HEADER TRANSCRIPTION/DNA 10-DEC-97 1A1F
TITLE DSNR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GACC SITE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*AP*GP*CP*GP*TP*GP*GP*GP*AP*CP*C)-3');
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*TP*GP*GP*TP*CP*CP*CP*AP*CP*GP*C)-3');
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: THREE-FINGER ZIF268 PEPTIDE;
COMPND 11 CHAIN: A;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PDSNR
KEYWDS COMPLEX (ZINC FINGER-DNA), ZINC FINGER, DNA-BINDING PROTEIN,
KEYWDS 2 TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ELROD-ERICKSON,T.E.BENSON,C.O.PABO
REVDAT 5 02-AUG-23 1A1F 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1A1F 1 VERSN
REVDAT 3 28-JUN-02 1A1F 1 REMARK
REVDAT 2 27-NOV-00 1A1F 5
REVDAT 1 10-JUN-98 1A1F 0
JRNL AUTH M.ELROD-ERICKSON,T.E.BENSON,C.O.PABO
JRNL TITL HIGH-RESOLUTION STRUCTURES OF VARIANT ZIF268-DNA COMPLEXES:
JRNL TITL 2 IMPLICATIONS FOR UNDERSTANDING ZINC FINGER-DNA RECOGNITION.
JRNL REF STRUCTURE V. 6 451 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9562555
JRNL DOI 10.1016/S0969-2126(98)00047-1
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.ELROD-ERICKSON,M.A.ROULD,L.NEKLUDOVA,C.O.PABO
REMARK 1 TITL ZIF268 PROTEIN-DNA COMPLEX REFINED AT 1.6 A: A MODEL SYSTEM
REMARK 1 TITL 2 FOR UNDERSTANDING ZINC FINGER-DNA INTERACTIONS
REMARK 1 REF STRUCTURE V. 4 1171 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.J.REBAR,C.O.PABO
REMARK 1 TITL ZINC FINGER PHAGE: AFFINITY SELECTION OF FINGERS WITH NEW
REMARK 1 TITL 2 DNA-BINDING SPECIFICITIES
REMARK 1 REF SCIENCE V. 263 671 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH N.P.PAVLETICH,C.O.PABO
REMARK 1 TITL ZINC FINGER-DNA RECOGNITION: CRYSTAL STRUCTURE OF A
REMARK 1 TITL 2 ZIF268-DNA COMPLEX AT 2.1 A
REMARK 1 REF SCIENCE V. 252 809 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 8173
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : BASED ON 1AAY TEST SET
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.900
REMARK 3 FREE R VALUE TEST SET COUNT : 893
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 807
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE : 0.4110
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 89
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.044
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 695
REMARK 3 NUCLEIC ACID ATOMS : 445
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 16.16200
REMARK 3 B22 (A**2) : 20.53400
REMARK 3 B33 (A**2) : 4.33200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.75
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.226
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED INDIVIDUAL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.207 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.251 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.888 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.564 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARNDBX.DNA
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPNDBX.DNA
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RMS DEVIATIONS FROM IDEAL VALUES (DNA)
REMARK 4
REMARK 4 1A1F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000170273.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NOV-95
REMARK 200 TEMPERATURE (KELVIN) : 130
REMARK 200 PH : 7.5
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : YALE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8185
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1AAY, WITHOUT WATERS AND WITHOUT SIDE
REMARK 200 CHAINS FOR RESIDUES 18 - 24
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 400, 200MM MGCL2, 100 MM HEPES
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.20000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.20000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 21.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.95000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.50000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.95000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.20000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.50000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 27.95000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.20000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.50000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 27.95000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 101
REMARK 465 GLU A 102
REMARK 465 ARG A 187
REMARK 465 GLN A 188
REMARK 465 LYS A 189
REMARK 465 ASP A 190
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 GLU A 110 122.00 -31.62
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 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 107 SG
REMARK 620 2 CYS A 112 SG 132.1
REMARK 620 3 HIS A 125 NE2 109.4 105.5
REMARK 620 4 HIS A 129 NE2 107.1 104.8 89.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 137 SG
REMARK 620 2 CYS A 140 SG 119.3
REMARK 620 3 HIS A 153 NE2 108.3 100.8
REMARK 620 4 HIS A 157 NE2 110.7 115.4 99.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 165 SG
REMARK 620 2 CYS A 168 SG 119.2
REMARK 620 3 HIS A 181 NE2 107.9 103.3
REMARK 620 4 HIS A 185 NE2 107.4 115.6 101.5
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 203
DBREF 1A1F A 102 190 UNP P08046 EGR1_MOUSE 308 396
DBREF 1A1F B 1 11 PDB 1A1F 1A1F 1 11
DBREF 1A1F C 51 61 PDB 1A1F 1A1F 51 61
SEQADV 1A1F ASP A 118 UNP P08046 ARG 324 VARIANT
SEQADV 1A1F SER A 120 UNP P08046 ASP 326 VARIANT
SEQADV 1A1F ASN A 121 UNP P08046 GLU 327 VARIANT
SEQRES 1 B 11 DA DG DC DG DT DG DG DG DA DC DC
SEQRES 1 C 11 DT DG DG DT DC DC DC DA DC DG DC
SEQRES 1 A 90 MET GLU ARG PRO TYR ALA CYS PRO VAL GLU SER CYS ASP
SEQRES 2 A 90 ARG ARG PHE SER ASP SER SER ASN LEU THR ARG HIS ILE
SEQRES 3 A 90 ARG ILE HIS THR GLY GLN LYS PRO PHE GLN CYS ARG ILE
SEQRES 4 A 90 CYS MET ARG ASN PHE SER ARG SER ASP HIS LEU THR THR
SEQRES 5 A 90 HIS ILE ARG THR HIS THR GLY GLU LYS PRO PHE ALA CYS
SEQRES 6 A 90 ASP ILE CYS GLY ARG LYS PHE ALA ARG SER ASP GLU ARG
SEQRES 7 A 90 LYS ARG HIS THR LYS ILE HIS LEU ARG GLN LYS ASP
HET ZN A 201 1
HET ZN A 202 1
HET ZN A 203 1
HETNAM ZN ZINC ION
FORMUL 4 ZN 3(ZN 2+)
FORMUL 7 HOH *88(H2 O)
HELIX 1 1 SER A 119 THR A 130 1 12
HELIX 2 2 SER A 147 THR A 158 1 12
HELIX 3 3 SER A 175 HIS A 185 1 11
SHEET 1 A 2 TYR A 105 ALA A 106 0
SHEET 2 A 2 ARG A 115 PHE A 116 -1 N PHE A 116 O TYR A 105
SHEET 1 B 2 PHE A 135 GLN A 136 0
SHEET 2 B 2 ASN A 143 PHE A 144 -1 N PHE A 144 O PHE A 135
SHEET 1 C 2 PHE A 163 ALA A 164 0
SHEET 2 C 2 LYS A 171 PHE A 172 -1 N PHE A 172 O PHE A 163
LINK SG CYS A 107 ZN ZN A 201 1555 1555 2.10
LINK SG CYS A 112 ZN ZN A 201 1555 1555 2.70
LINK NE2 HIS A 125 ZN ZN A 201 1555 1555 2.24
LINK NE2 HIS A 129 ZN ZN A 201 1555 1555 2.18
LINK SG CYS A 137 ZN ZN A 202 1555 1555 2.34
LINK SG CYS A 140 ZN ZN A 202 1555 1555 2.26
LINK NE2 HIS A 153 ZN ZN A 202 1555 1555 2.08
LINK NE2 HIS A 157 ZN ZN A 202 1555 1555 2.08
LINK SG CYS A 165 ZN ZN A 203 1555 1555 2.25
LINK SG CYS A 168 ZN ZN A 203 1555 1555 2.23
LINK NE2 HIS A 181 ZN ZN A 203 1555 1555 2.12
LINK NE2 HIS A 185 ZN ZN A 203 1555 1555 2.05
SITE 1 AC1 4 CYS A 107 CYS A 112 HIS A 125 HIS A 129
SITE 1 AC2 4 CYS A 137 CYS A 140 HIS A 153 HIS A 157
SITE 1 AC3 4 CYS A 165 CYS A 168 HIS A 181 HIS A 185
CRYST1 43.000 55.900 128.400 90.00 90.00 90.00 C 2 2 21 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 0.023256 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017889 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007788 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
