HEADER OXIDOREDUCTASE 23-OCT-09 2WWJ
TITLE STRUCTURE OF JMJD2A COMPLEXED WITH INHIBITOR 10A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 7-353;
COMPND 5 SYNONYM: JUMONJI DOMAIN CONTAINING PROTEIN 2A, JMJC DOMAIN-CONTAINING
COMPND 6 HISTONE DEMETHYLATION PROTEIN 3A;
COMPND 7 EC: 1.14.11.27;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PNIC28BSA4
KEYWDS CHROMATIN REGULATOR, DOUBLE-STRANDED BETA HELIX, OXIDOREDUCTASE,
KEYWDS 2 TRANSCRIPTION, OXYGENASE, HOST-VIRUS INTERACTION, TRANSCRIPTION
KEYWDS 3 REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.R.ROSE,I.J.CLIFTON,U.OPPERMANN,M.A.MCDONOUGH,C.J.SCHOFIELD
REVDAT 3 20-DEC-23 2WWJ 1 REMARK LINK
REVDAT 2 07-MAR-18 2WWJ 1 SOURCE AUTHOR JRNL
REVDAT 1 09-MAR-10 2WWJ 0
JRNL AUTH N.R.ROSE,E.C.WOON,G.L.KINGHAM,O.N.KING,J.MECINOVIC,
JRNL AUTH 2 I.J.CLIFTON,S.S.NG,J.TALIB-HARDY,U.OPPERMANN,M.A.MCDONOUGH,
JRNL AUTH 3 C.J.SCHOFIELD
JRNL TITL SELECTIVE INHIBITORS OF THE JMJD2 HISTONE DEMETHYLASES:
JRNL TITL 2 COMBINED NONDENATURING MASS SPECTROMETRIC SCREENING AND
JRNL TITL 3 CRYSTALLOGRAPHIC APPROACHES.
JRNL REF J. MED. CHEM. V. 53 1810 2010
JRNL REFN ISSN 1520-4804
JRNL PMID 20088513
JRNL DOI 10.1021/JM901680B
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 26102
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1191
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1874
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5697
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.58000
REMARK 3 B22 (A**2) : -0.27000
REMARK 3 B33 (A**2) : 0.85000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.726
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.311
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.504
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5944 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8036 ; 1.649 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 695 ; 6.690 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 287 ;33.143 ;23.171
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 999 ;18.486 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;19.524 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 816 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4603 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1504 ; 0.746 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2435 ; 1.489 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1049 ; 2.561 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1022 ; 4.097 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 8 A 53
REMARK 3 ORIGIN FOR THE GROUP (A): -42.1840 -26.4630 -32.5840
REMARK 3 T TENSOR
REMARK 3 T11: 0.0709 T22: 0.1225
REMARK 3 T33: 0.1295 T12: 0.0052
REMARK 3 T13: -0.0465 T23: -0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 3.0158 L22: 2.0563
REMARK 3 L33: 2.8023 L12: -0.6387
REMARK 3 L13: -0.1386 L23: 0.8457
REMARK 3 S TENSOR
REMARK 3 S11: 0.0385 S12: 0.3056 S13: -0.0432
REMARK 3 S21: -0.3007 S22: 0.0059 S23: 0.1709
REMARK 3 S31: 0.0493 S32: -0.1784 S33: -0.0443
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 54 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3730 -23.4220 -27.7920
REMARK 3 T TENSOR
REMARK 3 T11: 0.0785 T22: 0.1411
REMARK 3 T33: 0.0971 T12: 0.0176
REMARK 3 T13: 0.0385 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.9907 L22: 1.4762
REMARK 3 L33: 1.7979 L12: -0.0307
REMARK 3 L13: 0.1726 L23: -0.9649
REMARK 3 S TENSOR
REMARK 3 S11: 0.0445 S12: 0.3415 S13: 0.0166
REMARK 3 S21: -0.2780 S22: -0.0896 S23: -0.1140
REMARK 3 S31: 0.0266 S32: 0.1846 S33: 0.0450
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 120 A 306
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3240 -22.3240 -21.4010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0308 T22: 0.0561
REMARK 3 T33: 0.0451 T12: -0.0145
REMARK 3 T13: -0.0087 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.4109 L22: 1.0382
REMARK 3 L33: 0.7467 L12: -0.3637
REMARK 3 L13: -0.0786 L23: 0.1187
REMARK 3 S TENSOR
REMARK 3 S11: 0.0172 S12: 0.0819 S13: 0.0477
REMARK 3 S21: -0.0685 S22: -0.0245 S23: 0.0156
REMARK 3 S31: -0.0348 S32: -0.0114 S33: 0.0072
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 307 A 311
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6580 -11.2450 -6.4730
REMARK 3 T TENSOR
REMARK 3 T11: 1.5132 T22: 0.9103
REMARK 3 T33: 0.7353 T12: -0.2342
REMARK 3 T13: 0.4205 T23: 0.4770
REMARK 3 L TENSOR
REMARK 3 L11: 11.5649 L22: 35.6611
REMARK 3 L33: 9.5175 L12: 15.9647
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.3815 S12: 1.2275 S13: 1.5759
REMARK 3 S21: -0.9700 S22: 0.3229 S23: -0.4528
REMARK 3 S31: -0.3055 S32: -0.5784 S33: -0.7045
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 312 A 322
REMARK 3 ORIGIN FOR THE GROUP (A): -41.3260 -7.6240 -12.9420
REMARK 3 T TENSOR
REMARK 3 T11: 0.1766 T22: 0.1010
REMARK 3 T33: 0.1267 T12: 0.0263
REMARK 3 T13: -0.0179 T23: -0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 11.1852 L22: 2.6721
REMARK 3 L33: 4.9440 L12: 2.6074
REMARK 3 L13: -0.7986 L23: 1.0578
REMARK 3 S TENSOR
REMARK 3 S11: -0.1903 S12: -0.4139 S13: 0.4729
REMARK 3 S21: 0.1709 S22: 0.0963 S23: -0.0336
REMARK 3 S31: -0.2243 S32: -0.0729 S33: 0.0941
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 323 A 353
REMARK 3 ORIGIN FOR THE GROUP (A): -51.3830 -16.2130 -13.3850
REMARK 3 T TENSOR
REMARK 3 T11: 0.0225 T22: 0.1399
REMARK 3 T33: 0.1573 T12: -0.0006
REMARK 3 T13: 0.0106 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 1.3655 L22: 4.8375
REMARK 3 L33: 1.6132 L12: -0.7946
REMARK 3 L13: -0.9950 L23: 1.0776
REMARK 3 S TENSOR
REMARK 3 S11: -0.0613 S12: -0.0826 S13: -0.1161
REMARK 3 S21: 0.1535 S22: -0.0173 S23: 0.2182
REMARK 3 S31: 0.1047 S32: -0.1759 S33: 0.0787
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 7 B 109
REMARK 3 ORIGIN FOR THE GROUP (A): -42.2490 -54.5040 -4.7330
REMARK 3 T TENSOR
REMARK 3 T11: 0.1043 T22: 0.0808
REMARK 3 T33: 0.0788 T12: 0.0013
REMARK 3 T13: -0.0166 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 1.4495 L22: 0.9897
REMARK 3 L33: 1.1263 L12: 0.2476
REMARK 3 L13: -0.2571 L23: 0.1339
REMARK 3 S TENSOR
REMARK 3 S11: -0.0533 S12: 0.2450 S13: -0.1589
REMARK 3 S21: -0.1858 S22: 0.0247 S23: -0.0106
REMARK 3 S31: 0.1196 S32: -0.0840 S33: 0.0285
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 110 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8500 -52.5160 -4.1580
REMARK 3 T TENSOR
REMARK 3 T11: 0.1303 T22: 0.1848
REMARK 3 T33: 0.0614 T12: -0.0339
REMARK 3 T13: -0.0596 T23: 0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 3.6289 L22: 3.2404
REMARK 3 L33: 1.8023 L12: -1.3974
REMARK 3 L13: -1.3647 L23: 0.9020
REMARK 3 S TENSOR
REMARK 3 S11: 0.1260 S12: 0.2729 S13: 0.0228
REMARK 3 S21: -0.3665 S22: -0.1217 S23: 0.0281
REMARK 3 S31: -0.0629 S32: -0.0881 S33: -0.0044
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 154 B 163
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7530 -71.4660 2.7460
REMARK 3 T TENSOR
REMARK 3 T11: 0.5845 T22: 0.0453
REMARK 3 T33: 0.2087 T12: 0.0652
REMARK 3 T13: -0.1757 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 16.0708 L22: 15.7009
REMARK 3 L33: 8.2728 L12: 5.1037
REMARK 3 L13: -6.8681 L23: -1.9882
REMARK 3 S TENSOR
REMARK 3 S11: -0.0873 S12: 0.2800 S13: -1.5236
REMARK 3 S21: -0.5834 S22: -0.0934 S23: -0.2042
REMARK 3 S31: 1.6991 S32: 0.0427 S33: 0.1806
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 164 B 220
REMARK 3 ORIGIN FOR THE GROUP (A): -40.0960 -54.8670 2.7380
REMARK 3 T TENSOR
REMARK 3 T11: 0.0566 T22: 0.0555
REMARK 3 T33: 0.0555 T12: -0.0092
REMARK 3 T13: 0.0167 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 2.6417 L22: 0.9159
REMARK 3 L33: 2.4226 L12: -0.3445
REMARK 3 L13: 1.1333 L23: 0.1938
REMARK 3 S TENSOR
REMARK 3 S11: 0.0074 S12: -0.0896 S13: -0.2189
REMARK 3 S21: 0.0622 S22: 0.0211 S23: -0.0426
REMARK 3 S31: 0.2368 S32: 0.0936 S33: -0.0284
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 221 B 235
REMARK 3 ORIGIN FOR THE GROUP (A): -41.7500 -46.5690 22.1830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0311 T22: 0.0932
REMARK 3 T33: 0.0453 T12: 0.0035
REMARK 3 T13: -0.0256 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 8.4258 L22: 20.2434
REMARK 3 L33: 15.3084 L12: 2.0761
REMARK 3 L13: -1.4727 L23: -6.4144
REMARK 3 S TENSOR
REMARK 3 S11: 0.1520 S12: -0.4130 S13: -0.1066
REMARK 3 S21: 0.4280 S22: -0.2153 S23: -0.6147
REMARK 3 S31: -0.2729 S32: 0.6797 S33: 0.0633
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 236 B 306
REMARK 3 ORIGIN FOR THE GROUP (A): -37.2060 -50.9060 5.2070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0575 T22: 0.0750
REMARK 3 T33: 0.0875 T12: -0.0137
REMARK 3 T13: 0.0031 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.9759 L22: 0.9158
REMARK 3 L33: 1.2694 L12: 0.0318
REMARK 3 L13: 0.1844 L23: -0.0124
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: -0.0670 S13: -0.0149
REMARK 3 S21: 0.0269 S22: 0.0108 S23: -0.0734
REMARK 3 S31: 0.0398 S32: 0.0399 S33: -0.0164
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 307 B 311
REMARK 3 ORIGIN FOR THE GROUP (A): -43.8960 -63.5440 20.3120
REMARK 3 T TENSOR
REMARK 3 T11: 0.8905 T22: 0.3985
REMARK 3 T33: 0.9790 T12: 0.0754
REMARK 3 T13: -0.0132 T23: -0.3744
REMARK 3 L TENSOR
REMARK 3 L11: 2.7191 L22: 10.6033
REMARK 3 L33: 4.8038 L12: 3.9785
REMARK 3 L13: -0.4321 L23: -5.3624
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.8025 S13: -1.1467
REMARK 3 S21: -1.2013 S22: 0.6552 S23: -0.6884
REMARK 3 S31: 1.3105 S32: 0.4239 S33: -0.6593
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 312 B 353
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0860 -62.0920 12.1240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0720 T22: 0.1025
REMARK 3 T33: 0.1388 T12: 0.0141
REMARK 3 T13: -0.0073 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 1.9370 L22: 2.4082
REMARK 3 L33: 1.1793 L12: -0.7238
REMARK 3 L13: 1.0234 L23: -0.7782
REMARK 3 S TENSOR
REMARK 3 S11: -0.0242 S12: -0.1500 S13: -0.0407
REMARK 3 S21: 0.1479 S22: -0.0437 S23: -0.2241
REMARK 3 S31: 0.0044 S32: 0.1386 S33: 0.0678
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS
REMARK 4
REMARK 4 2WWJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1290041458.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-09
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) : 0.97860
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27338
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 49.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.640
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.370
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 2OQ6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN STOCK 11MG/ML JMJD2A, 10MM
REMARK 280 HEPES PH7.5, 500MM NACL, 5% GLYCEROL, 0.75MM INHIBITOR 10A.
REMARK 280 RESERVOIR: 0.1M CITRATE PH5.5, 18.5% PEG3350, 4MM NICL2. 1:1
REMARK 280 PROTEIN/RESERVOIR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 50.66500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.48500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.66500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.48500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 7
REMARK 465 THR A 354
REMARK 465 THR B 354
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CE LYS B 143 O HOH B 2031 1.82
REMARK 500 NH1 ARG B 328 OG1 THR B 339 1.89
REMARK 500 NZ LYS B 143 O HOH B 2031 1.91
REMARK 500 O LYS A 251 O HOH A 2052 1.99
REMARK 500 OD2 ASP B 258 O HOH B 2055 2.03
REMARK 500 CE MET B 312 O HOH B 2038 2.05
REMARK 500 N MET A 317 O HOH A 2068 2.07
REMARK 500 NH2 ARG A 328 OG1 THR A 339 2.13
REMARK 500 N ALA B 69 O HOH B 2011 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 112 -93.85 -80.81
REMARK 500 ARG A 152 69.33 -163.91
REMARK 500 ARG A 154 61.02 64.50
REMARK 500 VAL A 171 -60.62 -95.41
REMARK 500 MET A 192 14.74 59.76
REMARK 500 PHE A 202 167.24 174.27
REMARK 500 ALA A 236 48.71 -90.88
REMARK 500 ALA A 334 33.18 -81.56
REMARK 500 GLU A 349 0.10 -66.84
REMARK 500 TYR B 59 50.76 -118.94
REMARK 500 ASP B 61 20.79 -67.29
REMARK 500 ALA B 91 151.66 -49.89
REMARK 500 TYR B 111 155.46 177.88
REMARK 500 SER B 112 -72.88 -98.04
REMARK 500 ARG B 152 67.61 -160.81
REMARK 500 ARG B 154 78.29 36.44
REMARK 500 ILE B 156 12.24 -65.10
REMARK 500 ASP B 158 -37.14 -36.43
REMARK 500 LEU B 159 -5.68 -50.14
REMARK 500 GLU B 161 -66.43 -104.42
REMARK 500 LYS B 162 -30.35 -27.67
REMARK 500 SER B 164 -11.00 -144.59
REMARK 500 VAL B 171 -69.87 -100.42
REMARK 500 MET B 192 19.82 50.77
REMARK 500 CYS B 234 118.04 -161.26
REMARK 500 ALA B 236 37.36 -88.74
REMARK 500 LYS B 310 48.44 -77.90
REMARK 500 ASP B 311 69.75 102.23
REMARK 500 ASP B 318 -51.57 -25.89
REMARK 500 GLU B 349 -6.45 -55.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 501 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 188 NE2
REMARK 620 2 GLU A 190 OE2 98.0
REMARK 620 3 HIS A 276 NE2 91.5 82.0
REMARK 620 4 Y28 A1354 OAW 91.0 165.9 108.6
REMARK 620 5 Y28 A1354 OAX 165.6 94.1 97.9 75.7
REMARK 620 6 HOH A2035 O 90.9 84.4 166.4 84.7 82.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 HIS A 240 NE2 111.2
REMARK 620 3 CYS A 306 SG 119.5 103.7
REMARK 620 4 CYS A 308 SG 117.7 101.4 101.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 501 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 188 NE2
REMARK 620 2 GLU B 190 OE2 107.6
REMARK 620 3 HIS B 276 NE2 90.7 90.9
REMARK 620 4 Y28 B1354 OAW 91.5 157.7 100.4
REMARK 620 5 Y28 B1354 OAX 164.2 87.8 85.6 74.1
REMARK 620 6 HOH B2073 O 93.4 87.7 175.8 79.7 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 234 SG
REMARK 620 2 HIS B 240 NE2 107.6
REMARK 620 3 CYS B 306 SG 120.2 113.1
REMARK 620 4 CYS B 308 SG 104.7 94.2 113.8
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 Y28 A 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y28 B 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GP3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC CORE COMAIN OF JMJD2A
REMARK 900 RELATED ID: 2GFA RELATED DB: PDB
REMARK 900 DOUBLE TUDOR DOMAIN COMPLEX STRUCTURE
REMARK 900 RELATED ID: 2VD7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJD2A COMPLEXED WITH INHIBITOR PYRIDINE-2,4-
REMARK 900 DICARBOXYLIC ACID
REMARK 900 RELATED ID: 2GP5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC CORE DOMAIN OF JMJD2ACOMPLEXED WITH
REMARK 900 ALPHA-KETOGLUTARATE
REMARK 900 RELATED ID: 2GF7 RELATED DB: PDB
REMARK 900 DOUBLE TUDOR DOMAIN STRUCTURE
DBREF 2WWJ A 7 353 UNP O75164 KDM4A_HUMAN 7 353
DBREF 2WWJ A 354 354 PDB 2WWJ 2WWJ 354 354
DBREF 2WWJ B 7 353 UNP O75164 KDM4A_HUMAN 7 353
DBREF 2WWJ B 354 354 PDB 2WWJ 2WWJ 354 354
SEQRES 1 A 348 THR LEU ASN PRO SER ALA ARG ILE MET THR PHE TYR PRO
SEQRES 2 A 348 THR MET GLU GLU PHE ARG ASN PHE SER ARG TYR ILE ALA
SEQRES 3 A 348 TYR ILE GLU SER GLN GLY ALA HIS ARG ALA GLY LEU ALA
SEQRES 4 A 348 LYS VAL VAL PRO PRO LYS GLU TRP LYS PRO ARG ALA SER
SEQRES 5 A 348 TYR ASP ASP ILE ASP ASP LEU VAL ILE PRO ALA PRO ILE
SEQRES 6 A 348 GLN GLN LEU VAL THR GLY GLN SER GLY LEU PHE THR GLN
SEQRES 7 A 348 TYR ASN ILE GLN LYS LYS ALA MET THR VAL ARG GLU PHE
SEQRES 8 A 348 ARG LYS ILE ALA ASN SER ASP LYS TYR CYS THR PRO ARG
SEQRES 9 A 348 TYR SER GLU PHE GLU GLU LEU GLU ARG LYS TYR TRP LYS
SEQRES 10 A 348 ASN LEU THR PHE ASN PRO PRO ILE TYR GLY ALA ASP VAL
SEQRES 11 A 348 ASN GLY THR LEU TYR GLU LYS HIS VAL ASP GLU TRP ASN
SEQRES 12 A 348 ILE GLY ARG LEU ARG THR ILE LEU ASP LEU VAL GLU LYS
SEQRES 13 A 348 GLU SER GLY ILE THR ILE GLU GLY VAL ASN THR PRO TYR
SEQRES 14 A 348 LEU TYR PHE GLY MET TRP LYS THR SER PHE ALA TRP HIS
SEQRES 15 A 348 THR GLU ASP MET ASP LEU TYR SER ILE ASN TYR LEU HIS
SEQRES 16 A 348 PHE GLY GLU PRO LYS SER TRP TYR SER VAL PRO PRO GLU
SEQRES 17 A 348 HIS GLY LYS ARG LEU GLU ARG LEU ALA LYS GLY PHE PHE
SEQRES 18 A 348 PRO GLY SER ALA GLN SER CYS GLU ALA PHE LEU ARG HIS
SEQRES 19 A 348 LYS MET THR LEU ILE SER PRO LEU MET LEU LYS LYS TYR
SEQRES 20 A 348 GLY ILE PRO PHE ASP LYS VAL THR GLN GLU ALA GLY GLU
SEQRES 21 A 348 PHE MET ILE THR PHE PRO TYR GLY TYR HIS ALA GLY PHE
SEQRES 22 A 348 ASN HIS GLY PHE ASN CYS ALA GLU SER THR ASN PHE ALA
SEQRES 23 A 348 THR ARG ARG TRP ILE GLU TYR GLY LYS GLN ALA VAL LEU
SEQRES 24 A 348 CYS SER CYS ARG LYS ASP MET VAL LYS ILE SER MET ASP
SEQRES 25 A 348 VAL PHE VAL ARG LYS PHE GLN PRO GLU ARG TYR LYS LEU
SEQRES 26 A 348 TRP LYS ALA GLY LYS ASP ASN THR VAL ILE ASP HIS THR
SEQRES 27 A 348 LEU PRO THR PRO GLU ALA ALA GLU PHE THR
SEQRES 1 B 348 THR LEU ASN PRO SER ALA ARG ILE MET THR PHE TYR PRO
SEQRES 2 B 348 THR MET GLU GLU PHE ARG ASN PHE SER ARG TYR ILE ALA
SEQRES 3 B 348 TYR ILE GLU SER GLN GLY ALA HIS ARG ALA GLY LEU ALA
SEQRES 4 B 348 LYS VAL VAL PRO PRO LYS GLU TRP LYS PRO ARG ALA SER
SEQRES 5 B 348 TYR ASP ASP ILE ASP ASP LEU VAL ILE PRO ALA PRO ILE
SEQRES 6 B 348 GLN GLN LEU VAL THR GLY GLN SER GLY LEU PHE THR GLN
SEQRES 7 B 348 TYR ASN ILE GLN LYS LYS ALA MET THR VAL ARG GLU PHE
SEQRES 8 B 348 ARG LYS ILE ALA ASN SER ASP LYS TYR CYS THR PRO ARG
SEQRES 9 B 348 TYR SER GLU PHE GLU GLU LEU GLU ARG LYS TYR TRP LYS
SEQRES 10 B 348 ASN LEU THR PHE ASN PRO PRO ILE TYR GLY ALA ASP VAL
SEQRES 11 B 348 ASN GLY THR LEU TYR GLU LYS HIS VAL ASP GLU TRP ASN
SEQRES 12 B 348 ILE GLY ARG LEU ARG THR ILE LEU ASP LEU VAL GLU LYS
SEQRES 13 B 348 GLU SER GLY ILE THR ILE GLU GLY VAL ASN THR PRO TYR
SEQRES 14 B 348 LEU TYR PHE GLY MET TRP LYS THR SER PHE ALA TRP HIS
SEQRES 15 B 348 THR GLU ASP MET ASP LEU TYR SER ILE ASN TYR LEU HIS
SEQRES 16 B 348 PHE GLY GLU PRO LYS SER TRP TYR SER VAL PRO PRO GLU
SEQRES 17 B 348 HIS GLY LYS ARG LEU GLU ARG LEU ALA LYS GLY PHE PHE
SEQRES 18 B 348 PRO GLY SER ALA GLN SER CYS GLU ALA PHE LEU ARG HIS
SEQRES 19 B 348 LYS MET THR LEU ILE SER PRO LEU MET LEU LYS LYS TYR
SEQRES 20 B 348 GLY ILE PRO PHE ASP LYS VAL THR GLN GLU ALA GLY GLU
SEQRES 21 B 348 PHE MET ILE THR PHE PRO TYR GLY TYR HIS ALA GLY PHE
SEQRES 22 B 348 ASN HIS GLY PHE ASN CYS ALA GLU SER THR ASN PHE ALA
SEQRES 23 B 348 THR ARG ARG TRP ILE GLU TYR GLY LYS GLN ALA VAL LEU
SEQRES 24 B 348 CYS SER CYS ARG LYS ASP MET VAL LYS ILE SER MET ASP
SEQRES 25 B 348 VAL PHE VAL ARG LYS PHE GLN PRO GLU ARG TYR LYS LEU
SEQRES 26 B 348 TRP LYS ALA GLY LYS ASP ASN THR VAL ILE ASP HIS THR
SEQRES 27 B 348 LEU PRO THR PRO GLU ALA ALA GLU PHE THR
HET NI A 501 1
HET ZN A 502 1
HET Y28 A1354 25
HET NI B 501 1
HET ZN B 502 1
HET Y28 B1354 25
HETNAM NI NICKEL (II) ION
HETNAM ZN ZINC ION
HETNAM Y28 O-BENZYL-N-(CARBOXYCARBONYL)-D-TYROSINE
HETSYN Y28 (2R)-2-(CARBOXYCARBONYLAMINO)-3-(4-
HETSYN 2 Y28 PHENYLMETHOXYPHENYL)PROPANOIC ACID
FORMUL 3 NI 2(NI 2+)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 5 Y28 2(C18 H17 N O6)
FORMUL 9 HOH *144(H2 O)
HELIX 1 1 THR A 20 ARG A 25 1 6
HELIX 2 2 ASN A 26 GLN A 37 1 12
HELIX 3 3 GLY A 38 ALA A 42 5 5
HELIX 4 4 VAL A 94 SER A 103 1 10
HELIX 5 5 GLU A 113 LEU A 125 1 13
HELIX 6 6 THR A 155 LEU A 157 5 3
HELIX 7 7 ASP A 158 GLY A 165 1 8
HELIX 8 8 GLU A 190 LEU A 194 5 5
HELIX 9 9 PRO A 212 GLU A 214 5 3
HELIX 10 10 HIS A 215 PHE A 227 1 13
HELIX 11 11 PHE A 227 CYS A 234 1 8
HELIX 12 12 ALA A 236 LYS A 241 5 6
HELIX 13 13 SER A 246 TYR A 253 1 8
HELIX 14 14 ARG A 295 ALA A 303 1 9
HELIX 15 15 MET A 317 GLN A 325 1 9
HELIX 16 16 ARG A 328 ALA A 334 1 7
HELIX 17 17 THR A 347 ALA A 351 5 5
HELIX 18 18 THR B 20 ARG B 25 1 6
HELIX 19 19 ASN B 26 GLN B 37 1 12
HELIX 20 20 GLY B 38 ALA B 42 5 5
HELIX 21 21 VAL B 94 ASN B 102 1 9
HELIX 22 22 GLU B 113 LEU B 125 1 13
HELIX 23 23 LEU B 157 GLU B 161 5 5
HELIX 24 24 GLU B 190 LEU B 194 5 5
HELIX 25 25 PRO B 212 GLU B 214 5 3
HELIX 26 26 HIS B 215 PHE B 227 1 13
HELIX 27 27 PHE B 227 CYS B 234 1 8
HELIX 28 28 ALA B 236 LYS B 241 5 6
HELIX 29 29 SER B 246 TYR B 253 1 8
HELIX 30 30 ARG B 295 ALA B 303 1 9
HELIX 31 31 MET B 317 GLN B 325 1 9
HELIX 32 32 GLN B 325 ALA B 334 1 10
HELIX 33 33 THR B 347 ALA B 351 5 5
SHEET 1 AA10 MET A 15 PHE A 17 0
SHEET 2 AA10 LEU A 44 VAL A 47 1 O LEU A 44 N MET A 15
SHEET 3 AA10 PHE A 267 THR A 270 -1 O PHE A 267 N VAL A 47
SHEET 4 AA10 TYR A 195 GLY A 203 -1 O SER A 196 N THR A 270
SHEET 5 AA10 ASN A 284 PHE A 291 -1 O CYS A 285 N HIS A 201
SHEET 6 AA10 TYR A 175 GLY A 179 -1 O TYR A 175 N SER A 288
SHEET 7 AA10 ILE A 131 ASN A 137 -1 O GLY A 133 N PHE A 178
SHEET 8 AA10 ILE A 71 GLN A 78 -1 O ILE A 71 N TYR A 132
SHEET 9 AA10 LEU A 81 GLN A 88 -1 O LEU A 81 N GLN A 78
SHEET 10 AA10 THR A 243 ILE A 245 -1 O LEU A 244 N PHE A 82
SHEET 1 AB 2 VAL A 66 ILE A 67 0
SHEET 2 AB 2 MET A 92 THR A 93 -1 O MET A 92 N ILE A 67
SHEET 1 AC 4 SER A 184 HIS A 188 0
SHEET 2 AC 4 HIS A 276 ASN A 280 -1 O HIS A 276 N HIS A 188
SHEET 3 AC 4 LYS A 206 SER A 210 -1 O SER A 207 N PHE A 279
SHEET 4 AC 4 ASP A 258 GLN A 262 -1 O ASP A 258 N SER A 210
SHEET 1 BA10 MET B 15 PHE B 17 0
SHEET 2 BA10 LEU B 44 VAL B 47 1 O LEU B 44 N MET B 15
SHEET 3 BA10 PHE B 267 THR B 270 -1 O PHE B 267 N VAL B 47
SHEET 4 BA10 TYR B 195 GLY B 203 -1 O SER B 196 N THR B 270
SHEET 5 BA10 ASN B 284 PHE B 291 -1 O CYS B 285 N HIS B 201
SHEET 6 BA10 TYR B 175 GLY B 179 -1 O TYR B 175 N SER B 288
SHEET 7 BA10 ILE B 131 ASN B 137 -1 O GLY B 133 N PHE B 178
SHEET 8 BA10 ILE B 71 GLN B 78 -1 O ILE B 71 N TYR B 132
SHEET 9 BA10 LEU B 81 GLN B 88 -1 O LEU B 81 N GLN B 78
SHEET 10 BA10 THR B 243 ILE B 245 -1 O LEU B 244 N PHE B 82
SHEET 1 BB 2 VAL B 66 ILE B 67 0
SHEET 2 BB 2 MET B 92 THR B 93 -1 O MET B 92 N ILE B 67
SHEET 1 BC 4 SER B 184 HIS B 188 0
SHEET 2 BC 4 TYR B 275 ASN B 280 -1 O HIS B 276 N HIS B 188
SHEET 3 BC 4 LYS B 206 VAL B 211 -1 O SER B 207 N PHE B 279
SHEET 4 BC 4 ASP B 258 GLN B 262 -1 O ASP B 258 N SER B 210
LINK NE2 HIS A 188 NI NI A 501 1555 1555 2.32
LINK OE2 GLU A 190 NI NI A 501 1555 1555 2.02
LINK SG CYS A 234 ZN ZN A 502 1555 1555 2.34
LINK NE2 HIS A 240 ZN ZN A 502 1555 1555 2.09
LINK NE2 HIS A 276 NI NI A 501 1555 1555 2.14
LINK SG CYS A 306 ZN ZN A 502 1555 1555 2.26
LINK SG CYS A 308 ZN ZN A 502 1555 1555 2.41
LINK NI NI A 501 OAW Y28 A1354 1555 1555 2.19
LINK NI NI A 501 OAX Y28 A1354 1555 1555 2.18
LINK NI NI A 501 O HOH A2035 1555 1555 1.88
LINK NE2 HIS B 188 NI NI B 501 1555 1555 2.13
LINK OE2 GLU B 190 NI NI B 501 1555 1555 2.15
LINK SG CYS B 234 ZN ZN B 502 1555 1555 2.26
LINK NE2 HIS B 240 ZN ZN B 502 1555 1555 2.10
LINK NE2 HIS B 276 NI NI B 501 1555 1555 2.16
LINK SG CYS B 306 ZN ZN B 502 1555 1555 2.30
LINK SG CYS B 308 ZN ZN B 502 1555 1555 2.40
LINK NI NI B 501 OAW Y28 B1354 1555 1555 2.31
LINK NI NI B 501 OAX Y28 B1354 1555 1555 2.22
LINK NI NI B 501 O HOH B2073 1555 1555 2.18
SITE 1 AC1 18 ILE A 71 GLN A 84 ASN A 86 TYR A 132
SITE 2 AC1 18 TYR A 177 PHE A 185 ALA A 186 HIS A 188
SITE 3 AC1 18 GLU A 190 SER A 196 ASN A 198 LYS A 206
SITE 4 AC1 18 TRP A 208 LYS A 241 HIS A 276 SER A 288
SITE 5 AC1 18 NI A 501 HOH A2035
SITE 1 AC2 5 HIS A 188 GLU A 190 HIS A 276 Y28 A1354
SITE 2 AC2 5 HOH A2035
SITE 1 AC3 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC4 17 ILE B 71 GLN B 84 ASN B 86 TYR B 132
SITE 2 AC4 17 TYR B 177 PHE B 185 HIS B 188 GLU B 190
SITE 3 AC4 17 SER B 196 ASN B 198 LYS B 206 TRP B 208
SITE 4 AC4 17 LYS B 241 HIS B 276 SER B 288 NI B 501
SITE 5 AC4 17 HOH B2073
SITE 1 AC5 5 HIS B 188 GLU B 190 HIS B 276 Y28 B1354
SITE 2 AC5 5 HOH B2073
SITE 1 AC6 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
CRYST1 101.330 148.970 57.110 90.00 90.00 90.00 P 21 21 2 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 0.009869 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017510 0.00000
MTRIX1 1 -0.998847 0.034129 0.033748 -67.16800 1
MTRIX2 1 -0.029647 -0.991664 0.125396 -77.68600 1
MTRIX3 1 0.037746 0.124251 0.991533 -16.89600 1
(ATOM LINES ARE NOT SHOWN.)
END
