ALA A 1312 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU PRO A 1313 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ALA A 1314 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU THR A 1315 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY A 1316 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY A 1317 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY A 1318 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU SER A 1319 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU SER A 1320 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY A 1321 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU SER A 1322 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU LEU B 1296 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLU B 1297 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU VAL B 1298 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU LEU B 1299 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU PHE B 1300 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLN B 1302 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY B 1303 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU PRO B 1304 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU THR B 1305 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU LYS B 1306 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ALA B 1307 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ALA B 1308 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ARG B 1309 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU LYS B 1310 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU SER B 1311 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ALA B 1312 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU PRO B 1313 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU ALA B 1314 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU THR B 1315 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY B 1316 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY B 1317 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY B 1318 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU SER B 1319 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU SER B 1320 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU GLY B 1321 UNP Q5NCY0 SEE REMARK 999
SEQADV 4EYU SER B 1322 UNP Q5NCY0 SEE REMARK 999
SEQRES 1 A 486 GLU SER TYR LEU SER PRO ALA GLN SER VAL LYS PRO LYS
SEQRES 2 A 486 ILE ASN THR GLU GLU LYS LEU PRO ARG GLU LYS LEU ASN
SEQRES 3 A 486 PRO PRO THR PRO SER ILE TYR LEU GLU SER LYS ARG ASP
SEQRES 4 A 486 ALA PHE SER PRO VAL LEU LEU GLN PHE CYS THR ASP PRO
SEQRES 5 A 486 ARG ASN PRO ILE THR VAL ILE ARG GLY LEU ALA GLY SER
SEQRES 6 A 486 LEU ARG LEU ASN LEU GLY LEU PHE SER THR LYS THR LEU
SEQRES 7 A 486 VAL GLU ALA SER GLY GLU HIS THR VAL GLU VAL ARG THR
SEQRES 8 A 486 GLN VAL GLN GLN PRO SER ASP GLU ASN TRP ASP LEU THR
SEQRES 9 A 486 GLY THR ARG GLN ILE TRP PRO CYS GLU SER SER ARG SER
SEQRES 10 A 486 HIS THR THR ILE ALA LYS TYR ALA GLN TYR GLN ALA SER
SEQRES 11 A 486 SER PHE GLN GLU SER LEU GLN GLU GLU LEU GLU VAL LEU
SEQRES 12 A 486 PHE GLN GLY PRO THR LYS ALA ALA ARG LYS SER ALA PRO
SEQRES 13 A 486 ALA THR GLY GLY GLY SER SER GLY SER HIS HIS ILE ILE
SEQRES 14 A 486 LYS PHE GLY THR ASN ILE ASP LEU SER ASP ALA LYS ARG
SEQRES 15 A 486 TRP LYS PRO GLN LEU GLN GLU LEU LEU LYS LEU PRO ALA
SEQRES 16 A 486 PHE MET ARG VAL THR SER THR GLY ASN MET LEU SER HIS
SEQRES 17 A 486 VAL GLY HIS THR ILE LEU GLY MET ASN THR VAL GLN LEU
SEQRES 18 A 486 TYR MET LYS VAL PRO GLY SER ARG THR PRO GLY HIS GLN
SEQRES 19 A 486 GLU ASN ASN ASN PHE CYS SER VAL ASN ILE ASN ILE GLY
SEQRES 20 A 486 PRO GLY ASP CYS GLU TRP PHE ALA VAL HIS GLU HIS TYR
SEQRES 21 A 486 TRP GLU THR ILE SER ALA PHE CYS ASP ARG HIS GLY VAL
SEQRES 22 A 486 ASP TYR LEU THR GLY SER TRP TRP PRO ILE LEU ASP ASP
SEQRES 23 A 486 LEU TYR ALA SER ASN ILE PRO VAL TYR ARG PHE VAL GLN
SEQRES 24 A 486 ARG PRO GLY ASP LEU VAL TRP ILE ASN ALA GLY THR VAL
SEQRES 25 A 486 HIS TRP VAL GLN ALA THR GLY TRP CYS ASN ASN ILE ALA
SEQRES 26 A 486 TRP ASN VAL GLY PRO LEU THR ALA TYR GLN TYR GLN LEU
SEQRES 27 A 486 ALA LEU GLU ARG TYR GLU TRP ASN GLU VAL LYS ASN VAL
SEQRES 28 A 486 LYS SER ILE VAL PRO MET ILE HIS VAL SER TRP ASN VAL
SEQRES 29 A 486 ALA ARG THR VAL LYS ILE SER ASP PRO ASP LEU PHE LYS
SEQRES 30 A 486 MET ILE LYS PHE CYS LEU LEU GLN SER MET LYS HIS CYS
SEQRES 31 A 486 GLN VAL GLN ARG GLU SER LEU VAL ARG ALA GLY LYS LYS
SEQRES 32 A 486 ILE ALA TYR GLN GLY ARG VAL LYS ASP GLU PRO ALA TYR
SEQRES 33 A 486 TYR CYS ASN GLU CYS ASP VAL GLU VAL PHE ASN ILE LEU
SEQRES 34 A 486 PHE VAL THR SER GLU ASN GLY SER ARG ASN THR TYR LEU
SEQRES 35 A 486 VAL HIS CYS GLU GLY CYS ALA ARG ARG ARG SER ALA GLY
SEQRES 36 A 486 LEU GLN GLY VAL VAL VAL LEU GLU GLN TYR ARG THR GLU
SEQRES 37 A 486 GLU LEU ALA GLN ALA TYR ASP ALA PHE THR LEU ALA PRO
SEQRES 38 A 486 ALA SER THR SER ARG
SEQRES 1 B 486 GLU SER TYR LEU SER PRO ALA GLN SER VAL LYS PRO LYS
SEQRES 2 B 486 ILE ASN THR GLU GLU LYS LEU PRO ARG GLU LYS LEU ASN
SEQRES 3 B 486 PRO PRO THR PRO SER ILE TYR LEU GLU SER LYS ARG ASP
SEQRES 4 B 486 ALA PHE SER PRO VAL LEU LEU GLN PHE CYS THR ASP PRO
SEQRES 5 B 486 ARG ASN PRO ILE THR VAL ILE ARG GLY LEU ALA GLY SER
SEQRES 6 B 486 LEU ARG LEU ASN LEU GLY LEU PHE SER THR LYS THR LEU
SEQRES 7 B 486 VAL GLU ALA SER GLY GLU HIS THR VAL GLU VAL ARG THR
SEQRES 8 B 486 GLN VAL GLN GLN PRO SER ASP GLU ASN TRP ASP LEU THR
SEQRES 9 B 486 GLY THR ARG GLN ILE TRP PRO CYS GLU SER SER ARG SER
SEQRES 10 B 486 HIS THR THR ILE ALA LYS TYR ALA GLN TYR GLN ALA SER
SEQRES 11 B 486 SER PHE GLN GLU SER LEU GLN GLU GLU LEU GLU VAL LEU
SEQRES 12 B 486 PHE GLN GLY PRO THR LYS ALA ALA ARG LYS SER ALA PRO
SEQRES 13 B 486 ALA THR GLY GLY GLY SER SER GLY SER HIS HIS ILE ILE
SEQRES 14 B 486 LYS PHE GLY THR ASN ILE ASP LEU SER ASP ALA LYS ARG
SEQRES 15 B 486 TRP LYS PRO GLN LEU GLN GLU LEU LEU LYS LEU PRO ALA
SEQRES 16 B 486 PHE MET ARG VAL THR SER THR GLY ASN MET LEU SER HIS
SEQRES 17 B 486 VAL GLY HIS THR ILE LEU GLY MET ASN THR VAL GLN LEU
SEQRES 18 B 486 TYR MET LYS VAL PRO GLY SER ARG THR PRO GLY HIS GLN
SEQRES 19 B 486 GLU ASN ASN ASN PHE CYS SER VAL ASN ILE ASN ILE GLY
SEQRES 20 B 486 PRO GLY ASP CYS GLU TRP PHE ALA VAL HIS GLU HIS TYR
SEQRES 21 B 486 TRP GLU THR ILE SER ALA PHE CYS ASP ARG HIS GLY VAL
SEQRES 22 B 486 ASP TYR LEU THR GLY SER TRP TRP PRO ILE LEU ASP ASP
SEQRES 23 B 486 LEU TYR ALA SER ASN ILE PRO VAL TYR ARG PHE VAL GLN
SEQRES 24 B 486 ARG PRO GLY ASP LEU VAL TRP ILE ASN ALA GLY THR VAL
SEQRES 25 B 486 HIS TRP VAL GLN ALA THR GLY TRP CYS ASN ASN ILE ALA
SEQRES 26 B 486 TRP ASN VAL GLY PRO LEU THR ALA TYR GLN TYR GLN LEU
SEQRES 27 B 486 ALA LEU GLU ARG TYR GLU TRP ASN GLU VAL LYS ASN VAL
SEQRES 28 B 486 LYS SER ILE VAL PRO MET ILE HIS VAL SER TRP ASN VAL
SEQRES 29 B 486 ALA ARG THR VAL LYS ILE SER ASP PRO ASP LEU PHE LYS
SEQRES 30 B 486 MET ILE LYS PHE CYS LEU LEU GLN SER MET LYS HIS CYS
SEQRES 31 B 486 GLN VAL GLN ARG GLU SER LEU VAL ARG ALA GLY LYS LYS
SEQRES 32 B 486 ILE ALA TYR GLN GLY ARG VAL LYS ASP GLU PRO ALA TYR
SEQRES 33 B 486 TYR CYS ASN GLU CYS ASP VAL GLU VAL PHE ASN ILE LEU
SEQRES 34 B 486 PHE VAL THR SER GLU ASN GLY SER ARG ASN THR TYR LEU
SEQRES 35 B 486 VAL HIS CYS GLU GLY CYS ALA ARG ARG ARG SER ALA GLY
SEQRES 36 B 486 LEU GLN GLY VAL VAL VAL LEU GLU GLN TYR ARG THR GLU
SEQRES 37 B 486 GLU LEU ALA GLN ALA TYR ASP ALA PHE THR LEU ALA PRO
SEQRES 38 B 486 ALA SER THR SER ARG
HET OGA A1700 10
HET NI A1701 1
HET ZN A1702 1
HET OGA B1700 10
HET NI B1701 1
HET ZN B1702 1
HETNAM OGA N-OXALYLGLYCINE
HETNAM NI NICKEL (II) ION
HETNAM ZN ZINC ION
FORMUL 3 OGA 2(C4 H5 N O5)
FORMUL 4 NI 2(NI 2+)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 9 HOH *178(H2 O)
HELIX 1 1 SER A 1161 SER A 1165 5 5
HELIX 2 2 PRO A 1177 ASN A 1182 1 6
HELIX 3 3 SER A 1192 PHE A 1197 5 6
HELIX 4 4 SER A 1198 THR A 1206 1 9
HELIX 5 5 GLY A 1217 ARG A 1223 1 7
HELIX 6 6 ASN A 1225 PHE A 1229 5 5
HELIX 7 7 SER A 1230 SER A 1238 1 9
HELIX 8 8 ILE A 1277 GLN A 1301 1 25
HELIX 9 9 TRP A 1340 LEU A 1347 1 8
HELIX 10 10 LEU A 1348 LEU A 1350 5 3
HELIX 11 11 PRO A 1351 ARG A 1355 5 5
HELIX 12 12 ASN A 1361 VAL A 1366 5 6
HELIX 13 13 GLU A 1392 PHE A 1396 5 5
HELIX 14 14 HIS A 1414 HIS A 1416 5 3
HELIX 15 15 TYR A 1417 HIS A 1428 1 12
HELIX 16 16 ILE A 1440 SER A 1447 1 8
HELIX 17 17 THR A 1489 LYS A 1506 1 18
HELIX 18 18 PRO A 1513 VAL A 1525 1 13
HELIX 19 19 ASP A 1529 ARG A 1556 1 28
HELIX 20 20 CYS A 1602 SER A 1610 1 9
HELIX 21 21 ARG A 1623 PHE A 1634 1 12
HELIX 22 22 SER B 1161 SER B 1165 5 5
HELIX 23 23 PRO B 1177 ASN B 1182 1 6
HELIX 24 24 SER B 1192 PHE B 1197 5 6
HELIX 25 25 SER B 1198 THR B 1206 1 9
HELIX 26 26 GLY B 1217 LEU B 1222 1 6
HELIX 27 27 ASN B 1225 PHE B 1229 5 5
HELIX 28 28 SER B 1230 SER B 1238 1 9
HELIX 29 29 ILE B 1277 PHE B 1300 1 24
HELIX 30 30 TRP B 1340 LEU B 1347 1 8
HELIX 31 31 LEU B 1348 LEU B 1350 5 3
HELIX 32 32 PRO B 1351 ARG B 1355 5 5
HELIX 33 33 ASN B 1361 VAL B 1366 5 6
HELIX 34 34 GLU B 1392 PHE B 1396 5 5
HELIX 35 35 HIS B 1414 HIS B 1416 5 3
HELIX 36 36 TYR B 1417 HIS B 1428 1 12
HELIX 37 37 ILE B 1440 SER B 1447 1 8
HELIX 38 38 THR B 1489 LYS B 1506 1 18
HELIX 39 39 PRO B 1513 VAL B 1525 1 13
HELIX 40 40 ASP B 1529 ARG B 1556 1 28
HELIX 41 41 CYS B 1602 SER B 1610 1 9
HELIX 42 42 ARG B 1623 PHE B 1634 1 12
SHEET 1 A 9 SER A1187 TYR A1189 0
SHEET 2 A 9 ILE A1212 ARG A1216 1 O ARG A1216 N ILE A1188
SHEET 3 A 9 LEU A1461 ILE A1464 -1 O LEU A1461 N ILE A1215
SHEET 4 A 9 CYS A1397 PRO A1405 -1 N ASN A1400 O VAL A1462
SHEET 5 A 9 CYS A1478 VAL A1485 -1 O ILE A1481 N ILE A1401
SHEET 6 A 9 GLN A1377 LYS A1381 -1 N TYR A1379 O ASN A1480
SHEET 7 A 9 ILE A1325 ASP A1333 -1 N GLY A1329 O MET A1380
SHEET 8 A 9 THR A1242 VAL A1249 -1 N GLU A1244 O THR A1330
SHEET 9 A 9 SER A1271 THR A1276 -1 O THR A1275 N VAL A1243
SHEET 1 B 4 ARG A1386 HIS A1390 0
SHEET 2 B 4 VAL A1469 ALA A1474 -1 O VAL A1472 N THR A1387
SHEET 3 B 4 CYS A1408 VAL A1413 -1 N GLU A1409 O GLN A1473
SHEET 4 B 4 TYR A1452 GLN A1456 -1 O GLN A1456 N CYS A1408
SHEET 1 C 4 ILE A1561 TYR A1563 0
SHEET 2 C 4 VAL A1617 GLU A1620 1 O GLU A1620 N ALA A1562
SHEET 3 C 4 ILE A1585 THR A1589 -1 N LEU A1586 O LEU A1619
SHEET 4 C 4 LEU A1599 HIS A1601 -1 O HIS A1601 N PHE A1587
SHEET 1 D 2 TYR A1573 TYR A1574 0
SHEET 2 D 2 GLU A1581 VAL A1582 -1 O VAL A1582 N TYR A1573
SHEET 1 E 9 SER B1187 TYR B1189 0
SHEET 2 E 9 ILE B1212 ARG B1216 1 O VAL B1214 N ILE B1188
SHEET 3 E 9 LEU B1461 ILE B1464 -1 O LEU B1461 N ILE B1215
SHEET 4 E 9 CYS B1397 ASN B1402 -1 N ASN B1400 O VAL B1462
SHEET 5 E 9 CYS B1478 VAL B1485 -1 O ILE B1481 N ILE B1401
SHEET 6 E 9 GLN B1377 LYS B1381 -1 N TYR B1379 O ASN B1480
SHEET 7 E 9 ILE B1325 ASP B1333 -1 N GLY B1329 O MET B1380
SHEET 8 E 9 THR B1242 VAL B1249 -1 N GLU B1244 O THR B1330
SHEET 9 E 9 SER B1271 THR B1276 -1 O SER B1271 N THR B1247
SHEET 1 F 4 ARG B1386 HIS B1390 0
SHEET 2 F 4 VAL B1469 ALA B1474 -1 O VAL B1472 N THR B1387
SHEET 3 F 4 CYS B1408 VAL B1413 -1 N GLU B1409 O GLN B1473
SHEET 4 F 4 TYR B1452 GLN B1456 -1 O GLN B1456 N CYS B1408
SHEET 1 G 4 ILE B1561 TYR B1563 0
SHEET 2 G 4 VAL B1617 GLU B1620 1 O GLU B1620 N ALA B1562
SHEET 3 G 4 LEU B1586 SER B1590 -1 N LEU B1586 O LEU B1619
SHEET 4 G 4 TYR B1598 HIS B1601 -1 O HIS B1601 N PHE B1587
SHEET 1 H 2 TYR B1573 TYR B1574 0
SHEET 2 H 2 GLU B1581 VAL B1582 -1 O VAL B1582 N TYR B1573
LINK NE2 HIS A1390 NI NI A1701 1555 1555 2.16
LINK OE2 GLU A1392 NI NI A1701 1555 1555 1.83
LINK NE2 HIS A1470 NI NI A1701 1555 1555 2.19
LINK SG CYS A1575 ZN ZN A1702 1555 1555 2.24
LINK SG CYS A1578 ZN ZN A1702 1555 1555 2.41
LINK SG CYS A1602 ZN ZN A1702 1555 1555 2.38
LINK SG CYS A1605 ZN ZN A1702 1555 1555 2.46
LINK O2 OGA A1700 NI NI A1701 1555 1555 2.07
LINK O2' OGA A1700 NI NI A1701 1555 1555 2.11
LINK NI NI A1701 O HOH A1827 1555 1555 2.14
LINK NE2 HIS B1390 NI NI B1701 1555 1555 2.18
LINK OE2 GLU B1392 NI NI B1701 1555 1555 1.85
LINK NE2 HIS B1470 NI NI B1701 1555 1555 2.30
LINK SG CYS B1575 ZN ZN B1702 1555 1555 2.28
LINK SG CYS B1578 ZN ZN B1702 1555 1555 2.41
LINK SG CYS B1602 ZN ZN B1702 1555 1555 2.40
LINK SG CYS B1605 ZN ZN B1702 1555 1555 2.38
LINK O2 OGA B1700 NI NI B1701 1555 1555 1.98
LINK O2' OGA B1700 NI NI B1701 1555 1555 2.17
LINK NI NI B1701 O HOH B1832 1555 1555 2.26
CISPEP 1 GLY A 1404 PRO A 1405 0 0.76
CISPEP 2 GLY B 1404 PRO B 1405 0 -2.50
SITE 1 AC1 10 LYS A1381 THR A1387 HIS A1390 GLU A1392
SITE 2 AC1 10 SER A1398 ASN A1400 HIS A1470 NI A1701
SITE 3 AC1 10 HOH A1801 HOH A1827
SITE 1 AC2 5 HIS A1390 GLU A1392 HIS A1470 OGA A1700
SITE 2 AC2 5 HOH A1827
SITE 1 AC3 4 CYS A1575 CYS A1578 CYS A1602 CYS A1605
SITE 1 AC4 10 LYS B1381 THR B1387 HIS B1390 GLU B1392
SITE 2 AC4 10 SER B1398 ASN B1400 HIS B1470 NI B1701
SITE 3 AC4 10 HOH B1807 HOH B1832
SITE 1 AC5 5 HIS B1390 GLU B1392 HIS B1470 OGA B1700
SITE 2 AC5 5 HOH B1832
SITE 1 AC6 4 CYS B1575 CYS B1578 CYS B1602 CYS B1605
CRYST1 82.977 102.284 145.302 90.00 90.00 90.00 P 21 21 21 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 0.012052 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009777 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006882 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
