HEADER OXIDOREDUCTASE 08-FEB-12 4AI9
TITLE JMJD2A COMPLEXED WITH DAMINOZIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1-359;
COMPND 5 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A,
COMPND 6 JUMONJI DOMAIN-CONTAINING PROTEIN 2A;
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);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS OXIDOREDUCTASE, DIOXYGENASE, OXYGENASE, DOUBLE-STRANDED BETA HELIX,
KEYWDS 2 FACIAL TRIAD, EPIGENETIC AND TRANSCRIPTION REGULATION, CHROMATIN
KEYWDS 3 REGULATOR, HYDROXYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CHOWDHURY,C.J.SCHOFIELD
REVDAT 5 20-DEC-23 4AI9 1 REMARK LINK
REVDAT 4 30-JAN-19 4AI9 1 REMARK
REVDAT 3 28-MAR-18 4AI9 1 TITLE JRNL
REVDAT 2 24-JAN-18 4AI9 1 JRNL
REVDAT 1 03-OCT-12 4AI9 0
JRNL AUTH N.R.ROSE,E.C.WOON,A.TUMBER,L.J.WALPORT,R.CHOWDHURY,X.S.LI,
JRNL AUTH 2 O.N.KING,C.LEJEUNE,S.S.NG,T.KROJER,M.C.CHAN,A.M.RYDZIK,
JRNL AUTH 3 R.J.HOPKINSON,K.H.CHE,M.DANIEL,C.STRAIN-DAMERELL,C.GILEADI,
JRNL AUTH 4 G.KOCHAN,I.K.LEUNG,J.DUNFORD,K.K.YEOH,P.J.RATCLIFFE,
JRNL AUTH 5 N.BURGESS-BROWN,F.VON DELFT,S.MULLER,B.MARSDEN,P.E.BRENNAN,
JRNL AUTH 6 M.A.MCDONOUGH,U.OPPERMANN,R.J.KLOSE,C.J.SCHOFIELD,A.KAWAMURA
JRNL TITL PLANT GROWTH REGULATOR DAMINOZIDE IS A SELECTIVE INHIBITOR
JRNL TITL 2 OF HUMAN KDM2/7 HISTONE DEMETHYLASES.
JRNL REF J. MED. CHEM. V. 55 6639 2012
JRNL REFN ISSN 1520-4804
JRNL PMID 22724510
JRNL DOI 10.1021/JM300677J
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 62825.450
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 40190
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 SET) : 0.216
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400
REMARK 3 FREE R VALUE TEST SET COUNT : 2059
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3981
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 158
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5689
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 568
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.46000
REMARK 3 B22 (A**2) : 2.66000
REMARK 3 B33 (A**2) : 5.80000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.30
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.990
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.860 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.720 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 54.16
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : DZA.PAR
REMARK 3 PARAMETER FILE 5 : GOL.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : DZA.TOP
REMARK 3 TOPOLOGY FILE 5 : GOL.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 4AI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1290051235.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91730
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40190
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 45.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.64000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2OX0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRATE PH 5.5, 4MM NICL2, 20%
REMARK 280 PEG 3350, VAPOUR DIFFUSION, SITTING DROP, TEMPERATURE 277K,
REMARK 280 VAPOR DIFFUSION, SITTING DROP
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 50.23800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.87600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.23800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.87600
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 MET A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLU A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 GLU A 356
REMARK 465 SER A 357
REMARK 465 GLU A 358
REMARK 465 LEU A 359
REMARK 465 MET B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 VAL B -11
REMARK 465 ASP B -10
REMARK 465 LEU B -9
REMARK 465 GLY B -8
REMARK 465 THR B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLU B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 GLU B 356
REMARK 465 SER B 357
REMARK 465 GLU B 358
REMARK 465 LEU B 359
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 104 CG OD1 OD2
REMARK 470 GLN A 232 CG CD OE1 NE2
REMARK 470 LYS A 336 CE NZ
REMARK 470 ARG B 95 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 99 CG CD CE NZ
REMARK 470 ASP B 104 CG OD1 OD2
REMARK 470 ARG B 221 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 232 CG CD OE1 NE2
REMARK 470 GLU B 235 CG CD OE1 OE2
REMARK 470 ASP B 311 CG OD1 OD2
REMARK 470 LYS B 330 CD CE NZ
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 VAL A 66 O HOH A 2063 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 TYR A 59 46.03 -108.50
REMARK 500 ASP A 63 -9.71 -58.36
REMARK 500 ALA A 91 151.98 -49.83
REMARK 500 LYS A 143 -5.58 -49.89
REMARK 500 ARG A 152 70.43 -158.87
REMARK 500 VAL A 171 -61.19 -95.62
REMARK 500 GLU A 349 -8.47 -51.44
REMARK 500 LYS B 51 -31.53 -34.63
REMARK 500 TYR B 59 42.69 -101.72
REMARK 500 ASP B 63 -8.53 -58.59
REMARK 500 ALA B 69 73.40 -155.76
REMARK 500 ASN B 128 68.53 35.94
REMARK 500 LYS B 143 -2.74 -51.17
REMARK 500 ARG B 152 75.99 -161.28
REMARK 500 VAL B 171 -61.31 -97.40
REMARK 500 MET B 192 18.18 56.54
REMARK 500 ALA B 236 54.47 -151.34
REMARK 500 GLU B 349 -6.15 -57.67
REMARK 500 GLU B 352 -9.11 -58.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2096 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A2123 DISTANCE = 5.88 ANGSTROMS
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 104.9
REMARK 620 3 HIS A 276 NE2 81.1 82.9
REMARK 620 4 DZA A 605 O01 96.3 155.7 89.0
REMARK 620 5 DZA A 605 N04 157.5 95.5 111.3 66.2
REMARK 620 6 HOH A2159 O 81.3 96.3 161.6 98.4 87.1
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 107.3
REMARK 620 3 CYS A 306 SG 119.9 109.5
REMARK 620 4 CYS A 308 SG 115.0 86.5 113.0
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 100.0
REMARK 620 3 HIS B 276 NE2 89.2 89.0
REMARK 620 4 DZA B 603 O01 103.4 153.2 104.2
REMARK 620 5 DZA B 603 N04 108.0 89.2 162.7 71.3
REMARK 620 6 DZA B 603 C06 75.0 84.3 161.5 89.2 34.7
REMARK 620 7 HOH B2182 O 177.2 80.6 93.6 75.5 69.2 102.3
REMARK 620 N 1 2 3 4 5 6
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 104.4
REMARK 620 3 CYS B 306 SG 116.2 113.2
REMARK 620 4 CYS B 308 SG 116.9 89.5 113.0
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 NI A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DZA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DZA A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DZA B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GF7 RELATED DB: PDB
REMARK 900 DOUBLE TUDOR DOMAIN STRUCTURE
REMARK 900 RELATED ID: 2GFA RELATED DB: PDB
REMARK 900 DOUBLE TUDOR DOMAIN COMPLEX STRUCTURE
REMARK 900 RELATED ID: 2GP3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC CORE COMAIN OF JMJD2A
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: 2VD7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJD2A COMPLEXED WITH INHIBITOR PYRIDINE-2,4-
REMARK 900 DICARBOXYLIC ACID
REMARK 900 RELATED ID: 2WWJ RELATED DB: PDB
REMARK 900 STRUCTURE OF JMJD2A COMPLEXED WITH INHIBITOR 10A
REMARK 900 RELATED ID: 2YBK RELATED DB: PDB
REMARK 900 JMJD2A COMPLEXED WITH R-2-HYDROXYGLUTARATE
REMARK 900 RELATED ID: 2YBP RELATED DB: PDB
REMARK 900 JMJD2A COMPLEXED WITH R-2-HYDROXYGLUTARATE AND HISTONE H3K36ME3
REMARK 900 PEPTIDE (30-41)
REMARK 900 RELATED ID: 2YBS RELATED DB: PDB
REMARK 900 JMJD2A COMPLEXED WITH S-2-HYDROXYGLUTARATE AND HISTONE H3K36ME3
REMARK 900 PEPTIDE (30-41)
DBREF 4AI9 A 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 4AI9 B 1 359 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 4AI9 MET A -21 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS A -20 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS A -19 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS A -18 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS A -17 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS A -16 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS A -15 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 SER A -14 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 SER A -13 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 GLY A -12 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 VAL A -11 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 ASP A -10 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 LEU A -9 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 GLY A -8 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 THR A -7 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 GLU A -6 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 ASN A -5 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 LEU A -4 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 TYR A -3 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 PHE A -2 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 GLN A -1 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 SER A 0 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 MET B -21 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS B -20 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS B -19 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS B -18 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS B -17 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS B -16 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 HIS B -15 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 SER B -14 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 SER B -13 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 GLY B -12 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 VAL B -11 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 ASP B -10 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 LEU B -9 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 GLY B -8 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 THR B -7 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 GLU B -6 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 ASN B -5 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 LEU B -4 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 TYR B -3 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 PHE B -2 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 GLN B -1 UNP O75164 EXPRESSION TAG
SEQADV 4AI9 SER B 0 UNP O75164 EXPRESSION TAG
SEQRES 1 A 381 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 381 GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER GLU
SEQRES 3 A 381 SER GLU THR LEU ASN PRO SER ALA ARG ILE MET THR PHE
SEQRES 4 A 381 TYR PRO THR MET GLU GLU PHE ARG ASN PHE SER ARG TYR
SEQRES 5 A 381 ILE ALA TYR ILE GLU SER GLN GLY ALA HIS ARG ALA GLY
SEQRES 6 A 381 LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP LYS PRO ARG
SEQRES 7 A 381 ALA SER TYR ASP ASP ILE ASP ASP LEU VAL ILE PRO ALA
SEQRES 8 A 381 PRO ILE GLN GLN LEU VAL THR GLY GLN SER GLY LEU PHE
SEQRES 9 A 381 THR GLN TYR ASN ILE GLN LYS LYS ALA MET THR VAL ARG
SEQRES 10 A 381 GLU PHE ARG LYS ILE ALA ASN SER ASP LYS TYR CYS THR
SEQRES 11 A 381 PRO ARG TYR SER GLU PHE GLU GLU LEU GLU ARG LYS TYR
SEQRES 12 A 381 TRP LYS ASN LEU THR PHE ASN PRO PRO ILE TYR GLY ALA
SEQRES 13 A 381 ASP VAL ASN GLY THR LEU TYR GLU LYS HIS VAL ASP GLU
SEQRES 14 A 381 TRP ASN ILE GLY ARG LEU ARG THR ILE LEU ASP LEU VAL
SEQRES 15 A 381 GLU LYS GLU SER GLY ILE THR ILE GLU GLY VAL ASN THR
SEQRES 16 A 381 PRO TYR LEU TYR PHE GLY MET TRP LYS THR SER PHE ALA
SEQRES 17 A 381 TRP HIS THR GLU ASP MET ASP LEU TYR SER ILE ASN TYR
SEQRES 18 A 381 LEU HIS PHE GLY GLU PRO LYS SER TRP TYR SER VAL PRO
SEQRES 19 A 381 PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU ALA LYS GLY
SEQRES 20 A 381 PHE PHE PRO GLY SER ALA GLN SER CYS GLU ALA PHE LEU
SEQRES 21 A 381 ARG HIS LYS MET THR LEU ILE SER PRO LEU MET LEU LYS
SEQRES 22 A 381 LYS TYR GLY ILE PRO PHE ASP LYS VAL THR GLN GLU ALA
SEQRES 23 A 381 GLY GLU PHE MET ILE THR PHE PRO TYR GLY TYR HIS ALA
SEQRES 24 A 381 GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU SER THR ASN
SEQRES 25 A 381 PHE ALA THR ARG ARG TRP ILE GLU TYR GLY LYS GLN ALA
SEQRES 26 A 381 VAL LEU CYS SER CYS ARG LYS ASP MET VAL LYS ILE SER
SEQRES 27 A 381 MET ASP VAL PHE VAL ARG LYS PHE GLN PRO GLU ARG TYR
SEQRES 28 A 381 LYS LEU TRP LYS ALA GLY LYS ASP ASN THR VAL ILE ASP
SEQRES 29 A 381 HIS THR LEU PRO THR PRO GLU ALA ALA GLU PHE LEU LYS
SEQRES 30 A 381 GLU SER GLU LEU
SEQRES 1 B 381 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 381 GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER GLU
SEQRES 3 B 381 SER GLU THR LEU ASN PRO SER ALA ARG ILE MET THR PHE
SEQRES 4 B 381 TYR PRO THR MET GLU GLU PHE ARG ASN PHE SER ARG TYR
SEQRES 5 B 381 ILE ALA TYR ILE GLU SER GLN GLY ALA HIS ARG ALA GLY
SEQRES 6 B 381 LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP LYS PRO ARG
SEQRES 7 B 381 ALA SER TYR ASP ASP ILE ASP ASP LEU VAL ILE PRO ALA
SEQRES 8 B 381 PRO ILE GLN GLN LEU VAL THR GLY GLN SER GLY LEU PHE
SEQRES 9 B 381 THR GLN TYR ASN ILE GLN LYS LYS ALA MET THR VAL ARG
SEQRES 10 B 381 GLU PHE ARG LYS ILE ALA ASN SER ASP LYS TYR CYS THR
SEQRES 11 B 381 PRO ARG TYR SER GLU PHE GLU GLU LEU GLU ARG LYS TYR
SEQRES 12 B 381 TRP LYS ASN LEU THR PHE ASN PRO PRO ILE TYR GLY ALA
SEQRES 13 B 381 ASP VAL ASN GLY THR LEU TYR GLU LYS HIS VAL ASP GLU
SEQRES 14 B 381 TRP ASN ILE GLY ARG LEU ARG THR ILE LEU ASP LEU VAL
SEQRES 15 B 381 GLU LYS GLU SER GLY ILE THR ILE GLU GLY VAL ASN THR
SEQRES 16 B 381 PRO TYR LEU TYR PHE GLY MET TRP LYS THR SER PHE ALA
SEQRES 17 B 381 TRP HIS THR GLU ASP MET ASP LEU TYR SER ILE ASN TYR
SEQRES 18 B 381 LEU HIS PHE GLY GLU PRO LYS SER TRP TYR SER VAL PRO
SEQRES 19 B 381 PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU ALA LYS GLY
SEQRES 20 B 381 PHE PHE PRO GLY SER ALA GLN SER CYS GLU ALA PHE LEU
SEQRES 21 B 381 ARG HIS LYS MET THR LEU ILE SER PRO LEU MET LEU LYS
SEQRES 22 B 381 LYS TYR GLY ILE PRO PHE ASP LYS VAL THR GLN GLU ALA
SEQRES 23 B 381 GLY GLU PHE MET ILE THR PHE PRO TYR GLY TYR HIS ALA
SEQRES 24 B 381 GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU SER THR ASN
SEQRES 25 B 381 PHE ALA THR ARG ARG TRP ILE GLU TYR GLY LYS GLN ALA
SEQRES 26 B 381 VAL LEU CYS SER CYS ARG LYS ASP MET VAL LYS ILE SER
SEQRES 27 B 381 MET ASP VAL PHE VAL ARG LYS PHE GLN PRO GLU ARG TYR
SEQRES 28 B 381 LYS LEU TRP LYS ALA GLY LYS ASP ASN THR VAL ILE ASP
SEQRES 29 B 381 HIS THR LEU PRO THR PRO GLU ALA ALA GLU PHE LEU LYS
SEQRES 30 B 381 GLU SER GLU LEU
HET NI A 501 1
HET ZN A 502 1
HET CL A 503 1
HET DZA A 601 11
HET DZA A 605 11
HET NI B 501 1
HET ZN B 502 1
HET CL B 503 1
HET DZA B 603 11
HET GOL B 701 6
HETNAM NI NICKEL (II) ION
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM DZA DAMINOZIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NI 2(NI 2+)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 5 CL 2(CL 1-)
FORMUL 6 DZA 3(C6 H12 N2 O3)
FORMUL 12 GOL C3 H8 O3
FORMUL 13 HOH *568(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 ASP A 61 ASP A 64 5 4
HELIX 5 5 VAL A 94 SER A 103 1 10
HELIX 6 6 GLU A 113 LEU A 125 1 13
HELIX 7 7 THR A 155 LEU A 157 5 3
HELIX 8 8 ASP A 158 GLY A 165 1 8
HELIX 9 9 GLU A 190 LEU A 194 5 5
HELIX 10 10 PRO A 212 GLU A 214 5 3
HELIX 11 11 HIS A 215 PHE A 227 1 13
HELIX 12 12 PHE A 227 CYS A 234 1 8
HELIX 13 13 ALA A 236 LYS A 241 5 6
HELIX 14 14 SER A 246 TYR A 253 1 8
HELIX 15 15 ARG A 295 ALA A 303 1 9
HELIX 16 16 MET A 317 GLN A 325 1 9
HELIX 17 17 ARG A 328 ALA A 334 1 7
HELIX 18 18 THR A 347 LEU A 354 5 8
HELIX 19 19 THR B 20 ARG B 25 1 6
HELIX 20 20 ASN B 26 GLN B 37 1 12
HELIX 21 21 GLY B 38 ALA B 42 5 5
HELIX 22 22 ASP B 61 ASP B 64 5 4
HELIX 23 23 VAL B 94 SER B 103 1 10
HELIX 24 24 GLU B 113 LEU B 125 1 13
HELIX 25 25 THR B 155 LEU B 157 5 3
HELIX 26 26 ASP B 158 GLY B 165 1 8
HELIX 27 27 GLU B 190 LEU B 194 5 5
HELIX 28 28 PRO B 212 GLU B 214 5 3
HELIX 29 29 HIS B 215 PHE B 227 1 13
HELIX 30 30 PHE B 227 CYS B 234 1 8
HELIX 31 31 ALA B 236 LYS B 241 5 6
HELIX 32 32 SER B 246 TYR B 253 1 8
HELIX 33 33 ARG B 295 ALA B 303 1 9
HELIX 34 34 MET B 317 GLN B 325 1 9
HELIX 35 35 ARG B 328 ALA B 334 1 7
HELIX 36 36 THR B 347 LEU B 354 5 8
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 TYR A 275 ASN A 280 -1 O HIS A 276 N HIS A 188
SHEET 3 AC 4 LYS A 206 VAL A 211 -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 2.15
LINK OE2 GLU A 190 NI NI A 501 1555 1555 2.13
LINK SG CYS A 234 ZN ZN A 502 1555 1555 2.34
LINK NE2 HIS A 240 ZN ZN A 502 1555 1555 2.29
LINK NE2 HIS A 276 NI NI A 501 1555 1555 2.31
LINK SG CYS A 306 ZN ZN A 502 1555 1555 2.39
LINK SG CYS A 308 ZN ZN A 502 1555 1555 2.48
LINK NI NI A 501 O01 DZA A 605 1555 1555 2.27
LINK NI NI A 501 N04 DZA A 605 1555 1555 2.33
LINK NI NI A 501 O HOH A2159 1555 1555 2.63
LINK NE2 HIS B 188 NI NI B 501 1555 1555 2.26
LINK OE2 GLU B 190 NI NI B 501 1555 1555 2.15
LINK SG CYS B 234 ZN ZN B 502 1555 1555 2.39
LINK NE2 HIS B 240 ZN ZN B 502 1555 1555 2.18
LINK NE2 HIS B 276 NI NI B 501 1555 1555 2.10
LINK SG CYS B 306 ZN ZN B 502 1555 1555 2.31
LINK SG CYS B 308 ZN ZN B 502 1555 1555 2.54
LINK NI NI B 501 O01 DZA B 603 1555 1555 2.19
LINK NI NI B 501 N04 DZA B 603 1555 1555 2.20
LINK NI NI B 501 C06 DZA B 603 1555 1555 2.59
LINK NI NI B 501 O HOH B2182 1555 1555 2.52
SITE 1 AC1 5 HIS A 188 GLU A 190 HIS A 276 DZA A 605
SITE 2 AC1 5 HOH A2159
SITE 1 AC2 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC3 2 PHE A 227 GLY A 229
SITE 1 AC4 3 GLU A 23 TYR A 33 PHE A 353
SITE 1 AC5 11 TYR A 132 PHE A 185 HIS A 188 GLU A 190
SITE 2 AC5 11 SER A 196 LYS A 206 TRP A 208 THR A 270
SITE 3 AC5 11 HIS A 276 NI A 501 HOH A2265
SITE 1 AC6 5 HIS B 188 GLU B 190 HIS B 276 DZA B 603
SITE 2 AC6 5 HOH B2182
SITE 1 AC7 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC8 3 PHE B 227 GLY B 229 SER B 230
SITE 1 AC9 10 TYR B 132 PHE B 185 HIS B 188 GLU B 190
SITE 2 AC9 10 ASN B 198 LYS B 206 LYS B 241 HIS B 276
SITE 3 AC9 10 NI B 501 HOH B2182
SITE 1 BC1 4 ARG B 294 PHE B 324 GLN B 325 HOH B2240
CRYST1 100.476 149.752 57.533 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 0.009953 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006678 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017381 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
