HEADER OXIDOREDUCTASE 12-NOV-10 2XXZ
TITLE CRYSTAL STRUCTURE OF THE HUMAN JMJD3 JUMONJI DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 6B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: JUMONJI DOMAIN, RESIDUES 1173-1502;
COMPND 5 SYNONYM: JMJD3, JMJC DOMAIN-CONTAINING PROTEIN 3, JUMONJI DOMAIN-
COMPND 6 CONTAINING PROTEIN 3, LYSINE DEMETHYLASE 6B;
COMPND 7 EC: 1.14.11.-;
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-PRARE2;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS OXIDOREDUCTASE, HISTONE DEMETHYLATION, OXYGENASE, CHROMATIN
KEYWDS 2 MODIFICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.H.CHE,W.W.YUE,T.KROJER,J.R.C.MUNIZ,S.S.NG,A.TUMBER,M.DANIEL,
AUTHOR 2 N.BURGESS-BROWN,P.SAVITSKY,E.UGOCHUKWU,P.FILIPPAKOPOULOS,
AUTHOR 3 C.ARROWSMITH,J.WEIGELT,A.EDWARDS,C.BOUNTRA,U.OPPERMANN
REVDAT 4 24-JAN-18 2XXZ 1 JRNL
REVDAT 3 14-JAN-15 2XXZ 1 REMARK VERSN FORMUL
REVDAT 2 01-DEC-10 2XXZ 1 JRNL
REVDAT 1 24-NOV-10 2XXZ 0
JRNL AUTH K.H.CHE,W.W.YUE,T.KROJER,J.R.C.MUNIZ,S.S.NG,A.TUMBER,
JRNL AUTH 2 M.DANIEL,N.BURGESS-BROWN,P.SAVITSKY,F.VON DELFT,E.UGOCHUKWU,
JRNL AUTH 3 P.FILIPPAKOPOULOS,C.ARROWSMITH,J.WEIGELT,A.EDWARDS,
JRNL AUTH 4 C.BOUNTRA,U.OPPERMANN
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN JMJD3 JUMONJI DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 61100
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3016
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4968
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE SET COUNT : 265
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4612
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 319
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 1.26000
REMARK 3 B33 (A**2) : -1.45000
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): 0.103
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.236
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4906 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3250 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6714 ; 1.351 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7900 ; 1.053 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 603 ; 5.971 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 232 ;33.913 ;24.095
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 761 ;13.374 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;20.631 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 723 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5506 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1006 ; 0.002 ; 0.020
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): 2949 ; 1.688 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1178 ; 0.404 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4804 ; 2.871 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1957 ; 4.105 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1902 ; 6.069 ;11.000
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 : 10
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 1175 A 1212
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9007 48.2989 -13.8463
REMARK 3 T TENSOR
REMARK 3 T11: 0.1221 T22: 0.1863
REMARK 3 T33: 0.1533 T12: 0.0021
REMARK 3 T13: 0.0054 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.9421 L22: 0.9109
REMARK 3 L33: 1.5247 L12: 0.4975
REMARK 3 L13: -0.0145 L23: -0.5395
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: 0.0763 S13: -0.0191
REMARK 3 S21: -0.0143 S22: -0.0187 S23: -0.0221
REMARK 3 S31: 0.1225 S32: 0.0794 S33: 0.0275
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 1213 A 1246
REMARK 3 ORIGIN FOR THE GROUP (A): 51.9917 54.4655 10.4149
REMARK 3 T TENSOR
REMARK 3 T11: 0.0821 T22: 0.2205
REMARK 3 T33: 0.1761 T12: 0.0026
REMARK 3 T13: -0.0006 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.9288 L22: 0.6320
REMARK 3 L33: 2.1837 L12: 0.2186
REMARK 3 L13: 0.0690 L23: -0.4078
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: -0.0564 S13: 0.0542
REMARK 3 S21: 0.0783 S22: 0.0089 S23: 0.0193
REMARK 3 S31: -0.1193 S32: -0.0452 S33: 0.0037
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 1247 A 1266
REMARK 3 ORIGIN FOR THE GROUP (A): 50.3588 26.0087 9.8115
REMARK 3 T TENSOR
REMARK 3 T11: 0.6595 T22: 0.2147
REMARK 3 T33: 0.1692 T12: 0.1830
REMARK 3 T13: 0.0368 T23: 0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 6.2658 L22: 3.2935
REMARK 3 L33: 3.9547 L12: -0.6355
REMARK 3 L13: 1.1018 L23: -2.7949
REMARK 3 S TENSOR
REMARK 3 S11: -0.2004 S12: -0.5539 S13: -0.5901
REMARK 3 S21: 0.1186 S22: 0.1108 S23: -0.0687
REMARK 3 S31: 0.9193 S32: 0.2853 S33: 0.0895
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 1267 A 1325
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1112 43.7475 18.2481
REMARK 3 T TENSOR
REMARK 3 T11: 0.1433 T22: 0.2251
REMARK 3 T33: 0.1621 T12: -0.0005
REMARK 3 T13: 0.0015 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 2.8404 L22: 1.6504
REMARK 3 L33: 0.8267 L12: 0.7802
REMARK 3 L13: 0.2240 L23: -0.2082
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: -0.1324 S13: -0.1712
REMARK 3 S21: 0.1060 S22: 0.0501 S23: -0.0792
REMARK 3 S31: 0.1585 S32: 0.0094 S33: -0.0343
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 1326 A 1493
REMARK 3 ORIGIN FOR THE GROUP (A): 43.9322 46.4734 0.7549
REMARK 3 T TENSOR
REMARK 3 T11: 0.0967 T22: 0.1790
REMARK 3 T33: 0.1737 T12: -0.0196
REMARK 3 T13: 0.0058 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.4915 L22: 0.4974
REMARK 3 L33: 1.3970 L12: -0.2375
REMARK 3 L13: 0.2676 L23: -0.0337
REMARK 3 S TENSOR
REMARK 3 S11: 0.0089 S12: -0.0481 S13: -0.0337
REMARK 3 S21: 0.0388 S22: 0.0002 S23: 0.0571
REMARK 3 S31: 0.1048 S32: -0.1377 S33: -0.0091
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 : B 1175 B 1214
REMARK 3 ORIGIN FOR THE GROUP (A): 45.1405 48.7691 -24.7710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1437 T22: 0.2070
REMARK 3 T33: 0.1441 T12: -0.0160
REMARK 3 T13: 0.0144 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.7773 L22: 1.5465
REMARK 3 L33: 2.0369 L12: -0.3633
REMARK 3 L13: -0.0048 L23: 0.4381
REMARK 3 S TENSOR
REMARK 3 S11: 0.0240 S12: -0.0274 S13: 0.0344
REMARK 3 S21: 0.0251 S22: -0.0574 S23: 0.0768
REMARK 3 S31: 0.1793 S32: -0.1424 S33: 0.0334
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 1215 B 1251
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5983 54.9251 -48.0549
REMARK 3 T TENSOR
REMARK 3 T11: 0.2845 T22: 0.2245
REMARK 3 T33: 0.1440 T12: -0.0666
REMARK 3 T13: -0.0699 T23: 0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 1.5921 L22: 2.1619
REMARK 3 L33: 1.9935 L12: 1.7165
REMARK 3 L13: 0.8351 L23: 0.4508
REMARK 3 S TENSOR
REMARK 3 S11: -0.3125 S12: 0.2302 S13: 0.1558
REMARK 3 S21: -0.5474 S22: 0.2617 S23: 0.2052
REMARK 3 S31: -0.0721 S32: -0.0632 S33: 0.0507
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 1252 B 1354
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3729 48.8428 -49.7312
REMARK 3 T TENSOR
REMARK 3 T11: 0.2733 T22: 0.2152
REMARK 3 T33: 0.0858 T12: -0.0602
REMARK 3 T13: -0.0074 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 1.5628 L22: 2.4398
REMARK 3 L33: 1.5072 L12: 1.3623
REMARK 3 L13: 0.6305 L23: 0.7672
REMARK 3 S TENSOR
REMARK 3 S11: -0.2874 S12: 0.2774 S13: 0.0317
REMARK 3 S21: -0.6007 S22: 0.2210 S23: 0.0365
REMARK 3 S31: -0.1097 S32: -0.0194 S33: 0.0664
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 1355 B 1484
REMARK 3 ORIGIN FOR THE GROUP (A): 44.9821 40.8140 -38.8798
REMARK 3 T TENSOR
REMARK 3 T11: 0.2052 T22: 0.1149
REMARK 3 T33: 0.1349 T12: -0.0051
REMARK 3 T13: 0.0002 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.4453 L22: 1.3847
REMARK 3 L33: 1.9709 L12: 0.0974
REMARK 3 L13: 0.4831 L23: 0.1002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0194 S12: 0.0481 S13: -0.0411
REMARK 3 S21: -0.1735 S22: 0.0302 S23: 0.0014
REMARK 3 S31: 0.1962 S32: 0.0161 S33: -0.0108
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 1485 B 1499
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5671 58.4688 -24.1731
REMARK 3 T TENSOR
REMARK 3 T11: 0.1075 T22: 0.2649
REMARK 3 T33: 0.2163 T12: -0.0099
REMARK 3 T13: -0.0202 T23: 0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 2.0776 L22: 3.7115
REMARK 3 L33: 5.5379 L12: 0.4430
REMARK 3 L13: 2.1406 L23: 0.4130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0369 S12: 0.2432 S13: -0.0511
REMARK 3 S21: -0.0560 S22: -0.1332 S23: -0.2793
REMARK 3 S31: -0.3745 S32: 0.5131 S33: 0.1701
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.
REMARK 4
REMARK 4 2XXZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1290046225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : SI (111)
REMARK 200 OPTICS : NULL
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 : 61104
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.96000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 28.37850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.84900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.71550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.84900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.37850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.71550
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 SER A 1171
REMARK 465 MET A 1172
REMARK 465 LEU A 1173
REMARK 465 PRO A 1174
REMARK 465 LYS A 1293
REMARK 465 GLU A 1294
REMARK 465 SER A 1295
REMARK 465 GLU A 1296
REMARK 465 ASP A 1297
REMARK 465 GLU A 1298
REMARK 465 GLU A 1299
REMARK 465 SER A 1300
REMARK 465 GLU A 1301
REMARK 465 GLU A 1302
REMARK 465 PRO A 1303
REMARK 465 ASP A 1304
REMARK 465 SER A 1305
REMARK 465 THR A 1306
REMARK 465 THR A 1307
REMARK 465 GLY A 1308
REMARK 465 THR A 1309
REMARK 465 PRO A 1310
REMARK 465 PRO A 1311
REMARK 465 SER A 1312
REMARK 465 SER A 1313
REMARK 465 ALA A 1314
REMARK 465 PRO A 1315
REMARK 465 ASP A 1316
REMARK 465 PRO A 1317
REMARK 465 LYS A 1318
REMARK 465 ASN A 1319
REMARK 465 LEU A 1494
REMARK 465 GLU A 1495
REMARK 465 ARG A 1496
REMARK 465 TYR A 1497
REMARK 465 GLU A 1498
REMARK 465 TRP A 1499
REMARK 465 ASN A 1500
REMARK 465 GLU A 1501
REMARK 465 VAL A 1502
REMARK 465 SER B 1171
REMARK 465 MET B 1172
REMARK 465 LEU B 1173
REMARK 465 PRO B 1174
REMARK 465 GLU B 1291
REMARK 465 GLU B 1292
REMARK 465 LYS B 1293
REMARK 465 GLU B 1294
REMARK 465 SER B 1295
REMARK 465 GLU B 1296
REMARK 465 ASP B 1297
REMARK 465 GLU B 1298
REMARK 465 GLU B 1299
REMARK 465 SER B 1300
REMARK 465 GLU B 1301
REMARK 465 GLU B 1302
REMARK 465 PRO B 1303
REMARK 465 ASP B 1304
REMARK 465 SER B 1305
REMARK 465 THR B 1306
REMARK 465 THR B 1307
REMARK 465 GLY B 1308
REMARK 465 THR B 1309
REMARK 465 PRO B 1310
REMARK 465 PRO B 1311
REMARK 465 SER B 1312
REMARK 465 SER B 1313
REMARK 465 ALA B 1314
REMARK 465 PRO B 1315
REMARK 465 ASP B 1316
REMARK 465 PRO B 1317
REMARK 465 LYS B 1318
REMARK 465 ASN B 1319
REMARK 465 GLY B 1357
REMARK 465 ASN B 1358
REMARK 465 MET B 1359
REMARK 465 LEU B 1360
REMARK 465 SER B 1361
REMARK 465 HIS B 1362
REMARK 465 VAL B 1363
REMARK 465 GLY B 1364
REMARK 465 HIS B 1365
REMARK 465 THR B 1366
REMARK 465 ASN B 1500
REMARK 465 GLU B 1501
REMARK 465 VAL B 1502
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 ARG A1175 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1177 CE NZ
REMARK 470 ARG A1260 NE CZ NH1 NH2
REMARK 470 GLU A1292 CG CD OE1 OE2
REMARK 470 ARG B1175 NE CZ NH1 NH2
REMARK 470 GLU B1176 CG CD OE1 OE2
REMARK 470 ARG B1260 CG CD NE CZ NH1 NH2
REMARK 470 HIS B1320 CG ND1 CD2 CE1 NE2
REMARK 470 THR B1356 OG1 CG2
REMARK 470 LEU B1368 CD1 CD2
REMARK 470 GLU B1498 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 2018 O HOH B 2019 1.82
REMARK 500 O HOH A 2019 O HOH B 2018 1.87
REMARK 500 O HOH B 2023 O HOH B 2140 2.02
REMARK 500 N LEU B 1215 O HOH B 2030 2.04
REMARK 500 O HOH A 2127 O HOH A 2160 2.09
REMARK 500 OE1 GLU A 1241 O HOH A 2034 2.10
REMARK 500 O HOH B 2068 O HOH B 2078 2.14
REMARK 500 OD2 ASP A 1428 OG1 THR A 1431 2.15
REMARK 500 O HOH A 2105 O HOH A 2107 2.16
REMARK 500 OE2 GLU A 1412 O HOH A 2120 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2058 O HOH B 2100 3754 2.13
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 ASN A1179 60.60 -117.18
REMARK 500 SER A1235 37.26 -155.60
REMARK 500 SER A1355 -133.22 59.01
REMARK 500 ASN B1179 61.37 -119.94
REMARK 500 SER B1235 72.06 -157.33
REMARK 500 THR B1272 -162.55 -162.79
REMARK 500 ASP B1333 96.32 -68.50
REMARK 500 ARG B1352 -51.48 -125.69
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 A2494 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 8XQ A3001 OAC
REMARK 620 2 8XQ A3001 NAI 83.8
REMARK 620 3 HIS A1387 NE2 94.0 97.5
REMARK 620 4 GLU A1389 OE2 85.6 167.4 90.0
REMARK 620 5 HOH A2098 O 174.2 97.9 91.3 92.0
REMARK 620 6 HOH A2103 O 87.6 82.7 178.4 90.1 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2495 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2012 O
REMARK 620 2 HOH B2013 O 73.9
REMARK 620 3 HOH B2011 O 101.6 167.9
REMARK 620 4 GLU A1287 OE2 155.3 81.4 102.8
REMARK 620 5 GLU B1188 OE1 83.9 79.5 88.9 92.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A2500 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2054 O
REMARK 620 2 HOH A2060 O 87.7
REMARK 620 3 HOH A2015 O 87.5 172.5
REMARK 620 4 HOH B2150 O 179.4 91.7 93.1
REMARK 620 5 HOH A2013 O 87.7 90.6 83.4 92.3
REMARK 620 6 HOH A2059 O 94.3 91.7 94.4 85.7 176.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B2500 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2155 O
REMARK 620 2 HOH B2083 O 88.4
REMARK 620 3 GLU B1389 OE2 89.9 94.5
REMARK 620 4 HIS B1387 NE2 178.3 92.0 88.5
REMARK 620 5 8XQ B3001 NAI 83.0 97.4 165.9 98.5
REMARK 620 6 8XQ B3001 OAC 85.0 172.5 89.1 94.7 78.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 2494
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 2500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 2500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 2495
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2496
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2499
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8XQ A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8XQ B 3001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XUE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJD3
DBREF 2XXZ A 1173 1502 UNP O15054 KDM6B_HUMAN 1173 1502
DBREF 2XXZ B 1173 1502 UNP O15054 KDM6B_HUMAN 1173 1502
SEQADV 2XXZ SER A 1171 UNP O15054 EXPRESSION TAG
SEQADV 2XXZ MET A 1172 UNP O15054 EXPRESSION TAG
SEQADV 2XXZ SER B 1171 UNP O15054 EXPRESSION TAG
SEQADV 2XXZ MET B 1172 UNP O15054 EXPRESSION TAG
SEQRES 1 A 332 SER MET LEU PRO ARG GLU LYS LEU ASN PRO PRO THR PRO
SEQRES 2 A 332 SER ILE TYR LEU GLU SER LYS ARG ASP ALA PHE SER PRO
SEQRES 3 A 332 VAL LEU LEU GLN PHE CYS THR ASP PRO ARG ASN PRO ILE
SEQRES 4 A 332 THR VAL ILE ARG GLY LEU ALA GLY SER LEU ARG LEU ASN
SEQRES 5 A 332 LEU GLY LEU PHE SER THR LYS THR LEU VAL GLU ALA SER
SEQRES 6 A 332 GLY GLU HIS THR VAL GLU VAL ARG THR GLN VAL GLN GLN
SEQRES 7 A 332 PRO SER ASP GLU ASN TRP ASP LEU THR GLY THR ARG GLN
SEQRES 8 A 332 ILE TRP PRO CYS GLU SER SER ARG SER HIS THR THR ILE
SEQRES 9 A 332 ALA LYS TYR ALA GLN TYR GLN ALA SER SER PHE GLN GLU
SEQRES 10 A 332 SER LEU GLN GLU GLU LYS GLU SER GLU ASP GLU GLU SER
SEQRES 11 A 332 GLU GLU PRO ASP SER THR THR GLY THR PRO PRO SER SER
SEQRES 12 A 332 ALA PRO ASP PRO LYS ASN HIS HIS ILE ILE LYS PHE GLY
SEQRES 13 A 332 THR ASN ILE ASP LEU SER ASP ALA LYS ARG TRP LYS PRO
SEQRES 14 A 332 GLN LEU GLN GLU LEU LEU LYS LEU PRO ALA PHE MET ARG
SEQRES 15 A 332 VAL THR SER THR GLY ASN MET LEU SER HIS VAL GLY HIS
SEQRES 16 A 332 THR ILE LEU GLY MET ASN THR VAL GLN LEU TYR MET LYS
SEQRES 17 A 332 VAL PRO GLY SER ARG THR PRO GLY HIS GLN GLU ASN ASN
SEQRES 18 A 332 ASN PHE CYS SER VAL ASN ILE ASN ILE GLY PRO GLY ASP
SEQRES 19 A 332 CYS GLU TRP PHE ALA VAL HIS GLU HIS TYR TRP GLU THR
SEQRES 20 A 332 ILE SER ALA PHE CYS ASP ARG HIS GLY VAL ASP TYR LEU
SEQRES 21 A 332 THR GLY SER TRP TRP PRO ILE LEU ASP ASP LEU TYR ALA
SEQRES 22 A 332 SER ASN ILE PRO VAL TYR ARG PHE VAL GLN ARG PRO GLY
SEQRES 23 A 332 ASP LEU VAL TRP ILE ASN ALA GLY THR VAL HIS TRP VAL
SEQRES 24 A 332 GLN ALA THR GLY TRP CYS ASN ASN ILE ALA TRP ASN VAL
SEQRES 25 A 332 GLY PRO LEU THR ALA TYR GLN TYR GLN LEU ALA LEU GLU
SEQRES 26 A 332 ARG TYR GLU TRP ASN GLU VAL
SEQRES 1 B 332 SER MET LEU PRO ARG GLU LYS LEU ASN PRO PRO THR PRO
SEQRES 2 B 332 SER ILE TYR LEU GLU SER LYS ARG ASP ALA PHE SER PRO
SEQRES 3 B 332 VAL LEU LEU GLN PHE CYS THR ASP PRO ARG ASN PRO ILE
SEQRES 4 B 332 THR VAL ILE ARG GLY LEU ALA GLY SER LEU ARG LEU ASN
SEQRES 5 B 332 LEU GLY LEU PHE SER THR LYS THR LEU VAL GLU ALA SER
SEQRES 6 B 332 GLY GLU HIS THR VAL GLU VAL ARG THR GLN VAL GLN GLN
SEQRES 7 B 332 PRO SER ASP GLU ASN TRP ASP LEU THR GLY THR ARG GLN
SEQRES 8 B 332 ILE TRP PRO CYS GLU SER SER ARG SER HIS THR THR ILE
SEQRES 9 B 332 ALA LYS TYR ALA GLN TYR GLN ALA SER SER PHE GLN GLU
SEQRES 10 B 332 SER LEU GLN GLU GLU LYS GLU SER GLU ASP GLU GLU SER
SEQRES 11 B 332 GLU GLU PRO ASP SER THR THR GLY THR PRO PRO SER SER
SEQRES 12 B 332 ALA PRO ASP PRO LYS ASN HIS HIS ILE ILE LYS PHE GLY
SEQRES 13 B 332 THR ASN ILE ASP LEU SER ASP ALA LYS ARG TRP LYS PRO
SEQRES 14 B 332 GLN LEU GLN GLU LEU LEU LYS LEU PRO ALA PHE MET ARG
SEQRES 15 B 332 VAL THR SER THR GLY ASN MET LEU SER HIS VAL GLY HIS
SEQRES 16 B 332 THR ILE LEU GLY MET ASN THR VAL GLN LEU TYR MET LYS
SEQRES 17 B 332 VAL PRO GLY SER ARG THR PRO GLY HIS GLN GLU ASN ASN
SEQRES 18 B 332 ASN PHE CYS SER VAL ASN ILE ASN ILE GLY PRO GLY ASP
SEQRES 19 B 332 CYS GLU TRP PHE ALA VAL HIS GLU HIS TYR TRP GLU THR
SEQRES 20 B 332 ILE SER ALA PHE CYS ASP ARG HIS GLY VAL ASP TYR LEU
SEQRES 21 B 332 THR GLY SER TRP TRP PRO ILE LEU ASP ASP LEU TYR ALA
SEQRES 22 B 332 SER ASN ILE PRO VAL TYR ARG PHE VAL GLN ARG PRO GLY
SEQRES 23 B 332 ASP LEU VAL TRP ILE ASN ALA GLY THR VAL HIS TRP VAL
SEQRES 24 B 332 GLN ALA THR GLY TRP CYS ASN ASN ILE ALA TRP ASN VAL
SEQRES 25 B 332 GLY PRO LEU THR ALA TYR GLN TYR GLN LEU ALA LEU GLU
SEQRES 26 B 332 ARG TYR GLU TRP ASN GLU VAL
HET NI A2494 1
HET NA A2495 1
HET NI A2500 1
HET EDO A2496 4
HET EDO A2497 4
HET EDO A2498 4
HET EDO A2499 4
HET 8XQ A3001 14
HET NI B2500 1
HET EDO B2501 4
HET 8XQ B3001 14
HETNAM NI NICKEL (II) ION
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 8XQ 8-HYDROXYQUINOLINE-5-CARBOXYLIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NI 3(NI 2+)
FORMUL 4 NA NA 1+
FORMUL 6 EDO 5(C2 H6 O2)
FORMUL 10 8XQ 2(C10 H7 N O3)
FORMUL 14 HOH *319(H2 O)
HELIX 1 1 SER A 1189 ALA A 1193 5 5
HELIX 2 2 SER A 1195 ASP A 1204 1 10
HELIX 3 3 GLY A 1214 ARG A 1220 1 7
HELIX 4 4 ASN A 1222 PHE A 1226 5 5
HELIX 5 5 SER A 1227 GLY A 1236 1 10
HELIX 6 6 ILE A 1274 GLU A 1287 1 14
HELIX 7 7 ASP A 1333 LEU A 1345 1 13
HELIX 8 8 PRO A 1348 ARG A 1352 5 5
HELIX 9 9 GLU A 1389 PHE A 1393 5 5
HELIX 10 10 HIS A 1411 HIS A 1413 5 3
HELIX 11 11 TYR A 1414 HIS A 1425 1 12
HELIX 12 12 ILE A 1437 SER A 1444 1 8
HELIX 13 13 ALA A 1487 ALA A 1493 5 7
HELIX 14 14 ARG B 1175 ASN B 1179 5 5
HELIX 15 15 SER B 1189 SER B 1195 1 7
HELIX 16 16 SER B 1195 ASP B 1204 1 10
HELIX 17 17 GLY B 1214 ARG B 1220 1 7
HELIX 18 18 ASN B 1222 PHE B 1226 5 5
HELIX 19 19 SER B 1227 GLY B 1236 1 10
HELIX 20 20 ILE B 1274 GLN B 1290 1 17
HELIX 21 21 TRP B 1337 LEU B 1345 1 9
HELIX 22 22 PRO B 1348 ARG B 1352 5 5
HELIX 23 23 GLU B 1389 PHE B 1393 5 5
HELIX 24 24 HIS B 1411 HIS B 1413 5 3
HELIX 25 25 TYR B 1414 HIS B 1425 1 12
HELIX 26 26 ILE B 1437 SER B 1444 1 8
HELIX 27 27 THR B 1486 TRP B 1499 1 14
SHEET 1 AA 9 SER A1184 TYR A1186 0
SHEET 2 AA 9 ILE A1209 ARG A1213 1 O VAL A1211 N ILE A1185
SHEET 3 AA 9 LEU A1458 ILE A1461 -1 O LEU A1458 N ILE A1212
SHEET 4 AA 9 CYS A1394 PRO A1402 -1 O SER A1395 N ILE A1461
SHEET 5 AA 9 CYS A1475 GLY A1483 -1 O ASN A1476 N ILE A1400
SHEET 6 AA 9 VAL A1373 LYS A1378 -1 O GLN A1374 N ALA A1479
SHEET 7 AA 9 ILE A1322 ASP A1330 -1 O GLY A1326 N MET A1377
SHEET 8 AA 9 THR A1239 VAL A1246 -1 O GLU A1241 N THR A1327
SHEET 9 AA 9 SER A1268 THR A1273 -1 O SER A1268 N THR A1244
SHEET 1 AB 2 SER A1361 HIS A1362 0
SHEET 2 AB 2 HIS A1365 THR A1366 -1 O HIS A1365 N HIS A1362
SHEET 1 AC 4 ARG A1383 HIS A1387 0
SHEET 2 AC 4 VAL A1466 ALA A1471 -1 O HIS A1467 N HIS A1387
SHEET 3 AC 4 CYS A1405 VAL A1410 -1 O GLU A1406 N GLN A1470
SHEET 4 AC 4 TYR A1449 GLN A1453 -1 O TYR A1449 N ALA A1409
SHEET 1 BA 9 SER B1184 TYR B1186 0
SHEET 2 BA 9 ILE B1209 ARG B1213 1 O VAL B1211 N ILE B1185
SHEET 3 BA 9 LEU B1458 ILE B1461 -1 O LEU B1458 N ILE B1212
SHEET 4 BA 9 CYS B1394 PRO B1402 -1 O SER B1395 N ILE B1461
SHEET 5 BA 9 CYS B1475 VAL B1482 -1 O ASN B1476 N ILE B1400
SHEET 6 BA 9 GLN B1374 LYS B1378 -1 O GLN B1374 N ALA B1479
SHEET 7 BA 9 ILE B1322 ASP B1330 -1 O GLY B1326 N MET B1377
SHEET 8 BA 9 THR B1239 VAL B1246 -1 O GLU B1241 N THR B1327
SHEET 9 BA 9 SER B1268 THR B1273 -1 O SER B1268 N THR B1244
SHEET 1 BB 4 ARG B1383 HIS B1387 0
SHEET 2 BB 4 VAL B1466 ALA B1471 -1 O HIS B1467 N HIS B1387
SHEET 3 BB 4 CYS B1405 VAL B1410 -1 O GLU B1406 N GLN B1470
SHEET 4 BB 4 TYR B1449 GLN B1453 -1 O TYR B1449 N ALA B1409
LINK NI NI A2494 OAC 8XQ A3001 1555 1555 2.07
LINK NI NI A2494 NAI 8XQ A3001 1555 1555 2.15
LINK NI NI A2494 NE2 HIS A1387 1555 1555 2.02
LINK NI NI A2494 OE2 GLU A1389 1555 1555 2.13
LINK NI NI A2494 O HOH A2098 1555 1555 2.08
LINK NI NI A2494 O HOH A2103 1555 1555 2.37
LINK NA NA A2495 O HOH B2012 1555 4565 2.30
LINK NA NA A2495 O HOH B2013 1555 4565 2.08
LINK NA NA A2495 O HOH B2011 1555 4565 2.41
LINK NA NA A2495 OE2 GLU A1287 1555 1555 2.05
LINK NA NA A2495 OE1 GLU B1188 1555 4565 2.03
LINK NI NI A2500 O HOH A2054 1555 1555 2.16
LINK NI NI A2500 O HOH A2060 1555 1555 2.16
LINK NI NI A2500 O HOH A2015 1555 4465 2.18
LINK NI NI A2500 O HOH B2150 1555 4465 2.11
LINK NI NI A2500 O HOH A2013 1555 4465 2.19
LINK NI NI A2500 O HOH A2059 1555 1555 2.02
LINK NI NI B2500 O HOH B2155 1555 1555 2.17
LINK NI NI B2500 O HOH B2083 1555 1555 2.17
LINK NI NI B2500 OE2 GLU B1389 1555 1555 2.03
LINK NI NI B2500 NE2 HIS B1387 1555 1555 2.07
LINK NI NI B2500 NAI 8XQ B3001 1555 1555 2.15
LINK NI NI B2500 OAC 8XQ B3001 1555 1555 2.12
CISPEP 1 GLY A 1401 PRO A 1402 0 2.40
CISPEP 2 GLY B 1401 PRO B 1402 0 4.84
SITE 1 AC1 5 HIS A1387 GLU A1389 HOH A2098 HOH A2103
SITE 2 AC1 5 8XQ A3001
SITE 1 AC2 6 HOH A2013 HOH A2015 HOH A2054 HOH A2059
SITE 2 AC2 6 HOH A2060 HOH B2150
SITE 1 AC3 5 HIS B1387 GLU B1389 HOH B2083 HOH B2155
SITE 2 AC3 5 8XQ B3001
SITE 1 AC4 5 GLU A1287 GLU B1188 HOH B2011 HOH B2012
SITE 2 AC4 5 HOH B2013
SITE 1 AC5 4 ILE A1185 TYR A1186 GLN B1200 HOH B2020
SITE 1 AC6 7 ASP A1204 GLN A1489 HOH A2163 HOH A2164
SITE 2 AC6 7 PRO B1183 SER B1184 PHE B1201
SITE 1 AC7 3 ASP A1330 MET A1370 HOH A2015
SITE 1 AC8 4 ARG A1191 LYS B1190 ARG B1191 TYR B1497
SITE 1 AC9 4 SER A1227 THR A1228 GLY A1401 ASN A1476
SITE 1 BC1 12 TYR A1376 LYS A1378 THR A1384 HIS A1387
SITE 2 BC1 12 GLU A1389 ASN A1397 TRP A1407 ILE A1461
SITE 3 BC1 12 HIS A1467 ASN A1477 HOH A2103 NI A2494
SITE 1 BC2 11 TYR B1376 LYS B1378 THR B1384 HIS B1387
SITE 2 BC2 11 GLU B1389 ASN B1397 TRP B1407 HIS B1467
SITE 3 BC2 11 HOH B2091 HOH B2155 NI B2500
CRYST1 56.757 71.431 159.698 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017619 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006262 0.00000
(ATOM LINES ARE NOT SHOWN.)
END