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- PDB-1f7w: SOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA -

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Basic information

Entry
Database: PDB / ID: 1f7w
TitleSOLUTION STRUCTURE OF C-TERMINAL DOMAIN ZIPA
ComponentsCELL DIVISION PROTEIN ZIPA
KeywordsCELL CYCLE / Alpha-Beta fold / CELL DIVISION / SEPTATION / TRANSMEMBRANE
Function / homology
Function and homology information


divisome complex / division septum assembly / FtsZ-dependent cytokinesis / cell division site / cell division / protein homodimerization activity / plasma membrane
Similarity search - Function
Cell Division Protein Zipa; Chain: A, / ZipA, C-terminal FtsZ-binding domain / ZipA, C-terminal FtsZ-binding domain / Cell division protein ZipA / ZipA, C-terminal FtsZ-binding domain superfamily / ZipA, C-terminal FtsZ-binding domain / ZipA, C-terminal domain (FtsZ-binding) / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Cell division protein ZipA
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / distance geometry simulated annealing
AuthorsMoy, F.J. / Glasfeld, E. / Mosyak, L. / Powers, R.
Citation
Journal: Biochemistry / Year: 2000
Title: Solution structure of ZipA, a crucial component of Escherichia coli cell division.
Authors: Moy, F.J. / Glasfeld, E. / Mosyak, L. / Powers, R.
#1: Journal: To be Published
Title: 1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of ZipA
Authors: Moy, F.J. / Glasfeld, E. / Powers, R.
History
DepositionJun 28, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 28, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CELL DIVISION PROTEIN ZIPA


Theoretical massNumber of molelcules
Total (without water)16,1351
Polymers16,1351
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
RepresentativeModel #1nmr, minimized average structure

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Components

#1: Protein CELL DIVISION PROTEIN ZIPA


Mass: 16135.430 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN, RESIDUES 185-328
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PEG041 / Production host: Escherichia coli (E. coli) / References: UniProt: P77173

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1123D 13C-separated NOESY
1233D 15N-separated NOESY
133HNHA
1432D 15N HSQC
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy. refinement program: x-plor V3.840, authors: brunger

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Sample preparation

Details
Solution-IDContentsSolvent system
11 mM ZipA U-15N,13C; 50mM phosphate buffer; 2 mM NaN3; 50 mM KCl; 90% H2O, 10% D2O; pH 5.590% H2O/10% D2O
21 mM ZipA U-15N,13C; 50mM phosphate buffer; 2 mM NaN3; 50 mM KCl; 100% D2O; pH 5.5100% D2O
31 mM ZipA U-15N; 50mM phosphate buffer; 2 mM NaN3; 50 mM KCl; 90% H2O, 10% D2O; pH 5.590% H2O/10% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
150 mM KCl 5.5ambient 298 K
250 mM KCl 5.5ambient 298 K
350 mM KCl 5.5ambient 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLORV3.840Brungerstructure solution
NMRPipe1.7Delaglioprocessing
PIPP4.2.8Garrettdata analysis
XwinNMR2Brukercollection
X-PLORV3.840Brungerrefinement
RefinementMethod: distance geometry simulated annealing / Software ordinal: 1
Details: The structures are based on a total of 2758 restraints, 2038 are NOE-derived distance constraints, 377 dihedral angle restraints, 84 distance restraints from hydrogen bonds, 113 3JNHa ...Details: The structures are based on a total of 2758 restraints, 2038 are NOE-derived distance constraints, 377 dihedral angle restraints, 84 distance restraints from hydrogen bonds, 113 3JNHa coupling restraints, 230 secondary Ca/Cb chemical shift restraints, and a conformational database. The coordinates in this entry corrospond to the refined minimized average structure determined from an ensemble of 30 structures
NMR representativeSelection criteria: nmr, minimized average structure
NMR ensembleConformers submitted total number: 1

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