HEADER OXIDOREDUCTASE 15-JUN-16 5LBB
TITLE HIF PROLYL HYDROXYLASE 2 (PHD2/EGLN1) R396T VARIANT IN COMPLEX WITH
TITLE 2 MN(II) AND N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE
TITLE 3 (IOX3/UN9)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EGL NINE HOMOLOG 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 181-426;
COMPND 5 SYNONYM: HYPOXIA-INDUCIBLE FACTOR PROLYL HYDROXYLASE 2,HPH-2,PROLYL
COMPND 6 HYDROXYLASE DOMAIN-CONTAINING PROTEIN 2,PHD2,SM-20;
COMPND 7 EC: 1.14.11.29;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: EGLN1, C1ORF12, PNAS-118, PNAS-137;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS OXIDOREDUCTASE, NON-HEME DIOXYGENASE, IRON, 2-OXOGLUTARATE, HYPOXIA-
KEYWDS 2 INDUCIBLE FACTOR, HIF, HIF PROLYL HYDROXYLASE DOMAIN 2, PHD2, EGLN1,
KEYWDS 3 OXYGENASE, HYPOXIA, DNA-BINDING, METAL-BINDING, TRANSCRIPTION,
KEYWDS 4 HELIX-LOOP-HELIX-BETA, DSBH, FACIAL TRIAD, CYTOPLASM,
KEYWDS 5 TRANSCRIPTION/EPIGENETIC REGULATION, SIGNALING, DEVELOPMENT, CELL
KEYWDS 6 STRUCTURE, BETA-HYDROXYLATION, TRANSCRIPTION ACTIVATOR/INHIBITOR,
KEYWDS 7 UBL CONJUGATION, POLYMORPHISM, VITAMIN C, ZINC-FINGER, FAMILIAL
KEYWDS 8 ERYTHROCYTOSIS, BREAST CANCER, TRANSCRIPTION COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CHOWDHURY,C.J.SCHOFIELD
REVDAT 3 10-JAN-24 5LBB 1 LINK
REVDAT 2 07-SEP-16 5LBB 1 JRNL
REVDAT 1 31-AUG-16 5LBB 0
JRNL AUTH R.CHOWDHURY,I.K.LEUNG,Y.M.TIAN,M.I.ABBOUD,W.GE,C.DOMENE,
JRNL AUTH 2 F.X.CANTRELLE,I.LANDRIEU,A.P.HARDY,C.W.PUGH,P.J.RATCLIFFE,
JRNL AUTH 3 T.D.CLARIDGE,C.J.SCHOFIELD
JRNL TITL STRUCTURAL BASIS FOR OXYGEN DEGRADATION DOMAIN SELECTIVITY
JRNL TITL 2 OF THE HIF PROLYL HYDROXYLASES.
JRNL REF NAT COMMUN V. 7 12673 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27561929
JRNL DOI 10.1038/NCOMMS12673
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.CHOWDHURY,J.I.CANDELA-LENA,M.C.CHAN,D.J.GREENALD,K.K.YEOH,
REMARK 1 AUTH 2 Y.M.TIAN,M.A.MCDONOUGH,A.TUMBER,N.R.ROSE,A.CONEJO-GARCIA,
REMARK 1 AUTH 3 M.DEMETRIADES,S.MATHAVAN,A.KAWAMURA,M.K.LEE,F.VAN EEDEN,
REMARK 1 AUTH 4 C.W.PUGH,P.J.RATCLIFFE,C.J.SCHOFIELD
REMARK 1 TITL SELECTIVE SMALL MOLECULE PROBES FOR THE HYPOXIA INDUCIBLE
REMARK 1 TITL 2 FACTOR (HIF) PROLYL HYDROXYLASES.
REMARK 1 REF ACS CHEM. BIOL. V. 8 1488 2013
REMARK 1 REFN ESSN 1554-8937
REMARK 1 PMID 23683440
REMARK 1 DOI 10.1021/CB400088Q
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.CHOWDHURY,M.A.MCDONOUGH,J.MECINOVIC,C.LOENARZ,E.FLASHMAN,
REMARK 1 AUTH 2 K.S.HEWITSON,C.DOMENE,C.J.SCHOFIELD
REMARK 1 TITL STRUCTURAL BASIS FOR BINDING OF HYPOXIA-INDUCIBLE FACTOR TO
REMARK 1 TITL 2 THE OXYGEN-SENSING PROLYL HYDROXYLASES.
REMARK 1 REF STRUCTURE V. 17 981 2009
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 19604478
REMARK 1 DOI 10.1016/J.STR.2009.06.002
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 29896
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1500
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 36.0792 - 3.7795 0.96 2645 130 0.1406 0.1475
REMARK 3 2 3.7795 - 3.0004 0.95 2524 140 0.1430 0.1748
REMARK 3 3 3.0004 - 2.6213 0.96 2553 142 0.1582 0.1942
REMARK 3 4 2.6213 - 2.3816 0.98 2594 144 0.1549 0.1918
REMARK 3 5 2.3816 - 2.2110 0.98 2588 135 0.1449 0.1649
REMARK 3 6 2.2110 - 2.0806 0.98 2588 132 0.1531 0.1911
REMARK 3 7 2.0806 - 1.9764 0.99 2620 123 0.1634 0.2304
REMARK 3 8 1.9764 - 1.8904 0.99 2572 146 0.1827 0.2030
REMARK 3 9 1.8904 - 1.8176 0.98 2583 153 0.1926 0.2300
REMARK 3 10 1.8176 - 1.7549 0.98 2577 125 0.2109 0.2379
REMARK 3 11 1.7549 - 1.7000 0.97 2552 130 0.2369 0.2565
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.43
REMARK 3 B_SOL : 59.40
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.84000
REMARK 3 B22 (A**2) : -1.84000
REMARK 3 B33 (A**2) : 3.68000
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 : 0.017 1857
REMARK 3 ANGLE : 1.451 2522
REMARK 3 CHIRALITY : 0.079 268
REMARK 3 PLANARITY : 0.011 334
REMARK 3 DIHEDRAL : 16.465 1100
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 188:204)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3028 -33.6530 -1.6134
REMARK 3 T TENSOR
REMARK 3 T11: 0.2681 T22: 0.5001
REMARK 3 T33: 0.4006 T12: -0.0119
REMARK 3 T13: 0.1046 T23: 0.1241
REMARK 3 L TENSOR
REMARK 3 L11: 0.2265 L22: 2.5325
REMARK 3 L33: 0.2381 L12: 0.2899
REMARK 3 L13: 0.1622 L23: 0.6264
REMARK 3 S TENSOR
REMARK 3 S11: 0.1796 S12: 0.3318 S13: 0.3427
REMARK 3 S21: 0.2657 S22: 0.3869 S23: -0.2988
REMARK 3 S31: -0.2866 S32: -0.8035 S33: 0.2095
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 205:215)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7357 -32.4281 0.1593
REMARK 3 T TENSOR
REMARK 3 T11: 0.3796 T22: 0.2852
REMARK 3 T33: 0.3368 T12: -0.1308
REMARK 3 T13: 0.0374 T23: 0.0918
REMARK 3 L TENSOR
REMARK 3 L11: 0.8587 L22: 0.7919
REMARK 3 L33: 0.5437 L12: -0.4617
REMARK 3 L13: -0.3692 L23: 0.4589
REMARK 3 S TENSOR
REMARK 3 S11: -0.2629 S12: 0.1413 S13: 0.4880
REMARK 3 S21: -0.1305 S22: 0.2429 S23: -0.4648
REMARK 3 S31: -0.2076 S32: 0.5514 S33: 0.1536
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 216:232)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2286 -34.3085 -11.3347
REMARK 3 T TENSOR
REMARK 3 T11: 0.4544 T22: 0.4230
REMARK 3 T33: 0.3835 T12: 0.0497
REMARK 3 T13: -0.0370 T23: 0.1561
REMARK 3 L TENSOR
REMARK 3 L11: 0.4037 L22: 0.9788
REMARK 3 L33: 0.7512 L12: -0.4292
REMARK 3 L13: -0.1105 L23: 0.5677
REMARK 3 S TENSOR
REMARK 3 S11: -0.2610 S12: 0.0581 S13: 0.3249
REMARK 3 S21: -0.6973 S22: -0.1686 S23: 0.4423
REMARK 3 S31: -0.2313 S32: 0.0423 S33: -0.2200
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 233:266)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3438 -47.7321 -1.8283
REMARK 3 T TENSOR
REMARK 3 T11: 0.3315 T22: 0.3890
REMARK 3 T33: 0.3814 T12: -0.0203
REMARK 3 T13: 0.0482 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 1.3827 L22: 1.0499
REMARK 3 L33: 0.8597 L12: 0.2357
REMARK 3 L13: 1.1574 L23: 0.3511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: 0.2886 S13: -0.1486
REMARK 3 S21: 0.0508 S22: -0.1812 S23: 0.4567
REMARK 3 S31: 0.0857 S32: -0.6425 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 267:283)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2564 -39.8682 -11.4050
REMARK 3 T TENSOR
REMARK 3 T11: 0.3953 T22: 0.5145
REMARK 3 T33: 0.3458 T12: -0.0219
REMARK 3 T13: 0.0737 T23: 0.1091
REMARK 3 L TENSOR
REMARK 3 L11: 0.0650 L22: 1.0127
REMARK 3 L33: 0.3046 L12: -0.0757
REMARK 3 L13: -0.0003 L23: 0.5278
REMARK 3 S TENSOR
REMARK 3 S11: 0.0098 S12: 0.5262 S13: 0.1300
REMARK 3 S21: -0.2758 S22: -0.0412 S23: -0.5615
REMARK 3 S31: -0.4709 S32: 0.0857 S33: 0.0229
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 284:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9638 -47.1395 -2.1559
REMARK 3 T TENSOR
REMARK 3 T11: 0.4527 T22: 0.4481
REMARK 3 T33: 0.4953 T12: 0.0272
REMARK 3 T13: 0.0236 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 0.1168 L22: 0.1985
REMARK 3 L33: 0.0917 L12: -0.0800
REMARK 3 L13: -0.1114 L23: 0.1348
REMARK 3 S TENSOR
REMARK 3 S11: 0.1797 S12: 0.1777 S13: 0.0975
REMARK 3 S21: 0.5843 S22: 0.1264 S23: -0.7335
REMARK 3 S31: 0.1542 S32: 0.4437 S33: 0.0005
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 294:306)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8890 -43.8259 -2.3495
REMARK 3 T TENSOR
REMARK 3 T11: 0.2640 T22: 0.2930
REMARK 3 T33: 0.3132 T12: 0.0159
REMARK 3 T13: 0.0541 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.3687 L22: 0.3543
REMARK 3 L33: 0.5482 L12: 0.2798
REMARK 3 L13: 0.4972 L23: 0.4685
REMARK 3 S TENSOR
REMARK 3 S11: -0.0831 S12: 0.1000 S13: 0.0223
REMARK 3 S21: -0.0447 S22: -0.0104 S23: 0.1247
REMARK 3 S31: -0.0060 S32: -0.0874 S33: -0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 307:320)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1379 -48.5858 9.4605
REMARK 3 T TENSOR
REMARK 3 T11: 0.2885 T22: 0.2819
REMARK 3 T33: 0.2998 T12: 0.0308
REMARK 3 T13: 0.0897 T23: 0.0784
REMARK 3 L TENSOR
REMARK 3 L11: 0.6011 L22: 0.6148
REMARK 3 L33: 0.7489 L12: 0.2480
REMARK 3 L13: -0.1886 L23: 0.0730
REMARK 3 S TENSOR
REMARK 3 S11: -0.2214 S12: -0.2458 S13: -0.7736
REMARK 3 S21: 0.1937 S22: -0.0324 S23: 0.2904
REMARK 3 S31: 0.2762 S32: 0.0416 S33: -0.0050
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 321:335)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4341 -36.8447 -0.0645
REMARK 3 T TENSOR
REMARK 3 T11: 0.2900 T22: 0.2224
REMARK 3 T33: 0.2674 T12: 0.0145
REMARK 3 T13: 0.0575 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 0.9013 L22: 0.7051
REMARK 3 L33: 0.9845 L12: 0.8737
REMARK 3 L13: 0.2045 L23: 0.0113
REMARK 3 S TENSOR
REMARK 3 S11: -0.1747 S12: 0.0209 S13: 0.3022
REMARK 3 S21: 0.1501 S22: 0.0863 S23: -0.2169
REMARK 3 S31: -0.2084 S32: 0.0864 S33: -0.0003
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 336:350)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6174 -36.1967 12.7345
REMARK 3 T TENSOR
REMARK 3 T11: 0.3504 T22: 0.3291
REMARK 3 T33: 0.2843 T12: 0.0578
REMARK 3 T13: 0.0075 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 0.2215 L22: 0.6399
REMARK 3 L33: 0.4262 L12: 0.3420
REMARK 3 L13: 0.0502 L23: 0.4054
REMARK 3 S TENSOR
REMARK 3 S11: -0.1968 S12: -0.4991 S13: 0.3247
REMARK 3 S21: 0.5637 S22: 0.1706 S23: -0.3065
REMARK 3 S31: -0.3052 S32: -0.0073 S33: 0.0045
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 351:361)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8355 -32.1422 8.0304
REMARK 3 T TENSOR
REMARK 3 T11: 0.3863 T22: 0.3283
REMARK 3 T33: 0.3256 T12: -0.0348
REMARK 3 T13: -0.0013 T23: 0.0496
REMARK 3 L TENSOR
REMARK 3 L11: 0.5024 L22: 0.4548
REMARK 3 L33: 0.2366 L12: 0.0250
REMARK 3 L13: -0.2144 L23: 0.2915
REMARK 3 S TENSOR
REMARK 3 S11: -0.1308 S12: -0.1212 S13: 0.5090
REMARK 3 S21: 0.3752 S22: -0.3359 S23: -0.1119
REMARK 3 S31: -0.8951 S32: 0.4994 S33: 0.0007
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 362:371)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7861 -43.0095 5.9328
REMARK 3 T TENSOR
REMARK 3 T11: 0.2783 T22: 0.2788
REMARK 3 T33: 0.2940 T12: 0.0064
REMARK 3 T13: 0.0313 T23: 0.0525
REMARK 3 L TENSOR
REMARK 3 L11: 0.2000 L22: 0.1343
REMARK 3 L33: -0.0186 L12: 0.0047
REMARK 3 L13: 0.0970 L23: 0.0300
REMARK 3 S TENSOR
REMARK 3 S11: 0.0578 S12: 0.0348 S13: -0.0484
REMARK 3 S21: -0.1018 S22: -0.0261 S23: -0.2217
REMARK 3 S31: -0.0299 S32: 0.3359 S33: 0.0001
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN A AND RESID 372:381)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5386 -39.0326 10.4679
REMARK 3 T TENSOR
REMARK 3 T11: 0.2909 T22: 0.3216
REMARK 3 T33: 0.2913 T12: 0.0531
REMARK 3 T13: 0.0828 T23: -0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 0.6999 L22: 0.8262
REMARK 3 L33: 0.2330 L12: 0.4395
REMARK 3 L13: -0.1165 L23: 0.2693
REMARK 3 S TENSOR
REMARK 3 S11: -0.0257 S12: -0.7985 S13: 0.3905
REMARK 3 S21: 0.2820 S22: -0.0551 S23: -0.0438
REMARK 3 S31: -0.0355 S32: -0.1273 S33: 0.0291
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN A AND RESID 382:392)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1558 -43.3870 -2.1691
REMARK 3 T TENSOR
REMARK 3 T11: 0.2461 T22: 0.2332
REMARK 3 T33: 0.2635 T12: 0.0165
REMARK 3 T13: 0.0613 T23: 0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 0.4818 L22: 0.8855
REMARK 3 L33: 0.2998 L12: 0.6837
REMARK 3 L13: 0.2162 L23: 0.5233
REMARK 3 S TENSOR
REMARK 3 S11: 0.1251 S12: 0.1456 S13: 0.1250
REMARK 3 S21: -0.1807 S22: -0.0993 S23: -0.1665
REMARK 3 S31: -0.1194 S32: -0.0079 S33: -0.0001
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN A AND RESID 393:405)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3678 -61.9708 -0.7727
REMARK 3 T TENSOR
REMARK 3 T11: 0.3470 T22: 0.3359
REMARK 3 T33: 0.4547 T12: 0.0265
REMARK 3 T13: 0.0127 T23: -0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 0.1964 L22: 0.2027
REMARK 3 L33: 0.2600 L12: -0.0843
REMARK 3 L13: -0.0188 L23: -0.0700
REMARK 3 S TENSOR
REMARK 3 S11: -0.0393 S12: 0.0093 S13: 0.1344
REMARK 3 S21: 0.0152 S22: 0.1809 S23: 0.5518
REMARK 3 S31: 0.5274 S32: -0.0277 S33: -0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN A AND RESID 411:417)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3574 -74.3541 -9.2705
REMARK 3 T TENSOR
REMARK 3 T11: 0.7164 T22: 0.5835
REMARK 3 T33: 0.5130 T12: -0.0243
REMARK 3 T13: -0.2097 T23: 0.2091
REMARK 3 L TENSOR
REMARK 3 L11: 1.6444 L22: 0.7206
REMARK 3 L33: 0.3576 L12: 1.0840
REMARK 3 L13: 0.7630 L23: 0.4989
REMARK 3 S TENSOR
REMARK 3 S11: -0.1028 S12: -0.7239 S13: 0.5677
REMARK 3 S21: -0.2761 S22: -0.1495 S23: 0.6579
REMARK 3 S31: 0.3516 S32: -0.8575 S33: 0.0334
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 5LBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29903
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 36.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.70100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4BQX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 2.1 M AMMONIUM
REMARK 280 SULPHATE, 2% V/V DIOXANE, 0.002 M MNCL2, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.85850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.85850
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.85850
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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 BIOMT1 2 -0.500000 -0.866025 0.000000 -55.09950
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -95.43513
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 55.09950
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -95.43513
REMARK 350 BIOMT3 3 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 175
REMARK 465 SER A 176
REMARK 465 HIS A 177
REMARK 465 MET A 178
REMARK 465 ALA A 179
REMARK 465 SER A 180
REMARK 465 PRO A 181
REMARK 465 LYS A 186
REMARK 465 PRO A 187
REMARK 465 GLU A 407
REMARK 465 LYS A 408
REMARK 465 ASN A 415
REMARK 465 LYS A 416
REMARK 465 PRO A 417
REMARK 465 SER A 418
REMARK 465 ASP A 419
REMARK 465 SER A 420
REMARK 465 VAL A 421
REMARK 465 GLY A 422
REMARK 465 LYS A 423
REMARK 465 ASP A 424
REMARK 465 VAL A 425
REMARK 465 PHE A 426
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 ASN A 182 CG OD1 ND2
REMARK 470 THR A 185 OG1 CG2
REMARK 470 LYS A 216 CD CE NZ
REMARK 470 GLU A 217 CG CD OE1 OE2
REMARK 470 LYS A 234 CE NZ
REMARK 470 LYS A 244 CG CD CE NZ
REMARK 470 SER A 245 OG
REMARK 470 SER A 248 OG
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 LYS A 255 NZ
REMARK 470 LYS A 297 CE NZ
REMARK 470 LYS A 332 NZ
REMARK 470 LYS A 337 CG CD CE NZ
REMARK 470 LYS A 350 CD CE NZ
REMARK 470 LYS A 359 CE NZ
REMARK 470 LYS A 402 CD CE NZ
REMARK 470 TYR A 403 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 413 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 HH TYR A 290 HH22 ARG A 371 1.26
REMARK 500 HH22 ARG A 312 O HOH A 606 1.58
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 ALA A 190 5.23 -155.16
REMARK 500 TYR A 197 -55.76 -128.89
REMARK 500 PHE A 346 72.09 -119.08
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 MN A 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 313 NE2
REMARK 620 2 ASP A 315 OD1 91.3
REMARK 620 3 HIS A 374 NE2 87.6 88.2
REMARK 620 4 UN9 A 502 N8 87.6 116.9 154.5
REMARK 620 5 UN9 A 502 O13 100.3 165.6 83.8 72.5
REMARK 620 6 HOH A 641 O 169.9 84.1 101.2 86.5 85.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UN9 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HQR RELATED DB: PDB
REMARK 900 RELATED ID: 4BQX RELATED DB: PDB
REMARK 900 RELATED ID: 5L9B RELATED DB: PDB
REMARK 900 RELATED ID: 5L9V RELATED DB: PDB
REMARK 900 RELATED ID: 5L9R RELATED DB: PDB
REMARK 900 RELATED ID: 5LA9 RELATED DB: PDB
REMARK 900 RELATED ID: 5LAS RELATED DB: PDB
REMARK 900 RELATED ID: 5LAT RELATED DB: PDB
REMARK 900 RELATED ID: 5LB6 RELATED DB: PDB
DBREF 5LBB A 181 426 UNP Q9GZT9 EGLN1_HUMAN 181 426
SEQADV 5LBB GLY A 175 UNP Q9GZT9 EXPRESSION TAG
SEQADV 5LBB SER A 176 UNP Q9GZT9 EXPRESSION TAG
SEQADV 5LBB HIS A 177 UNP Q9GZT9 EXPRESSION TAG
SEQADV 5LBB MET A 178 UNP Q9GZT9 EXPRESSION TAG
SEQADV 5LBB ALA A 179 UNP Q9GZT9 EXPRESSION TAG
SEQADV 5LBB SER A 180 UNP Q9GZT9 EXPRESSION TAG
SEQADV 5LBB THR A 396 UNP Q9GZT9 ARG 396 ENGINEERED MUTATION
SEQRES 1 A 252 GLY SER HIS MET ALA SER PRO ASN GLY GLN THR LYS PRO
SEQRES 2 A 252 LEU PRO ALA LEU LYS LEU ALA LEU GLU TYR ILE VAL PRO
SEQRES 3 A 252 CYS MET ASN LYS HIS GLY ILE CYS VAL VAL ASP ASP PHE
SEQRES 4 A 252 LEU GLY LYS GLU THR GLY GLN GLN ILE GLY ASP GLU VAL
SEQRES 5 A 252 ARG ALA LEU HIS ASP THR GLY LYS PHE THR ASP GLY GLN
SEQRES 6 A 252 LEU VAL SER GLN LYS SER ASP SER SER LYS ASP ILE ARG
SEQRES 7 A 252 GLY ASP LYS ILE THR TRP ILE GLU GLY LYS GLU PRO GLY
SEQRES 8 A 252 CYS GLU THR ILE GLY LEU LEU MET SER SER MET ASP ASP
SEQRES 9 A 252 LEU ILE ARG HIS CYS ASN GLY LYS LEU GLY SER TYR LYS
SEQRES 10 A 252 ILE ASN GLY ARG THR LYS ALA MET VAL ALA CYS TYR PRO
SEQRES 11 A 252 GLY ASN GLY THR GLY TYR VAL ARG HIS VAL ASP ASN PRO
SEQRES 12 A 252 ASN GLY ASP GLY ARG CYS VAL THR CYS ILE TYR TYR LEU
SEQRES 13 A 252 ASN LYS ASP TRP ASP ALA LYS VAL SER GLY GLY ILE LEU
SEQRES 14 A 252 ARG ILE PHE PRO GLU GLY LYS ALA GLN PHE ALA ASP ILE
SEQRES 15 A 252 GLU PRO LYS PHE ASP ARG LEU LEU PHE PHE TRP SER ASP
SEQRES 16 A 252 ARG ARG ASN PRO HIS GLU VAL GLN PRO ALA TYR ALA THR
SEQRES 17 A 252 ARG TYR ALA ILE THR VAL TRP TYR PHE ASP ALA ASP GLU
SEQRES 18 A 252 THR ALA ARG ALA LYS VAL LYS TYR LEU THR GLY GLU LYS
SEQRES 19 A 252 GLY VAL ARG VAL GLU LEU ASN LYS PRO SER ASP SER VAL
SEQRES 20 A 252 GLY LYS ASP VAL PHE
HET MN A 501 1
HET UN9 A 502 27
HET BCT A 503 5
HETNAM MN MANGANESE (II) ION
HETNAM UN9 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE
HETNAM BCT BICARBONATE ION
FORMUL 2 MN MN 2+
FORMUL 3 UN9 C12 H9 CL N2 O4
FORMUL 4 BCT C H O3 1-
FORMUL 5 HOH *122(H2 O)
HELIX 1 AA1 ALA A 190 TYR A 197 1 8
HELIX 2 AA2 TYR A 197 GLY A 206 1 10
HELIX 3 AA3 GLY A 215 THR A 232 1 18
HELIX 4 AA4 CYS A 266 CYS A 283 1 18
HELIX 5 AA5 ASP A 335 GLY A 340 1 6
HELIX 6 AA6 ALA A 393 TYR A 403 1 11
SHEET 1 AA1 7 GLY A 183 GLN A 184 0
SHEET 2 AA1 7 ILE A 207 ASP A 211 1 O ASP A 211 N GLY A 183
SHEET 3 AA1 7 LEU A 363 TRP A 367 -1 O LEU A 363 N VAL A 210
SHEET 4 AA1 7 ARG A 322 TYR A 329 -1 N THR A 325 O PHE A 366
SHEET 5 AA1 7 ARG A 383 ASP A 392 -1 O ILE A 386 N TYR A 328
SHEET 6 AA1 7 ALA A 298 TYR A 303 -1 N MET A 299 O THR A 387
SHEET 7 AA1 7 LYS A 255 ILE A 259 -1 N LYS A 255 O CYS A 302
SHEET 1 AA2 6 GLY A 183 GLN A 184 0
SHEET 2 AA2 6 ILE A 207 ASP A 211 1 O ASP A 211 N GLY A 183
SHEET 3 AA2 6 LEU A 363 TRP A 367 -1 O LEU A 363 N VAL A 210
SHEET 4 AA2 6 ARG A 322 TYR A 329 -1 N THR A 325 O PHE A 366
SHEET 5 AA2 6 ARG A 383 ASP A 392 -1 O ILE A 386 N TYR A 328
SHEET 6 AA2 6 ILE A 292 ARG A 295 -1 N GLY A 294 O PHE A 391
SHEET 1 AA3 2 LEU A 240 SER A 242 0
SHEET 2 AA3 2 ILE A 251 ARG A 252 -1 O ILE A 251 N VAL A 241
SHEET 1 AA4 4 TYR A 310 HIS A 313 0
SHEET 2 AA4 4 HIS A 374 VAL A 376 -1 O VAL A 376 N TYR A 310
SHEET 3 AA4 4 LEU A 343 ILE A 345 -1 N ARG A 344 O GLU A 375
SHEET 4 AA4 4 ALA A 354 ILE A 356 -1 O ILE A 356 N LEU A 343
SSBOND 1 CYS A 201 CYS A 208 1555 1555 2.13
LINK NE2 HIS A 313 MN MN A 501 1555 1555 2.23
LINK OD1 ASP A 315 MN MN A 501 1555 1555 2.21
LINK NE2 HIS A 374 MN MN A 501 1555 1555 2.23
LINK MN MN A 501 N8 UN9 A 502 1555 1555 2.37
LINK MN MN A 501 O13 UN9 A 502 1555 1555 2.22
LINK MN MN A 501 O HOH A 641 1555 1555 2.23
SITE 1 AC1 5 HIS A 313 ASP A 315 HIS A 374 UN9 A 502
SITE 2 AC1 5 HOH A 641
SITE 1 AC2 16 ASP A 254 ILE A 256 MET A 299 TYR A 303
SITE 2 AC2 16 TYR A 310 HIS A 313 ASP A 315 TYR A 329
SITE 3 AC2 16 LEU A 343 HIS A 374 VAL A 376 ARG A 383
SITE 4 AC2 16 ARG A 398 MN A 501 HOH A 631 HOH A 641
SITE 1 AC3 3 LYS A 262 ARG A 312 PRO A 373
CRYST1 110.199 110.199 39.717 90.00 90.00 120.00 P 63 6
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 0.009074 0.005239 0.000000 0.00000
SCALE2 0.000000 0.010478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025178 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
