HEADER TRANSFERASE 22-APR-10 3MO5
TITLE HUMAN G9A-LIKE (GLP, ALSO KNOWN AS EHMT1) IN COMPLEX WITH INHIBITOR
TITLE 2 E72
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC 5;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: C-TERMINAL SET DOMAIN;
COMPND 5 SYNONYM: HISTONE H3-K9 METHYLTRANSFERASE 5, H3-K9-HMTASE 5,
COMPND 6 EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1, EU-HMTASE1, G9A-
COMPND 7 LIKE PROTEIN 1, GLP1, LYSINE N-METHYLTRANSFERASE 1D;
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: EHMT1, EUHMTASE1, KIAA1876, KMT1D;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EPIGENETICS, HISTONE LYSINE METHYLATION, ENZYMATIC INHIBITION, LYSINE
KEYWDS 2 MIMICS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.CHANG,J.R.HORTON,X.CHENG
REVDAT 2 06-SEP-23 3MO5 1 REMARK LINK
REVDAT 1 30-JUN-10 3MO5 0
JRNL AUTH Y.CHANG,T.GANESH,J.R.HORTON,A.SPANNHOFF,J.LIU,A.SUN,X.ZHANG,
JRNL AUTH 2 M.T.BEDFORD,Y.SHINKAI,J.P.SNYDER,X.CHENG
JRNL TITL ADDING A LYSINE MIMIC IN THE DESIGN OF POTENT INHIBITORS OF
JRNL TITL 2 HISTONE LYSINE METHYLTRANSFERASES.
JRNL REF J.MOL.BIOL. V. 400 1 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20434463
JRNL DOI 10.1016/J.JMB.2010.04.048
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 317304.280
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 67126
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) : 0.196
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3430
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.22
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5729
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 277
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8144
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 224
REMARK 3 SOLVENT ATOMS : 699
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.14000
REMARK 3 B22 (A**2) : -2.03000
REMARK 3 B33 (A**2) : 7.17000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 8.65000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 35.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
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) : 1.350 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.990 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.900 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 71.57
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : E72_2.PAR
REMARK 3 PARAMETER FILE 5 : SAH_XPLOR.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 : E67_MOD.TOP
REMARK 3 TOPOLOGY FILE 5 : SAH_XPLOR.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3MO5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058789.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72239
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 34.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.55500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3FPD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 14% POLYETHYLENE
REMARK 280 GLYCOL 4000, 9% ISOPROPANOL, AND 12% DIMETHYL SULFOXIDE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
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 81.45000
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, 4, 5, 6
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 300 REMARK: 4 COMPLEXES PER ASYMMETRIC UNIT
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 ASN A 951
REMARK 465 SER A 952
REMARK 465 GLN A 953
REMARK 465 VAL A 954
REMARK 465 TRP A 955
REMARK 465 SER A 956
REMARK 465 ALA A 957
REMARK 465 LEU A 958
REMARK 465 GLN A 959
REMARK 465 MET A 960
REMARK 465 SER A 961
REMARK 465 LYS A 962
REMARK 465 ALA A 963
REMARK 465 LEU A 964
REMARK 465 GLN A 965
REMARK 465 ASP A 966
REMARK 465 SER A 967
REMARK 465 ALA A 968
REMARK 465 PRO A 969
REMARK 465 ASP A 970
REMARK 465 ARG A 971
REMARK 465 PRO A 972
REMARK 465 SER A 973
REMARK 465 PRO A 974
REMARK 465 VAL A 975
REMARK 465 GLU A 976
REMARK 465 ARG A 977
REMARK 465 ASN A 1148
REMARK 465 LYS A 1149
REMARK 465 ASP A 1150
REMARK 465 ASN B 951
REMARK 465 SER B 952
REMARK 465 GLN B 953
REMARK 465 VAL B 954
REMARK 465 TRP B 955
REMARK 465 SER B 956
REMARK 465 ALA B 957
REMARK 465 LEU B 958
REMARK 465 GLN B 959
REMARK 465 MET B 960
REMARK 465 SER B 961
REMARK 465 LYS B 962
REMARK 465 ALA B 963
REMARK 465 LEU B 964
REMARK 465 GLN B 965
REMARK 465 ASP B 966
REMARK 465 SER B 967
REMARK 465 ALA B 968
REMARK 465 PRO B 969
REMARK 465 ASP B 970
REMARK 465 ARG B 971
REMARK 465 PRO B 972
REMARK 465 SER B 973
REMARK 465 PRO B 974
REMARK 465 VAL B 975
REMARK 465 ASP B 1150
REMARK 465 GLY B 1151
REMARK 465 ASN C 951
REMARK 465 SER C 952
REMARK 465 GLN C 953
REMARK 465 VAL C 954
REMARK 465 TRP C 955
REMARK 465 SER C 956
REMARK 465 ALA C 957
REMARK 465 LEU C 958
REMARK 465 GLN C 959
REMARK 465 MET C 960
REMARK 465 SER C 961
REMARK 465 LYS C 962
REMARK 465 ALA C 963
REMARK 465 LEU C 964
REMARK 465 GLN C 965
REMARK 465 ASP C 966
REMARK 465 SER C 967
REMARK 465 ALA C 968
REMARK 465 PRO C 969
REMARK 465 ASP C 970
REMARK 465 ARG C 971
REMARK 465 PRO C 972
REMARK 465 SER C 973
REMARK 465 PRO C 974
REMARK 465 ASN C 1148
REMARK 465 LYS C 1149
REMARK 465 ASP C 1150
REMARK 465 ASN D 951
REMARK 465 SER D 952
REMARK 465 GLN D 953
REMARK 465 VAL D 954
REMARK 465 TRP D 955
REMARK 465 SER D 956
REMARK 465 ALA D 957
REMARK 465 LEU D 958
REMARK 465 GLN D 959
REMARK 465 MET D 960
REMARK 465 SER D 961
REMARK 465 LYS D 962
REMARK 465 ALA D 963
REMARK 465 LEU D 964
REMARK 465 GLN D 965
REMARK 465 ASP D 966
REMARK 465 SER D 967
REMARK 465 ALA D 968
REMARK 465 PRO D 969
REMARK 465 ASP D 970
REMARK 465 ARG D 971
REMARK 465 PRO D 972
REMARK 465 SER D 973
REMARK 465 PRO D 974
REMARK 465 VAL D 975
REMARK 465 ASN D 1148
REMARK 465 LYS D 1149
REMARK 465 ASP D 1150
REMARK 465 GLY D 1151
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 ILE A 978 CG1 CG2 CD1
REMARK 470 LYS A1055 CG CD CE NZ
REMARK 470 ARG A1103 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1104 CG OD1 OD2
REMARK 470 MET A1105 CG SD CE
REMARK 470 GLU A1138 CG CD OE1 OE2
REMARK 470 GLU A1173 CG CD OE1 OE2
REMARK 470 LEU A1222 CG CD1 CD2
REMARK 470 ARG A1226 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 977 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 981 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1067 CG CD OE1 OE2
REMARK 470 ARG B1103 CG CD NE CZ NH1 NH2
REMARK 470 GLN B1113 CG CD OE1 NE2
REMARK 470 GLU B1138 CG CD OE1 OE2
REMARK 470 ASN B1148 CG OD1 ND2
REMARK 470 LYS B1149 CG CD CE NZ
REMARK 470 GLU B1213 CG CD OE1 OE2
REMARK 470 VAL C 975 CG1 CG2
REMARK 470 ARG C 981 CG CD NE CZ NH1 NH2
REMARK 470 ARG C1103 CG CD NE CZ NH1 NH2
REMARK 470 ASP C1104 CG OD1 OD2
REMARK 470 GLU C1138 CG CD OE1 OE2
REMARK 470 ASP C1147 CG OD1 OD2
REMARK 470 LYS C1221 CG CD CE NZ
REMARK 470 LYS C1231 CG CD CE NZ
REMARK 470 GLU D 976 CG CD OE1 OE2
REMARK 470 ARG D 977 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1055 CG CD CE NZ
REMARK 470 ARG D1094 CG CD NE CZ NH1 NH2
REMARK 470 ARG D1103 CG CD NE CZ NH1 NH2
REMARK 470 ASP D1104 CG OD1 OD2
REMARK 470 GLU D1139 CG CD OE1 OE2
REMARK 470 GLU D1173 CG CD OE1 OE2
REMARK 470 GLU D1213 CG CD OE1 OE2
REMARK 470 LYS D1221 CG CD CE NZ
REMARK 470 ARG D1226 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1231 CG CD CE NZ
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 982 110.51 -170.27
REMARK 500 VAL A 998 -60.44 -96.98
REMARK 500 ASP A 999 -151.20 -130.74
REMARK 500 SER A1005 11.35 -143.57
REMARK 500 ASN A1006 43.20 -91.88
REMARK 500 SER A1017 -174.18 -174.45
REMARK 500 ASP A1035 -149.88 -112.99
REMARK 500 ASP A1036 31.81 -99.22
REMARK 500 MET A1049 -46.85 92.06
REMARK 500 ASN A1086 43.45 -86.00
REMARK 500 VAL A1088 -60.79 -135.70
REMARK 500 ASP A1104 20.14 -66.82
REMARK 500 VAL A1121 -60.78 -99.34
REMARK 500 LEU A1146 55.85 -112.85
REMARK 500 GLU A1152 106.65 61.37
REMARK 500 ASN A1163 -162.60 -113.59
REMARK 500 MET A1183 -91.81 -124.28
REMARK 500 ARG A1199 -178.64 -171.57
REMARK 500 SER B 980 134.76 -175.16
REMARK 500 ASP B 982 105.97 -173.44
REMARK 500 ASP B 999 -152.53 -151.37
REMARK 500 SER B1005 20.17 -147.56
REMARK 500 ASN B1006 33.99 -98.09
REMARK 500 SER B1017 -179.45 -175.28
REMARK 500 ASN B1020 49.94 -75.54
REMARK 500 ASP B1035 -148.15 -96.48
REMARK 500 MET B1049 -46.57 88.68
REMARK 500 ASN B1086 48.51 -87.61
REMARK 500 VAL B1088 -65.44 -131.06
REMARK 500 ASP B1104 9.62 -68.30
REMARK 500 ASN B1163 -163.61 -112.37
REMARK 500 MET B1183 -92.83 -133.23
REMARK 500 ARG B1199 -173.91 -177.88
REMARK 500 SER C 980 135.52 -176.05
REMARK 500 ASP C 982 101.33 -170.05
REMARK 500 ASP C 999 -155.72 -133.85
REMARK 500 SER C1005 18.67 -143.31
REMARK 500 ASN C1006 35.38 -91.77
REMARK 500 ASP C1035 -144.26 -99.27
REMARK 500 MET C1049 -47.19 94.22
REMARK 500 ASN C1086 49.45 -92.39
REMARK 500 VAL C1088 -65.15 -132.82
REMARK 500 ASP C1104 23.44 -148.89
REMARK 500 ASN C1163 -161.79 -116.81
REMARK 500 MET C1183 -90.80 -130.01
REMARK 500 ASP D 982 103.71 -177.44
REMARK 500 VAL D 998 -92.52 -86.33
REMARK 500 SER D1005 17.56 -150.21
REMARK 500 ASN D1006 36.96 -96.43
REMARK 500 SER D1017 -177.00 -179.75
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
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 A 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1031 SG
REMARK 620 2 CYS A1044 SG 113.3
REMARK 620 3 CYS A1074 SG 108.3 109.1
REMARK 620 4 CYS A1078 SG 107.5 98.3 120.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1037 SG
REMARK 620 2 CYS A1074 SG 113.6
REMARK 620 3 CYS A1080 SG 104.4 109.0
REMARK 620 4 CYS A1084 SG 112.0 105.6 112.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 3 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1031 SG
REMARK 620 2 CYS A1033 SG 103.5
REMARK 620 3 CYS A1037 SG 108.9 106.2
REMARK 620 4 CYS A1042 SG 110.7 104.3 121.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 4 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1172 SG
REMARK 620 2 CYS A1225 SG 124.2
REMARK 620 3 CYS A1227 SG 109.9 101.2
REMARK 620 4 CYS A1232 SG 105.5 102.5 113.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 5 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1031 SG
REMARK 620 2 CYS B1044 SG 120.6
REMARK 620 3 CYS B1074 SG 112.6 104.2
REMARK 620 4 CYS B1078 SG 103.5 98.3 117.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 6 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1037 SG
REMARK 620 2 CYS B1074 SG 115.7
REMARK 620 3 CYS B1080 SG 105.2 113.3
REMARK 620 4 CYS B1084 SG 108.2 103.7 110.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 7 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1031 SG
REMARK 620 2 CYS B1033 SG 105.9
REMARK 620 3 CYS B1037 SG 107.6 102.2
REMARK 620 4 CYS B1042 SG 115.9 107.6 116.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 8 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1172 SG
REMARK 620 2 CYS B1225 SG 120.1
REMARK 620 3 CYS B1227 SG 112.7 104.6
REMARK 620 4 CYS B1232 SG 102.8 98.2 118.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1031 SG
REMARK 620 2 CYS C1044 SG 117.0
REMARK 620 3 CYS C1074 SG 111.0 105.7
REMARK 620 4 CYS C1078 SG 106.2 92.7 123.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1037 SG
REMARK 620 2 CYS C1074 SG 111.5
REMARK 620 3 CYS C1080 SG 108.8 110.2
REMARK 620 4 CYS C1084 SG 110.8 102.2 113.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 3 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1031 SG
REMARK 620 2 CYS C1033 SG 105.6
REMARK 620 3 CYS C1037 SG 105.6 108.0
REMARK 620 4 CYS C1042 SG 111.8 106.1 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 4 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1172 SG
REMARK 620 2 CYS C1225 SG 112.4
REMARK 620 3 CYS C1227 SG 112.2 102.2
REMARK 620 4 CYS C1232 SG 100.6 108.6 121.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 5 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 548 O
REMARK 620 2 CYS D1031 SG 65.3
REMARK 620 3 CYS D1044 SG 178.6 113.4
REMARK 620 4 CYS D1074 SG 68.3 110.9 112.8
REMARK 620 5 CYS D1078 SG 82.0 101.8 98.0 119.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 6 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 548 O
REMARK 620 2 CYS D1037 SG 94.9
REMARK 620 3 CYS D1074 SG 66.3 108.8
REMARK 620 4 CYS D1080 SG 59.1 101.7 118.7
REMARK 620 5 CYS D1084 SG 152.2 112.4 107.7 107.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 7 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1031 SG
REMARK 620 2 CYS D1033 SG 102.7
REMARK 620 3 CYS D1037 SG 113.2 102.6
REMARK 620 4 CYS D1042 SG 113.7 102.4 119.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 8 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1172 SG
REMARK 620 2 CYS D1225 SG 113.2
REMARK 620 3 CYS D1227 SG 116.9 100.0
REMARK 620 4 CYS D1232 SG 102.5 105.8 118.3
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E72 A 1236
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E72 B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH C 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E72 C 1236
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH D 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E72 D 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FPD RELATED DB: PDB
REMARK 900 BIX-01294
REMARK 900 RELATED ID: 3MO2 RELATED DB: PDB
REMARK 900 E67 (BIX ANALOG)
REMARK 900 RELATED ID: 3MO0 RELATED DB: PDB
REMARK 900 E11 (BIX ANALOG)
DBREF 3MO5 A 951 1235 UNP Q9H9B1 EHMT1_HUMAN 951 1235
DBREF 3MO5 B 951 1235 UNP Q9H9B1 EHMT1_HUMAN 951 1235
DBREF 3MO5 C 951 1235 UNP Q9H9B1 EHMT1_HUMAN 951 1235
DBREF 3MO5 D 951 1235 UNP Q9H9B1 EHMT1_HUMAN 951 1235
SEQRES 1 A 285 ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA
SEQRES 2 A 285 LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU
SEQRES 3 A 285 ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG
SEQRES 4 A 285 ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO
SEQRES 5 A 285 CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL
SEQRES 6 A 285 THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU
SEQRES 7 A 285 GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN
SEQRES 8 A 285 CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP
SEQRES 9 A 285 LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU
SEQRES 10 A 285 PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS
SEQRES 11 A 285 TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU
SEQRES 12 A 285 ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY
SEQRES 13 A 285 TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR
SEQRES 14 A 285 PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER
SEQRES 15 A 285 GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP
SEQRES 16 A 285 LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA
SEQRES 17 A 285 ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS
SEQRES 18 A 285 CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA
SEQRES 19 A 285 HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER
SEQRES 20 A 285 THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP
SEQRES 21 A 285 TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE
SEQRES 22 A 285 SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER
SEQRES 1 B 285 ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA
SEQRES 2 B 285 LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU
SEQRES 3 B 285 ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG
SEQRES 4 B 285 ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO
SEQRES 5 B 285 CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL
SEQRES 6 B 285 THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU
SEQRES 7 B 285 GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN
SEQRES 8 B 285 CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP
SEQRES 9 B 285 LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU
SEQRES 10 B 285 PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS
SEQRES 11 B 285 TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU
SEQRES 12 B 285 ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY
SEQRES 13 B 285 TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR
SEQRES 14 B 285 PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER
SEQRES 15 B 285 GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP
SEQRES 16 B 285 LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA
SEQRES 17 B 285 ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS
SEQRES 18 B 285 CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA
SEQRES 19 B 285 HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER
SEQRES 20 B 285 THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP
SEQRES 21 B 285 TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE
SEQRES 22 B 285 SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER
SEQRES 1 C 285 ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA
SEQRES 2 C 285 LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU
SEQRES 3 C 285 ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG
SEQRES 4 C 285 ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO
SEQRES 5 C 285 CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL
SEQRES 6 C 285 THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU
SEQRES 7 C 285 GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN
SEQRES 8 C 285 CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP
SEQRES 9 C 285 LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU
SEQRES 10 C 285 PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS
SEQRES 11 C 285 TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU
SEQRES 12 C 285 ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY
SEQRES 13 C 285 TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR
SEQRES 14 C 285 PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER
SEQRES 15 C 285 GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP
SEQRES 16 C 285 LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA
SEQRES 17 C 285 ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS
SEQRES 18 C 285 CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA
SEQRES 19 C 285 HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER
SEQRES 20 C 285 THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP
SEQRES 21 C 285 TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE
SEQRES 22 C 285 SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER
SEQRES 1 D 285 ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA
SEQRES 2 D 285 LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU
SEQRES 3 D 285 ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG
SEQRES 4 D 285 ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO
SEQRES 5 D 285 CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL
SEQRES 6 D 285 THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU
SEQRES 7 D 285 GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN
SEQRES 8 D 285 CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP
SEQRES 9 D 285 LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU
SEQRES 10 D 285 PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS
SEQRES 11 D 285 TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU
SEQRES 12 D 285 ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY
SEQRES 13 D 285 TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR
SEQRES 14 D 285 PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER
SEQRES 15 D 285 GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP
SEQRES 16 D 285 LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA
SEQRES 17 D 285 ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS
SEQRES 18 D 285 CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA
SEQRES 19 D 285 HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER
SEQRES 20 D 285 THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP
SEQRES 21 D 285 TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE
SEQRES 22 D 285 SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER
HET ZN A 1 1
HET ZN A 2 1
HET ZN A 3 1
HET ZN A 4 1
HET E72 A1236 39
HET ZN B 5 1
HET ZN B 6 1
HET ZN B 7 1
HET ZN B 8 1
HET E72 B 2 39
HET ZN C 1 1
HET ZN C 2 1
HET ZN C 3 1
HET ZN C 4 1
HET SAH C 103 26
HET E72 C1236 39
HET ZN D 5 1
HET ZN D 6 1
HET ZN D 7 1
HET ZN D 8 1
HET SAH D 104 26
HET E72 D 4 39
HETNAM ZN ZINC ION
HETNAM E72 7-[(5-AMINOPENTYL)OXY]-N~4~-[1-(5-AMINOPENTYL)
HETNAM 2 E72 PIPERIDIN-4-YL]-N~2~-[3-(DIMETHYLAMINO)PROPYL]-6-
HETNAM 3 E72 METHOXYQUINAZOLINE-2,4-DIAMINE
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 5 ZN 16(ZN 2+)
FORMUL 9 E72 4(C29 H52 N8 O2)
FORMUL 19 SAH 2(C14 H20 N6 O5 S)
FORMUL 27 HOH *699(H2 O)
HELIX 1 1 ASN A 1024 LEU A 1028 5 5
HELIX 2 2 CYS A 1042 SER A 1048 1 7
HELIX 3 3 VAL A 1088 GLY A 1092 5 5
HELIX 4 4 ASP A 1131 ASP A 1135 1 5
HELIX 5 5 VAL A 1164 ILE A 1168 5 5
HELIX 6 6 GLY A 1212 GLY A 1220 1 9
HELIX 7 7 ASN B 1024 LEU B 1028 5 5
HELIX 8 8 CYS B 1042 SER B 1048 1 7
HELIX 9 9 VAL B 1088 GLY B 1092 5 5
HELIX 10 10 ASP B 1131 ASP B 1135 1 5
HELIX 11 11 VAL B 1164 ILE B 1168 5 5
HELIX 12 12 GLY B 1212 GLY B 1220 1 9
HELIX 13 13 ASN C 1024 LEU C 1028 5 5
HELIX 14 14 CYS C 1042 SER C 1048 1 7
HELIX 15 15 VAL C 1088 GLY C 1092 5 5
HELIX 16 16 ASP C 1131 ASP C 1135 1 5
HELIX 17 17 VAL C 1164 ILE C 1168 5 5
HELIX 18 18 GLY C 1212 GLY C 1220 1 9
HELIX 19 19 ASN D 1024 LEU D 1028 5 5
HELIX 20 20 CYS D 1042 SER D 1048 1 7
HELIX 21 21 VAL D 1088 GLY D 1092 5 5
HELIX 22 22 ASP D 1131 ASP D 1135 1 5
HELIX 23 23 VAL D 1164 ILE D 1168 5 5
HELIX 24 24 GLY D 1212 GLY D 1220 1 9
SHEET 1 A 3 CYS A 994 VAL A 995 0
SHEET 2 A 3 LEU A1097 ARG A1101 1 O LEU A1099 N VAL A 995
SHEET 3 A 3 TRP A1107 SER A1111 -1 O GLY A1108 N TYR A1100
SHEET 1 B 3 LYS A1008 TYR A1009 0
SHEET 2 B 3 TYR A1154 GLY A1162 1 O PHE A1160 N LYS A1008
SHEET 3 B 3 GLY A1126 SER A1130 -1 N GLU A1127 O ASP A1157
SHEET 1 C 3 LYS A1008 TYR A1009 0
SHEET 2 C 3 TYR A1154 GLY A1162 1 O PHE A1160 N LYS A1008
SHEET 3 C 3 LEU A1143 LEU A1146 -1 N LEU A1146 O TYR A1154
SHEET 1 D 4 ILE A1071 PHE A1072 0
SHEET 2 D 4 LEU A1176 PHE A1182 1 O PHE A1182 N ILE A1071
SHEET 3 D 4 ARG A1192 SER A1197 -1 O ALA A1194 N VAL A1179
SHEET 4 D 4 PHE A1120 GLU A1123 -1 N VAL A1121 O PHE A1195
SHEET 1 E 2 ASN A1169 HIS A1170 0
SHEET 2 E 2 GLY A1208 PHE A1209 1 O PHE A1209 N ASN A1169
SHEET 1 F 4 ARG B 977 SER B 980 0
SHEET 2 F 4 CYS B 994 ASN B 996 -1 O CYS B 994 N SER B 980
SHEET 3 F 4 LEU B1097 ARG B1101 1 O LEU B1099 N VAL B 995
SHEET 4 F 4 TRP B1107 SER B1111 -1 O GLY B1108 N TYR B1100
SHEET 1 G 3 LYS B1008 TYR B1009 0
SHEET 2 G 3 TYR B1154 GLY B1162 1 O PHE B1160 N LYS B1008
SHEET 3 G 3 GLY B1126 SER B1130 -1 N ILE B1129 O CYS B1155
SHEET 1 H 3 LYS B1008 TYR B1009 0
SHEET 2 H 3 TYR B1154 GLY B1162 1 O PHE B1160 N LYS B1008
SHEET 3 H 3 LEU B1143 ASP B1145 -1 N PHE B1144 O ILE B1156
SHEET 1 I 4 ILE B1071 PHE B1072 0
SHEET 2 I 4 LEU B1176 PHE B1182 1 O ARG B1180 N ILE B1071
SHEET 3 I 4 ARG B1192 SER B1197 -1 O ARG B1192 N VAL B1181
SHEET 4 I 4 PHE B1120 TYR B1124 -1 N VAL B1121 O PHE B1195
SHEET 1 J 2 ASN B1169 HIS B1170 0
SHEET 2 J 2 GLY B1208 PHE B1209 1 O PHE B1209 N ASN B1169
SHEET 1 K 4 ARG C 977 SER C 980 0
SHEET 2 K 4 CYS C 994 ASN C 996 -1 O CYS C 994 N SER C 980
SHEET 3 K 4 LEU C1097 ARG C1101 1 O LEU C1099 N VAL C 995
SHEET 4 K 4 TRP C1107 SER C1111 -1 O GLY C1108 N TYR C1100
SHEET 1 L 3 LYS C1008 TYR C1009 0
SHEET 2 L 3 TYR C1154 GLY C1162 1 O PHE C1160 N LYS C1008
SHEET 3 L 3 GLY C1126 SER C1130 -1 N GLU C1127 O ASP C1157
SHEET 1 M 3 LYS C1008 TYR C1009 0
SHEET 2 M 3 TYR C1154 GLY C1162 1 O PHE C1160 N LYS C1008
SHEET 3 M 3 LEU C1143 ASP C1145 -1 N PHE C1144 O ILE C1156
SHEET 1 N 4 ILE C1071 PHE C1072 0
SHEET 2 N 4 LEU C1176 PHE C1182 1 O PHE C1182 N ILE C1071
SHEET 3 N 4 ARG C1192 SER C1197 -1 O ALA C1194 N VAL C1179
SHEET 4 N 4 PHE C1120 TYR C1124 -1 N VAL C1121 O PHE C1195
SHEET 1 O 2 ASN C1169 HIS C1170 0
SHEET 2 O 2 GLY C1208 PHE C1209 1 O PHE C1209 N ASN C1169
SHEET 1 P 4 ARG D 977 SER D 980 0
SHEET 2 P 4 CYS D 994 ASN D 996 -1 O CYS D 994 N SER D 980
SHEET 3 P 4 LEU D1097 ARG D1101 1 O LEU D1099 N VAL D 995
SHEET 4 P 4 TRP D1107 SER D1111 -1 O GLY D1108 N TYR D1100
SHEET 1 Q 3 LYS D1008 TYR D1009 0
SHEET 2 Q 3 TYR D1154 GLY D1162 1 O PHE D1160 N LYS D1008
SHEET 3 Q 3 GLY D1126 SER D1130 -1 N ILE D1129 O CYS D1155
SHEET 1 R 3 LYS D1008 TYR D1009 0
SHEET 2 R 3 TYR D1154 GLY D1162 1 O PHE D1160 N LYS D1008
SHEET 3 R 3 LEU D1143 ASP D1145 -1 N PHE D1144 O ILE D1156
SHEET 1 S 4 ILE D1071 PHE D1072 0
SHEET 2 S 4 LEU D1176 PHE D1182 1 O PHE D1182 N ILE D1071
SHEET 3 S 4 ARG D1192 SER D1197 -1 O ARG D1192 N VAL D1181
SHEET 4 S 4 PHE D1120 GLU D1123 -1 N VAL D1121 O PHE D1195
SHEET 1 T 2 ASN D1169 HIS D1170 0
SHEET 2 T 2 GLY D1208 PHE D1209 1 O PHE D1209 N ASN D1169
LINK ZN ZN A 1 SG CYS A1031 1555 1555 2.46
LINK ZN ZN A 1 SG CYS A1044 1555 1555 2.31
LINK ZN ZN A 1 SG CYS A1074 1555 1555 2.39
LINK ZN ZN A 1 SG CYS A1078 1555 1555 2.36
LINK ZN ZN A 2 SG CYS A1037 1555 1555 2.31
LINK ZN ZN A 2 SG CYS A1074 1555 1555 2.33
LINK ZN ZN A 2 SG CYS A1080 1555 1555 2.30
LINK ZN ZN A 2 SG CYS A1084 1555 1555 2.37
LINK ZN ZN A 3 SG CYS A1031 1555 1555 2.36
LINK ZN ZN A 3 SG CYS A1033 1555 1555 2.43
LINK ZN ZN A 3 SG CYS A1037 1555 1555 2.34
LINK ZN ZN A 3 SG CYS A1042 1555 1555 2.34
LINK ZN ZN A 4 SG CYS A1172 1555 1555 2.45
LINK ZN ZN A 4 SG CYS A1225 1555 1555 2.36
LINK ZN ZN A 4 SG CYS A1227 1555 1555 2.37
LINK ZN ZN A 4 SG CYS A1232 1555 1555 2.61
LINK ZN ZN B 5 SG CYS B1031 1555 1555 2.38
LINK ZN ZN B 5 SG CYS B1044 1555 1555 2.37
LINK ZN ZN B 5 SG CYS B1074 1555 1555 2.45
LINK ZN ZN B 5 SG CYS B1078 1555 1555 2.46
LINK ZN ZN B 6 SG CYS B1037 1555 1555 2.37
LINK ZN ZN B 6 SG CYS B1074 1555 1555 2.36
LINK ZN ZN B 6 SG CYS B1080 1555 1555 2.27
LINK ZN ZN B 6 SG CYS B1084 1555 1555 2.38
LINK ZN ZN B 7 SG CYS B1031 1555 1555 2.45
LINK ZN ZN B 7 SG CYS B1033 1555 1555 2.48
LINK ZN ZN B 7 SG CYS B1037 1555 1555 2.48
LINK ZN ZN B 7 SG CYS B1042 1555 1555 2.32
LINK ZN ZN B 8 SG CYS B1172 1555 1555 2.40
LINK ZN ZN B 8 SG CYS B1225 1555 1555 2.39
LINK ZN ZN B 8 SG CYS B1227 1555 1555 2.35
LINK ZN ZN B 8 SG CYS B1232 1555 1555 2.62
LINK ZN ZN C 1 SG CYS C1031 1555 1555 2.51
LINK ZN ZN C 1 SG CYS C1044 1555 1555 2.46
LINK ZN ZN C 1 SG CYS C1074 1555 1555 2.37
LINK ZN ZN C 1 SG CYS C1078 1555 1555 2.37
LINK ZN ZN C 2 SG CYS C1037 1555 1555 2.33
LINK ZN ZN C 2 SG CYS C1074 1555 1555 2.47
LINK ZN ZN C 2 SG CYS C1080 1555 1555 2.24
LINK ZN ZN C 2 SG CYS C1084 1555 1555 2.40
LINK ZN ZN C 3 SG CYS C1031 1555 1555 2.25
LINK ZN ZN C 3 SG CYS C1033 1555 1555 2.44
LINK ZN ZN C 3 SG CYS C1037 1555 1555 2.37
LINK ZN ZN C 3 SG CYS C1042 1555 1555 2.36
LINK ZN ZN C 4 SG CYS C1172 1555 1555 2.47
LINK ZN ZN C 4 SG CYS C1225 1555 1555 2.42
LINK ZN ZN C 4 SG CYS C1227 1555 1555 2.41
LINK ZN ZN C 4 SG CYS C1232 1555 1555 2.48
LINK ZN ZN D 5 O HOH D 548 1555 1555 2.19
LINK ZN ZN D 5 SG CYS D1031 1555 1555 2.54
LINK ZN ZN D 5 SG CYS D1044 1555 1555 2.34
LINK ZN ZN D 5 SG CYS D1074 1555 1555 2.47
LINK ZN ZN D 5 SG CYS D1078 1555 1555 2.45
LINK ZN ZN D 6 O HOH D 548 1555 1555 2.45
LINK ZN ZN D 6 SG CYS D1037 1555 1555 2.58
LINK ZN ZN D 6 SG CYS D1074 1555 1555 2.34
LINK ZN ZN D 6 SG CYS D1080 1555 1555 2.42
LINK ZN ZN D 6 SG CYS D1084 1555 1555 2.31
LINK ZN ZN D 7 SG CYS D1031 1555 1555 2.43
LINK ZN ZN D 7 SG CYS D1033 1555 1555 2.49
LINK ZN ZN D 7 SG CYS D1037 1555 1555 2.37
LINK ZN ZN D 7 SG CYS D1042 1555 1555 2.50
LINK ZN ZN D 8 SG CYS D1172 1555 1555 2.58
LINK ZN ZN D 8 SG CYS D1225 1555 1555 2.43
LINK ZN ZN D 8 SG CYS D1227 1555 1555 2.43
LINK ZN ZN D 8 SG CYS D1232 1555 1555 2.58
SITE 1 AC1 4 CYS A1031 CYS A1044 CYS A1074 CYS A1078
SITE 1 AC2 5 ZN A 3 CYS A1037 CYS A1074 CYS A1080
SITE 2 AC2 5 CYS A1084
SITE 1 AC3 5 ZN A 2 CYS A1031 CYS A1033 CYS A1037
SITE 2 AC3 5 CYS A1042
SITE 1 AC4 4 CYS A1172 CYS A1225 CYS A1227 CYS A1232
SITE 1 AC5 16 HOH A 245 HOH A 672 HOH A 674 TYR A1124
SITE 2 AC5 16 ASP A1131 ALA A1134 ASP A1135 ARG A1137
SITE 3 AC5 16 ASP A1140 SER A1141 LEU A1143 ASP A1145
SITE 4 AC5 16 TYR A1211 ARG A1214 PHE A1215 LYS A1219
SITE 1 AC6 5 ZN B 7 CYS B1031 CYS B1044 CYS B1074
SITE 2 AC6 5 CYS B1078
SITE 1 AC7 4 CYS B1037 CYS B1074 CYS B1080 CYS B1084
SITE 1 AC8 5 ZN B 5 CYS B1031 CYS B1033 CYS B1037
SITE 2 AC8 5 CYS B1042
SITE 1 AC9 4 CYS B1172 CYS B1225 CYS B1227 CYS B1232
SITE 1 BC1 19 HOH B 86 HOH B 197 ASP B1131 ALA B1134
SITE 2 BC1 19 ASP B1135 VAL B1136 ARG B1137 ASP B1140
SITE 3 BC1 19 SER B1141 LEU B1143 ASP B1145 TYR B1211
SITE 4 BC1 19 ARG B1214 PHE B1215 ILE B1218 LYS B1219
SITE 5 BC1 19 HOH D 153 ASP D1022 ARG D1189
SITE 1 BC2 5 ZN C 2 CYS C1031 CYS C1044 CYS C1074
SITE 2 BC2 5 CYS C1078
SITE 1 BC3 5 ZN C 1 CYS C1037 CYS C1074 CYS C1080
SITE 2 BC3 5 CYS C1084
SITE 1 BC4 4 CYS C1031 CYS C1033 CYS C1037 CYS C1042
SITE 1 BC5 4 CYS C1172 CYS C1225 CYS C1227 CYS C1232
SITE 1 BC6 12 HOH C 362 MET C1105 GLY C1106 TRP C1107
SITE 2 BC6 12 TYR C1142 ARG C1166 ASN C1169 HIS C1170
SITE 3 BC6 12 TYR C1211 CYS C1225 ARG C1226 CYS C1227
SITE 1 BC7 19 HOH A 132 HOH A 244 ASP A1022 GLU A1152
SITE 2 BC7 19 ASP A1187 ARG A1189 HOH C 172 HOH C 398
SITE 3 BC7 19 ASP C1131 ALA C1134 ASP C1135 ASP C1140
SITE 4 BC7 19 SER C1141 LEU C1143 ASP C1145 TYR C1211
SITE 5 BC7 19 ARG C1214 PHE C1215 LYS C1219
SITE 1 BC8 5 HOH D 548 CYS D1031 CYS D1044 CYS D1074
SITE 2 BC8 5 CYS D1078
SITE 1 BC9 5 HOH D 548 CYS D1037 CYS D1074 CYS D1080
SITE 2 BC9 5 CYS D1084
SITE 1 CC1 4 CYS D1031 CYS D1033 CYS D1037 CYS D1042
SITE 1 CC2 4 CYS D1172 CYS D1225 CYS D1227 CYS D1232
SITE 1 CC3 12 MET D1105 GLY D1106 TRP D1107 TYR D1142
SITE 2 CC3 12 ARG D1166 ASN D1169 HIS D1170 TYR D1211
SITE 3 CC3 12 PHE D1215 PHE D1223 CYS D1225 ARG D1226
SITE 1 CC4 14 HOH D 453 ASP D1131 ALA D1134 ASP D1135
SITE 2 CC4 14 VAL D1136 ARG D1137 ASP D1140 SER D1141
SITE 3 CC4 14 LEU D1143 ASP D1145 TYR D1211 ARG D1214
SITE 4 CC4 14 PHE D1215 ILE D1218
CRYST1 59.900 162.900 69.100 90.00 99.00 90.00 P 1 21 1 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 0.016694 0.000000 0.002644 0.00000
SCALE2 0.000000 0.006139 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014652 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
