HEADER OXIDOREDUCTASE 23-JUL-18 6H4Y
TITLE CRYSTAL STRUCTURE OF HUMAN KDM4A IN COMPLEX WITH COMPOUND 17E
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 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 6H4Y 1 LINK
REVDAT 1 12-JUN-19 6H4Y 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. 2.38 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) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 65150
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780
REMARK 3 FREE R VALUE TEST SET COUNT : 3112
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 : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1303
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2188
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1245
REMARK 3 BIN R VALUE (WORKING SET) : 0.2182
REMARK 3 BIN FREE R VALUE : 0.2313
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.45
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 10697
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 495
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 70.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.37780
REMARK 3 B22 (A**2) : 0.65520
REMARK 3 B33 (A**2) : 0.72260
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.53790
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.280
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.308
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.204
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.314
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.207
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 : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 11211 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 15255 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3588 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1962 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 11211 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1409 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 5 ; 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 : 12978 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.23
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.09
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|8 - 70}
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9522 -4.5579 -55.9648
REMARK 3 T TENSOR
REMARK 3 T11: -0.0073 T22: -0.1370
REMARK 3 T33: -0.0663 T12: -0.0949
REMARK 3 T13: 0.0835 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 1.9638 L22: 6.4635
REMARK 3 L33: 2.4248 L12: 0.4358
REMARK 3 L13: -0.2241 L23: -2.7958
REMARK 3 S TENSOR
REMARK 3 S11: 0.2194 S12: -0.1058 S13: 0.4288
REMARK 3 S21: 0.3581 S22: -0.1874 S23: -0.3768
REMARK 3 S31: -0.5052 S32: 0.2882 S33: -0.0319
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|71 - 124}
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6231 -26.8375 -61.2965
REMARK 3 T TENSOR
REMARK 3 T11: -0.0501 T22: -0.1138
REMARK 3 T33: -0.0668 T12: 0.0518
REMARK 3 T13: -0.0209 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 3.5852 L22: 3.1067
REMARK 3 L33: 3.5179 L12: 0.1429
REMARK 3 L13: 0.8219 L23: -1.6585
REMARK 3 S TENSOR
REMARK 3 S11: 0.2290 S12: 0.3296 S13: -0.0911
REMARK 3 S21: -0.3939 S22: -0.0926 S23: 0.0000
REMARK 3 S31: 0.1375 S32: 0.2114 S33: -0.1364
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|125 - 291}
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5068 -12.0513 -56.2138
REMARK 3 T TENSOR
REMARK 3 T11: -0.0355 T22: -0.1644
REMARK 3 T33: -0.0861 T12: 0.0429
REMARK 3 T13: 0.1101 T23: 0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 3.0888 L22: 2.3518
REMARK 3 L33: 1.9573 L12: 0.3007
REMARK 3 L13: -0.3726 L23: -1.0338
REMARK 3 S TENSOR
REMARK 3 S11: 0.2500 S12: -0.1266 S13: 0.4102
REMARK 3 S21: 0.2877 S22: 0.0519 S23: 0.1881
REMARK 3 S31: -0.4395 S32: -0.0267 S33: -0.3019
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|292 - 353}
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9066 4.7050 -47.0103
REMARK 3 T TENSOR
REMARK 3 T11: 0.2081 T22: -0.2849
REMARK 3 T33: -0.0877 T12: 0.1723
REMARK 3 T13: 0.2121 T23: -0.1079
REMARK 3 L TENSOR
REMARK 3 L11: 2.1194 L22: 5.4886
REMARK 3 L33: 3.1911 L12: -2.3236
REMARK 3 L13: -0.2252 L23: 2.3052
REMARK 3 S TENSOR
REMARK 3 S11: 0.0143 S12: -0.4885 S13: 0.4946
REMARK 3 S21: 0.3724 S22: -0.0179 S23: 0.1652
REMARK 3 S31: -0.5430 S32: -0.2952 S33: 0.0035
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {B|6 - 293}
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5897 -50.8301 -14.4466
REMARK 3 T TENSOR
REMARK 3 T11: -0.0770 T22: -0.0730
REMARK 3 T33: -0.1195 T12: -0.0358
REMARK 3 T13: -0.0098 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 2.0310 L22: 1.4676
REMARK 3 L33: 1.8496 L12: -0.1213
REMARK 3 L13: 0.3302 L23: 0.0145
REMARK 3 S TENSOR
REMARK 3 S11: 0.0879 S12: -0.0586 S13: -0.0190
REMARK 3 S21: 0.0529 S22: -0.0315 S23: 0.1705
REMARK 3 S31: -0.0032 S32: -0.2231 S33: -0.0565
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {B|294 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7936 -34.0219 -27.6061
REMARK 3 T TENSOR
REMARK 3 T11: 0.0129 T22: -0.0589
REMARK 3 T33: -0.0665 T12: -0.0558
REMARK 3 T13: -0.0006 T23: 0.0671
REMARK 3 L TENSOR
REMARK 3 L11: 1.7488 L22: 0.0000
REMARK 3 L33: 5.0857 L12: 1.8121
REMARK 3 L13: 0.1022 L23: -2.6462
REMARK 3 S TENSOR
REMARK 3 S11: 0.1655 S12: 0.3472 S13: 0.2676
REMARK 3 S21: -0.0192 S22: -0.0927 S23: 0.0540
REMARK 3 S31: -0.4268 S32: 0.3777 S33: -0.0728
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {C|10 - 70}
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1685 -56.4849 -52.9129
REMARK 3 T TENSOR
REMARK 3 T11: -0.0379 T22: -0.0294
REMARK 3 T33: -0.0466 T12: -0.1259
REMARK 3 T13: 0.0606 T23: -0.1007
REMARK 3 L TENSOR
REMARK 3 L11: 1.4662 L22: 4.2001
REMARK 3 L33: 2.2551 L12: -0.6520
REMARK 3 L13: -0.0986 L23: 1.4459
REMARK 3 S TENSOR
REMARK 3 S11: -0.1740 S12: -0.0298 S13: -0.3394
REMARK 3 S21: 0.3542 S22: 0.0716 S23: 0.5074
REMARK 3 S31: 0.5035 S32: -0.3485 S33: 0.1024
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {C|71 - 124}
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9657 -34.7527 -60.1794
REMARK 3 T TENSOR
REMARK 3 T11: -0.1731 T22: -0.1466
REMARK 3 T33: -0.0010 T12: 0.0653
REMARK 3 T13: -0.0864 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 5.9809 L22: 2.8408
REMARK 3 L33: 4.4504 L12: 1.0730
REMARK 3 L13: -2.6407 L23: 0.2322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0849 S12: 0.2626 S13: 0.6092
REMARK 3 S21: -0.3122 S22: 0.2049 S23: 0.1207
REMARK 3 S31: -0.4793 S32: -0.3423 S33: -0.2897
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {C|125 - 144}
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0499 -40.5789 -49.7581
REMARK 3 T TENSOR
REMARK 3 T11: -0.0416 T22: 0.0016
REMARK 3 T33: 0.0475 T12: 0.0674
REMARK 3 T13: -0.0302 T23: -0.0826
REMARK 3 L TENSOR
REMARK 3 L11: 2.4981 L22: 1.2929
REMARK 3 L33: 2.4453 L12: 0.0513
REMARK 3 L13: -0.5920 L23: 0.6628
REMARK 3 S TENSOR
REMARK 3 S11: -0.1155 S12: -0.2339 S13: 0.2617
REMARK 3 S21: 0.4633 S22: 0.0063 S23: 0.0161
REMARK 3 S31: 0.2512 S32: -0.1081 S33: 0.1093
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {C|145 - 226}
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6419 -52.3999 -52.1778
REMARK 3 T TENSOR
REMARK 3 T11: -0.0272 T22: -0.0973
REMARK 3 T33: -0.1533 T12: 0.0251
REMARK 3 T13: -0.0572 T23: -0.0630
REMARK 3 L TENSOR
REMARK 3 L11: 3.7287 L22: 3.0932
REMARK 3 L33: 1.5618 L12: 0.4065
REMARK 3 L13: -0.8316 L23: 0.5836
REMARK 3 S TENSOR
REMARK 3 S11: -0.0824 S12: -0.2544 S13: -0.1865
REMARK 3 S21: 0.5364 S22: 0.0014 S23: -0.1381
REMARK 3 S31: 0.5269 S32: -0.0436 S33: 0.0810
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {C|227 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5361 -58.3276 -54.1635
REMARK 3 T TENSOR
REMARK 3 T11: -0.0620 T22: -0.1954
REMARK 3 T33: -0.1355 T12: 0.0940
REMARK 3 T13: -0.0739 T23: -0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 3.4134 L22: 3.6329
REMARK 3 L33: 1.4768 L12: -0.1367
REMARK 3 L13: -0.7467 L23: 0.4814
REMARK 3 S TENSOR
REMARK 3 S11: -0.3150 S12: -0.3270 S13: -0.5163
REMARK 3 S21: 0.5932 S22: 0.2160 S23: -0.4520
REMARK 3 S31: 0.4753 S32: 0.1392 S33: 0.0990
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {D|10 - 36}
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2519 -1.3420 -12.5762
REMARK 3 T TENSOR
REMARK 3 T11: 0.0986 T22: -0.0268
REMARK 3 T33: -0.1092 T12: 0.1628
REMARK 3 T13: 0.0156 T23: -0.0735
REMARK 3 L TENSOR
REMARK 3 L11: -0.0656 L22: 3.6093
REMARK 3 L33: 2.9142 L12: -0.3377
REMARK 3 L13: 2.5638 L23: 0.0802
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: 0.0241 S13: -0.4258
REMARK 3 S21: -0.2293 S22: 0.1662 S23: -0.1137
REMARK 3 S31: 0.3790 S32: 0.2669 S33: -0.1774
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: {D|37 - 70}
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2097 12.7040 -19.6427
REMARK 3 T TENSOR
REMARK 3 T11: -0.0305 T22: 0.1408
REMARK 3 T33: -0.1652 T12: -0.0057
REMARK 3 T13: 0.0568 T23: 0.0784
REMARK 3 L TENSOR
REMARK 3 L11: 0.7804 L22: 2.8414
REMARK 3 L33: 1.5900 L12: -0.6794
REMARK 3 L13: 0.5409 L23: -0.5357
REMARK 3 S TENSOR
REMARK 3 S11: -0.0880 S12: 0.4572 S13: 0.0275
REMARK 3 S21: -0.3091 S22: 0.1135 S23: -0.3709
REMARK 3 S31: 0.1799 S32: 0.5622 S33: -0.0254
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: {D|71 - 124}
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1174 28.2517 -10.9928
REMARK 3 T TENSOR
REMARK 3 T11: -0.0441 T22: -0.1962
REMARK 3 T33: -0.0823 T12: -0.0972
REMARK 3 T13: -0.0583 T23: 0.0525
REMARK 3 L TENSOR
REMARK 3 L11: 6.3780 L22: 3.1885
REMARK 3 L33: 6.9462 L12: -0.0787
REMARK 3 L13: -2.1586 L23: -0.6792
REMARK 3 S TENSOR
REMARK 3 S11: -0.0376 S12: 0.1662 S13: 0.5819
REMARK 3 S21: 0.1777 S22: 0.3249 S23: -0.0035
REMARK 3 S31: -0.4941 S32: 0.2876 S33: -0.2873
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: {D|125 - 293}
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9941 12.6541 -14.6383
REMARK 3 T TENSOR
REMARK 3 T11: -0.0445 T22: -0.1013
REMARK 3 T33: -0.2080 T12: -0.0605
REMARK 3 T13: -0.0734 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 2.5696 L22: 2.8709
REMARK 3 L33: 3.0949 L12: -0.3691
REMARK 3 L13: -0.3512 L23: -0.5088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0940 S12: 0.2625 S13: -0.1686
REMARK 3 S21: -0.3628 S22: 0.1960 S23: 0.2944
REMARK 3 S31: 0.4147 S32: 0.0537 S33: -0.1020
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: {D|294 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2675 -5.3721 -19.7517
REMARK 3 T TENSOR
REMARK 3 T11: 0.1735 T22: -0.2037
REMARK 3 T33: 0.0337 T12: -0.1407
REMARK 3 T13: -0.1366 T23: -0.0800
REMARK 3 L TENSOR
REMARK 3 L11: 1.4700 L22: 0.0000
REMARK 3 L33: 2.1133 L12: 2.3931
REMARK 3 L13: -0.3311 L23: 3.3150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0843 S12: 0.5985 S13: -0.5255
REMARK 3 S21: -0.4374 S22: 0.0532 S23: 0.3603
REMARK 3 S31: 0.5253 S32: -0.2768 S33: 0.0311
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6H4Y 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_1200010446.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-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 : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65181
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
REMARK 200 RESOLUTION RANGE LOW (A) : 100.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.24900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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 (%): 50.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
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 50.38000
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 LEU A 354
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 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 GLU B 169
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 GLY C 165
REMARK 465 ILE C 166
REMARK 465 THR C 167
REMARK 465 ILE C 168
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 GLU D 4
REMARK 465 SER D 5
REMARK 465 GLU D 6
REMARK 465 THR D 7
REMARK 465 LEU D 8
REMARK 465 ASN D 9
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 LYS D 310
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 CG CD1 CD2
REMARK 470 ARG A 13 NH1 NH2
REMARK 470 GLU A 22 CG CD OE1 OE2
REMARK 470 ARG A 25 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 29 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 31 CD1
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 GLU A 52 OE2
REMARK 470 LYS A 54 CD CE NZ
REMARK 470 ILE A 71 CD1
REMARK 470 SER A 79 OG
REMARK 470 LYS A 89 NZ
REMARK 470 LYS A 90 CD CE NZ
REMARK 470 LYS A 99 NZ
REMARK 470 LYS A 105 NZ
REMARK 470 ARG A 110 CD NE CZ NH1 NH2
REMARK 470 SER A 112 OG
REMARK 470 GLU A 113 CD OE1 OE2
REMARK 470 LYS A 120 NZ
REMARK 470 LYS A 123 CE NZ
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 ARG A 154 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 LYS A 224 CD CE NZ
REMARK 470 GLN A 232 CD OE1 NE2
REMARK 470 SER A 233 OG
REMARK 470 GLU A 235 CG CD OE1 OE2
REMARK 470 LYS A 241 NZ
REMARK 470 LYS A 251 CE NZ
REMARK 470 LYS A 252 NZ
REMARK 470 ARG A 294 NE CZ NH1 NH2
REMARK 470 ILE A 297 CD1
REMARK 470 LYS A 301 CE NZ
REMARK 470 LYS A 310 NZ
REMARK 470 MET A 312 CG SD CE
REMARK 470 LYS A 314 CG CD CE NZ
REMARK 470 ILE A 315 CD1
REMARK 470 VAL A 319 CG1
REMARK 470 ARG A 322 CZ NH1 NH2
REMARK 470 LYS A 323 CE NZ
REMARK 470 GLN A 325 NE2
REMARK 470 GLU A 327 OE2
REMARK 470 ARG A 328 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 329 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 330 CG CD CE NZ
REMARK 470 LEU A 331 CG CD1 CD2
REMARK 470 LYS A 333 CG CD CE NZ
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 ASN A 338 CG OD1 ND2
REMARK 470 GLU A 352 OE1
REMARK 470 GLU B 6 CG CD OE1 OE2
REMARK 470 THR B 7 OG1 CG2
REMARK 470 ARG B 13 CD NE CZ NH1 NH2
REMARK 470 GLU B 22 CG CD OE1 OE2
REMARK 470 ARG B 29 NH1 NH2
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 LYS B 54 CD CE NZ
REMARK 470 ILE B 62 CD1
REMARK 470 LEU B 65 CD1 CD2
REMARK 470 ILE B 71 CD1
REMARK 470 ILE B 87 CD1
REMARK 470 LYS B 89 NZ
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 LYS B 99 NZ
REMARK 470 ILE B 100 CD1
REMARK 470 ARG B 110 CZ NH1 NH2
REMARK 470 SER B 112 OG
REMARK 470 LYS B 120 NZ
REMARK 470 LYS B 143 CD CE NZ
REMARK 470 GLU B 161 OE1 OE2
REMARK 470 LYS B 224 CG CD CE NZ
REMARK 470 GLN B 232 CG CD OE1 NE2
REMARK 470 ILE B 269 CD1
REMARK 470 LYS B 310 CD CE NZ
REMARK 470 ASP B 311 C O
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 CD CE NZ
REMARK 470 LYS B 336 CG CD CE NZ
REMARK 470 LEU B 354 CG CD1 CD2
REMARK 470 GLU C 22 CD OE1 OE2
REMARK 470 LYS C 51 CG CD CE NZ
REMARK 470 LYS C 54 CD CE NZ
REMARK 470 ILE C 71 CD1
REMARK 470 LYS C 89 CD CE NZ
REMARK 470 LYS C 90 CG CD CE NZ
REMARK 470 LYS C 99 NZ
REMARK 470 LYS C 105 CE NZ
REMARK 470 ARG C 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 113 OE1 OE2
REMARK 470 LYS C 120 NZ
REMARK 470 LYS C 123 CE NZ
REMARK 470 LYS C 143 CG CD CE NZ
REMARK 470 ARG C 154 NE CZ NH1 NH2
REMARK 470 LEU C 159 CD1
REMARK 470 GLU C 161 CD OE1 OE2
REMARK 470 LYS C 162 CD CE NZ
REMARK 470 SER C 164 OG
REMARK 470 GLU C 169 CG CD OE1 OE2
REMARK 470 ARG C 218 NH1 NH2
REMARK 470 LEU C 222 CD1
REMARK 470 LYS C 224 CE NZ
REMARK 470 GLN C 232 CG CD OE1 NE2
REMARK 470 GLU C 235 CG CD OE1 OE2
REMARK 470 LYS C 251 CD CE NZ
REMARK 470 LYS C 252 NZ
REMARK 470 LYS C 259 NZ
REMARK 470 ARG C 294 CD NE CZ NH1 NH2
REMARK 470 ILE C 297 CD1
REMARK 470 ARG C 309 C O CZ NH1 NH2
REMARK 470 MET C 312 CG SD CE
REMARK 470 LYS C 314 CG CD CE NZ
REMARK 470 SER C 316 OG
REMARK 470 ASP C 318 CG OD1 OD2
REMARK 470 ARG C 322 NH1 NH2
REMARK 470 LYS C 323 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 354 CD1 CD2
REMARK 470 GLU D 22 CG CD OE1 OE2
REMARK 470 ILE D 31 CD1
REMARK 470 LYS D 51 CG CD CE NZ
REMARK 470 LYS D 54 CG CD CE NZ
REMARK 470 ASP D 60 OD1 OD2
REMARK 470 ILE D 71 CD1
REMARK 470 LYS D 89 CE NZ
REMARK 470 LYS D 90 CD CE NZ
REMARK 470 LYS D 99 CD CE NZ
REMARK 470 ILE D 100 CD1
REMARK 470 ARG D 110 CD NE CZ NH1 NH2
REMARK 470 SER D 112 OG
REMARK 470 GLU D 113 CG CD OE1 OE2
REMARK 470 GLU D 115 CG CD OE1 OE2
REMARK 470 LYS D 123 NZ
REMARK 470 ILE D 131 CD1
REMARK 470 LYS D 143 CG CD CE NZ
REMARK 470 ARG D 154 CD NE CZ NH1 NH2
REMARK 470 ILE D 156 CD1
REMARK 470 LEU D 159 CD1 CD2
REMARK 470 LYS D 162 CD CE NZ
REMARK 470 GLY D 170 N
REMARK 470 VAL D 171 CG1 CG2
REMARK 470 ASN D 172 OD1 ND2
REMARK 470 ARG D 218 NH1 NH2
REMARK 470 LEU D 222 CD1
REMARK 470 LYS D 224 CG CD CE NZ
REMARK 470 GLN D 232 CG CD OE1 NE2
REMARK 470 GLU D 235 CG CD OE1 OE2
REMARK 470 LYS D 241 NZ
REMARK 470 LYS D 251 CD CE NZ
REMARK 470 LYS D 252 NZ
REMARK 470 ILE D 269 CD1
REMARK 470 ARG D 294 CZ NH1 NH2
REMARK 470 GLU D 298 CG CD OE1 OE2
REMARK 470 LYS D 301 CG CD CE NZ
REMARK 470 ARG D 309 C O
REMARK 470 ASP D 311 CG OD1 OD2
REMARK 470 MET D 312 CG SD CE
REMARK 470 LYS D 314 NZ
REMARK 470 ILE D 315 CD1
REMARK 470 SER D 316 OG
REMARK 470 LYS D 323 CD CE NZ
REMARK 470 GLU D 327 OE1 OE2
REMARK 470 ARG D 328 NE CZ NH1 NH2
REMARK 470 LYS D 330 CG CD CE NZ
REMARK 470 LEU D 331 CG CD1 CD2
REMARK 470 LYS D 333 CD CE NZ
REMARK 470 LYS D 336 CG CD CE NZ
REMARK 470 ASN D 338 CG OD1 ND2
REMARK 470 VAL D 340 CG2
REMARK 470 ILE D 341 CD1
REMARK 470 LEU D 354 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 -73.72 -91.61
REMARK 500 ASN A 128 67.50 38.96
REMARK 500 ARG A 152 67.74 -150.37
REMARK 500 PHE A 227 70.28 -119.51
REMARK 500 ALA A 236 50.96 -95.25
REMARK 500 SER B 112 -73.22 -91.55
REMARK 500 ASN B 128 67.79 38.45
REMARK 500 ARG B 152 66.63 -152.77
REMARK 500 ALA B 236 53.93 -94.32
REMARK 500 SER C 112 -73.48 -91.82
REMARK 500 ASN C 128 66.59 39.92
REMARK 500 ALA C 236 52.27 -94.26
REMARK 500 SER D 112 -73.09 -91.46
REMARK 500 ASN D 128 63.41 39.50
REMARK 500 ARG D 152 69.68 -151.06
REMARK 500 PHE D 227 69.64 -119.05
REMARK 500 ALA D 236 52.17 -94.44
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 630 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH C 609 DISTANCE = 6.27 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 FO8 A 403
REMARK 610 FO8 B 403
REMARK 610 FO8 C 403
REMARK 610 FO8 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 104.6
REMARK 620 3 HIS A 276 NE2 88.4 84.6
REMARK 620 4 FO8 A 403 N2 103.4 150.4 105.8
REMARK 620 5 FO8 A 403 N6 82.2 97.6 170.5 76.8
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 113.7
REMARK 620 3 CYS A 306 SG 113.9 109.0
REMARK 620 4 CYS A 308 SG 114.4 91.1 112.5
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 106.3
REMARK 620 3 HIS B 276 NE2 89.7 85.7
REMARK 620 4 FO8 B 403 N6 82.0 98.6 171.5
REMARK 620 5 FO8 B 403 N2 102.8 149.2 104.4 75.6
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 111.9
REMARK 620 3 CYS B 306 SG 112.2 110.5
REMARK 620 4 CYS B 308 SG 113.6 93.8 113.5
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 104.9
REMARK 620 3 HIS C 276 NE2 88.9 84.2
REMARK 620 4 FO8 C 403 N2 105.8 147.4 107.0
REMARK 620 5 FO8 C 403 N6 82.9 96.3 171.6 77.0
REMARK 620 N 1 2 3 4
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 119.2
REMARK 620 3 CYS C 306 SG 114.2 106.1
REMARK 620 4 CYS C 308 SG 116.6 89.0 108.7
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 106.5
REMARK 620 3 HIS D 276 NE2 87.5 83.6
REMARK 620 4 FO8 D 403 N6 83.6 99.9 171.0
REMARK 620 5 FO8 D 403 N2 103.8 149.2 103.5 77.8
REMARK 620 N 1 2 3 4
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 111.6
REMARK 620 3 CYS D 306 SG 107.2 104.1
REMARK 620 4 CYS D 308 SG 120.7 95.0 116.5
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 FO8 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FO8 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 405
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 FO8 C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS 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 FO8 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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS D 405
DBREF 6H4Y A 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 6H4Y B 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 6H4Y C 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 6H4Y D 1 359 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 6H4Y SER A 0 UNP O75164 EXPRESSION TAG
SEQADV 6H4Y SER B 0 UNP O75164 EXPRESSION TAG
SEQADV 6H4Y SER C 0 UNP O75164 EXPRESSION TAG
SEQADV 6H4Y 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 FO8 A 403 19
HET CL A 404 1
HET ZN B 401 1
HET ZN B 402 1
HET FO8 B 403 30
HET CL B 404 1
HET DMS B 405 4
HET ZN C 401 1
HET ZN C 402 1
HET FO8 C 403 19
HET CL C 404 1
HET GOL C 405 6
HET DMS C 406 4
HET ZN D 401 1
HET ZN D 402 1
HET FO8 D 403 25
HET DMS D 404 4
HET DMS D 405 4
HETNAM ZN ZINC ION
HETNAM FO8 8-[4-[2-[4-[4-(2-MORPHOLIN-4-YLETHYL)PHENYL]PIPERIDIN-
HETNAM 2 FO8 1-YL]ETHYL]PYRAZOL-1-YL]-3~{H}-PYRIDO[3,4-D]PYRIMIDIN-
HETNAM 3 FO8 4-ONE
HETNAM CL CHLORIDE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ZN 8(ZN 2+)
FORMUL 7 FO8 4(C29 H35 N7 O2)
FORMUL 8 CL 3(CL 1-)
FORMUL 13 DMS 4(C2 H6 O S)
FORMUL 18 GOL C3 H8 O3
FORMUL 25 HOH *495(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 GLU A 161 5 7
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 ALA A 303 1 9
HELIX 15 AB6 MET A 317 GLN A 325 1 9
HELIX 16 AB7 ARG A 328 ALA A 334 1 7
HELIX 17 AB8 THR A 347 ALA A 351 5 5
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 THR B 155 VAL B 160 5 6
HELIX 24 AC6 GLU B 190 LEU B 194 5 5
HELIX 25 AC7 PRO B 212 GLU B 214 5 3
HELIX 26 AC8 HIS B 215 PHE B 227 1 13
HELIX 27 AC9 PHE B 227 CYS B 234 1 8
HELIX 28 AD1 ALA B 236 LYS B 241 5 6
HELIX 29 AD2 SER B 246 TYR B 253 1 8
HELIX 30 AD3 ARG B 295 ALA B 303 1 9
HELIX 31 AD4 MET B 317 GLN B 325 1 9
HELIX 32 AD5 ARG B 328 ALA B 334 1 7
HELIX 33 AD6 THR B 347 PHE B 353 5 7
HELIX 34 AD7 THR C 20 ARG C 25 1 6
HELIX 35 AD8 ASN C 26 GLN C 37 1 12
HELIX 36 AD9 GLY C 38 ALA C 42 5 5
HELIX 37 AE1 VAL C 94 SER C 103 1 10
HELIX 38 AE2 GLU C 113 LEU C 125 1 13
HELIX 39 AE3 ASN C 149 LEU C 153 5 5
HELIX 40 AE4 THR C 155 LEU C 157 5 3
HELIX 41 AE5 ASP C 158 SER C 164 1 7
HELIX 42 AE6 GLU C 190 LEU C 194 5 5
HELIX 43 AE7 PRO C 212 GLU C 214 5 3
HELIX 44 AE8 HIS C 215 PHE C 227 1 13
HELIX 45 AE9 PHE C 227 CYS C 234 1 8
HELIX 46 AF1 ALA C 236 LYS C 241 5 6
HELIX 47 AF2 SER C 246 TYR C 253 1 8
HELIX 48 AF3 ARG C 295 ALA C 303 1 9
HELIX 49 AF4 MET C 317 GLN C 325 1 9
HELIX 50 AF5 ARG C 328 ALA C 334 1 7
HELIX 51 AF6 THR C 347 GLU C 352 5 6
HELIX 52 AF7 THR D 20 ARG D 25 1 6
HELIX 53 AF8 ASN D 26 GLN D 37 1 12
HELIX 54 AF9 GLY D 38 ALA D 42 5 5
HELIX 55 AG1 VAL D 94 ASN D 102 1 9
HELIX 56 AG2 GLU D 113 LEU D 125 1 13
HELIX 57 AG3 ASN D 149 LEU D 153 5 5
HELIX 58 AG4 THR D 155 LEU D 157 5 3
HELIX 59 AG5 ASP D 158 SER D 164 1 7
HELIX 60 AG6 GLU D 190 LEU D 194 5 5
HELIX 61 AG7 PRO D 212 GLU D 214 5 3
HELIX 62 AG8 HIS D 215 PHE D 227 1 13
HELIX 63 AG9 PHE D 227 CYS D 234 1 8
HELIX 64 AH1 ALA D 236 LYS D 241 5 6
HELIX 65 AH2 SER D 246 TYR D 253 1 8
HELIX 66 AH3 ARG D 295 ALA D 303 1 9
HELIX 67 AH4 MET D 317 GLN D 325 1 9
HELIX 68 AH5 ARG D 328 ALA D 334 1 7
HELIX 69 AH6 THR D 347 PHE D 353 5 7
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 ASN A 198 O MET A 268
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 GLN A 262 N LYS A 206
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 MET B 15
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 HIS B 276 N HIS B 188
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 ILE C 269 N ALA C 45
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 175 O SER C 288
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 HIS C 276 N HIS C 188
SHEET 3 AA9 4 LYS C 206 VAL C 211 -1 N SER C 207 O PHE C 279
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 ILE D 269 N ALA D 45
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 2.14
LINK OE2 GLU A 190 ZN ZN A 401 1555 1555 2.12
LINK SG CYS A 234 ZN ZN A 402 1555 1555 2.24
LINK NE2 HIS A 240 ZN ZN A 402 1555 1555 2.12
LINK NE2 HIS A 276 ZN ZN A 401 1555 1555 2.27
LINK SG CYS A 306 ZN ZN A 402 1555 1555 2.17
LINK SG CYS A 308 ZN ZN A 402 1555 1555 2.43
LINK ZN ZN A 401 N2 FO8 A 403 1555 1555 2.06
LINK ZN ZN A 401 N6 FO8 A 403 1555 1555 2.26
LINK NE2 HIS B 188 ZN ZN B 401 1555 1555 2.11
LINK OE2 GLU B 190 ZN ZN B 401 1555 1555 2.10
LINK SG CYS B 234 ZN ZN B 402 1555 1555 2.30
LINK NE2 HIS B 240 ZN ZN B 402 1555 1555 2.06
LINK NE2 HIS B 276 ZN ZN B 401 1555 1555 2.25
LINK SG CYS B 306 ZN ZN B 402 1555 1555 2.20
LINK SG CYS B 308 ZN ZN B 402 1555 1555 2.38
LINK ZN ZN B 401 N6 FO8 B 403 1555 1555 2.26
LINK ZN ZN B 401 N2 FO8 B 403 1555 1555 2.10
LINK NE2 HIS C 188 ZN ZN C 401 1555 1555 2.11
LINK OE2 GLU C 190 ZN ZN C 401 1555 1555 2.16
LINK SG CYS C 234 ZN ZN C 402 1555 1555 2.16
LINK NE2 HIS C 240 ZN ZN C 402 1555 1555 2.07
LINK NE2 HIS C 276 ZN ZN C 401 1555 1555 2.30
LINK SG CYS C 306 ZN ZN C 402 1555 1555 2.21
LINK SG CYS C 308 ZN ZN C 402 1555 1555 2.49
LINK ZN ZN C 401 N2 FO8 C 403 1555 1555 2.02
LINK ZN ZN C 401 N6 FO8 C 403 1555 1555 2.25
LINK NE2 HIS D 188 ZN ZN D 401 1555 1555 2.10
LINK OE2 GLU D 190 ZN ZN D 401 1555 1555 2.09
LINK SG CYS D 234 ZN ZN D 402 1555 1555 2.30
LINK NE2 HIS D 240 ZN ZN D 402 1555 1555 2.11
LINK NE2 HIS D 276 ZN ZN D 401 1555 1555 2.37
LINK SG CYS D 306 ZN ZN D 402 1555 1555 2.24
LINK SG CYS D 308 ZN ZN D 402 1555 1555 2.27
LINK ZN ZN D 401 N6 FO8 D 403 1555 1555 2.22
LINK ZN ZN D 401 N2 FO8 D 403 1555 1555 2.06
SITE 1 AC1 4 HIS A 188 GLU A 190 HIS A 276 FO8 A 403
SITE 1 AC2 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC3 9 TYR A 132 TYR A 177 PHE A 185 HIS A 188
SITE 2 AC3 9 GLU A 190 LYS A 206 TRP A 208 HIS A 276
SITE 3 AC3 9 ZN A 401
SITE 1 AC4 1 HOH A 624
SITE 1 AC5 4 HIS B 188 GLU B 190 HIS B 276 FO8 B 403
SITE 1 AC6 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC7 11 TYR B 132 ASP B 135 TYR B 175 TYR B 177
SITE 2 AC7 11 PHE B 185 HIS B 188 GLU B 190 LYS B 206
SITE 3 AC7 11 TRP B 208 HIS B 276 ZN B 401
SITE 1 AC8 1 ARG B 98
SITE 1 AC9 1 TRP B 332
SITE 1 AD1 4 HIS C 188 GLU C 190 HIS C 276 FO8 C 403
SITE 1 AD2 4 CYS C 234 HIS C 240 CYS C 306 CYS C 308
SITE 1 AD3 9 TYR C 132 TYR C 177 PHE C 185 HIS C 188
SITE 2 AD3 9 GLU C 190 LYS C 206 TRP C 208 HIS C 276
SITE 3 AD3 9 ZN C 401
SITE 1 AD4 2 ARG C 98 HOH C 604
SITE 1 AD5 10 VAL A 75 THR A 76 GLY A 77 THR A 126
SITE 2 AD5 10 PHE A 127 VAL C 75 THR C 76 GLY C 77
SITE 3 AD5 10 THR C 126 PHE C 127
SITE 1 AD6 4 GLU C 118 ARG C 119 TRP C 122 LEU C 248
SITE 1 AD7 4 HIS D 188 GLU D 190 HIS D 276 FO8 D 403
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 175 TYR D 177
SITE 2 AD9 11 PHE D 185 HIS D 188 GLU D 190 LYS D 206
SITE 3 AD9 11 TRP D 208 HIS D 276 ZN D 401
SITE 1 AE1 2 ASP D 311 MET D 312
SITE 1 AE2 4 ASP D 193 LYS D 217 TYR D 273 HIS D 343
CRYST1 58.050 100.760 143.170 90.00 99.56 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 0.017227 0.000000 0.002901 0.00000
SCALE2 0.000000 0.009925 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007083 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
