HEADER OXIDOREDUCTASE 19-OCT-10 2XUE
TITLE CRYSTAL STRUCTURE OF JMJD3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 6B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1138-1640;
COMPND 5 SYNONYM: JMJD3, JMJC DOMAIN-CONTAINING PROTEIN 3, JUMONJI
COMPND 6 DOMAIN-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: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PFB-HTB
KEYWDS OXIDOREDUCTASE, HISTONE METHYLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHUNG,P.ROWLAND,J.MOSLEY,P.J.THOMAS
REVDAT 3 29-AUG-12 2XUE 1 JRNL
REVDAT 2 25-JUL-12 2XUE 1 JRNL
REVDAT 1 28-DEC-11 2XUE 0
JRNL AUTH L.KRUIDENIER,C.CHUNG,Z.CHENG,J.LIDDLE,K.CHE,G.JOBERTY,
JRNL AUTH 2 M.BANTSCHEFF,C.BOUNTRA,A.BRIDGES,H.DIALLO,D.EBERHARD,
JRNL AUTH 3 S.HUTCHINSON,E.JONES,R.KATSO,M.LEVERIDGE,P.K.MANDER,
JRNL AUTH 4 J.MOSLEY,C.RAMIREZ-MOLINA,P.ROWLAND,C.J.SCHOFIELD,
JRNL AUTH 5 R.J.SHEPPARD,J.E.SMITH,C.SWALES,R.TANNER,P.THOMAS,A.TUMBER,
JRNL AUTH 6 G.DREWES,U.OPPERMANN,D.J.PATEL,K.LEE,D.M.WILSON
JRNL TITL A SELECTIVE JUMONJI H3K27 DEMETHYLASE INHIBITOR MODULATES
JRNL TITL 2 THE PROINFLAMMATORY MACROPHAGE RESPONSE
JRNL REF NATURE V. 488 404 2012
JRNL REFN ISSN 0028-0836
JRNL PMID 22842901
JRNL DOI 10.1038/NATURE11262
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.76
REMARK 3 NUMBER OF REFLECTIONS : 59387
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) : 0.18081
REMARK 3 R VALUE (WORKING SET) : 0.17932
REMARK 3 FREE R VALUE : 0.21574
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2450
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) : 2.001
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.053
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2822
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.290
REMARK 3 BIN FREE R VALUE SET COUNT : 103
REMARK 3 BIN FREE R VALUE : 0.348
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6840
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.196
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.95
REMARK 3 B22 (A**2) : 1.40
REMARK 3 B33 (A**2) : 0.08
REMARK 3 B12 (A**2) : -2.46
REMARK 3 B13 (A**2) : -1.11
REMARK 3 B23 (A**2) : 1.85
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.189
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.488
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7068 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4722 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9612 ; 1.089 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11455 ; 0.806 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 852 ; 7.485 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 335 ;31.901 ;23.761
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1141 ;12.713 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;13.019 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1048 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7852 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1468 ; 0.001 ; 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): 4262 ; 0.876 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1712 ; 0.098 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6917 ; 1.722 ; 4.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2806 ; 2.025 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2695 ; 3.072 ; 6.000
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 : 2
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 1178 A 4000
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1601 17.0940 -13.7037
REMARK 3 T TENSOR
REMARK 3 T11: 0.0336 T22: 0.0185
REMARK 3 T33: 0.0249 T12: -0.0147
REMARK 3 T13: 0.0009 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.6615 L22: 0.3081
REMARK 3 L33: 0.6222 L12: -0.3322
REMARK 3 L13: 0.4244 L23: -0.3204
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: -0.0180 S13: -0.0178
REMARK 3 S21: -0.0038 S22: 0.0115 S23: 0.0061
REMARK 3 S31: -0.0018 S32: -0.0344 S33: -0.0107
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 : B 1181 B 4000
REMARK 3 ORIGIN FOR THE GROUP (A): 74.7027 45.6923 19.3965
REMARK 3 T TENSOR
REMARK 3 T11: 0.0355 T22: 0.0116
REMARK 3 T33: 0.0235 T12: -0.0103
REMARK 3 T13: 0.0116 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.5940 L22: 0.4552
REMARK 3 L33: 0.5281 L12: -0.2417
REMARK 3 L13: 0.2247 L23: -0.2752
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: 0.0028 S13: -0.0064
REMARK 3 S21: -0.0368 S22: 0.0224 S23: -0.0326
REMARK 3 S31: 0.0502 S32: -0.0428 S33: -0.0116
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 3 RIDING POSITIONS.
REMARK 3 ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS.
REMARK 3 ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2XUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-OCT-10.
REMARK 100 THE PDBE ID CODE IS EBI-45826.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-APR-10; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ESRF; ESRF
REMARK 200 BEAMLINE : ID14-4; ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9810 ; 0.9795
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC; ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61840
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 40.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 200 DATA REDUNDANCY : 2.3
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.1
REMARK 200 R MERGE FOR SHELL (I) : 0.51
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSHARP, RESOLVE
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS SCREEN (MOLECULAR
REMARK 280 DIMENSIONS) CONDITION A12 (0.03M MGCL2, 0.03M CACL2, 0.1M
REMARK 280 TRIS HCL/BICINE PH 8.5, 12.5%V/V MPD, 12.5%W/V PEG1000,
REMARK 280 12.5%W/V PEG3350)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 ASP A 1141
REMARK 465 VAL A 1142
REMARK 465 VAL A 1143
REMARK 465 ARG A 1144
REMARK 465 ALA A 1145
REMARK 465 SER A 1146
REMARK 465 ARG A 1147
REMARK 465 ASN A 1148
REMARK 465 ALA A 1149
REMARK 465 LYS A 1150
REMARK 465 VAL A 1151
REMARK 465 LYS A 1152
REMARK 465 GLY A 1153
REMARK 465 LYS A 1154
REMARK 465 PHE A 1155
REMARK 465 ARG A 1156
REMARK 465 GLU A 1157
REMARK 465 SER A 1158
REMARK 465 TYR A 1159
REMARK 465 LEU A 1160
REMARK 465 SER A 1161
REMARK 465 PRO A 1162
REMARK 465 ALA A 1163
REMARK 465 GLN A 1164
REMARK 465 SER A 1165
REMARK 465 VAL A 1166
REMARK 465 LYS A 1167
REMARK 465 PRO A 1168
REMARK 465 LYS A 1169
REMARK 465 ILE A 1170
REMARK 465 ASN A 1171
REMARK 465 THR A 1172
REMARK 465 GLU A 1173
REMARK 465 GLU A 1174
REMARK 465 LYS A 1175
REMARK 465 LEU A 1176
REMARK 465 PRO A 1177
REMARK 465 GLN A 1293
REMARK 465 GLU A 1294
REMARK 465 GLU A 1295
REMARK 465 LYS A 1296
REMARK 465 GLU A 1297
REMARK 465 SER A 1298
REMARK 465 GLU A 1299
REMARK 465 ASP A 1300
REMARK 465 GLU A 1301
REMARK 465 GLU A 1302
REMARK 465 SER A 1303
REMARK 465 GLU A 1304
REMARK 465 GLU A 1305
REMARK 465 PRO A 1306
REMARK 465 ASP A 1307
REMARK 465 SER A 1308
REMARK 465 THR A 1309
REMARK 465 THR A 1310
REMARK 465 GLY A 1311
REMARK 465 THR A 1312
REMARK 465 PRO A 1313
REMARK 465 PRO A 1314
REMARK 465 SER A 1315
REMARK 465 SER A 1316
REMARK 465 ALA A 1317
REMARK 465 PRO A 1318
REMARK 465 ASP A 1319
REMARK 465 PRO A 1320
REMARK 465 LYS A 1321
REMARK 465 ASN A 1322
REMARK 465 HIS A 1323
REMARK 465 GLY A 1593
REMARK 465 SER A 1594
REMARK 465 ARG A 1595
REMARK 465 ALA A 1639
REMARK 465 SER A 1640
REMARK 465 THR A 1641
REMARK 465 SER A 1642
REMARK 465 ARG A 1643
REMARK 465 HIS A 1644
REMARK 465 HIS A 1645
REMARK 465 HIS A 1646
REMARK 465 HIS A 1647
REMARK 465 HIS A 1648
REMARK 465 HIS A 1649
REMARK 465 ASP B 1141
REMARK 465 VAL B 1142
REMARK 465 VAL B 1143
REMARK 465 ARG B 1144
REMARK 465 ALA B 1145
REMARK 465 SER B 1146
REMARK 465 ARG B 1147
REMARK 465 ASN B 1148
REMARK 465 ALA B 1149
REMARK 465 LYS B 1150
REMARK 465 VAL B 1151
REMARK 465 LYS B 1152
REMARK 465 GLY B 1153
REMARK 465 LYS B 1154
REMARK 465 PHE B 1155
REMARK 465 ARG B 1156
REMARK 465 GLU B 1157
REMARK 465 SER B 1158
REMARK 465 TYR B 1159
REMARK 465 LEU B 1160
REMARK 465 SER B 1161
REMARK 465 PRO B 1162
REMARK 465 ALA B 1163
REMARK 465 GLN B 1164
REMARK 465 SER B 1165
REMARK 465 VAL B 1166
REMARK 465 LYS B 1167
REMARK 465 PRO B 1168
REMARK 465 LYS B 1169
REMARK 465 ILE B 1170
REMARK 465 ASN B 1171
REMARK 465 THR B 1172
REMARK 465 GLU B 1173
REMARK 465 GLU B 1174
REMARK 465 LYS B 1175
REMARK 465 LEU B 1176
REMARK 465 PRO B 1177
REMARK 465 ARG B 1178
REMARK 465 GLU B 1179
REMARK 465 LYS B 1180
REMARK 465 GLN B 1293
REMARK 465 GLU B 1294
REMARK 465 GLU B 1295
REMARK 465 LYS B 1296
REMARK 465 GLU B 1297
REMARK 465 SER B 1298
REMARK 465 GLU B 1299
REMARK 465 ASP B 1300
REMARK 465 GLU B 1301
REMARK 465 GLU B 1302
REMARK 465 SER B 1303
REMARK 465 GLU B 1304
REMARK 465 GLU B 1305
REMARK 465 PRO B 1306
REMARK 465 ASP B 1307
REMARK 465 SER B 1308
REMARK 465 THR B 1309
REMARK 465 THR B 1310
REMARK 465 GLY B 1311
REMARK 465 THR B 1312
REMARK 465 PRO B 1313
REMARK 465 PRO B 1314
REMARK 465 SER B 1315
REMARK 465 SER B 1316
REMARK 465 ALA B 1317
REMARK 465 PRO B 1318
REMARK 465 ASP B 1319
REMARK 465 PRO B 1320
REMARK 465 LYS B 1321
REMARK 465 ASN B 1322
REMARK 465 GLU B 1591
REMARK 465 ASN B 1592
REMARK 465 GLY B 1593
REMARK 465 SER B 1594
REMARK 465 ARG B 1595
REMARK 465 ALA B 1639
REMARK 465 SER B 1640
REMARK 465 THR B 1641
REMARK 465 SER B 1642
REMARK 465 ARG B 1643
REMARK 465 HIS B 1644
REMARK 465 HIS B 1645
REMARK 465 HIS B 1646
REMARK 465 HIS B 1647
REMARK 465 HIS B 1648
REMARK 465 HIS B 1649
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 GLU A1591 CG CD OE1 OE2
REMARK 470 ASN A1592 CG OD1 ND2
REMARK 470 ASN A1596 CG OD1 ND2
REMARK 470 THR A1597 OG1 CG2
REMARK 470 GLU B1290 CG CD OE1 OE2
REMARK 470 SER B1590 OG
REMARK 470 ASN B1596 CG OD1 ND2
REMARK 470 GLN B1629 CD
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 A1238 74.36 -162.44
REMARK 500 MET A1373 -71.36 -105.94
REMARK 500 ASN A1584 -74.04 73.37
REMARK 500 SER B1238 70.51 -160.89
REMARK 500 LEU B1334 40.10 -102.82
REMARK 500 MET B1373 -64.39 -106.10
REMARK 500 ASN B1584 -72.46 71.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 1404 PRO A 1405 71.51
REMARK 500 GLY B 1404 PRO B 1405 69.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A1404 10.40
REMARK 500 GLY B1404 10.66
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 ZN A2000 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1575 SG
REMARK 620 2 CYS A1578 SG 106.5
REMARK 620 3 CYS A1605 SG 100.7 118.5
REMARK 620 4 CYS A1602 SG 112.2 117.8 100.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2000 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1575 SG
REMARK 620 2 CYS B1578 SG 104.9
REMARK 620 3 CYS B1602 SG 111.4 118.0
REMARK 620 4 CYS B1605 SG 101.4 115.3 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A3000 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A1390 NE2
REMARK 620 2 AKG A4000 O5 88.7
REMARK 620 3 HIS A1470 NE2 83.2 97.0
REMARK 620 4 GLU A1392 OE1 94.5 167.4 95.5
REMARK 620 5 AKG A4000 O1 169.8 81.6 101.1 94.3
REMARK 620 6 HOH A2144 O 91.2 89.3 171.4 78.4 85.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B3000 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B1392 OE1
REMARK 620 2 HOH B2100 O 77.8
REMARK 620 3 AKG B4000 O1 92.0 86.2
REMARK 620 4 HIS B1390 NE2 95.9 86.9 168.1
REMARK 620 5 AKG B4000 O5 165.0 88.1 82.0 88.1
REMARK 620 6 HIS B1470 NE2 93.3 168.5 101.4 86.9 101.3
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 ZN A2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG A4000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG B4000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B5000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A5000
DBREF 2XUE A 1141 1643 UNP O15054 KDM6B_HUMAN 1138 1640
DBREF 2XUE B 1141 1643 UNP O15054 KDM6B_HUMAN 1138 1640
SEQADV 2XUE HIS A 1644 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS A 1645 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS A 1646 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS A 1647 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS A 1648 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS A 1649 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS B 1644 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS B 1645 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS B 1646 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS B 1647 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS B 1648 UNP O15054 EXPRESSION TAG
SEQADV 2XUE HIS B 1649 UNP O15054 EXPRESSION TAG
SEQRES 1 A 509 ASP VAL VAL ARG ALA SER ARG ASN ALA LYS VAL LYS GLY
SEQRES 2 A 509 LYS PHE ARG GLU SER TYR LEU SER PRO ALA GLN SER VAL
SEQRES 3 A 509 LYS PRO LYS ILE ASN THR GLU GLU LYS LEU PRO ARG GLU
SEQRES 4 A 509 LYS LEU ASN PRO PRO THR PRO SER ILE TYR LEU GLU SER
SEQRES 5 A 509 LYS ARG ASP ALA PHE SER PRO VAL LEU LEU GLN PHE CYS
SEQRES 6 A 509 THR ASP PRO ARG ASN PRO ILE THR VAL ILE ARG GLY LEU
SEQRES 7 A 509 ALA GLY SER LEU ARG LEU ASN LEU GLY LEU PHE SER THR
SEQRES 8 A 509 LYS THR LEU VAL GLU ALA SER GLY GLU HIS THR VAL GLU
SEQRES 9 A 509 VAL ARG THR GLN VAL GLN GLN PRO SER ASP GLU ASN TRP
SEQRES 10 A 509 ASP LEU THR GLY THR ARG GLN ILE TRP PRO CYS GLU SER
SEQRES 11 A 509 SER ARG SER HIS THR THR ILE ALA LYS TYR ALA GLN TYR
SEQRES 12 A 509 GLN ALA SER SER PHE GLN GLU SER LEU GLN GLU GLU LYS
SEQRES 13 A 509 GLU SER GLU ASP GLU GLU SER GLU GLU PRO ASP SER THR
SEQRES 14 A 509 THR GLY THR PRO PRO SER SER ALA PRO ASP PRO LYS ASN
SEQRES 15 A 509 HIS HIS ILE ILE LYS PHE GLY THR ASN ILE ASP LEU SER
SEQRES 16 A 509 ASP ALA LYS ARG TRP LYS PRO GLN LEU GLN GLU LEU LEU
SEQRES 17 A 509 LYS LEU PRO ALA PHE MET ARG VAL THR SER THR GLY ASN
SEQRES 18 A 509 MET LEU SER HIS VAL GLY HIS THR ILE LEU GLY MET ASN
SEQRES 19 A 509 THR VAL GLN LEU TYR MET LYS VAL PRO GLY SER ARG THR
SEQRES 20 A 509 PRO GLY HIS GLN GLU ASN ASN ASN PHE CYS SER VAL ASN
SEQRES 21 A 509 ILE ASN ILE GLY PRO GLY ASP CYS GLU TRP PHE ALA VAL
SEQRES 22 A 509 HIS GLU HIS TYR TRP GLU THR ILE SER ALA PHE CYS ASP
SEQRES 23 A 509 ARG HIS GLY VAL ASP TYR LEU THR GLY SER TRP TRP PRO
SEQRES 24 A 509 ILE LEU ASP ASP LEU TYR ALA SER ASN ILE PRO VAL TYR
SEQRES 25 A 509 ARG PHE VAL GLN ARG PRO GLY ASP LEU VAL TRP ILE ASN
SEQRES 26 A 509 ALA GLY THR VAL HIS TRP VAL GLN ALA THR GLY TRP CYS
SEQRES 27 A 509 ASN ASN ILE ALA TRP ASN VAL GLY PRO LEU THR ALA TYR
SEQRES 28 A 509 GLN TYR GLN LEU ALA LEU GLU ARG TYR GLU TRP ASN GLU
SEQRES 29 A 509 VAL LYS ASN VAL LYS SER ILE VAL PRO MET ILE HIS VAL
SEQRES 30 A 509 SER TRP ASN VAL ALA ARG THR VAL LYS ILE SER ASP PRO
SEQRES 31 A 509 ASP LEU PHE LYS MET ILE LYS PHE CYS LEU LEU GLN SER
SEQRES 32 A 509 MET LYS HIS CYS GLN VAL GLN ARG GLU SER LEU VAL ARG
SEQRES 33 A 509 ALA GLY LYS LYS ILE ALA TYR GLN GLY ARG VAL LYS ASP
SEQRES 34 A 509 GLU PRO ALA TYR TYR CYS ASN GLU CYS ASP VAL GLU VAL
SEQRES 35 A 509 PHE ASN ILE LEU PHE VAL THR SER GLU ASN GLY SER ARG
SEQRES 36 A 509 ASN THR TYR LEU VAL HIS CYS GLU GLY CYS ALA ARG ARG
SEQRES 37 A 509 ARG SER ALA GLY LEU GLN GLY VAL VAL VAL LEU GLU GLN
SEQRES 38 A 509 TYR ARG THR GLU GLU LEU ALA GLN ALA TYR ASP ALA PHE
SEQRES 39 A 509 THR LEU ALA PRO ALA SER THR SER ARG HIS HIS HIS HIS
SEQRES 40 A 509 HIS HIS
SEQRES 1 B 509 ASP VAL VAL ARG ALA SER ARG ASN ALA LYS VAL LYS GLY
SEQRES 2 B 509 LYS PHE ARG GLU SER TYR LEU SER PRO ALA GLN SER VAL
SEQRES 3 B 509 LYS PRO LYS ILE ASN THR GLU GLU LYS LEU PRO ARG GLU
SEQRES 4 B 509 LYS LEU ASN PRO PRO THR PRO SER ILE TYR LEU GLU SER
SEQRES 5 B 509 LYS ARG ASP ALA PHE SER PRO VAL LEU LEU GLN PHE CYS
SEQRES 6 B 509 THR ASP PRO ARG ASN PRO ILE THR VAL ILE ARG GLY LEU
SEQRES 7 B 509 ALA GLY SER LEU ARG LEU ASN LEU GLY LEU PHE SER THR
SEQRES 8 B 509 LYS THR LEU VAL GLU ALA SER GLY GLU HIS THR VAL GLU
SEQRES 9 B 509 VAL ARG THR GLN VAL GLN GLN PRO SER ASP GLU ASN TRP
SEQRES 10 B 509 ASP LEU THR GLY THR ARG GLN ILE TRP PRO CYS GLU SER
SEQRES 11 B 509 SER ARG SER HIS THR THR ILE ALA LYS TYR ALA GLN TYR
SEQRES 12 B 509 GLN ALA SER SER PHE GLN GLU SER LEU GLN GLU GLU LYS
SEQRES 13 B 509 GLU SER GLU ASP GLU GLU SER GLU GLU PRO ASP SER THR
SEQRES 14 B 509 THR GLY THR PRO PRO SER SER ALA PRO ASP PRO LYS ASN
SEQRES 15 B 509 HIS HIS ILE ILE LYS PHE GLY THR ASN ILE ASP LEU SER
SEQRES 16 B 509 ASP ALA LYS ARG TRP LYS PRO GLN LEU GLN GLU LEU LEU
SEQRES 17 B 509 LYS LEU PRO ALA PHE MET ARG VAL THR SER THR GLY ASN
SEQRES 18 B 509 MET LEU SER HIS VAL GLY HIS THR ILE LEU GLY MET ASN
SEQRES 19 B 509 THR VAL GLN LEU TYR MET LYS VAL PRO GLY SER ARG THR
SEQRES 20 B 509 PRO GLY HIS GLN GLU ASN ASN ASN PHE CYS SER VAL ASN
SEQRES 21 B 509 ILE ASN ILE GLY PRO GLY ASP CYS GLU TRP PHE ALA VAL
SEQRES 22 B 509 HIS GLU HIS TYR TRP GLU THR ILE SER ALA PHE CYS ASP
SEQRES 23 B 509 ARG HIS GLY VAL ASP TYR LEU THR GLY SER TRP TRP PRO
SEQRES 24 B 509 ILE LEU ASP ASP LEU TYR ALA SER ASN ILE PRO VAL TYR
SEQRES 25 B 509 ARG PHE VAL GLN ARG PRO GLY ASP LEU VAL TRP ILE ASN
SEQRES 26 B 509 ALA GLY THR VAL HIS TRP VAL GLN ALA THR GLY TRP CYS
SEQRES 27 B 509 ASN ASN ILE ALA TRP ASN VAL GLY PRO LEU THR ALA TYR
SEQRES 28 B 509 GLN TYR GLN LEU ALA LEU GLU ARG TYR GLU TRP ASN GLU
SEQRES 29 B 509 VAL LYS ASN VAL LYS SER ILE VAL PRO MET ILE HIS VAL
SEQRES 30 B 509 SER TRP ASN VAL ALA ARG THR VAL LYS ILE SER ASP PRO
SEQRES 31 B 509 ASP LEU PHE LYS MET ILE LYS PHE CYS LEU LEU GLN SER
SEQRES 32 B 509 MET LYS HIS CYS GLN VAL GLN ARG GLU SER LEU VAL ARG
SEQRES 33 B 509 ALA GLY LYS LYS ILE ALA TYR GLN GLY ARG VAL LYS ASP
SEQRES 34 B 509 GLU PRO ALA TYR TYR CYS ASN GLU CYS ASP VAL GLU VAL
SEQRES 35 B 509 PHE ASN ILE LEU PHE VAL THR SER GLU ASN GLY SER ARG
SEQRES 36 B 509 ASN THR TYR LEU VAL HIS CYS GLU GLY CYS ALA ARG ARG
SEQRES 37 B 509 ARG SER ALA GLY LEU GLN GLY VAL VAL VAL LEU GLU GLN
SEQRES 38 B 509 TYR ARG THR GLU GLU LEU ALA GLN ALA TYR ASP ALA PHE
SEQRES 39 B 509 THR LEU ALA PRO ALA SER THR SER ARG HIS HIS HIS HIS
SEQRES 40 B 509 HIS HIS
HET ZN A2000 1
HET FE A3000 1
HET AKG A4000 10
HET ZN B2000 1
HET FE B3000 1
HET AKG B4000 10
HET SO4 B5000 5
HET SO4 A5000 5
HETNAM ZN ZINC ION
HETNAM FE FE (III) ION
HETNAM AKG 2-OXOGLUTARIC ACID
HETNAM SO4 SULFATE ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 FE 2(FE 3+)
FORMUL 4 AKG 2(C5 H6 O5)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 7 HOH *560(H2 O)
HELIX 1 1 SER A 1192 PHE A 1197 1 6
HELIX 2 2 SER A 1198 ASP A 1207 1 10
HELIX 3 3 GLY A 1217 ARG A 1223 1 7
HELIX 4 4 ASN A 1225 PHE A 1229 5 5
HELIX 5 5 SER A 1230 GLY A 1239 1 10
HELIX 6 6 ILE A 1277 LEU A 1292 1 16
HELIX 7 7 TRP A 1340 LEU A 1347 1 8
HELIX 8 8 LEU A 1348 LEU A 1350 5 3
HELIX 9 9 PRO A 1351 ARG A 1355 5 5
HELIX 10 10 MET A 1362 VAL A 1366 5 5
HELIX 11 11 GLU A 1392 PHE A 1396 5 5
HELIX 12 12 HIS A 1414 HIS A 1416 5 3
HELIX 13 13 TYR A 1417 HIS A 1428 1 12
HELIX 14 14 ILE A 1440 SER A 1447 1 8
HELIX 15 15 THR A 1489 LYS A 1506 1 18
HELIX 16 16 PRO A 1513 VAL A 1525 1 13
HELIX 17 17 ASP A 1529 GLY A 1558 1 30
HELIX 18 18 CYS A 1602 ARG A 1608 1 7
HELIX 19 19 ARG A 1623 ALA A 1633 1 11
HELIX 20 20 SER B 1192 PHE B 1197 1 6
HELIX 21 21 SER B 1198 ASP B 1207 1 10
HELIX 22 22 GLY B 1217 LEU B 1222 1 6
HELIX 23 23 ASN B 1225 PHE B 1229 5 5
HELIX 24 24 SER B 1230 GLY B 1239 1 10
HELIX 25 25 ILE B 1277 GLU B 1290 1 14
HELIX 26 26 TRP B 1340 LEU B 1347 1 8
HELIX 27 27 LEU B 1348 LEU B 1350 5 3
HELIX 28 28 PRO B 1351 ARG B 1355 5 5
HELIX 29 29 MET B 1362 VAL B 1366 5 5
HELIX 30 30 GLU B 1392 PHE B 1396 5 5
HELIX 31 31 HIS B 1414 HIS B 1416 5 3
HELIX 32 32 TYR B 1417 HIS B 1428 1 12
HELIX 33 33 ILE B 1440 SER B 1447 1 8
HELIX 34 34 THR B 1489 LYS B 1506 1 18
HELIX 35 35 PRO B 1513 VAL B 1525 1 13
HELIX 36 36 ASP B 1529 GLY B 1558 1 30
HELIX 37 37 CYS B 1602 ARG B 1609 1 8
HELIX 38 38 ARG B 1623 PHE B 1634 1 12
SHEET 1 AA 9 SER A1187 TYR A1189 0
SHEET 2 AA 9 ILE A1212 ARG A1216 1 O VAL A1214 N ILE A1188
SHEET 3 AA 9 LEU A1461 ILE A1464 -1 O LEU A1461 N ILE A1215
SHEET 4 AA 9 CYS A1397 PRO A1405 -1 O SER A1398 N ILE A1464
SHEET 5 AA 9 CYS A1478 VAL A1485 -1 O ASN A1479 N ILE A1403
SHEET 6 AA 9 GLN A1377 LYS A1381 -1 O GLN A1377 N ALA A1482
SHEET 7 AA 9 ILE A1325 ASP A1333 -1 O GLY A1329 N MET A1380
SHEET 8 AA 9 THR A1242 VAL A1249 -1 O GLU A1244 N THR A1330
SHEET 9 AA 9 SER A1271 THR A1276 -1 O SER A1271 N THR A1247
SHEET 1 AB 4 ARG A1386 HIS A1390 0
SHEET 2 AB 4 VAL A1469 ALA A1474 -1 O HIS A1470 N HIS A1390
SHEET 3 AB 4 CYS A1408 VAL A1413 -1 O GLU A1409 N GLN A1473
SHEET 4 AB 4 TYR A1452 GLN A1456 -1 O TYR A1452 N ALA A1412
SHEET 1 AC 4 ALA A1562 TYR A1563 0
SHEET 2 AC 4 VAL A1617 GLU A1620 1 O VAL A1618 N ALA A1562
SHEET 3 AC 4 ILE A1585 SER A1590 -1 O LEU A1586 N LEU A1619
SHEET 4 AC 4 TYR A1598 HIS A1601 -1 O LEU A1599 N THR A1589
SHEET 1 AD 2 TYR A1573 TYR A1574 0
SHEET 2 AD 2 GLU A1581 VAL A1582 -1 O VAL A1582 N TYR A1573
SHEET 1 BA 9 SER B1187 TYR B1189 0
SHEET 2 BA 9 ILE B1212 ARG B1216 1 O VAL B1214 N ILE B1188
SHEET 3 BA 9 LEU B1461 ILE B1464 -1 O LEU B1461 N ILE B1215
SHEET 4 BA 9 CYS B1397 PRO B1405 -1 O SER B1398 N ILE B1464
SHEET 5 BA 9 CYS B1478 VAL B1485 -1 O ASN B1479 N ILE B1403
SHEET 6 BA 9 GLN B1377 LYS B1381 -1 O GLN B1377 N ALA B1482
SHEET 7 BA 9 ILE B1325 ASP B1333 -1 O GLY B1329 N MET B1380
SHEET 8 BA 9 THR B1242 VAL B1249 -1 O GLU B1244 N THR B1330
SHEET 9 BA 9 SER B1271 THR B1276 -1 O SER B1271 N THR B1247
SHEET 1 BB 4 ARG B1386 HIS B1390 0
SHEET 2 BB 4 VAL B1469 ALA B1474 -1 O HIS B1470 N HIS B1390
SHEET 3 BB 4 CYS B1408 VAL B1413 -1 O GLU B1409 N GLN B1473
SHEET 4 BB 4 TYR B1452 GLN B1456 -1 O TYR B1452 N ALA B1412
SHEET 1 BC 4 ILE B1561 TYR B1563 0
SHEET 2 BC 4 VAL B1617 GLU B1620 1 O VAL B1618 N ALA B1562
SHEET 3 BC 4 ILE B1585 THR B1589 -1 O LEU B1586 N LEU B1619
SHEET 4 BC 4 LEU B1599 HIS B1601 -1 O LEU B1599 N THR B1589
SHEET 1 BD 2 TYR B1573 TYR B1574 0
SHEET 2 BD 2 GLU B1581 VAL B1582 -1 O VAL B1582 N TYR B1573
LINK ZN ZN A2000 SG CYS A1575 1555 1555 2.33
LINK ZN ZN A2000 SG CYS A1578 1555 1555 2.32
LINK ZN ZN A2000 SG CYS A1605 1555 1555 2.34
LINK ZN ZN A2000 SG CYS A1602 1555 1555 2.32
LINK FE FE A3000 NE2 HIS A1390 1555 1555 2.13
LINK FE FE A3000 O5 AKG A4000 1555 1555 2.14
LINK FE FE A3000 NE2 HIS A1470 1555 1555 2.12
LINK FE FE A3000 O HOH A2144 1555 1555 2.16
LINK FE FE A3000 O1 AKG A4000 1555 1555 1.99
LINK FE FE A3000 OE1 GLU A1392 1555 1555 1.93
LINK ZN ZN B2000 SG CYS B1578 1555 1555 2.34
LINK ZN ZN B2000 SG CYS B1575 1555 1555 2.32
LINK ZN ZN B2000 SG CYS B1605 1555 1555 2.34
LINK ZN ZN B2000 SG CYS B1602 1555 1555 2.33
LINK FE FE B3000 O HOH B2100 1555 1555 2.26
LINK FE FE B3000 O1 AKG B4000 1555 1555 2.00
LINK FE FE B3000 NE2 HIS B1390 1555 1555 2.13
LINK FE FE B3000 O5 AKG B4000 1555 1555 2.13
LINK FE FE B3000 NE2 HIS B1470 1555 1555 2.14
LINK FE FE B3000 OE1 GLU B1392 1555 1555 1.89
SITE 1 AC1 4 CYS A1575 CYS A1578 CYS A1602 CYS A1605
SITE 1 AC2 5 HIS A1390 GLU A1392 HIS A1470 HOH A2144
SITE 2 AC2 5 AKG A4000
SITE 1 AC3 11 LYS A1381 THR A1387 HIS A1390 GLU A1392
SITE 2 AC3 11 SER A1398 ASN A1400 HIS A1470 ALA A1482
SITE 3 AC3 11 HOH A2144 HOH A2318 FE A3000
SITE 1 AC4 4 CYS B1575 CYS B1578 CYS B1602 CYS B1605
SITE 1 AC5 5 HIS B1390 GLU B1392 HIS B1470 HOH B2100
SITE 2 AC5 5 AKG B4000
SITE 1 AC6 11 LYS B1381 THR B1387 HIS B1390 GLU B1392
SITE 2 AC6 11 SER B1398 ASN B1400 HIS B1470 ALA B1482
SITE 3 AC6 11 HOH B2100 HOH B2241 FE B3000
SITE 1 AC7 4 TYR B1573 LEU B1586 VAL B1588 VAL B1600
SITE 1 AC8 4 GLU A1415 GLU A1498 HOH A2161 HOH A2317
CRYST1 61.215 65.154 77.462 86.09 67.19 68.26 P 1 2
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 0.016336 -0.006514 -0.007473 0.00000
SCALE2 0.000000 0.016523 0.001461 0.00000
SCALE3 0.000000 0.000000 0.014059 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
