Header list of 3znf.pdb file
Complete list - 16 202 Bytes
HEADER ZINC FINGER DNA BINDING DOMAIN 09-JUL-90 3ZNF
TITLE HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF A SINGLE ZINC FINGER
TITLE 2 FROM A HUMAN ENHANCER BINDING PROTEIN IN SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ZINC FINGER DNA BINDING DOMAIN
EXPDTA SOLUTION NMR
AUTHOR A.M.GRONENBORN,G.M.CLORE,J.G.OMICHINSKI
REVDAT 3 16-MAR-22 3ZNF 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 3ZNF 1 VERSN
REVDAT 1 15-JAN-92 3ZNF 0
JRNL AUTH J.G.OMICHINSKI,G.M.CLORE,E.APPELLA,K.SAKAGUCHI,
JRNL AUTH 2 A.M.GRONENBORN
JRNL TITL HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF A SINGLE ZINC
JRNL TITL 2 FINGER FROM A HUMAN ENHANCER BINDING PROTEIN IN SOLUTION.
JRNL REF BIOCHEMISTRY V. 29 9324 1990
JRNL REFN ISSN 0006-2960
JRNL PMID 2248949
JRNL DOI 10.1021/BI00492A004
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 3D STRUCTURE OF THE ZINC FINGER IN SOLUTION
REMARK 3 BY NMR IS BASED ON 487 APPROXIMATE INTERPROTON DISTANCE
REMARK 3 RESTRAINTS AND 63 TORSION ANGLE RESTRAINTS DERIVED FROM
REMARK 3 NOE AND COUPLING CONSTANT MEASUREMENTS. THE STRUCTURES
REMARK 3 ARE CALCULATED USING THE HYBRID METRIC MATRIX DISTANCE
REMARK 3 GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD DESCRIBED
REMARK 3 BY M. NILGES, G. M. CLORE, AND A. M. GRONENBORN (1988)
REMARK 3 FEBS LETT 229, 317.
REMARK 3
REMARK 3 THIS ENTRY REPRESENTS THE RESTRAINED MINIMIZED AVERAGE
REMARK 3 STRUCTURE (SA)$R DERIVED BY RESTRAINED LEAST SQUARE
REMARK 3 REFINEMENT OF THE MEAN STRUCTURE OBTAINED BY AVERAGING THE
REMARK 3 COORDINATES OF THE FINAL 41 SA STRUCTURES BEST FITTED TO
REMARK 3 EACH OTHER. THE ENTIRE SET OF 41 MODELS CAN BE FOUND IN
REMARK 3 PDB ENTRY 4ZNF.
REMARK 3
REMARK 3 THE FIELD IN THIS ENTRY THAT OCCUPIES COLUMNS 61 - 66
REMARK 3 (RESERVED FOR B-VALUES IN X-RAY CRYSTALLOGRAPHIC ENTRIES)
REMARK 3 GIVES THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SA
REMARK 3 STRUCTURES AND THE MEAN STRUCTURE.
REMARK 4
REMARK 4 3ZNF 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_1000179200.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: 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 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 HIS A 4 CG HIS A 4 ND1 -0.116
REMARK 500 HIS A 27 CG HIS A 27 ND1 -0.097
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 PRO A 2 7.99 -63.19
REMARK 500 CYS A 5 162.84 -45.11
REMARK 500 TYR A 7 -76.00 -160.62
REMARK 500 CYS A 8 -160.70 -59.19
REMARK 500 PHE A 10 98.43 -67.63
REMARK 500 SER A 24 175.05 -50.15
REMARK 500 LYS A 25 29.47 -76.94
REMARK 500 ALA A 26 -92.79 -46.94
REMARK 500 HIS A 27 75.19 -176.11
REMARK 500 SER A 28 47.11 -165.44
REMARK 500 LYS A 29 39.34 -84.90
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 1 0.30 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 31 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 8 SG 111.8
REMARK 620 3 HIS A 21 NE2 110.8 110.5
REMARK 620 4 HIS A 27 NE2 111.3 98.4 113.5
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 31
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZNF RELATED DB: PDB
DBREF 3ZNF A 1 30 UNP P15822 ZEP1_HUMAN 2113 2142
SEQADV 3ZNF SER A 6 UNP P15822 THR 2118 CONFLICT
SEQRES 1 A 30 ARG PRO TYR HIS CYS SER TYR CYS ASN PHE SER PHE LYS
SEQRES 2 A 30 THR LYS GLY ASN LEU THR LYS HIS MET LYS SER LYS ALA
SEQRES 3 A 30 HIS SER LYS LYS
HET ZN A 31 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 THR A 14 SER A 24 1 11
LINK SG CYS A 5 ZN ZN A 31 1555 1555 2.30
LINK SG CYS A 8 ZN ZN A 31 1555 1555 2.30
LINK NE2 HIS A 21 ZN ZN A 31 1555 1555 2.00
LINK NE2 HIS A 27 ZN ZN A 31 1555 1555 2.02
SITE 1 AC1 4 CYS A 5 CYS A 8 HIS A 21 HIS A 27
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 - 16 202 Bytes