HEADER TRANSFERASE 07-OCT-09 3K5K
TITLE DISCOVERY OF A 2,4-DIAMINO-7-AMINOALKOXY-QUINAZOLINE AS A POTENT
TITLE 2 INHIBITOR OF HISTONE LYSINE METHYLTRANSFERASE, G9A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC 3;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 913-1193, SET DOMAIN;
COMPND 5 SYNONYM: PROTEIN G9A, HISTONE H3-K9 METHYLTRANSFERASE 3, H3-K9-HMTASE
COMPND 6 3, EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 2, HLA-B-ASSOCIATED
COMPND 7 TRANSCRIPT 8, LYSINE N-METHYLTRANSFERASE 1C;
COMPND 8 EC: 2.1.1.43;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EHMT2, BAT8, C6ORF30, G9A, KMT1C, NG36;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC
KEYWDS HISTONE LYSINE METHYLTRANSFERASE, G9A, ANK REPEAT, CHROMATIN
KEYWDS 2 REGULATOR, METAL-BINDING, METHYLTRANSFERASE, NUCLEUS,
KEYWDS 3 PHOSPHOPROTEIN, S-ADENOSYL-L-METHIONINE, TRANSFERASE, STRUCTURAL
KEYWDS 4 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DONG,G.A.WASNEY,F.LIU,X.CHEN,A.ALLALI-HASSANI,G.SENISTERRA,I.CHAU,
AUTHOR 2 C.BOUNTRA,J.WEIGELT,A.M.EDWARDS,C.H.ARROWSMITH,S.V.FRYE,A.BOCHKAREV,
AUTHOR 3 P.J.BROWN,J.JIN,M.VEDADI,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 06-SEP-23 3K5K 1 REMARK SEQADV LINK
REVDAT 4 01-NOV-17 3K5K 1 REMARK
REVDAT 3 18-AUG-10 3K5K 1 JRNL
REVDAT 2 24-NOV-09 3K5K 1 AUTHOR
REVDAT 1 10-NOV-09 3K5K 0
JRNL AUTH F.LIU,X.CHEN,A.ALLALI-HASSANI,A.M.QUINN,G.A.WASNEY,A.DONG,
JRNL AUTH 2 D.BARSYTE,I.KOZIERADZKI,G.SENISTERRA,I.CHAU,A.SIARHEYEVA,
JRNL AUTH 3 D.B.KIREEV,A.JADHAV,J.M.HEROLD,S.V.FRYE,C.H.ARROWSMITH,
JRNL AUTH 4 P.J.BROWN,A.SIMEONOV,M.VEDADI,J.JIN
JRNL TITL DISCOVERY OF A 2,4-DIAMINO-7-AMINOALKOXYQUINAZOLINE AS A
JRNL TITL 2 POTENT AND SELECTIVE INHIBITOR OF HISTONE LYSINE
JRNL TITL 3 METHYLTRANSFERASE G9A.
JRNL REF J.MED.CHEM. V. 52 7950 2009
JRNL REFN ISSN 0022-2623
JRNL PMID 19891491
JRNL DOI 10.1021/JM901543M
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 66303
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1372
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3464
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.4270
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.4660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4190
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 136
REMARK 3 SOLVENT ATOMS : 459
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.52000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : 2.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.75000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.115
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.091
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4429 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6022 ; 1.309 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 541 ; 5.569 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 215 ;30.579 ;23.767
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 660 ;11.969 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;13.739 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 646 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3440 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2713 ; 0.755 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4345 ; 1.393 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1716 ; 1.841 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1677 ; 2.875 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3K5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VERIMAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67707
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.72700
REMARK 200 R SYM FOR SHELL (I) : 0.72700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.260
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 2O8J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM FLUORIDE, 0.1M BIS-TRIS
REMARK 280 PHOSPHATE PH 6.0, 18% POLYETHYLENE GLYCOL 3350 AND 10% ETHYLENE
REMARK 280 GLYCOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.03700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400
REMARK 400 COMPOUND
REMARK 400 LIGAND DXQ IS REFERRED AS 2,4-DIAMINO-7-AMINOALKOXY-QUINAZOLINE IN
REMARK 400 TITLE
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 GLY A 911
REMARK 465 SER A 912
REMARK 465 ASN A 913
REMARK 465 ARG A 914
REMARK 465 ALA A 915
REMARK 465 ILE A 916
REMARK 465 ASP A 1093
REMARK 465 GLY A 1094
REMARK 465 ARG A 1191
REMARK 465 LEU A 1192
REMARK 465 ASP A 1193
REMARK 465 GLY B 911
REMARK 465 SER B 912
REMARK 465 ASN B 913
REMARK 465 ARG B 914
REMARK 465 ALA B 915
REMARK 465 ILE B 916
REMARK 465 ARG B 917
REMARK 465 THR B 918
REMARK 465 LYS B 1092
REMARK 465 ASP B 1093
REMARK 465 GLY B 1094
REMARK 465 ARG B 1191
REMARK 465 LEU B 1192
REMARK 465 ASP B 1193
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 LYS A 920 CG CD CE NZ
REMARK 470 ARG A 924 CZ NH1 NH2
REMARK 470 VAL A 977 CG1 CG2
REMARK 470 SER A 983 OG
REMARK 470 ASN A 984 CG OD1 ND2
REMARK 470 LEU A 986 CD1
REMARK 470 ILE A 992 CG1 CG2 CD1
REMARK 470 LYS A 998 CG CD CE NZ
REMARK 470 GLN A1004 CG CD OE1 NE2
REMARK 470 LYS A1008 CE NZ
REMARK 470 GLU A1010 CG CD OE1 OE2
REMARK 470 LYS A1028 CE NZ
REMARK 470 LYS A1047 CE NZ
REMARK 470 GLU A1081 CG CD OE1 OE2
REMARK 470 ASP A1090 CG OD1 OD2
REMARK 470 LYS A1092 CG CD CE NZ
REMARK 470 GLU A1095 CG CD OE1 OE2
REMARK 470 ARG A1145 CZ NH1 NH2
REMARK 470 ARG A1157 NE CZ NH1 NH2
REMARK 470 LYS A1164 CG CD CE NZ
REMARK 470 GLU A1173 CG CD OE1 OE2
REMARK 470 LYS A1174 CG CD CE NZ
REMARK 470 LYS A1176 CG CD CE NZ
REMARK 470 GLU A1180 CG CD OE1 OE2
REMARK 470 GLU A1185 CG CD OE1 OE2
REMARK 470 GLN A1186 CG CD OE1 NE2
REMARK 470 ARG A1188 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1189 CG CD1 CD2
REMARK 470 LYS B 920 CG CD CE NZ
REMARK 470 ILE B 921 CG1 CG2 CD1
REMARK 470 ILE B 922 CD1
REMARK 470 ILE B 992 CG1 CG2 CD1
REMARK 470 LYS B 998 CG CD CE NZ
REMARK 470 GLN B1004 CG CD OE1 NE2
REMARK 470 LYS B1008 CG CD CE NZ
REMARK 470 ILE B1009 CG1 CG2 CD1
REMARK 470 LYS B1047 CE NZ
REMARK 470 GLU B1081 CG CD OE1 OE2
REMARK 470 GLU B1095 CG CD OE1 OE2
REMARK 470 ARG B1145 NE CZ NH1 NH2
REMARK 470 ARG B1157 CD NE CZ NH1 NH2
REMARK 470 LYS B1164 CG CD CE NZ
REMARK 470 GLU B1173 CG CD OE1 OE2
REMARK 470 LYS B1174 CG CD CE NZ
REMARK 470 LYS B1176 CG CD CE NZ
REMARK 470 GLU B1180 CG CD OE1 OE2
REMARK 470 GLN B1186 CG CD OE1 NE2
REMARK 470 SER B1187 OG
REMARK 470 ARG B1188 CG CD NE CZ NH1 NH2
REMARK 470 LEU B1189 CG CD1 CD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 1142 N CA C O CB CG CD
REMARK 480 ARG A 1142 NE CZ NH1 NH2
REMARK 480 SER B 1108 N CA C O CB OG
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 ASP A 925 104.80 -162.80
REMARK 500 ASP A 949 45.82 -94.08
REMARK 500 ASP A 978 -148.66 -130.04
REMARK 500 ILE A 992 -55.62 65.60
REMARK 500 ARG A1030 32.00 -140.14
REMARK 500 ILE A1064 -65.75 -105.08
REMARK 500 ASN A1106 -160.53 -107.71
REMARK 500 MET A1126 -92.28 -132.63
REMARK 500 GLU B 948 20.45 -140.32
REMARK 500 ASP B 949 48.96 -91.62
REMARK 500 ASP B 978 -153.11 -96.43
REMARK 500 ILE B 992 -58.63 78.96
REMARK 500 ASN B1029 49.79 -109.18
REMARK 500 ARG B1030 32.85 -144.04
REMARK 500 ILE B1064 -64.79 -106.56
REMARK 500 ASN B1106 -162.25 -113.05
REMARK 500 MET B1126 -94.41 -131.49
REMARK 500 LEU B1189 47.79 -87.93
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 A1194 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 974 SG
REMARK 620 2 CYS A 987 SG 114.1
REMARK 620 3 CYS A1017 SG 108.3 112.5
REMARK 620 4 CYS A1021 SG 104.4 101.9 115.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1196 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 974 SG
REMARK 620 2 CYS A 976 SG 104.8
REMARK 620 3 CYS A 980 SG 108.4 104.5
REMARK 620 4 CYS A 985 SG 114.0 105.8 118.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1195 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 980 SG
REMARK 620 2 CYS A1017 SG 104.9
REMARK 620 3 CYS A1023 SG 104.7 106.2
REMARK 620 4 CYS A1027 SG 119.4 109.2 111.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1197 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1115 SG
REMARK 620 2 CYS A1168 SG 116.9
REMARK 620 3 CYS A1170 SG 108.6 107.0
REMARK 620 4 CYS A1175 SG 103.7 112.5 107.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1194 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 974 SG
REMARK 620 2 CYS B 987 SG 110.8
REMARK 620 3 CYS B1017 SG 108.7 112.3
REMARK 620 4 CYS B1021 SG 107.0 101.8 116.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1196 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 974 SG
REMARK 620 2 CYS B 976 SG 106.3
REMARK 620 3 CYS B 980 SG 109.8 105.8
REMARK 620 4 CYS B 985 SG 109.9 106.6 117.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1195 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 980 SG
REMARK 620 2 CYS B1017 SG 111.6
REMARK 620 3 CYS B1023 SG 106.5 108.6
REMARK 620 4 CYS B1027 SG 114.0 105.7 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1197 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1115 SG
REMARK 620 2 CYS B1168 SG 113.2
REMARK 620 3 CYS B1170 SG 110.2 109.3
REMARK 620 4 CYS B1175 SG 103.1 109.8 111.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXQ A 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1194
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1195
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1196
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1197
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 1198
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXQ B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 3005
DBREF 3K5K A 913 1193 UNP Q96KQ7 EHMT2_HUMAN 913 1193
DBREF 3K5K B 913 1193 UNP Q96KQ7 EHMT2_HUMAN 913 1193
SEQADV 3K5K GLY A 911 UNP Q96KQ7 EXPRESSION TAG
SEQADV 3K5K SER A 912 UNP Q96KQ7 EXPRESSION TAG
SEQADV 3K5K GLY B 911 UNP Q96KQ7 EXPRESSION TAG
SEQADV 3K5K SER B 912 UNP Q96KQ7 EXPRESSION TAG
SEQRES 1 A 283 GLY SER ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS
SEQRES 2 A 283 ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO
SEQRES 3 A 283 CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP
SEQRES 4 A 283 TYR LYS TYR ILE SER GLU ASN CYS GLU THR SER THR MET
SEQRES 5 A 283 ASN ILE ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR
SEQRES 6 A 283 CYS VAL ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY
SEQRES 7 A 283 GLN LEU SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG
SEQRES 8 A 283 LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE
SEQRES 9 A 283 PHE GLU CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS
SEQRES 10 A 283 LYS ASN ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU
SEQRES 11 A 283 GLN LEU TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG
SEQRES 12 A 283 ALA LEU GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU
SEQRES 13 A 283 TYR VAL GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL
SEQRES 14 A 283 ARG GLU ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS
SEQRES 15 A 283 ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY
SEQRES 16 A 283 ASN ILE SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN
SEQRES 17 A 283 ILE ILE PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU
SEQRES 18 A 283 ARG PHE PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE
SEQRES 19 A 283 ARG THR GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG
SEQRES 20 A 283 PHE TRP ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS
SEQRES 21 A 283 GLY SER GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA
SEQRES 22 A 283 LEU GLU GLN SER ARG LEU ALA ARG LEU ASP
SEQRES 1 B 283 GLY SER ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS
SEQRES 2 B 283 ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO
SEQRES 3 B 283 CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP
SEQRES 4 B 283 TYR LYS TYR ILE SER GLU ASN CYS GLU THR SER THR MET
SEQRES 5 B 283 ASN ILE ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR
SEQRES 6 B 283 CYS VAL ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY
SEQRES 7 B 283 GLN LEU SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG
SEQRES 8 B 283 LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE
SEQRES 9 B 283 PHE GLU CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS
SEQRES 10 B 283 LYS ASN ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU
SEQRES 11 B 283 GLN LEU TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG
SEQRES 12 B 283 ALA LEU GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU
SEQRES 13 B 283 TYR VAL GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL
SEQRES 14 B 283 ARG GLU ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS
SEQRES 15 B 283 ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY
SEQRES 16 B 283 ASN ILE SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN
SEQRES 17 B 283 ILE ILE PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU
SEQRES 18 B 283 ARG PHE PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE
SEQRES 19 B 283 ARG THR GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG
SEQRES 20 B 283 PHE TRP ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS
SEQRES 21 B 283 GLY SER GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA
SEQRES 22 B 283 LEU GLU GLN SER ARG LEU ALA ARG LEU ASP
HET ZN A1194 1
HET ZN A1195 1
HET ZN A1196 1
HET ZN A1197 1
HET SAH A1198 26
HET DXQ A2000 35
HET CL A3001 1
HET CL A3004 1
HET UNX A1199 1
HET ZN B1194 1
HET ZN B1195 1
HET ZN B1196 1
HET ZN B1197 1
HET SAH B1198 26
HET DXQ B2001 35
HET CL B3003 1
HET CL B3005 1
HET UNX B1199 1
HETNAM ZN ZINC ION
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM DXQ 7-[3-(DIMETHYLAMINO)PROPOXY]-6-METHOXY-2-(4-METHYL-1,4-
HETNAM 2 DXQ DIAZEPAN-1-YL)-N-(1-METHYLPIPERIDIN-4-YL)QUINAZOLIN-4-
HETNAM 3 DXQ AMINE
HETNAM CL CHLORIDE ION
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 3 ZN 8(ZN 2+)
FORMUL 7 SAH 2(C14 H20 N6 O5 S)
FORMUL 8 DXQ 2(C26 H43 N7 O2)
FORMUL 9 CL 4(CL 1-)
FORMUL 11 UNX 2(X)
FORMUL 21 HOH *459(H2 O)
HELIX 1 1 ASN A 967 LEU A 971 5 5
HELIX 2 2 CYS A 985 SER A 991 1 7
HELIX 3 3 VAL A 1031 GLY A 1035 5 5
HELIX 4 4 ASP A 1074 ASP A 1078 1 5
HELIX 5 5 ILE A 1107 ILE A 1111 5 5
HELIX 6 6 GLY A 1155 SER A 1163 1 9
HELIX 7 7 SER A 1178 LEU A 1189 1 12
HELIX 8 8 ASN B 967 LEU B 971 5 5
HELIX 9 9 CYS B 985 SER B 991 1 7
HELIX 10 10 VAL B 1031 GLY B 1035 5 5
HELIX 11 11 ASP B 1074 ASP B 1078 1 5
HELIX 12 12 ILE B 1107 ILE B 1111 5 5
HELIX 13 13 GLY B 1155 SER B 1163 1 9
HELIX 14 14 SER B 1178 LEU B 1189 1 12
SHEET 1 A 4 LYS A 920 CYS A 923 0
SHEET 2 A 4 CYS A 937 ASN A 939 -1 O CYS A 937 N CYS A 923
SHEET 3 A 4 LEU A1040 ARG A1044 1 O LEU A1042 N VAL A 938
SHEET 4 A 4 TRP A1050 ALA A1054 -1 O GLY A1051 N TYR A1043
SHEET 1 B 4 LYS A 951 TYR A 952 0
SHEET 2 B 4 TYR A1097 GLY A1105 1 O TYR A1103 N LYS A 951
SHEET 3 B 4 GLY A1069 SER A1073 -1 N GLU A1070 O ASP A1100
SHEET 4 B 4 CYS A 957 GLU A 958 1 N CYS A 957 O LEU A1071
SHEET 1 C 3 LYS A 951 TYR A 952 0
SHEET 2 C 3 TYR A1097 GLY A1105 1 O TYR A1103 N LYS A 951
SHEET 3 C 3 LEU A1086 LEU A1089 -1 N PHE A1087 O ILE A1099
SHEET 1 D 4 ILE A1014 PHE A1015 0
SHEET 2 D 4 ILE A1119 PHE A1125 1 O ARG A1123 N ILE A1014
SHEET 3 D 4 ARG A1135 SER A1140 -1 O ALA A1137 N VAL A1122
SHEET 4 D 4 PHE A1063 TYR A1067 -1 N ILE A1064 O PHE A1138
SHEET 1 E 2 ASN A1112 HIS A1113 0
SHEET 2 E 2 GLY A1151 PHE A1152 1 O PHE A1152 N ASN A1112
SHEET 1 F 3 CYS B 937 VAL B 938 0
SHEET 2 F 3 LEU B1040 ARG B1044 1 O LEU B1042 N VAL B 938
SHEET 3 F 3 TRP B1050 ALA B1054 -1 O ARG B1053 N GLN B1041
SHEET 1 G 4 LYS B 951 TYR B 952 0
SHEET 2 G 4 TYR B1097 GLY B1105 1 O TYR B1103 N LYS B 951
SHEET 3 G 4 GLY B1069 SER B1073 -1 N GLU B1070 O ASP B1100
SHEET 4 G 4 CYS B 957 GLU B 958 1 N CYS B 957 O LEU B1071
SHEET 1 H 3 LYS B 951 TYR B 952 0
SHEET 2 H 3 TYR B1097 GLY B1105 1 O TYR B1103 N LYS B 951
SHEET 3 H 3 LEU B1086 LEU B1089 -1 N LEU B1089 O TYR B1097
SHEET 1 I 4 ILE B1014 PHE B1015 0
SHEET 2 I 4 ILE B1119 PHE B1125 1 O PHE B1125 N ILE B1014
SHEET 3 I 4 ARG B1135 SER B1140 -1 O ALA B1137 N VAL B1122
SHEET 4 I 4 PHE B1063 TYR B1067 -1 N ILE B1064 O PHE B1138
SHEET 1 J 2 ASN B1112 HIS B1113 0
SHEET 2 J 2 GLY B1151 PHE B1152 1 O PHE B1152 N ASN B1112
SSBOND 1 CYS B 937 CYS B 946 1555 1555 2.07
LINK SG CYS A 974 ZN ZN A1194 1555 1555 2.43
LINK SG CYS A 974 ZN ZN A1196 1555 1555 2.38
LINK SG CYS A 976 ZN ZN A1196 1555 1555 2.38
LINK SG CYS A 980 ZN ZN A1195 1555 1555 2.59
LINK SG CYS A 980 ZN ZN A1196 1555 1555 2.00
LINK SG CYS A 985 ZN ZN A1196 1555 1555 2.30
LINK SG CYS A 987 ZN ZN A1194 1555 1555 2.28
LINK SG CYS A1017 ZN ZN A1194 1555 1555 2.38
LINK SG CYS A1017 ZN ZN A1195 1555 1555 2.36
LINK SG CYS A1021 ZN ZN A1194 1555 1555 2.29
LINK SG CYS A1023 ZN ZN A1195 1555 1555 2.21
LINK SG CYS A1027 ZN ZN A1195 1555 1555 2.08
LINK SG CYS A1115 ZN ZN A1197 1555 1555 2.17
LINK SG CYS A1168 ZN ZN A1197 1555 1555 2.28
LINK SG CYS A1170 ZN ZN A1197 1555 1555 2.30
LINK SG CYS A1175 ZN ZN A1197 1555 1555 2.38
LINK SG CYS B 974 ZN ZN B1194 1555 1555 2.41
LINK SG CYS B 974 ZN ZN B1196 1555 1555 2.38
LINK SG CYS B 976 ZN ZN B1196 1555 1555 2.43
LINK SG CYS B 980 ZN ZN B1195 1555 1555 2.41
LINK SG CYS B 980 ZN ZN B1196 1555 1555 2.25
LINK SG CYS B 985 ZN ZN B1196 1555 1555 2.29
LINK SG CYS B 987 ZN ZN B1194 1555 1555 2.28
LINK SG CYS B1017 ZN ZN B1194 1555 1555 2.42
LINK SG CYS B1017 ZN ZN B1195 1555 1555 2.30
LINK SG CYS B1021 ZN ZN B1194 1555 1555 2.30
LINK SG CYS B1023 ZN ZN B1195 1555 1555 2.24
LINK SG CYS B1027 ZN ZN B1195 1555 1555 2.39
LINK SG CYS B1115 ZN ZN B1197 1555 1555 2.46
LINK SG CYS B1168 ZN ZN B1197 1555 1555 2.30
LINK SG CYS B1170 ZN ZN B1197 1555 1555 2.13
LINK SG CYS B1175 ZN ZN B1197 1555 1555 2.38
SITE 1 AC1 4 CYS A 974 CYS A 987 CYS A1017 CYS A1021
SITE 1 AC2 4 CYS A 980 CYS A1017 CYS A1023 CYS A1027
SITE 1 AC3 4 CYS A 974 CYS A 976 CYS A 980 CYS A 985
SITE 1 AC4 4 CYS A1115 CYS A1168 CYS A1170 CYS A1175
SITE 1 AC5 17 HOH A 27 HOH A 91 HOH A 192 HOH A 312
SITE 2 AC5 17 MET A1048 TRP A1050 SER A1084 TYR A1085
SITE 3 AC5 17 ARG A1109 ASN A1112 HIS A1113 TYR A1154
SITE 4 AC5 17 PHE A1158 PHE A1166 THR A1167 CYS A1168
SITE 5 AC5 17 GLN A1169
SITE 1 AC6 14 HOH A 453 ASP A1074 ALA A1077 ASP A1078
SITE 2 AC6 14 ARG A1080 ASP A1083 SER A1084 LEU A1086
SITE 3 AC6 14 ASP A1088 CYS A1098 PHE A1152 TYR A1154
SITE 4 AC6 14 ARG A1157 PHE A1158
SITE 1 AC7 2 ASN A 963 ARG A1132
SITE 1 AC8 2 CYS A 923 ARG A 924
SITE 1 AC9 4 CYS B 974 CYS B 987 CYS B1017 CYS B1021
SITE 1 BC1 4 CYS B 980 CYS B1017 CYS B1023 CYS B1027
SITE 1 BC2 4 CYS B 974 CYS B 976 CYS B 980 CYS B 985
SITE 1 BC3 4 CYS B1115 CYS B1168 CYS B1170 CYS B1175
SITE 1 BC4 18 HOH B 128 HOH B 225 HOH B 232 HOH B 336
SITE 2 BC4 18 MET B1048 TRP B1050 SER B1084 TYR B1085
SITE 3 BC4 18 ARG B1109 PHE B1110 ASN B1112 HIS B1113
SITE 4 BC4 18 TYR B1154 PHE B1158 PHE B1166 THR B1167
SITE 5 BC4 18 CYS B1168 GLN B1169
SITE 1 BC5 14 HOH B 324 HOH B 344 ASP B1074 ALA B1077
SITE 2 BC5 14 ASP B1078 ARG B1080 ASP B1083 SER B1084
SITE 3 BC5 14 LEU B1086 ASP B1088 CYS B1098 PHE B1152
SITE 4 BC5 14 TYR B1154 PHE B1158
SITE 1 BC6 3 THR A 961 ASN A 963 ASN B 963
SITE 1 BC7 1 ARG B 924
CRYST1 56.674 78.074 72.507 90.00 91.81 90.00 P 1 21 1 4
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 0.017645 0.000000 0.000558 0.00000
SCALE2 0.000000 0.012808 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013799 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
