Header list of 2gat.pdb file
Complete list - 9 20 Bytes
HEADER TRANSCRIPTION/DNA 07-NOV-97 2GAT
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF CHICKEN GATA-1 BOUND TO
TITLE 2 DNA, NMR, REGULARIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*GP*TP*TP*GP*CP*AP*GP*AP*TP*AP*AP*AP*CP*AP*TP*T)-
COMPND 3 3');
COMPND 4 CHAIN: B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(*AP*AP*TP*GP*TP*TP*TP*AP*TP*CP*TP*GP*CP*AP*AP*C)-
COMPND 8 3');
COMPND 9 CHAIN: C;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: ERYTHROID TRANSCRIPTION FACTOR GATA-1;
COMPND 13 CHAIN: A;
COMPND 14 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 15 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: GALLUS GALLUS;
SOURCE 7 ORGANISM_COMMON: CHICKEN;
SOURCE 8 ORGANISM_TAXID: 9031;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA BINDING PROTEIN, TRANSCRIPTION FACTOR, ZINC BINDING DOMAIN,
KEYWDS 2 COMPLEX (TRANSCRIPTION REGULATION-DNA), TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,N.TJANDRA,M.STARICH,J.G.OMICHINSKI,A.M.GRONENBORN
REVDAT 3 09-MAR-22 2GAT 1 REMARK LINK
REVDAT 2 24-FEB-09 2GAT 1 VERSN
REVDAT 1 28-JAN-98 2GAT 0
JRNL AUTH N.TJANDRA,J.G.OMICHINSKI,A.M.GRONENBORN,G.M.CLORE,A.BAX
JRNL TITL USE OF DIPOLAR 1H-15N AND 1H-13C COUPLINGS IN THE STRUCTURE
JRNL TITL 2 DETERMINATION OF MAGNETICALLY ORIENTED MACROMOLECULES IN
JRNL TITL 3 SOLUTION.
JRNL REF NAT.STRUCT.BIOL. V. 4 732 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9303001
JRNL DOI 10.1038/NSB0997-732
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.R.STARICH,M.WIKSTROM,S.SHUMACHER,H.N.ARST,A.M.GRONENBORN,
REMARK 1 AUTH 2 G.M.CLORE
REMARK 1 TITL THE SOLUTION STRUCTURE OF THE LEU22-->VAL MUTANT AREA DNA
REMARK 1 TITL 2 BINDING DOMAIN COMPLEXED WITH A TGATAG CORE ELEMENT DEFINES
REMARK 1 TITL 3 A ROLE FOR HYDROPHOBIC PACKING IN THE DETERMINATION OF
REMARK 1 TITL 4 SPECIFICITY
REMARK 1 REF J.MOL.BIOL. V. 277 621 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.G.OMICHINSKI,G.M.CLORE,O.SCHAAD,G.FELSENFELD,C.TRAINOR,
REMARK 1 AUTH 2 E.APPELLA,S.J.STAHL,A.M.GRONENBORN
REMARK 1 TITL NMR STRUCTURE OF A SPECIFIC DNA COMPLEX OF ZN-CONTAINING DNA
REMARK 1 TITL 2 BINDING DOMAIN OF GATA-1
REMARK 1 REF SCIENCE V. 261 438 1993
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT.
REMARK 3 229, 129 - 136 AND PROTEIN ENGINEERING 2, 27 - 38 USING
REMARK 3 THE PROGRAM X-PLOR MODIFIED TO INCORPORATE DIPOLAR
REMARK 3 COUPLING RESTRAINTS (TJANDRA ET AL. (1997) NATURE STRUCT
REMARK 3 BIOL 4, 732-738) AND A CONFORMATIONAL DATABASE POTENTIAL
REMARK 3 FOR PROTEINS AND NUCLEIC ACIDS (KUSZEWSKI ET AL. (1996)
REMARK 3 PROTEIN SCI 5, 1067 - 1080 AND (1997) J. MAGN. RESON. 125,
REMARK 3 171-177). THE EXPERIMENTAL RESTRAINTS ARE GIVEN IN
REMARK 3 R2GATMR.
REMARK 3
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1830 EXPERIMENTAL
REMARK 3 NMR RESTRAINTS COMPRISING: 1444 INTERPROTON DISTANCE
REMARK 3 RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 296 TORSION
REMARK 3 ANGLE RESTRAINTS; 90 RESIDUAL DIPOLAR COUPLINGS (52 N-H
REMARK 3 AND 38 C-H). THE NOE RESTRAINTS ARE SUBDIVIDED AS FOLLOWS:
REMARK 3 (A) WITHIN THE PROTEIN: 242 INTERRESIDUE SEQUENTIAL
REMARK 3 (|I-J|=1); 161 INTERRESIDUE SHORT RANGE (1(LESS
REMARK 3 THAN)|I-J|(LESS THAN)=5); 182 INTERRESIDUE LONG RANGE
REMARK 3 (|I-J|(GREATER THAN)5); AND. 334 INTRARESIDUE. (B) WITHIN
REMARK 3 THE DNA: 157 INTRARESIDUE; 180 SEQUENTIAL INTRASTRAND; 34
REMARK 3 INTERSTRAND; AND 37. H-BONDS (C) BETWEEN PROTEIN AND DNA:
REMARK 3 117. THE TORSION ANGLE RESTRAINTS ARE SUBDIVIDED AS
REMARK 3 FOLLOWS: 144 ANGLES FOR THE PROTEIN (58 PHI, 56 PSI, 26
REMARK 3 CHI1 AND 4 CHI2) AND. 152 FOR THE DNA. THE TORSION ANGLE
REMARK 3 RESTRAINTS FOR THE DNA COMPRISE LOOSE RESTRAINTS ON THE
REMARK 3 BACKBONE TORSION ANGLES ALPHA, BETA, GAMMA, EPSILON AND
REMARK 3 ZETA TO PREVENT PROBLEMS ASSOCIATED WITH LOCAL MIRROR
REMARK 3 IMAGES.
REMARK 3
REMARK 3 THE STRUCTURE IN THIS ENTRY IS THE RESTRAINED REGULARIZED
REMARK 3 MEAN STRUCTURE AND THE LAST NUMERIC COLUMN REPRESENTS THE
REMARK 3 RMS OF THE 34 INDIVIDUAL SIMULATED ANNEALING STRUCTURES
REMARK 3 FOUND IN PDB ENTRY 3GAT ABOUT THE MEAN COORDINATE
REMARK 3 POSITIONS. THE LAST NUMERIC COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES HAS NO MEANING.
REMARK 3
REMARK 3 THE FOLLOWING TWO SETS OF COORDINATES DEFINE THE PRINCIPAL
REMARK 3 AXIS OF THE MAGNETIC SUSCEPTIBILITY TENSOR:
REMARK 3 POINT 1 50.250 -27.763 2.413
REMARK 3 POINT 2 50.328 -26.611 3.418
REMARK 4
REMARK 4 2GAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178121.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 360 MHZ; 750
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AM360; DMX500; AMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR MODIFIED MODIFIED
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 34
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: DATA WERE RECORDED ON A 1:1 COMPLEX OF 1 MOLECULE OF DNA.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TYR A 35 H GLN A 39 1.44
REMARK 500 O6 DG B 107 H41 DC C 126 1.56
REMARK 500 O VAL A 58 H SER A 60 1.58
REMARK 500 H SER A 8 O PRO A 26 1.58
REMARK 500 O CYS A 7 H GLN A 11 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 DT B 103 C5 DT B 103 C7 0.036
REMARK 500 DT B 109 C5 DT B 109 C7 0.036
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DG B 101 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT B 102 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT B 103 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG B 104 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC B 105 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DA B 106 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DA B 106 N1 - C2 - N3 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DG B 107 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DA B 108 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA B 108 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DT B 109 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DA B 110 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA B 110 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DA B 111 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA B 111 N1 - C2 - N3 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DA B 112 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DA B 112 N1 - C2 - N3 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DA B 114 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA B 114 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DT B 115 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DT B 116 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DA C 117 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DA C 117 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DA C 118 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DA C 118 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DT C 119 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DG C 120 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT C 121 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DT C 121 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 DT C 122 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT C 123 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DA C 124 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA C 124 N1 - C2 - N3 ANGL. DEV. = -3.0 DEGREES
REMARK 500 DT C 125 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DC C 126 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT C 127 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG C 128 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC C 129 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA C 130 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA C 130 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DA C 131 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DA C 131 N1 - C2 - N3 ANGL. DEV. = -3.1 DEGREES
REMARK 500 DC C 132 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 11 2.36 59.97
REMARK 500 ASP A 49 -75.90 -58.94
REMARK 500 LYS A 57 178.89 -53.99
REMARK 500 SER A 59 35.51 -66.54
REMARK 500 LYS A 63 -75.13 1.59
REMARK 500 LYS A 64 -139.84 -142.06
REMARK 500 ARG A 65 -122.42 69.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 47 0.10 SIDE CHAIN
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 67 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 7 SG
REMARK 620 2 CYS A 10 SG 106.0
REMARK 620 3 CYS A 28 SG 111.8 112.5
REMARK 620 4 CYS A 31 SG 110.0 109.2 107.4
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 67
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GAT RELATED DB: PDB
REMARK 900 ENSEMBLE OF 34 STRUCTURES
DBREF 2GAT A 1 66 UNP P17678 GATA1_CHICK 158 223
DBREF 2GAT B 101 116 PDB 2GAT 2GAT 101 116
DBREF 2GAT C 117 132 PDB 2GAT 2GAT 117 132
SEQRES 1 B 16 DG DT DT DG DC DA DG DA DT DA DA DA DC
SEQRES 2 B 16 DA DT DT
SEQRES 1 C 16 DA DA DT DG DT DT DT DA DT DC DT DG DC
SEQRES 2 C 16 DA DA DC
SEQRES 1 A 66 LYS ARG ALA GLY THR VAL CYS SER ASN CYS GLN THR SER
SEQRES 2 A 66 THR THR THR LEU TRP ARG ARG SER PRO MET GLY ASP PRO
SEQRES 3 A 66 VAL CYS ASN ALA CYS GLY LEU TYR TYR LYS LEU HIS GLN
SEQRES 4 A 66 VAL ASN ARG PRO LEU THR MET ARG LYS ASP GLY ILE GLN
SEQRES 5 A 66 THR ARG ASN ARG LYS VAL SER SER LYS GLY LYS LYS ARG
SEQRES 6 A 66 ARG
HET ZN A 67 1
HETNAM ZN ZINC ION
FORMUL 4 ZN ZN 2+
HELIX 1 1 ASN A 29 HIS A 38 1 10
HELIX 2 2 LEU A 44 MET A 46 5 3
SHEET 1 A 2 TRP A 18 ARG A 20 0
SHEET 2 A 2 PRO A 26 CYS A 28 -1 N VAL A 27 O ARG A 19
LINK SG CYS A 7 ZN ZN A 67 1555 1555 2.27
LINK SG CYS A 10 ZN ZN A 67 1555 1555 2.27
LINK SG CYS A 28 ZN ZN A 67 1555 1555 2.33
LINK SG CYS A 31 ZN ZN A 67 1555 1555 2.28
SITE 1 AC1 4 CYS A 7 CYS A 10 CYS A 28 CYS A 31
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 9 20 Bytes