HEADER OXIDOREDUCTASE 23-JUL-18 6H4O
TITLE CRYSTAL STRUCTURE OF HUMAN KDM4A IN COMPLEX WITH COMPOUND 18A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A,
COMPND 5 JUMONJI DOMAIN-CONTAINING PROTEIN 2A;
COMPND 6 EC: 1.14.11.-;
COMPND 7 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: KDM4A, JHDM3A, JMJD2, JMJD2A, KIAA0677;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HISTONE DEMETHYLASE, INHIBITOR, TRANSCRIPTION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.V.LE BIHAN,R.L.M.VAN MONTFORT
REVDAT 2 17-JAN-24 6H4O 1 LINK
REVDAT 1 12-JUN-19 6H4O 0
JRNL AUTH Y.V.LE BIHAN,R.M.LANIGAN,B.ATRASH,M.G.MCLAUGHLIN,
JRNL AUTH 2 S.VELUPILLAI,A.G.MALCOLM,K.S.ENGLAND,G.F.RUDA,N.Y.MOK,
JRNL AUTH 3 A.TUMBER,K.TOMLIN,H.SAVILLE,E.SHEHU,C.MCANDREW,L.CARMICHAEL,
JRNL AUTH 4 J.M.BENNETT,F.JEGANATHAN,P.EVE,A.DONOVAN,A.HAYES,F.WOOD,
JRNL AUTH 5 F.I.RAYNAUD,O.FEDOROV,P.E.BRENNAN,R.BURKE,
JRNL AUTH 6 R.L.M.VAN MONTFORT,O.W.ROSSANESE,J.BLAGG,V.BAVETSIAS
JRNL TITL C8-SUBSTITUTED PYRIDO[3,4-D]PYRIMIDIN-4(3H)-ONES: STUDIES
JRNL TITL 2 TOWARDS THE IDENTIFICATION OF POTENT, CELL PENETRANT JUMONJI
JRNL TITL 3 C DOMAIN CONTAINING HISTONE LYSINE DEMETHYLASE 4 SUBFAMILY
JRNL TITL 4 (KDM4) INHIBITORS, COMPOUND PROFILING IN CELL-BASED TARGET
JRNL TITL 5 ENGAGEMENT ASSAYS.
JRNL REF EUR.J.MED.CHEM. V. 177 316 2019
JRNL REFN ISSN 0223-5234
JRNL PMID 31158747
JRNL DOI 10.1016/J.EJMECH.2019.05.041
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 76551
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3826
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5661
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2112
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5361
REMARK 3 BIN R VALUE (WORKING SET) : 0.2096
REMARK 3 BIN FREE R VALUE : 0.2408
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 300
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10569
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 139
REMARK 3 SOLVENT ATOMS : 467
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.46530
REMARK 3 B22 (A**2) : -2.68010
REMARK 3 B33 (A**2) : -1.78520
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.26590
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.260
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.221
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.171
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.226
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.174
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 11111 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 15155 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3492 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 203 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1747 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 11111 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 6 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1421 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 7 ; 1.000 ; HARMONIC
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 12915 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.04
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.13
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.87
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|8 - 36}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9544 2.4182 -58.4612
REMARK 3 T TENSOR
REMARK 3 T11: 0.0860 T22: -0.1682
REMARK 3 T33: 0.0297 T12: -0.0163
REMARK 3 T13: 0.1664 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 2.0295 L22: 5.8156
REMARK 3 L33: -0.2250 L12: 2.3695
REMARK 3 L13: -2.4392 L23: -1.0788
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: 0.0520 S13: 0.3534
REMARK 3 S21: -0.0549 S22: -0.1228 S23: -0.2949
REMARK 3 S31: -0.4499 S32: 0.1589 S33: 0.1100
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|37 - 101}
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7629 -20.7753 -53.7804
REMARK 3 T TENSOR
REMARK 3 T11: -0.0420 T22: -0.1058
REMARK 3 T33: -0.1519 T12: 0.0580
REMARK 3 T13: 0.0780 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 2.0936 L22: 3.9137
REMARK 3 L33: 1.8338 L12: 0.2437
REMARK 3 L13: 0.4830 L23: -0.7815
REMARK 3 S TENSOR
REMARK 3 S11: 0.2662 S12: -0.1613 S13: -0.1347
REMARK 3 S21: 0.1841 S22: -0.1319 S23: -0.3229
REMARK 3 S31: 0.0272 S32: 0.1634 S33: -0.1343
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|102 - 291}
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3980 -14.9635 -57.8356
REMARK 3 T TENSOR
REMARK 3 T11: -0.0408 T22: -0.1334
REMARK 3 T33: -0.1510 T12: 0.0478
REMARK 3 T13: 0.1087 T23: 0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 2.1882 L22: 2.5616
REMARK 3 L33: 2.0392 L12: -0.0142
REMARK 3 L13: 0.2007 L23: -0.3241
REMARK 3 S TENSOR
REMARK 3 S11: 0.1162 S12: -0.0688 S13: 0.0880
REMARK 3 S21: 0.0662 S22: 0.0235 S23: 0.0846
REMARK 3 S31: -0.1379 S32: -0.0321 S33: -0.1397
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|292 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6743 4.1800 -46.9349
REMARK 3 T TENSOR
REMARK 3 T11: 0.1266 T22: -0.1502
REMARK 3 T33: -0.1753 T12: 0.1707
REMARK 3 T13: 0.2127 T23: -0.0994
REMARK 3 L TENSOR
REMARK 3 L11: 6.6009 L22: 5.1849
REMARK 3 L33: 3.7995 L12: -1.8601
REMARK 3 L13: -1.9777 L23: 0.6406
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: -0.4755 S13: 0.3777
REMARK 3 S21: 0.3561 S22: -0.0104 S23: 0.1933
REMARK 3 S31: -0.4908 S32: -0.3867 S33: 0.0206
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {B|7 - 293}
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5755 -52.0179 -14.4124
REMARK 3 T TENSOR
REMARK 3 T11: -0.0613 T22: -0.1003
REMARK 3 T33: -0.1142 T12: -0.0263
REMARK 3 T13: 0.0467 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.7936 L22: 1.8594
REMARK 3 L33: 1.6353 L12: -0.0256
REMARK 3 L13: 0.3159 L23: 0.0184
REMARK 3 S TENSOR
REMARK 3 S11: 0.0634 S12: -0.0218 S13: -0.0154
REMARK 3 S21: -0.0218 S22: -0.0722 S23: 0.1601
REMARK 3 S31: -0.0258 S32: -0.1216 S33: 0.0088
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {B|294 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0808 -34.5208 -27.2562
REMARK 3 T TENSOR
REMARK 3 T11: 0.0294 T22: -0.1016
REMARK 3 T33: -0.1312 T12: -0.0572
REMARK 3 T13: 0.0123 T23: 0.0831
REMARK 3 L TENSOR
REMARK 3 L11: 2.7857 L22: 2.3106
REMARK 3 L33: 7.0270 L12: 1.4711
REMARK 3 L13: -0.8782 L23: -2.5812
REMARK 3 S TENSOR
REMARK 3 S11: 0.0620 S12: 0.2656 S13: 0.1896
REMARK 3 S21: -0.0388 S22: -0.2643 S23: 0.0500
REMARK 3 S31: -0.4388 S32: 0.5869 S33: 0.2023
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {C|11 - 53}
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1541 -63.8950 -55.7514
REMARK 3 T TENSOR
REMARK 3 T11: 0.0001 T22: -0.0536
REMARK 3 T33: -0.0676 T12: -0.1458
REMARK 3 T13: 0.0320 T23: -0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 2.4111 L22: 6.0037
REMARK 3 L33: 2.6567 L12: 1.1589
REMARK 3 L13: 2.6238 L23: -1.2119
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: -0.2526 S13: -0.4383
REMARK 3 S21: 0.1096 S22: 0.1133 S23: 0.3136
REMARK 3 S31: 0.5644 S32: -0.5280 S33: -0.1450
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {C|54 - 124}
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0628 -37.0091 -55.7091
REMARK 3 T TENSOR
REMARK 3 T11: -0.1449 T22: -0.2305
REMARK 3 T33: 0.0096 T12: 0.1000
REMARK 3 T13: -0.0393 T23: -0.0723
REMARK 3 L TENSOR
REMARK 3 L11: 6.3836 L22: 2.3065
REMARK 3 L33: 5.4670 L12: 0.1988
REMARK 3 L13: -2.8937 L23: 0.4958
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.2274 S13: 0.5515
REMARK 3 S21: -0.0335 S22: 0.0392 S23: 0.2362
REMARK 3 S31: -0.4238 S32: -0.3975 S33: -0.0313
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {C|125 - 293}
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4249 -50.9865 -54.4426
REMARK 3 T TENSOR
REMARK 3 T11: -0.1176 T22: -0.1078
REMARK 3 T33: -0.1561 T12: 0.0314
REMARK 3 T13: -0.0060 T23: -0.0814
REMARK 3 L TENSOR
REMARK 3 L11: 3.4426 L22: 3.2361
REMARK 3 L33: 2.2371 L12: 0.9021
REMARK 3 L13: -0.6451 L23: -0.0716
REMARK 3 S TENSOR
REMARK 3 S11: -0.1145 S12: -0.2401 S13: 0.0042
REMARK 3 S21: 0.1562 S22: -0.0138 S23: -0.2561
REMARK 3 S31: 0.2842 S32: -0.1247 S33: 0.1283
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {C|294 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7308 -69.4545 -47.8581
REMARK 3 T TENSOR
REMARK 3 T11: 0.1522 T22: -0.2017
REMARK 3 T33: 0.0073 T12: 0.1382
REMARK 3 T13: 0.0013 T23: 0.0952
REMARK 3 L TENSOR
REMARK 3 L11: 1.8513 L22: 0.8880
REMARK 3 L33: 3.4112 L12: -2.6707
REMARK 3 L13: 0.2201 L23: -1.6516
REMARK 3 S TENSOR
REMARK 3 S11: -0.0753 S12: -0.3499 S13: -0.3117
REMARK 3 S21: 0.0986 S22: 0.0379 S23: -0.3215
REMARK 3 S31: 0.4027 S32: 0.1434 S33: 0.0374
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {D|4 - 53}
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5781 -1.4684 -11.5540
REMARK 3 T TENSOR
REMARK 3 T11: 0.0367 T22: -0.1228
REMARK 3 T33: -0.1163 T12: 0.1284
REMARK 3 T13: 0.0699 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 3.9673 L22: 5.5518
REMARK 3 L33: 2.5298 L12: -1.4191
REMARK 3 L13: 2.1602 L23: -0.0234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0700 S12: 0.3792 S13: -0.4491
REMARK 3 S21: -0.1653 S22: 0.1553 S23: -0.2635
REMARK 3 S31: 0.5828 S32: 0.4828 S33: -0.2254
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {D|54 - 78}
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5698 23.6708 -22.1711
REMARK 3 T TENSOR
REMARK 3 T11: -0.0326 T22: -0.0247
REMARK 3 T33: -0.1456 T12: -0.1297
REMARK 3 T13: 0.0519 T23: 0.1321
REMARK 3 L TENSOR
REMARK 3 L11: 2.2866 L22: 3.6529
REMARK 3 L33: 3.5332 L12: -1.1384
REMARK 3 L13: -0.8048 L23: -0.3725
REMARK 3 S TENSOR
REMARK 3 S11: -0.1025 S12: 0.3057 S13: 0.2908
REMARK 3 S21: -0.4256 S22: -0.0170 S23: -0.1396
REMARK 3 S31: -0.1903 S32: 0.3684 S33: 0.1195
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: {D|79 - 124}
REMARK 3 ORIGIN FOR THE GROUP (A): 28.2804 27.3161 -11.0824
REMARK 3 T TENSOR
REMARK 3 T11: -0.0572 T22: -0.2469
REMARK 3 T33: -0.0206 T12: -0.0574
REMARK 3 T13: 0.0135 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 8.2517 L22: 3.3961
REMARK 3 L33: 6.5305 L12: -0.3110
REMARK 3 L13: -2.6612 L23: -1.5588
REMARK 3 S TENSOR
REMARK 3 S11: -0.0254 S12: -0.0366 S13: 0.5448
REMARK 3 S21: 0.1845 S22: 0.0895 S23: -0.2087
REMARK 3 S31: -0.5297 S32: 0.2843 S33: -0.0641
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: {D|125 - 293}
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6310 12.2183 -14.5373
REMARK 3 T TENSOR
REMARK 3 T11: -0.0552 T22: -0.0928
REMARK 3 T33: -0.1603 T12: -0.0300
REMARK 3 T13: 0.0004 T23: 0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 2.4219 L22: 3.2674
REMARK 3 L33: 2.2558 L12: -0.1868
REMARK 3 L13: -0.4746 L23: -0.2864
REMARK 3 S TENSOR
REMARK 3 S11: -0.1317 S12: 0.2013 S13: -0.0413
REMARK 3 S21: -0.2874 S22: 0.1884 S23: 0.2966
REMARK 3 S31: 0.2145 S32: 0.0252 S33: -0.0567
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: {D|294 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6889 -6.6069 -19.4151
REMARK 3 T TENSOR
REMARK 3 T11: 0.1966 T22: -0.2531
REMARK 3 T33: -0.0180 T12: -0.1417
REMARK 3 T13: -0.0413 T23: -0.0742
REMARK 3 L TENSOR
REMARK 3 L11: 3.6298 L22: 1.6968
REMARK 3 L33: 2.9208 L12: 2.6512
REMARK 3 L13: 0.2129 L23: 1.6681
REMARK 3 S TENSOR
REMARK 3 S11: -0.0779 S12: 0.3147 S13: -0.5317
REMARK 3 S21: -0.4059 S22: 0.0641 S23: 0.3744
REMARK 3 S31: 0.5169 S32: -0.3176 S33: 0.0138
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6H4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1200009261.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76575
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 48.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.12800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 1.87400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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: 2OQ7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLISATION SOLUTION IS 0.1M BIS
REMARK 280 -TRIS-PROPANE PH7.5, 12-16% PEG-4000. INHIBITOR IS SOAKED IN
REMARK 280 CRYSTALS BY ADDITION DIRECTLY TO THE DROPS OF DMSO DISSOLVED
REMARK 280 COMPOUND, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 50.68700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLU A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 LYS A 162
REMARK 465 GLU A 163
REMARK 465 SER A 164
REMARK 465 GLY A 165
REMARK 465 ILE A 166
REMARK 465 THR A 167
REMARK 465 ILE A 168
REMARK 465 GLU A 169
REMARK 465 ASP A 311
REMARK 465 LYS A 355
REMARK 465 GLU A 356
REMARK 465 SER A 357
REMARK 465 GLU A 358
REMARK 465 LEU A 359
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLU B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 LYS B 162
REMARK 465 GLU B 163
REMARK 465 SER B 164
REMARK 465 GLY B 165
REMARK 465 ILE B 166
REMARK 465 THR B 167
REMARK 465 ILE B 168
REMARK 465 LYS B 310
REMARK 465 ASP B 311
REMARK 465 LYS B 355
REMARK 465 GLU B 356
REMARK 465 SER B 357
REMARK 465 GLU B 358
REMARK 465 LEU B 359
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 SER C 3
REMARK 465 GLU C 4
REMARK 465 SER C 5
REMARK 465 GLU C 6
REMARK 465 THR C 7
REMARK 465 LEU C 8
REMARK 465 ASN C 9
REMARK 465 PRO C 10
REMARK 465 ARG C 309
REMARK 465 LYS C 310
REMARK 465 ASP C 311
REMARK 465 LYS C 355
REMARK 465 GLU C 356
REMARK 465 SER C 357
REMARK 465 GLU C 358
REMARK 465 LEU C 359
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 SER D 3
REMARK 465 LYS D 162
REMARK 465 GLU D 163
REMARK 465 SER D 164
REMARK 465 GLY D 165
REMARK 465 ILE D 166
REMARK 465 THR D 167
REMARK 465 ILE D 168
REMARK 465 GLU D 169
REMARK 465 ARG D 309
REMARK 465 LYS D 310
REMARK 465 ASP D 311
REMARK 465 LYS D 355
REMARK 465 GLU D 356
REMARK 465 SER D 357
REMARK 465 GLU D 358
REMARK 465 LEU D 359
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 LEU A 8 CD1
REMARK 470 GLU A 22 CD OE1 OE2
REMARK 470 ARG A 29 CD NE CZ NH1 NH2
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 GLU A 52 CD OE1 OE2
REMARK 470 LYS A 54 CD CE NZ
REMARK 470 SER A 79 OG
REMARK 470 LYS A 90 CD CE NZ
REMARK 470 LYS A 99 CD CE NZ
REMARK 470 LYS A 105 NZ
REMARK 470 ARG A 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 113 CG CD OE1 OE2
REMARK 470 GLU A 116 OE1 OE2
REMARK 470 LYS A 120 CE NZ
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 ARG A 154 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 156 CD1
REMARK 470 LEU A 159 CD1 CD2
REMARK 470 GLU A 161 CG CD OE1 OE2
REMARK 470 ASN A 172 CG OD1 ND2
REMARK 470 ARG A 221 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 224 CD CE NZ
REMARK 470 SER A 230 OG
REMARK 470 GLN A 232 CG CD OE1 NE2
REMARK 470 SER A 233 OG
REMARK 470 GLU A 235 CD OE1 OE2
REMARK 470 LYS A 241 NZ
REMARK 470 LYS A 251 NZ
REMARK 470 LYS A 252 NZ
REMARK 470 ARG A 294 NH1 NH2
REMARK 470 LYS A 301 NZ
REMARK 470 SER A 307 OG
REMARK 470 ARG A 309 CG CD NE CZ NH1 NH2
REMARK 470 MET A 312 CG SD CE
REMARK 470 LYS A 314 CG CD CE NZ
REMARK 470 VAL A 319 CG1 CG2
REMARK 470 ARG A 322 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 323 CE NZ
REMARK 470 GLU A 327 CG CD OE1 OE2
REMARK 470 ARG A 328 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 329 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 330 CG CD CE NZ
REMARK 470 LEU A 331 CD1 CD2
REMARK 470 LYS A 333 CE NZ
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 GLU A 352 CD OE1 OE2
REMARK 470 THR B 7 N CB OG1 CG2
REMARK 470 LEU B 8 CD1 CD2
REMARK 470 ARG B 13 CD NE CZ NH1 NH2
REMARK 470 GLU B 22 CG CD OE1 OE2
REMARK 470 GLU B 23 OE2
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 LYS B 54 CE NZ
REMARK 470 ILE B 62 CD1
REMARK 470 LEU B 65 CD1
REMARK 470 LYS B 89 NZ
REMARK 470 LYS B 90 CD CE NZ
REMARK 470 LYS B 99 CD CE NZ
REMARK 470 ILE B 100 CD1
REMARK 470 LYS B 105 CE NZ
REMARK 470 ARG B 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 113 CG CD OE1 OE2
REMARK 470 GLU B 115 CD OE1 OE2
REMARK 470 LYS B 120 NZ
REMARK 470 LYS B 123 CD CE NZ
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 ASP B 146 CG OD1 OD2
REMARK 470 ARG B 154 CZ NH1 NH2
REMARK 470 LEU B 159 CD2
REMARK 470 GLU B 161 CG CD OE1 OE2
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 LYS B 224 CG CD CE NZ
REMARK 470 GLN B 232 CG CD OE1 NE2
REMARK 470 GLU B 235 CD OE1 OE2
REMARK 470 LYS B 241 NZ
REMARK 470 LYS B 252 NZ
REMARK 470 ARG B 309 O CG CD NE CZ NH1 NH2
REMARK 470 MET B 312 CG SD CE
REMARK 470 LYS B 314 CD CE NZ
REMARK 470 LYS B 323 NZ
REMARK 470 LYS B 330 CG CD CE NZ
REMARK 470 LYS B 333 CD CE NZ
REMARK 470 LYS B 336 CE NZ
REMARK 470 GLU B 352 OE1 OE2
REMARK 470 LEU B 354 CG CD1 CD2
REMARK 470 GLU C 22 CG CD OE1 OE2
REMARK 470 ARG C 25 CD NE CZ NH1 NH2
REMARK 470 ILE C 31 CD1
REMARK 470 ILE C 34 CD1
REMARK 470 LYS C 51 CG CD CE NZ
REMARK 470 GLU C 52 CD OE1 OE2
REMARK 470 LYS C 54 CG CD CE NZ
REMARK 470 ILE C 67 CD1
REMARK 470 LYS C 89 CE NZ
REMARK 470 LYS C 90 CG CD CE NZ
REMARK 470 LYS C 99 CG CD CE NZ
REMARK 470 ASP C 104 CG OD1 OD2
REMARK 470 LYS C 105 CD CE NZ
REMARK 470 ARG C 110 CG CD NE CZ NH1 NH2
REMARK 470 SER C 112 OG
REMARK 470 GLU C 113 CD OE1 OE2
REMARK 470 GLU C 116 CD OE1 OE2
REMARK 470 ARG C 119 CZ NH1 NH2
REMARK 470 LYS C 120 CD CE NZ
REMARK 470 LYS C 123 CD CE NZ
REMARK 470 LYS C 143 CG CD CE NZ
REMARK 470 ASP C 146 CG OD1 OD2
REMARK 470 ARG C 154 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 159 CG CD1 CD2
REMARK 470 GLU C 161 CG CD OE1 OE2
REMARK 470 LYS C 162 CG CD CE NZ
REMARK 470 SER C 164 OG
REMARK 470 ILE C 166 CG1 CG2 CD1
REMARK 470 THR C 167 OG1 CG2
REMARK 470 ILE C 168 CG1 CG2 CD1
REMARK 470 GLU C 169 CG CD OE1 OE2
REMARK 470 VAL C 171 CG1
REMARK 470 ASN C 172 CG OD1 ND2
REMARK 470 THR C 173 CG2
REMARK 470 LYS C 182 NZ
REMARK 470 LYS C 217 NZ
REMARK 470 ARG C 218 NH1 NH2
REMARK 470 LYS C 224 CG CD CE NZ
REMARK 470 GLN C 232 CG CD OE1 NE2
REMARK 470 SER C 233 OG
REMARK 470 GLU C 235 CG CD OE1 OE2
REMARK 470 LYS C 241 NZ
REMARK 470 LYS C 251 CD CE NZ
REMARK 470 LYS C 252 NZ
REMARK 470 LYS C 259 CE NZ
REMARK 470 SER C 288 OG
REMARK 470 ARG C 294 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 297 CD1
REMARK 470 GLU C 298 CG CD OE1 OE2
REMARK 470 GLN C 302 CG CD OE1 NE2
REMARK 470 LEU C 305 CG CD1 CD2
REMARK 470 SER C 307 OG
REMARK 470 MET C 312 CG SD CE
REMARK 470 VAL C 313 CG1 CG2
REMARK 470 LYS C 314 CG CD CE NZ
REMARK 470 ILE C 315 CG1 CG2 CD1
REMARK 470 SER C 316 OG
REMARK 470 ASP C 318 OD1 OD2
REMARK 470 VAL C 319 CG1
REMARK 470 VAL C 321 CG1 CG2
REMARK 470 ARG C 322 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 323 CG CD CE NZ
REMARK 470 ARG C 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 330 CG CD CE NZ
REMARK 470 LEU C 331 CG CD1 CD2
REMARK 470 LYS C 333 CG CD CE NZ
REMARK 470 LYS C 336 CG CD CE NZ
REMARK 470 ASN C 338 CG OD1 ND2
REMARK 470 LEU C 345 CD1 CD2
REMARK 470 GLU C 352 OE1 OE2
REMARK 470 LEU C 354 CG CD1 CD2
REMARK 470 GLU D 4 CG CD OE1 OE2
REMARK 470 GLU D 6 CD OE1 OE2
REMARK 470 LEU D 8 CD1 CD2
REMARK 470 ARG D 13 NH1 NH2
REMARK 470 LYS D 51 CG CD CE NZ
REMARK 470 LYS D 54 CG CD CE NZ
REMARK 470 ASP D 60 CG OD1 OD2
REMARK 470 ASP D 61 CG OD1 OD2
REMARK 470 ILE D 62 CD1
REMARK 470 LEU D 65 CD1 CD2
REMARK 470 ILE D 87 CD1
REMARK 470 LYS D 89 CD CE NZ
REMARK 470 LYS D 90 CD CE NZ
REMARK 470 LYS D 99 CE NZ
REMARK 470 ASP D 104 CG OD1 OD2
REMARK 470 LYS D 105 CD CE NZ
REMARK 470 ARG D 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 113 CG CD OE1 OE2
REMARK 470 GLU D 115 CG CD OE1 OE2
REMARK 470 GLU D 116 CD OE1 OE2
REMARK 470 LYS D 123 CE NZ
REMARK 470 LYS D 143 CD CE NZ
REMARK 470 ARG D 154 NH1 NH2
REMARK 470 VAL D 171 CG1 CG2
REMARK 470 ASN D 172 OD1 ND2
REMARK 470 GLU D 214 CD OE1 OE2
REMARK 470 ARG D 218 NH1 NH2
REMARK 470 LYS D 224 CG CD CE NZ
REMARK 470 GLN D 232 CG CD OE1 NE2
REMARK 470 SER D 233 OG
REMARK 470 GLU D 235 CG CD OE1 OE2
REMARK 470 LYS D 241 CE NZ
REMARK 470 LYS D 251 CE NZ
REMARK 470 LYS D 252 CE NZ
REMARK 470 GLU D 263 OE1 OE2
REMARK 470 SER D 288 OG
REMARK 470 ILE D 297 CD1
REMARK 470 LYS D 301 NZ
REMARK 470 LEU D 305 CD1 CD2
REMARK 470 LYS D 314 CG CD CE NZ
REMARK 470 ILE D 315 CD1
REMARK 470 SER D 316 OG
REMARK 470 ASP D 318 CG OD1 OD2
REMARK 470 ARG D 322 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 323 CE NZ
REMARK 470 GLU D 327 CG CD OE1 OE2
REMARK 470 LYS D 330 CG CD CE NZ
REMARK 470 LEU D 331 CG CD1 CD2
REMARK 470 LYS D 333 CG CD CE NZ
REMARK 470 LYS D 336 CG CD CE NZ
REMARK 470 ASN D 338 CG OD1 ND2
REMARK 470 LEU D 354 O CG CD1 CD2
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 SER A 112 -73.73 -91.36
REMARK 500 ARG A 152 69.59 -165.62
REMARK 500 TYR B 18 72.94 -115.78
REMARK 500 SER B 112 -76.57 -84.48
REMARK 500 ARG B 152 69.52 -151.66
REMARK 500 LYS B 182 3.76 80.59
REMARK 500 PHE B 227 77.34 -117.91
REMARK 500 TYR C 18 73.93 -118.31
REMARK 500 ASN C 128 71.98 39.79
REMARK 500 VAL C 145 107.27 -54.61
REMARK 500 ARG C 152 67.83 -152.39
REMARK 500 LYS C 182 -3.30 78.82
REMARK 500 ALA C 236 51.23 -111.62
REMARK 500 SER D 112 -70.73 -92.26
REMARK 500 ASN D 128 63.52 37.93
REMARK 500 ARG D 152 74.18 -154.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 611 DISTANCE = 6.57 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 FQH A 403
REMARK 610 FQH B 403
REMARK 610 FQH D 403
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 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 188 NE2
REMARK 620 2 GLU A 190 OE2 114.6
REMARK 620 3 HIS A 276 NE2 91.0 87.0
REMARK 620 4 FQH A 403 N3 100.7 141.7 107.3
REMARK 620 5 FQH A 403 N2 80.3 98.3 171.1 72.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 HIS A 240 NE2 98.8
REMARK 620 3 CYS A 306 SG 122.4 112.1
REMARK 620 4 CYS A 308 SG 109.2 89.8 118.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 188 NE2
REMARK 620 2 GLU B 190 OE2 98.4
REMARK 620 3 HIS B 276 NE2 85.1 81.1
REMARK 620 4 FQH B 403 N2 80.1 100.5 165.2
REMARK 620 5 FQH B 403 N3 105.0 155.8 106.4 78.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 234 SG
REMARK 620 2 HIS B 240 NE2 112.3
REMARK 620 3 CYS B 306 SG 118.5 111.4
REMARK 620 4 CYS B 308 SG 114.3 85.6 110.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 188 NE2
REMARK 620 2 GLU C 190 OE2 99.2
REMARK 620 3 HIS C 276 NE2 89.5 88.0
REMARK 620 4 FQH C 403 N3 101.4 155.1 106.0
REMARK 620 5 FQH C 403 N2 74.8 96.1 164.2 76.2
REMARK 620 6 HOH C 501 O 176.0 77.1 88.9 82.6 106.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 234 SG
REMARK 620 2 HIS C 240 NE2 123.2
REMARK 620 3 CYS C 306 SG 114.1 99.2
REMARK 620 4 CYS C 308 SG 113.5 95.2 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 188 NE2
REMARK 620 2 GLU D 190 OE2 99.0
REMARK 620 3 HIS D 276 NE2 87.7 94.9
REMARK 620 4 FQH D 403 N2 79.4 90.2 166.8
REMARK 620 5 FQH D 403 N3 99.8 154.7 102.8 76.7
REMARK 620 6 HOH D 506 O 177.6 82.3 90.2 102.6 79.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 234 SG
REMARK 620 2 HIS D 240 NE2 110.7
REMARK 620 3 CYS D 306 SG 122.1 108.4
REMARK 620 4 CYS D 308 SG 107.4 101.9 104.2
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 ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FQH A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FQH B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FQH C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FQH D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS D 404
DBREF 6H4O A 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 6H4O B 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 6H4O C 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 6H4O D 1 359 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 6H4O SER A 0 UNP O75164 EXPRESSION TAG
SEQADV 6H4O SER B 0 UNP O75164 EXPRESSION TAG
SEQADV 6H4O SER C 0 UNP O75164 EXPRESSION TAG
SEQADV 6H4O SER D 0 UNP O75164 EXPRESSION TAG
SEQRES 1 A 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 A 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 A 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 A 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 A 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 A 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 A 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 A 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 A 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 A 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 A 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 A 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 A 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 A 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 A 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 A 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 A 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 A 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 A 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 A 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 A 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 A 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 A 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 A 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 A 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 A 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 A 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 A 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 B 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 B 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 B 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 B 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 B 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 B 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 B 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 B 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 B 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 B 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 B 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 B 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 B 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 B 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 B 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 B 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 B 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 B 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 B 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 B 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 B 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 B 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 B 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 B 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 B 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 B 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 B 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 B 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 C 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 C 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 C 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 C 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 C 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 C 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 C 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 C 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 C 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 C 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 C 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 C 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 C 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 C 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 C 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 C 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 C 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 C 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 C 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 C 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 C 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 C 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 C 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 C 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 C 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 C 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 C 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 C 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 D 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 D 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 D 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 D 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 D 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 D 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 D 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 D 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 D 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 D 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 D 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 D 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 D 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 D 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 D 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 D 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 D 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 D 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 D 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 D 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 D 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 D 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 D 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 D 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 D 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 D 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 D 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 D 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
HET ZN A 401 1
HET ZN A 402 1
HET FQH A 403 21
HET GOL A 404 6
HET CL A 405 1
HET ZN B 401 1
HET ZN B 402 1
HET FQH B 403 25
HET GOL B 404 6
HET ZN C 401 1
HET ZN C 402 1
HET FQH C 403 34
HET DMS C 404 4
HET DMS C 405 4
HET CL C 406 1
HET ZN D 401 1
HET ZN D 402 1
HET FQH D 403 25
HET DMS D 404 4
HETNAM ZN ZINC ION
HETNAM FQH 8-[4-[2-[4-[3-(TRIFLUOROMETHYL)PHENYL]PIPERIDIN-1-
HETNAM 2 FQH YL]ETHYL]PYRAZOL-1-YL]-3~{H}-PYRIDO[3,4-D]PYRIMIDIN-4-
HETNAM 3 FQH ONE
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ZN 8(ZN 2+)
FORMUL 7 FQH 4(C24 H23 F3 N6 O)
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 9 CL 2(CL 1-)
FORMUL 17 DMS 3(C2 H6 O S)
FORMUL 24 HOH *467(H2 O)
HELIX 1 AA1 THR A 20 ARG A 25 1 6
HELIX 2 AA2 ASN A 26 GLN A 37 1 12
HELIX 3 AA3 GLY A 38 ALA A 42 5 5
HELIX 4 AA4 VAL A 94 ASN A 102 1 9
HELIX 5 AA5 GLU A 113 LEU A 125 1 13
HELIX 6 AA6 ASN A 149 LEU A 153 5 5
HELIX 7 AA7 THR A 155 VAL A 160 5 6
HELIX 8 AA8 GLU A 190 LEU A 194 5 5
HELIX 9 AA9 PRO A 212 GLU A 214 5 3
HELIX 10 AB1 HIS A 215 PHE A 227 1 13
HELIX 11 AB2 PHE A 227 CYS A 234 1 8
HELIX 12 AB3 ALA A 236 LYS A 241 5 6
HELIX 13 AB4 SER A 246 TYR A 253 1 8
HELIX 14 AB5 ARG A 295 GLN A 302 1 8
HELIX 15 AB6 MET A 317 GLN A 325 1 9
HELIX 16 AB7 ARG A 328 GLY A 335 1 8
HELIX 17 AB8 THR A 347 LEU A 354 5 8
HELIX 18 AB9 THR B 20 ARG B 25 1 6
HELIX 19 AC1 ASN B 26 GLN B 37 1 12
HELIX 20 AC2 GLY B 38 ALA B 42 5 5
HELIX 21 AC3 VAL B 94 SER B 103 1 10
HELIX 22 AC4 GLU B 113 LEU B 125 1 13
HELIX 23 AC5 ASN B 149 LEU B 153 5 5
HELIX 24 AC6 THR B 155 GLU B 161 5 7
HELIX 25 AC7 GLU B 190 LEU B 194 5 5
HELIX 26 AC8 PRO B 212 GLU B 214 5 3
HELIX 27 AC9 HIS B 215 PHE B 227 1 13
HELIX 28 AD1 PHE B 227 CYS B 234 1 8
HELIX 29 AD2 ALA B 236 LYS B 241 5 6
HELIX 30 AD3 SER B 246 TYR B 253 1 8
HELIX 31 AD4 ARG B 295 ALA B 303 1 9
HELIX 32 AD5 MET B 317 GLN B 325 1 9
HELIX 33 AD6 ARG B 328 GLY B 335 1 8
HELIX 34 AD7 THR B 347 LEU B 354 5 8
HELIX 35 AD8 ASN C 26 SER C 36 1 11
HELIX 36 AD9 GLY C 38 ALA C 42 5 5
HELIX 37 AE1 VAL C 94 ASN C 102 1 9
HELIX 38 AE2 GLU C 113 LEU C 125 1 13
HELIX 39 AE3 THR C 155 LEU C 157 5 3
HELIX 40 AE4 ASP C 158 SER C 164 1 7
HELIX 41 AE5 GLU C 190 LEU C 194 5 5
HELIX 42 AE6 PRO C 212 GLU C 214 5 3
HELIX 43 AE7 HIS C 215 PHE C 227 1 13
HELIX 44 AE8 PHE C 227 CYS C 234 1 8
HELIX 45 AE9 ALA C 236 LYS C 241 5 6
HELIX 46 AF1 SER C 246 TYR C 253 1 8
HELIX 47 AF2 ARG C 295 ALA C 303 1 9
HELIX 48 AF3 MET C 317 GLN C 325 1 9
HELIX 49 AF4 GLN C 325 GLY C 335 1 11
HELIX 50 AF5 THR C 347 LEU C 354 5 8
HELIX 51 AF6 THR D 20 ARG D 25 1 6
HELIX 52 AF7 ASN D 26 GLN D 37 1 12
HELIX 53 AF8 GLY D 38 ALA D 42 5 5
HELIX 54 AF9 VAL D 94 ASN D 102 1 9
HELIX 55 AG1 GLU D 113 LEU D 125 1 13
HELIX 56 AG2 ASN D 149 LEU D 153 5 5
HELIX 57 AG3 THR D 155 VAL D 160 5 6
HELIX 58 AG4 GLU D 190 LEU D 194 5 5
HELIX 59 AG5 PRO D 212 GLU D 214 5 3
HELIX 60 AG6 HIS D 215 PHE D 227 1 13
HELIX 61 AG7 PHE D 227 CYS D 234 1 8
HELIX 62 AG8 ALA D 236 LYS D 241 5 6
HELIX 63 AG9 SER D 246 TYR D 253 1 8
HELIX 64 AH1 ARG D 295 ALA D 303 1 9
HELIX 65 AH2 MET D 317 GLN D 325 1 9
HELIX 66 AH3 ARG D 328 ALA D 334 1 7
HELIX 67 AH4 THR D 347 LEU D 354 5 8
SHEET 1 AA110 MET A 15 PHE A 17 0
SHEET 2 AA110 LEU A 44 VAL A 47 1 O LYS A 46 N MET A 15
SHEET 3 AA110 PHE A 267 THR A 270 -1 O ILE A 269 N ALA A 45
SHEET 4 AA110 TYR A 195 GLY A 203 -1 N SER A 196 O THR A 270
SHEET 5 AA110 ASN A 284 PHE A 291 -1 O GLU A 287 N TYR A 199
SHEET 6 AA110 TYR A 175 GLY A 179 -1 N TYR A 175 O SER A 288
SHEET 7 AA110 ILE A 131 ASN A 137 -1 N VAL A 136 O LEU A 176
SHEET 8 AA110 ILE A 71 GLN A 78 -1 N ILE A 71 O TYR A 132
SHEET 9 AA110 LEU A 81 GLN A 88 -1 O TYR A 85 N LEU A 74
SHEET 10 AA110 THR A 243 ILE A 245 -1 O LEU A 244 N PHE A 82
SHEET 1 AA2 2 VAL A 66 ILE A 67 0
SHEET 2 AA2 2 MET A 92 THR A 93 -1 O MET A 92 N ILE A 67
SHEET 1 AA3 4 SER A 184 HIS A 188 0
SHEET 2 AA3 4 TYR A 275 ASN A 280 -1 O HIS A 276 N HIS A 188
SHEET 3 AA3 4 LYS A 206 VAL A 211 -1 N SER A 207 O PHE A 279
SHEET 4 AA3 4 ASP A 258 GLN A 262 -1 O VAL A 260 N TRP A 208
SHEET 1 AA410 MET B 15 PHE B 17 0
SHEET 2 AA410 LEU B 44 VAL B 47 1 O LYS B 46 N PHE B 17
SHEET 3 AA410 PHE B 267 THR B 270 -1 O ILE B 269 N ALA B 45
SHEET 4 AA410 TYR B 195 GLY B 203 -1 N ASN B 198 O MET B 268
SHEET 5 AA410 ASN B 284 PHE B 291 -1 O GLU B 287 N TYR B 199
SHEET 6 AA410 TYR B 175 GLY B 179 -1 N TYR B 175 O SER B 288
SHEET 7 AA410 ILE B 131 ASN B 137 -1 N VAL B 136 O LEU B 176
SHEET 8 AA410 ILE B 71 GLN B 78 -1 N ILE B 71 O TYR B 132
SHEET 9 AA410 LEU B 81 GLN B 88 -1 O TYR B 85 N LEU B 74
SHEET 10 AA410 THR B 243 ILE B 245 -1 O LEU B 244 N PHE B 82
SHEET 1 AA5 2 VAL B 66 ILE B 67 0
SHEET 2 AA5 2 MET B 92 THR B 93 -1 O MET B 92 N ILE B 67
SHEET 1 AA6 4 SER B 184 HIS B 188 0
SHEET 2 AA6 4 TYR B 275 ASN B 280 -1 O GLY B 278 N PHE B 185
SHEET 3 AA6 4 LYS B 206 VAL B 211 -1 N SER B 207 O PHE B 279
SHEET 4 AA6 4 ASP B 258 GLN B 262 -1 O GLN B 262 N LYS B 206
SHEET 1 AA710 MET C 15 PHE C 17 0
SHEET 2 AA710 LEU C 44 VAL C 47 1 O LYS C 46 N MET C 15
SHEET 3 AA710 PHE C 267 THR C 270 -1 O PHE C 267 N VAL C 47
SHEET 4 AA710 TYR C 195 GLY C 203 -1 N ASN C 198 O MET C 268
SHEET 5 AA710 ASN C 284 PHE C 291 -1 O GLU C 287 N TYR C 199
SHEET 6 AA710 TYR C 175 GLY C 179 -1 N TYR C 177 O ALA C 286
SHEET 7 AA710 ILE C 131 ASN C 137 -1 N VAL C 136 O LEU C 176
SHEET 8 AA710 ILE C 71 GLN C 78 -1 N ILE C 71 O TYR C 132
SHEET 9 AA710 LEU C 81 GLN C 88 -1 O TYR C 85 N LEU C 74
SHEET 10 AA710 THR C 243 ILE C 245 -1 O LEU C 244 N PHE C 82
SHEET 1 AA8 2 VAL C 66 ILE C 67 0
SHEET 2 AA8 2 MET C 92 THR C 93 -1 O MET C 92 N ILE C 67
SHEET 1 AA9 4 SER C 184 HIS C 188 0
SHEET 2 AA9 4 TYR C 275 ASN C 280 -1 O GLY C 278 N PHE C 185
SHEET 3 AA9 4 LYS C 206 VAL C 211 -1 N TYR C 209 O ALA C 277
SHEET 4 AA9 4 ASP C 258 GLN C 262 -1 O GLN C 262 N LYS C 206
SHEET 1 AB110 MET D 15 PHE D 17 0
SHEET 2 AB110 LEU D 44 VAL D 47 1 O LYS D 46 N MET D 15
SHEET 3 AB110 PHE D 267 THR D 270 -1 O PHE D 267 N VAL D 47
SHEET 4 AB110 TYR D 195 GLY D 203 -1 N ASN D 198 O MET D 268
SHEET 5 AB110 ASN D 284 PHE D 291 -1 O GLU D 287 N TYR D 199
SHEET 6 AB110 TYR D 175 GLY D 179 -1 N TYR D 175 O SER D 288
SHEET 7 AB110 ILE D 131 ASN D 137 -1 N VAL D 136 O LEU D 176
SHEET 8 AB110 ILE D 71 GLN D 78 -1 N ILE D 71 O TYR D 132
SHEET 9 AB110 LEU D 81 GLN D 88 -1 O TYR D 85 N LEU D 74
SHEET 10 AB110 THR D 243 ILE D 245 -1 O LEU D 244 N PHE D 82
SHEET 1 AB2 2 VAL D 66 ILE D 67 0
SHEET 2 AB2 2 MET D 92 THR D 93 -1 O MET D 92 N ILE D 67
SHEET 1 AB3 4 SER D 184 HIS D 188 0
SHEET 2 AB3 4 TYR D 275 ASN D 280 -1 O HIS D 276 N HIS D 188
SHEET 3 AB3 4 LYS D 206 VAL D 211 -1 N SER D 207 O PHE D 279
SHEET 4 AB3 4 ASP D 258 GLN D 262 -1 O GLN D 262 N LYS D 206
LINK NE2 HIS A 188 ZN ZN A 401 1555 1555 2.06
LINK OE2 GLU A 190 ZN ZN A 401 1555 1555 1.96
LINK SG CYS A 234 ZN ZN A 402 1555 1555 2.17
LINK NE2 HIS A 240 ZN ZN A 402 1555 1555 2.11
LINK NE2 HIS A 276 ZN ZN A 401 1555 1555 2.15
LINK SG CYS A 306 ZN ZN A 402 1555 1555 2.17
LINK SG CYS A 308 ZN ZN A 402 1555 1555 2.36
LINK ZN ZN A 401 N3 FQH A 403 1555 1555 2.14
LINK ZN ZN A 401 N2 FQH A 403 1555 1555 2.30
LINK NE2 HIS B 188 ZN ZN B 401 1555 1555 2.02
LINK OE2 GLU B 190 ZN ZN B 401 1555 1555 2.12
LINK SG CYS B 234 ZN ZN B 402 1555 1555 2.24
LINK NE2 HIS B 240 ZN ZN B 402 1555 1555 2.26
LINK NE2 HIS B 276 ZN ZN B 401 1555 1555 2.20
LINK SG CYS B 306 ZN ZN B 402 1555 1555 2.19
LINK SG CYS B 308 ZN ZN B 402 1555 1555 2.39
LINK ZN ZN B 401 N2 FQH B 403 1555 1555 2.13
LINK ZN ZN B 401 N3 FQH B 403 1555 1555 2.04
LINK NE2 HIS C 188 ZN ZN C 401 1555 1555 2.10
LINK OE2 GLU C 190 ZN ZN C 401 1555 1555 2.10
LINK SG CYS C 234 ZN ZN C 402 1555 1555 2.17
LINK NE2 HIS C 240 ZN ZN C 402 1555 1555 1.97
LINK NE2 HIS C 276 ZN ZN C 401 1555 1555 2.28
LINK SG CYS C 306 ZN ZN C 402 1555 1555 2.17
LINK SG CYS C 308 ZN ZN C 402 1555 1555 2.73
LINK ZN ZN C 401 N3 FQH C 403 1555 1555 2.05
LINK ZN ZN C 401 N2 FQH C 403 1555 1555 2.22
LINK ZN ZN C 401 O HOH C 501 1555 1555 2.05
LINK NE2 HIS D 188 ZN ZN D 401 1555 1555 2.05
LINK OE2 GLU D 190 ZN ZN D 401 1555 1555 2.11
LINK SG CYS D 234 ZN ZN D 402 1555 1555 2.18
LINK NE2 HIS D 240 ZN ZN D 402 1555 1555 2.03
LINK NE2 HIS D 276 ZN ZN D 401 1555 1555 2.11
LINK SG CYS D 306 ZN ZN D 402 1555 1555 2.15
LINK SG CYS D 308 ZN ZN D 402 1555 1555 2.41
LINK ZN ZN D 401 N2 FQH D 403 1555 1555 2.18
LINK ZN ZN D 401 N3 FQH D 403 1555 1555 2.07
LINK ZN ZN D 401 O HOH D 506 1555 1555 2.10
SITE 1 AC1 4 HIS A 188 GLU A 190 HIS A 276 FQH A 403
SITE 1 AC2 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC3 11 TYR A 132 TYR A 177 PHE A 185 HIS A 188
SITE 2 AC3 11 GLU A 190 ASP A 191 LYS A 206 TRP A 208
SITE 3 AC3 11 HIS A 276 ZN A 401 HOH A 576
SITE 1 AC4 11 VAL A 75 THR A 76 GLY A 77 THR A 126
SITE 2 AC4 11 PHE A 127 HOH A 550 VAL C 75 THR C 76
SITE 3 AC4 11 GLY C 77 THR C 126 PHE C 127
SITE 1 AC5 1 TYR A 59
SITE 1 AC6 4 HIS B 188 GLU B 190 HIS B 276 FQH B 403
SITE 1 AC7 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC8 10 TYR B 132 TYR B 175 TYR B 177 PHE B 185
SITE 2 AC8 10 HIS B 188 GLU B 190 LYS B 206 TRP B 208
SITE 3 AC8 10 HIS B 276 ZN B 401
SITE 1 AC9 10 VAL B 75 THR B 76 GLY B 77 THR B 126
SITE 2 AC9 10 PHE B 127 VAL D 75 THR D 76 GLY D 77
SITE 3 AC9 10 THR D 126 PHE D 127
SITE 1 AD1 5 HIS C 188 GLU C 190 HIS C 276 FQH C 403
SITE 2 AD1 5 HOH C 501
SITE 1 AD2 4 CYS C 234 HIS C 240 CYS C 306 CYS C 308
SITE 1 AD3 14 TYR C 132 ASP C 135 GLU C 169 TYR C 175
SITE 2 AD3 14 TYR C 177 PHE C 185 HIS C 188 GLU C 190
SITE 3 AD3 14 ASP C 191 LYS C 206 TRP C 208 HIS C 276
SITE 4 AD3 14 ZN C 401 HOH C 501
SITE 1 AD4 4 ALA C 12 ARG C 13 PHE C 257 HOH C 543
SITE 1 AD5 2 ARG C 294 PHE C 324
SITE 1 AD6 1 HOH C 592
SITE 1 AD7 5 HIS D 188 GLU D 190 HIS D 276 FQH D 403
SITE 2 AD7 5 HOH D 506
SITE 1 AD8 4 CYS D 234 HIS D 240 CYS D 306 CYS D 308
SITE 1 AD9 11 TYR D 132 ASP D 135 TYR D 177 PHE D 185
SITE 2 AD9 11 HIS D 188 GLU D 190 LYS D 206 TRP D 208
SITE 3 AD9 11 HIS D 276 ZN D 401 HOH D 506
SITE 1 AE1 6 ASP D 193 LYS D 217 TYR D 273 TYR D 299
SITE 2 AE1 6 GLN D 302 HIS D 343
CRYST1 57.516 101.374 142.544 90.00 99.50 90.00 P 1 21 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 0.017386 0.000000 0.002909 0.00000
SCALE2 0.000000 0.009864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007113 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
