HEADER TRANSFERASE 23-MAR-17 5V9I
TITLE CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF G9A WITH MS0105
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 913-1193;
COMPND 5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 2,HLA-B-
COMPND 6 ASSOCIATED TRANSCRIPT 8,HISTONE H3-K9 METHYLTRANSFERASE 3,H3-K9-
COMPND 7 HMTASE 3,LYSINE N-METHYLTRANSFERASE 1C,PROTEIN G9A;
COMPND 8 EC: 2.1.1.-,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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC
KEYWDS EHMT2, BAT8, METHYLTRANSFERASE, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DONG,H.ZENG,J.LIU,Y.XIONG,N.BABAULT,J.JIN,J.R.WALKER,C.BOUNTRA,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,H.WU,P.J.BROWN,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 2 04-OCT-23 5V9I 1 LINK
REVDAT 1 21-MAR-18 5V9I 0
JRNL AUTH H.ZENG,A.DONG,J.LIU,Y.XIONG,N.BABAULT,J.JIN,J.R.WALKER,
JRNL AUTH 2 C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,H.WU,P.J.BROWN
JRNL TITL CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF G9A WITH MS0105
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 119034
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1188
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.78
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.99
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 8809
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2340
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8710
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.12
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 99
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8321
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 290
REMARK 3 SOLVENT ATOMS : 700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.79960
REMARK 3 B22 (A**2) : -3.66100
REMARK 3 B33 (A**2) : -1.13860
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.91560
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.270
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.142
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.136
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.139
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.135
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9048 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 12322 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3200 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 228 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1480 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9048 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1183 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 11205 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.96
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.37
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.52
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|916 - A|1506 }
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5360 1.0129 76.2360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1766 T22: 0.3161
REMARK 3 T33: 0.1058 T12: 0.1075
REMARK 3 T13: -0.0341 T23: -0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 1.5986 L22: 0.6948
REMARK 3 L33: 1.2462 L12: -0.0455
REMARK 3 L13: 0.8662 L23: 0.1601
REMARK 3 S TENSOR
REMARK 3 S11: -0.0980 S12: -0.4796 S13: 0.0043
REMARK 3 S21: 0.2142 S22: 0.1972 S23: -0.1281
REMARK 3 S31: -0.0200 S32: -0.3202 S33: -0.0992
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|918 - B|1506 }
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2630 1.6738 43.8565
REMARK 3 T TENSOR
REMARK 3 T11: 0.1063 T22: 0.0950
REMARK 3 T33: 0.1026 T12: -0.0131
REMARK 3 T13: -0.0010 T23: 0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 2.5518 L22: 0.4805
REMARK 3 L33: 0.5932 L12: -0.2038
REMARK 3 L13: 0.6897 L23: -0.1069
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: 0.1331 S13: 0.0808
REMARK 3 S21: -0.0616 S22: 0.0520 S23: 0.0212
REMARK 3 S31: 0.0432 S32: 0.0310 S33: -0.0432
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|916 - C|1506 }
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0173 -1.6003 8.8736
REMARK 3 T TENSOR
REMARK 3 T11: 0.1062 T22: 0.1023
REMARK 3 T33: 0.1347 T12: 0.0458
REMARK 3 T13: -0.0072 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.1423 L22: 0.6532
REMARK 3 L33: 0.9833 L12: 0.1351
REMARK 3 L13: 0.4454 L23: 0.1951
REMARK 3 S TENSOR
REMARK 3 S11: 0.0201 S12: -0.1295 S13: -0.0501
REMARK 3 S21: 0.1724 S22: 0.0650 S23: -0.0904
REMARK 3 S31: 0.0248 S32: -0.1159 S33: -0.0851
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|918 - D|1506 }
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3106 -0.5400 -23.0070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0781 T22: 0.0992
REMARK 3 T33: 0.1017 T12: -0.0234
REMARK 3 T13: 0.0062 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 2.0659 L22: 0.6764
REMARK 3 L33: 0.7092 L12: -0.0384
REMARK 3 L13: 0.5597 L23: -0.1401
REMARK 3 S TENSOR
REMARK 3 S11: -0.0278 S12: 0.2114 S13: 0.0604
REMARK 3 S21: -0.1051 S22: 0.0562 S23: 0.0466
REMARK 3 S31: 0.0476 S32: 0.0370 S33: -0.0284
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V9I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119624
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.59600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 2O8J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2 M NACL, 0.1 M BIS
REMARK 280 -TRIS PH6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 38.75450
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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 ASN A 1091
REMARK 465 LYS A 1092
REMARK 465 ASP A 1093
REMARK 465 GLY A 1094
REMARK 465 GLN A 1186
REMARK 465 SER A 1187
REMARK 465 ARG A 1188
REMARK 465 LEU A 1189
REMARK 465 ALA A 1190
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 ASN B 1091
REMARK 465 LYS B 1092
REMARK 465 ASP B 1093
REMARK 465 GLY B 1094
REMARK 465 ALA B 1190
REMARK 465 ARG B 1191
REMARK 465 LEU B 1192
REMARK 465 ASP B 1193
REMARK 465 GLY C 911
REMARK 465 SER C 912
REMARK 465 ASN C 913
REMARK 465 ARG C 914
REMARK 465 ALA C 915
REMARK 465 ASN C 1091
REMARK 465 LYS C 1092
REMARK 465 ASP C 1093
REMARK 465 GLY C 1094
REMARK 465 GLU C 1185
REMARK 465 GLN C 1186
REMARK 465 SER C 1187
REMARK 465 ARG C 1188
REMARK 465 LEU C 1189
REMARK 465 ALA C 1190
REMARK 465 ARG C 1191
REMARK 465 LEU C 1192
REMARK 465 ASP C 1193
REMARK 465 GLY D 911
REMARK 465 SER D 912
REMARK 465 ASN D 913
REMARK 465 ARG D 914
REMARK 465 ALA D 915
REMARK 465 ILE D 916
REMARK 465 ARG D 917
REMARK 465 ASN D 1091
REMARK 465 LYS D 1092
REMARK 465 ASP D 1093
REMARK 465 GLY D 1094
REMARK 465 SER D 1187
REMARK 465 ARG D 1188
REMARK 465 LEU D 1189
REMARK 465 ALA D 1190
REMARK 465 ARG D 1191
REMARK 465 LEU D 1192
REMARK 465 ASP D 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 ILE A 916 CG1 CG2 CD1
REMARK 470 ARG A 917 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 920 CG CD CE NZ
REMARK 470 ARG A 924 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 972 OE1 NE2
REMARK 470 VAL A 977 CG1 CG2
REMARK 470 SER A 983 OG
REMARK 470 ILE A 992 CD1
REMARK 470 ARG A 993 CD NE CZ NH1 NH2
REMARK 470 LYS A 998 NZ
REMARK 470 GLN A1004 CG CD OE1 NE2
REMARK 470 LYS A1008 CE NZ
REMARK 470 LYS A1028 NZ
REMARK 470 GLU A1081 CG CD OE1 OE2
REMARK 470 ASP A1090 CG OD1 OD2
REMARK 470 GLU A1095 N CB CG CD OE1 OE2
REMARK 470 ARG A1145 CD NE CZ NH1 NH2
REMARK 470 ILE A1161 CD1
REMARK 470 LYS A1164 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 ILE A1182 CG1 CG2 CD1
REMARK 470 GLU A1185 CG CD OE1 OE2
REMARK 470 THR B 918 OG1 CG2
REMARK 470 LYS B 920 CG CD CE NZ
REMARK 470 ASN B 963 CG OD1 ND2
REMARK 470 GLN B1004 CD OE1 NE2
REMARK 470 GLU B1005 CG CD OE1 OE2
REMARK 470 ILE B1009 CD1
REMARK 470 GLU B1010 CG CD OE1 OE2
REMARK 470 LYS B1047 CE NZ
REMARK 470 GLU B1081 CG CD OE1 OE2
REMARK 470 ASP B1090 CG OD1 OD2
REMARK 470 GLU B1095 N CB CG CD OE1 OE2
REMARK 470 ARG B1145 CD NE CZ NH1 NH2
REMARK 470 GLU B1173 CG CD OE1 OE2
REMARK 470 LYS B1174 CE NZ
REMARK 470 LYS B1176 CE NZ
REMARK 470 ARG C 917 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 920 CG CD CE NZ
REMARK 470 ARG C 924 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 977 CG1 CG2
REMARK 470 SER C 983 OG
REMARK 470 ILE C 992 CD1
REMARK 470 ARG C 993 NE CZ NH1 NH2
REMARK 470 LYS C 998 CE NZ
REMARK 470 GLN C1004 CG CD OE1 NE2
REMARK 470 ILE C1009 CD1
REMARK 470 GLU C1010 CG CD OE1 OE2
REMARK 470 LYS C1047 NZ
REMARK 470 GLU C1081 CG CD OE1 OE2
REMARK 470 ASP C1090 CG OD1 OD2
REMARK 470 GLU C1095 N CA CB CG CD OE1 OE2
REMARK 470 ARG C1145 CD NE CZ NH1 NH2
REMARK 470 LYS C1164 CE NZ
REMARK 470 GLU C1173 CG CD OE1 OE2
REMARK 470 LYS C1174 NZ
REMARK 470 LYS C1176 CG CD CE NZ
REMARK 470 ILE C1182 CG1 CG2 CD1
REMARK 470 LEU C1184 CG CD1 CD2
REMARK 470 THR D 918 OG1 CG2
REMARK 470 LYS D 920 CG CD CE NZ
REMARK 470 ILE D 992 CG1 CG2 CD1
REMARK 470 GLN D1004 CG CD OE1 NE2
REMARK 470 GLU D1005 CD OE1 OE2
REMARK 470 ILE D1009 CG1 CG2 CD1
REMARK 470 GLU D1010 CG CD OE1 OE2
REMARK 470 LYS D1047 CG CD CE NZ
REMARK 470 GLU D1081 CG CD OE1 OE2
REMARK 470 GLU D1095 N CB CG CD OE1 OE2
REMARK 470 ARG D1145 CD NE CZ NH1 NH2
REMARK 470 LYS D1164 NZ
REMARK 470 GLU D1173 CG CD OE1 OE2
REMARK 470 LYS D1174 CD CE NZ
REMARK 470 LEU D1184 CG CD1 CD2
REMARK 470 GLU D1185 CG CD OE1 OE2
REMARK 470 GLN D1186 CG CD OE1 NE2
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 978 -158.58 -84.10
REMARK 500 ILE A 992 -55.46 73.31
REMARK 500 ASN A1029 50.48 -113.89
REMARK 500 ILE A1064 -67.10 -103.10
REMARK 500 LEU A1089 70.79 -109.69
REMARK 500 LEU A1089 69.05 -109.95
REMARK 500 ASN A1106 -160.92 -110.17
REMARK 500 MET A1126 -93.22 -128.14
REMARK 500 ASP B 925 105.68 -160.22
REMARK 500 ASP B 978 -151.40 -102.37
REMARK 500 ILE B 992 -57.72 78.96
REMARK 500 ASN B1029 51.19 -109.13
REMARK 500 ARG B1030 33.31 -149.08
REMARK 500 ILE B1064 -65.04 -103.84
REMARK 500 ASN B1106 -161.03 -106.07
REMARK 500 ASP B1116 78.59 -115.71
REMARK 500 MET B1126 -89.96 -131.12
REMARK 500 ASP C 925 108.07 -163.33
REMARK 500 ASP C 978 -156.03 -83.75
REMARK 500 ILE C 992 -51.79 72.48
REMARK 500 ASN C1029 54.58 -111.72
REMARK 500 ARG C1030 19.13 -142.89
REMARK 500 ILE C1064 -64.58 -101.52
REMARK 500 LEU C1089 73.09 -107.64
REMARK 500 ASN C1106 -162.28 -107.06
REMARK 500 ASP C1116 77.81 -115.74
REMARK 500 MET C1126 -92.78 -128.77
REMARK 500 ASP D 978 -150.33 -105.35
REMARK 500 ILE D 992 -53.07 83.02
REMARK 500 ASN D1029 55.35 -113.31
REMARK 500 ARG D1030 30.34 -151.96
REMARK 500 ILE D1064 -65.76 -103.17
REMARK 500 ASN D1106 -161.83 -108.28
REMARK 500 ASP D1116 78.50 -117.51
REMARK 500 MET D1126 -89.92 -129.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 90P A 1506
REMARK 610 90P B 1506
REMARK 610 90P C 1506
REMARK 610 90P D 1506
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 A1501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 974 SG
REMARK 620 2 CYS A 987 SG 118.4
REMARK 620 3 CYS A1017 SG 98.6 114.4
REMARK 620 4 CYS A1021 SG 108.0 105.0 112.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 974 SG
REMARK 620 2 CYS A 976 SG 97.9
REMARK 620 3 CYS A 980 SG 107.4 107.5
REMARK 620 4 CYS A 985 SG 113.8 106.9 120.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 980 SG
REMARK 620 2 CYS A1017 SG 108.1
REMARK 620 3 CYS A1023 SG 103.6 104.3
REMARK 620 4 CYS A1027 SG 115.4 110.0 114.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1115 SG
REMARK 620 2 CYS A1168 SG 112.7
REMARK 620 3 CYS A1170 SG 109.0 107.0
REMARK 620 4 CYS A1175 SG 106.3 115.5 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 974 SG
REMARK 620 2 CYS B 987 SG 113.2
REMARK 620 3 CYS B1017 SG 107.3 111.1
REMARK 620 4 CYS B1021 SG 108.6 99.3 117.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 974 SG
REMARK 620 2 CYS B 976 SG 105.0
REMARK 620 3 CYS B 980 SG 107.4 103.6
REMARK 620 4 CYS B 985 SG 113.3 108.0 118.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 980 SG
REMARK 620 2 CYS B1017 SG 111.4
REMARK 620 3 CYS B1023 SG 104.1 106.1
REMARK 620 4 CYS B1027 SG 114.9 105.6 114.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1115 SG
REMARK 620 2 CYS B1168 SG 111.5
REMARK 620 3 CYS B1170 SG 110.9 108.8
REMARK 620 4 CYS B1175 SG 105.4 110.6 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 974 SG
REMARK 620 2 CYS C 987 SG 116.4
REMARK 620 3 CYS C1017 SG 104.4 113.5
REMARK 620 4 CYS C1021 SG 103.6 100.6 118.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 974 SG
REMARK 620 2 CYS C 976 SG 101.5
REMARK 620 3 CYS C 980 SG 105.6 106.8
REMARK 620 4 CYS C 985 SG 115.5 107.0 118.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 980 SG
REMARK 620 2 CYS C1017 SG 107.3
REMARK 620 3 CYS C1023 SG 106.5 102.8
REMARK 620 4 CYS C1027 SG 118.0 105.9 115.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1115 SG
REMARK 620 2 CYS C1168 SG 110.9
REMARK 620 3 CYS C1170 SG 110.3 107.1
REMARK 620 4 CYS C1175 SG 104.9 113.1 110.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 974 SG
REMARK 620 2 CYS D 987 SG 114.3
REMARK 620 3 CYS D1017 SG 106.5 112.6
REMARK 620 4 CYS D1021 SG 106.0 100.8 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 974 SG
REMARK 620 2 CYS D 976 SG 104.3
REMARK 620 3 CYS D 980 SG 105.6 108.9
REMARK 620 4 CYS D 985 SG 114.7 107.2 115.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 980 SG
REMARK 620 2 CYS D1017 SG 112.1
REMARK 620 3 CYS D1023 SG 108.9 106.3
REMARK 620 4 CYS D1027 SG 111.1 104.2 114.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1115 SG
REMARK 620 2 CYS D1168 SG 109.6
REMARK 620 3 CYS D1170 SG 111.2 106.3
REMARK 620 4 CYS D1175 SG 106.0 112.8 111.1
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 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 90P A 1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 90P B 1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM C 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 90P C 1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM D 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 90P D 1506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 1507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 1508
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V9J RELATED DB: PDB
DBREF 5V9I A 913 1193 UNP Q96KQ7 EHMT2_HUMAN 913 1193
DBREF 5V9I B 913 1193 UNP Q96KQ7 EHMT2_HUMAN 913 1193
DBREF 5V9I C 913 1193 UNP Q96KQ7 EHMT2_HUMAN 913 1193
DBREF 5V9I D 913 1193 UNP Q96KQ7 EHMT2_HUMAN 913 1193
SEQADV 5V9I GLY A 911 UNP Q96KQ7 EXPRESSION TAG
SEQADV 5V9I SER A 912 UNP Q96KQ7 EXPRESSION TAG
SEQADV 5V9I GLY B 911 UNP Q96KQ7 EXPRESSION TAG
SEQADV 5V9I SER B 912 UNP Q96KQ7 EXPRESSION TAG
SEQADV 5V9I GLY C 911 UNP Q96KQ7 EXPRESSION TAG
SEQADV 5V9I SER C 912 UNP Q96KQ7 EXPRESSION TAG
SEQADV 5V9I GLY D 911 UNP Q96KQ7 EXPRESSION TAG
SEQADV 5V9I SER D 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
SEQRES 1 C 283 GLY SER ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS
SEQRES 2 C 283 ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO
SEQRES 3 C 283 CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP
SEQRES 4 C 283 TYR LYS TYR ILE SER GLU ASN CYS GLU THR SER THR MET
SEQRES 5 C 283 ASN ILE ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR
SEQRES 6 C 283 CYS VAL ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY
SEQRES 7 C 283 GLN LEU SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG
SEQRES 8 C 283 LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE
SEQRES 9 C 283 PHE GLU CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS
SEQRES 10 C 283 LYS ASN ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU
SEQRES 11 C 283 GLN LEU TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG
SEQRES 12 C 283 ALA LEU GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU
SEQRES 13 C 283 TYR VAL GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL
SEQRES 14 C 283 ARG GLU ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS
SEQRES 15 C 283 ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY
SEQRES 16 C 283 ASN ILE SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN
SEQRES 17 C 283 ILE ILE PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU
SEQRES 18 C 283 ARG PHE PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE
SEQRES 19 C 283 ARG THR GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG
SEQRES 20 C 283 PHE TRP ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS
SEQRES 21 C 283 GLY SER GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA
SEQRES 22 C 283 LEU GLU GLN SER ARG LEU ALA ARG LEU ASP
SEQRES 1 D 283 GLY SER ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS
SEQRES 2 D 283 ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO
SEQRES 3 D 283 CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP
SEQRES 4 D 283 TYR LYS TYR ILE SER GLU ASN CYS GLU THR SER THR MET
SEQRES 5 D 283 ASN ILE ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR
SEQRES 6 D 283 CYS VAL ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY
SEQRES 7 D 283 GLN LEU SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG
SEQRES 8 D 283 LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE
SEQRES 9 D 283 PHE GLU CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS
SEQRES 10 D 283 LYS ASN ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU
SEQRES 11 D 283 GLN LEU TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG
SEQRES 12 D 283 ALA LEU GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU
SEQRES 13 D 283 TYR VAL GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL
SEQRES 14 D 283 ARG GLU ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS
SEQRES 15 D 283 ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY
SEQRES 16 D 283 ASN ILE SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN
SEQRES 17 D 283 ILE ILE PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU
SEQRES 18 D 283 ARG PHE PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE
SEQRES 19 D 283 ARG THR GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG
SEQRES 20 D 283 PHE TRP ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS
SEQRES 21 D 283 GLY SER GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA
SEQRES 22 D 283 LEU GLU GLN SER ARG LEU ALA ARG LEU ASP
HET ZN A1501 1
HET ZN A1502 1
HET ZN A1503 1
HET ZN A1504 1
HET SAM A1505 27
HET 90P A1506 27
HET GOL A1507 6
HET GOL A1508 6
HET GOL A1509 6
HET UNX A1510 1
HET ZN B1501 1
HET ZN B1502 1
HET ZN B1503 1
HET ZN B1504 1
HET SAM B1505 27
HET 90P B1506 27
HET GOL B1507 6
HET GOL B1508 6
HET GOL B1509 6
HET UNX B1510 1
HET UNX B1511 1
HET ZN C1501 1
HET ZN C1502 1
HET ZN C1503 1
HET ZN C1504 1
HET SAM C1505 27
HET 90P C1506 32
HET GOL C1507 6
HET UNX C1508 1
HET ZN D1501 1
HET ZN D1502 1
HET ZN D1503 1
HET ZN D1504 1
HET SAM D1505 27
HET 90P D1506 32
HET GOL D1507 6
HET GOL D1508 6
HETNAM ZN ZINC ION
HETNAM SAM S-ADENOSYLMETHIONINE
HETNAM 90P N~2~-CYCLOHEXYL-N~4~-(1-ETHYLPIPERIDIN-4-YL)-6,7-
HETNAM 2 90P DIMETHOXY-N~2~-METHYLQUINAZOLINE-2,4-DIAMINE
HETNAM GOL GLYCEROL
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ZN 16(ZN 2+)
FORMUL 9 SAM 4(C15 H22 N6 O5 S)
FORMUL 10 90P 4(C24 H37 N5 O2)
FORMUL 11 GOL 9(C3 H8 O3)
FORMUL 14 UNX 4(X)
FORMUL 42 HOH *700(H2 O)
HELIX 1 AA1 ASN A 967 LEU A 971 5 5
HELIX 2 AA2 CYS A 985 LEU A 990 1 6
HELIX 3 AA3 VAL A 1031 GLY A 1035 5 5
HELIX 4 AA4 ASP A 1074 ASP A 1078 1 5
HELIX 5 AA5 ILE A 1107 ILE A 1111 5 5
HELIX 6 AA6 GLY A 1155 SER A 1163 1 9
HELIX 7 AA7 SER A 1178 GLU A 1185 1 8
HELIX 8 AA8 ASN B 967 LEU B 971 5 5
HELIX 9 AA9 CYS B 985 SER B 991 1 7
HELIX 10 AB1 VAL B 1031 GLY B 1035 5 5
HELIX 11 AB2 ASP B 1074 ASP B 1078 1 5
HELIX 12 AB3 ILE B 1107 ILE B 1111 5 5
HELIX 13 AB4 GLY B 1155 SER B 1163 1 9
HELIX 14 AB5 SER B 1178 LEU B 1189 1 12
HELIX 15 AB6 ASN C 967 LEU C 971 5 5
HELIX 16 AB7 CYS C 985 LEU C 990 1 6
HELIX 17 AB8 VAL C 1031 GLY C 1035 5 5
HELIX 18 AB9 ASP C 1074 ASP C 1078 1 5
HELIX 19 AC1 ILE C 1107 ILE C 1111 5 5
HELIX 20 AC2 GLY C 1155 SER C 1163 1 9
HELIX 21 AC3 SER C 1178 LEU C 1184 1 7
HELIX 22 AC4 ASN D 967 LEU D 971 5 5
HELIX 23 AC5 CYS D 985 SER D 991 1 7
HELIX 24 AC6 VAL D 1031 GLY D 1035 5 5
HELIX 25 AC7 ASP D 1074 ASP D 1078 1 5
HELIX 26 AC8 ILE D 1107 ILE D 1111 5 5
HELIX 27 AC9 GLY D 1155 SER D 1163 1 9
HELIX 28 AD1 SER D 1178 GLN D 1186 1 9
SHEET 1 AA1 4 LYS A 920 CYS A 923 0
SHEET 2 AA1 4 CYS A 937 ASN A 939 -1 O CYS A 937 N CYS A 923
SHEET 3 AA1 4 LEU A1040 ARG A1044 1 O LEU A1042 N VAL A 938
SHEET 4 AA1 4 TRP A1050 ALA A1054 -1 O GLY A1051 N TYR A1043
SHEET 1 AA2 4 LYS A 951 TYR A 952 0
SHEET 2 AA2 4 TYR A1097 GLY A1105 1 O TYR A1103 N LYS A 951
SHEET 3 AA2 4 GLY A1069 SER A1073 -1 N GLU A1070 O ASP A1100
SHEET 4 AA2 4 CYS A 957 GLU A 958 1 N CYS A 957 O LEU A1071
SHEET 1 AA3 3 LYS A 951 TYR A 952 0
SHEET 2 AA3 3 TYR A1097 GLY A1105 1 O TYR A1103 N LYS A 951
SHEET 3 AA3 3 LEU A1086 LEU A1089 -1 N PHE A1087 O ILE A1099
SHEET 1 AA4 4 ILE A1014 PHE A1015 0
SHEET 2 AA4 4 ILE A1119 PHE A1125 1 O ARG A1123 N ILE A1014
SHEET 3 AA4 4 ARG A1135 SER A1140 -1 O ALA A1137 N VAL A1122
SHEET 4 AA4 4 PHE A1063 TYR A1067 -1 N TYR A1067 O ILE A1136
SHEET 1 AA5 2 ASN A1112 HIS A1113 0
SHEET 2 AA5 2 GLY A1151 PHE A1152 1 O PHE A1152 N ASN A1112
SHEET 1 AA6 4 LYS B 920 CYS B 923 0
SHEET 2 AA6 4 CYS B 937 ASN B 939 -1 O CYS B 937 N CYS B 923
SHEET 3 AA6 4 LEU B1040 ARG B1044 1 O LEU B1042 N VAL B 938
SHEET 4 AA6 4 TRP B1050 ALA B1054 -1 O GLY B1051 N TYR B1043
SHEET 1 AA7 4 LYS B 951 TYR B 952 0
SHEET 2 AA7 4 TYR B1097 GLY B1105 1 O TYR B1103 N LYS B 951
SHEET 3 AA7 4 GLY B1069 SER B1073 -1 N ILE B1072 O CYS B1098
SHEET 4 AA7 4 CYS B 957 GLU B 958 1 N CYS B 957 O LEU B1071
SHEET 1 AA8 3 LYS B 951 TYR B 952 0
SHEET 2 AA8 3 TYR B1097 GLY B1105 1 O TYR B1103 N LYS B 951
SHEET 3 AA8 3 LEU B1086 LEU B1089 -1 N PHE B1087 O ILE B1099
SHEET 1 AA9 4 ILE B1014 PHE B1015 0
SHEET 2 AA9 4 ILE B1119 PHE B1125 1 O PHE B1125 N ILE B1014
SHEET 3 AA9 4 ARG B1135 SER B1140 -1 O ALA B1137 N VAL B1122
SHEET 4 AA9 4 PHE B1063 TYR B1067 -1 N CYS B1065 O PHE B1138
SHEET 1 AB1 2 ASN B1112 HIS B1113 0
SHEET 2 AB1 2 GLY B1151 PHE B1152 1 O PHE B1152 N ASN B1112
SHEET 1 AB2 4 LYS C 920 CYS C 923 0
SHEET 2 AB2 4 CYS C 937 ASN C 939 -1 O CYS C 937 N CYS C 923
SHEET 3 AB2 4 LEU C1040 ARG C1044 1 O LEU C1042 N VAL C 938
SHEET 4 AB2 4 TRP C1050 ALA C1054 -1 O GLY C1051 N TYR C1043
SHEET 1 AB3 4 LYS C 951 TYR C 952 0
SHEET 2 AB3 4 TYR C1097 GLY C1105 1 O TYR C1103 N LYS C 951
SHEET 3 AB3 4 GLY C1069 SER C1073 -1 N GLU C1070 O ASP C1100
SHEET 4 AB3 4 CYS C 957 GLU C 958 1 N CYS C 957 O LEU C1071
SHEET 1 AB4 3 LYS C 951 TYR C 952 0
SHEET 2 AB4 3 TYR C1097 GLY C1105 1 O TYR C1103 N LYS C 951
SHEET 3 AB4 3 LEU C1086 LEU C1089 -1 N PHE C1087 O ILE C1099
SHEET 1 AB5 4 ILE C1014 PHE C1015 0
SHEET 2 AB5 4 ILE C1119 PHE C1125 1 O ARG C1123 N ILE C1014
SHEET 3 AB5 4 ARG C1135 SER C1140 -1 O ALA C1137 N VAL C1122
SHEET 4 AB5 4 PHE C1063 TYR C1067 -1 N ILE C1064 O PHE C1138
SHEET 1 AB6 2 ASN C1112 HIS C1113 0
SHEET 2 AB6 2 GLY C1151 PHE C1152 1 O PHE C1152 N ASN C1112
SHEET 1 AB7 4 LYS D 920 CYS D 923 0
SHEET 2 AB7 4 CYS D 937 ASN D 939 -1 O CYS D 937 N CYS D 923
SHEET 3 AB7 4 LEU D1040 ARG D1044 1 O LEU D1042 N VAL D 938
SHEET 4 AB7 4 TRP D1050 ALA D1054 -1 O GLY D1051 N TYR D1043
SHEET 1 AB8 4 LYS D 951 TYR D 952 0
SHEET 2 AB8 4 TYR D1097 GLY D1105 1 O TYR D1103 N LYS D 951
SHEET 3 AB8 4 GLY D1069 SER D1073 -1 N GLU D1070 O ASP D1100
SHEET 4 AB8 4 CYS D 957 GLU D 958 1 N CYS D 957 O LEU D1071
SHEET 1 AB9 3 LYS D 951 TYR D 952 0
SHEET 2 AB9 3 TYR D1097 GLY D1105 1 O TYR D1103 N LYS D 951
SHEET 3 AB9 3 LEU D1086 LEU D1089 -1 N PHE D1087 O ILE D1099
SHEET 1 AC1 4 ILE D1014 PHE D1015 0
SHEET 2 AC1 4 ILE D1119 PHE D1125 1 O PHE D1125 N ILE D1014
SHEET 3 AC1 4 ARG D1135 SER D1140 -1 O PHE D1139 N ILE D1120
SHEET 4 AC1 4 PHE D1063 TYR D1067 -1 N CYS D1065 O PHE D1138
SHEET 1 AC2 2 ASN D1112 HIS D1113 0
SHEET 2 AC2 2 GLY D1151 PHE D1152 1 O PHE D1152 N ASN D1112
LINK SG CYS A 974 ZN ZN A1501 1555 1555 2.55
LINK SG CYS A 974 ZN ZN A1503 1555 1555 2.43
LINK SG CYS A 976 ZN ZN A1503 1555 1555 2.54
LINK SG CYS A 980 ZN ZN A1502 1555 1555 2.48
LINK SG CYS A 980 ZN ZN A1503 1555 1555 2.19
LINK SG CYS A 985 ZN ZN A1503 1555 1555 2.22
LINK SG CYS A 987 ZN ZN A1501 1555 1555 2.21
LINK SG CYS A1017 ZN ZN A1501 1555 1555 2.48
LINK SG CYS A1017 ZN ZN A1502 1555 1555 2.34
LINK SG CYS A1021 ZN ZN A1501 1555 1555 2.30
LINK SG CYS A1023 ZN ZN A1502 1555 1555 2.24
LINK SG CYS A1027 ZN ZN A1502 1555 1555 2.23
LINK SG CYS A1115 ZN ZN A1504 1555 1555 2.34
LINK SG CYS A1168 ZN ZN A1504 1555 1555 2.15
LINK SG CYS A1170 ZN ZN A1504 1555 1555 2.41
LINK SG CYS A1175 ZN ZN A1504 1555 1555 2.24
LINK SG CYS B 974 ZN ZN B1501 1555 1555 2.46
LINK SG CYS B 974 ZN ZN B1503 1555 1555 2.36
LINK SG CYS B 976 ZN ZN B1503 1555 1555 2.44
LINK SG CYS B 980 ZN ZN B1502 1555 1555 2.40
LINK SG CYS B 980 ZN ZN B1503 1555 1555 2.33
LINK SG CYS B 985 ZN ZN B1503 1555 1555 2.34
LINK SG CYS B 987 ZN ZN B1501 1555 1555 2.37
LINK SG CYS B1017 ZN ZN B1501 1555 1555 2.42
LINK SG CYS B1017 ZN ZN B1502 1555 1555 2.39
LINK SG CYS B1021 ZN ZN B1501 1555 1555 2.20
LINK SG CYS B1023 ZN ZN B1502 1555 1555 2.28
LINK SG CYS B1027 ZN ZN B1502 1555 1555 2.34
LINK SG CYS B1115 ZN ZN B1504 1555 1555 2.39
LINK SG CYS B1168 ZN ZN B1504 1555 1555 2.26
LINK SG CYS B1170 ZN ZN B1504 1555 1555 2.37
LINK SG CYS B1175 ZN ZN B1504 1555 1555 2.28
LINK SG CYS C 974 ZN ZN C1501 1555 1555 2.57
LINK SG CYS C 974 ZN ZN C1503 1555 1555 2.41
LINK SG CYS C 976 ZN ZN C1503 1555 1555 2.41
LINK SG CYS C 980 ZN ZN C1502 1555 1555 2.31
LINK SG CYS C 980 ZN ZN C1503 1555 1555 2.27
LINK SG CYS C 985 ZN ZN C1503 1555 1555 2.25
LINK SG CYS C 987 ZN ZN C1501 1555 1555 2.27
LINK SG CYS C1017 ZN ZN C1501 1555 1555 2.41
LINK SG CYS C1017 ZN ZN C1502 1555 1555 2.43
LINK SG CYS C1021 ZN ZN C1501 1555 1555 2.25
LINK SG CYS C1023 ZN ZN C1502 1555 1555 2.24
LINK SG CYS C1027 ZN ZN C1502 1555 1555 2.23
LINK SG CYS C1115 ZN ZN C1504 1555 1555 2.47
LINK SG CYS C1168 ZN ZN C1504 1555 1555 2.29
LINK SG CYS C1170 ZN ZN C1504 1555 1555 2.33
LINK SG CYS C1175 ZN ZN C1504 1555 1555 2.34
LINK SG CYS D 974 ZN ZN D1501 1555 1555 2.50
LINK SG CYS D 974 ZN ZN D1503 1555 1555 2.35
LINK SG CYS D 976 ZN ZN D1503 1555 1555 2.40
LINK SG CYS D 980 ZN ZN D1502 1555 1555 2.19
LINK SG CYS D 980 ZN ZN D1503 1555 1555 2.54
LINK SG CYS D 985 ZN ZN D1503 1555 1555 2.28
LINK SG CYS D 987 ZN ZN D1501 1555 1555 2.30
LINK SG CYS D1017 ZN ZN D1501 1555 1555 2.41
LINK SG CYS D1017 ZN ZN D1502 1555 1555 2.43
LINK SG CYS D1021 ZN ZN D1501 1555 1555 2.28
LINK SG CYS D1023 ZN ZN D1502 1555 1555 2.16
LINK SG CYS D1027 ZN ZN D1502 1555 1555 2.34
LINK SG CYS D1115 ZN ZN D1504 1555 1555 2.38
LINK SG CYS D1168 ZN ZN D1504 1555 1555 2.21
LINK SG CYS D1170 ZN ZN D1504 1555 1555 2.46
LINK SG CYS D1175 ZN ZN D1504 1555 1555 2.26
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 18 MET A1048 TRP A1050 SER A1084 TYR A1085
SITE 2 AC5 18 ARG A1109 PHE A1110 ASN A1112 HIS A1113
SITE 3 AC5 18 TYR A1154 PHE A1158 PHE A1166 THR A1167
SITE 4 AC5 18 CYS A1168 GLN A1169 HOH A1610 HOH A1663
SITE 5 AC5 18 HOH A1696 HOH A1706
SITE 1 AC6 12 ASP A1074 ALA A1077 ASP A1078 ARG A1080
SITE 2 AC6 12 ASP A1083 LEU A1086 ASP A1088 CYS A1098
SITE 3 AC6 12 ARG A1157 PHE A1158 LYS A1162 GOL A1509
SITE 1 AC7 12 GLU A 931 VAL A1032 GLY A1035 ILE A1036
SITE 2 AC7 12 PHE A1063 CYS A1065 GLU A1066 ASN A1106
SITE 3 AC7 12 HOH A1601 HOH A1613 HOH A1623 HOH A1674
SITE 1 AC8 4 ILE A 921 PRO A 936 VAL A 938 GLN A1041
SITE 1 AC9 10 LEU A1086 PHE A1087 ASP A1088 PHE A1152
SITE 2 AC9 10 ASP A1153 TYR A1154 90P A1506 HOH A1603
SITE 3 AC9 10 HOH A1632 HOH A1723
SITE 1 AD1 4 CYS B 974 CYS B 987 CYS B1017 CYS B1021
SITE 1 AD2 4 CYS B 980 CYS B1017 CYS B1023 CYS B1027
SITE 1 AD3 4 CYS B 974 CYS B 976 CYS B 980 CYS B 985
SITE 1 AD4 4 CYS B1115 CYS B1168 CYS B1170 CYS B1175
SITE 1 AD5 19 MET B1048 TRP B1050 SER B1084 TYR B1085
SITE 2 AD5 19 ARG B1109 PHE B1110 ILE B1111 ASN B1112
SITE 3 AD5 19 HIS B1113 TYR B1154 PHE B1158 PHE B1166
SITE 4 AD5 19 THR B1167 CYS B1168 GLN B1169 HOH B1608
SITE 5 AD5 19 HOH B1649 HOH B1735 HOH B1756
SITE 1 AD6 11 ASP B1074 ALA B1077 ASP B1078 ARG B1080
SITE 2 AD6 11 ASP B1083 LEU B1086 ASP B1088 CYS B1098
SITE 3 AD6 11 ARG B1157 PHE B1158 HOH B1715
SITE 1 AD7 9 VAL B1032 GLY B1035 ILE B1036 PHE B1063
SITE 2 AD7 9 GLU B1066 ASN B1106 HOH B1604 HOH B1638
SITE 3 AD7 9 HOH B1648
SITE 1 AD8 8 ASP B 942 ARG B1044 THR B1045 ALA B1046
SITE 2 AD8 8 LYS B1047 MET B1048 GLY B1049 HOH B1657
SITE 1 AD9 7 ASN B 956 LEU B1071 HIS B1128 PHE B1133
SITE 2 AD9 7 PRO B1134 ARG B1135 HOH B1623
SITE 1 AE1 4 CYS C 974 CYS C 987 CYS C1017 CYS C1021
SITE 1 AE2 4 CYS C 980 CYS C1017 CYS C1023 CYS C1027
SITE 1 AE3 4 CYS C 974 CYS C 976 CYS C 980 CYS C 985
SITE 1 AE4 4 CYS C1115 CYS C1168 CYS C1170 CYS C1175
SITE 1 AE5 19 MET C1048 TRP C1050 SER C1084 TYR C1085
SITE 2 AE5 19 ARG C1109 PHE C1110 ILE C1111 ASN C1112
SITE 3 AE5 19 HIS C1113 TYR C1154 PHE C1158 PHE C1166
SITE 4 AE5 19 CYS C1168 GLN C1169 HOH C1613 HOH C1618
SITE 5 AE5 19 HOH C1627 HOH C1670 HOH C1740
SITE 1 AE6 10 ASP C1074 ALA C1077 ASP C1078 ARG C1080
SITE 2 AE6 10 ASP C1083 LEU C1086 ASP C1088 CYS C1098
SITE 3 AE6 10 ARG C1157 PHE C1158
SITE 1 AE7 11 VAL C1032 GLY C1035 ILE C1036 PHE C1063
SITE 2 AE7 11 CYS C1065 GLU C1066 ASN C1106 ARG C1135
SITE 3 AE7 11 HOH C1642 HOH C1649 HOH C1658
SITE 1 AE8 4 CYS D 974 CYS D 987 CYS D1017 CYS D1021
SITE 1 AE9 4 CYS D 980 CYS D1017 CYS D1023 CYS D1027
SITE 1 AF1 4 CYS D 974 CYS D 976 CYS D 980 CYS D 985
SITE 1 AF2 4 CYS D1115 CYS D1168 CYS D1170 CYS D1175
SITE 1 AF3 19 MET D1048 TRP D1050 SER D1084 TYR D1085
SITE 2 AF3 19 ARG D1109 PHE D1110 ASN D1112 HIS D1113
SITE 3 AF3 19 TYR D1154 PHE D1158 PHE D1166 CYS D1168
SITE 4 AF3 19 GLN D1169 HOH D1617 HOH D1618 HOH D1692
SITE 5 AF3 19 HOH D1696 HOH D1704 HOH D1734
SITE 1 AF4 11 ASP D1074 ALA D1077 ASP D1078 ARG D1080
SITE 2 AF4 11 ASP D1083 LEU D1086 ASP D1088 CYS D1098
SITE 3 AF4 11 ARG D1157 PHE D1158 LYS D1162
SITE 1 AF5 7 TRP C1024 ASP D 925 GLY D 929 GLU D 931
SITE 2 AF5 7 ASN D 932 VAL D 933 PRO D 934
SITE 1 AF6 6 ASP D 942 THR D1045 ALA D1046 MET D1048
SITE 2 AF6 6 GLY D1049 HOH D1711
CRYST1 56.607 77.509 134.794 90.00 91.41 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 0.017666 0.000000 0.000435 0.00000
SCALE2 0.000000 0.012902 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007421 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
