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- PDB-2mmv: ZapA mutant dimer from Geobacillus stearothermophilus -

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Basic information

Entry
Database: PDB / ID: 2mmv
TitleZapA mutant dimer from Geobacillus stearothermophilus
ComponentsCell division protein ZapA
KeywordsCELL CYCLE / ZapA
Function / homology
Function and homology information


septin ring assembly / cell septum / division septum assembly / FtsZ-dependent cytokinesis / cell division site / plasma membrane / cytosol
Similarity search - Function
Cell division protein ZapA, firmicutes / : / Cell division protein ZapA-like / Cell division protein ZapA-like superfamily / Cell division protein ZapA
Similarity search - Domain/homology
Cell division protein ZapA
Similarity search - Component
Biological speciesGeobacillus stearothermophilus (bacteria)
MethodSOLUTION NMR / torsion angle dynamics, SIMULATED ANNEALING
Model detailsfewest violations, model1
AuthorsNogueira, M.L. / Sforca, M. / Zeri, A.
CitationJournal: Biomol.Nmr Assign. / Year: 2015
Title: Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ.
Authors: Nogueira, M.L. / Sforca, M.L. / Chin, Y.K. / Mobli, M. / Handler, A. / Gorbatyuk, V.Y. / Robson, S.A. / King, G.F. / Gueiros-Filho, F.J. / Zeri, A.C.
History
DepositionMar 19, 2014Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jun 17, 2015Provider: repository / Type: Initial release
Revision 1.1Dec 14, 2022Group: Data collection / Database references
Category: citation / citation_author ...citation / citation_author / database_2 / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.2Jun 14, 2023Group: Other / Category: pdbx_database_status / Item: _pdbx_database_status.status_code_nmr_data
Revision 1.3May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Cell division protein ZapA
B: Cell division protein ZapA


Theoretical massNumber of molelcules
Total (without water)19,8052
Polymers19,8052
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3510 Å2
ΔGint-36 kcal/mol
Surface area11880 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -structures with the least restraint violations
RepresentativeModel #1

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Components

#1: Protein Cell division protein ZapA


Mass: 9902.428 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Geobacillus stearothermophilus (bacteria)
Description: mutant protein / Gene: zapa / Production host: Escherichia coli (E. coli) / References: UniProt: A0A078N0N2

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N NOESY
22115NHSQC
33115N13C ALI NOE HBHA(CO)NH
441(H)CCH
551HN(CA)CB
661TOCSY
771CCH CCHTOCSY
881HCCHTOCSY
991NOESYCHSQC AR

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Sample preparation

DetailsContents: 50 Mm NaPhosp, 50 Mm KCl
Sample conditionsIonic strength: 100 / pH: 6.5 / Pressure: AMBIENT / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE9001
Agilent INOVAAgilentINOVA6002

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Processing

NMR software
NameVersionDeveloperClassification
CYANA2.1P.GUNTERT ET AL.refinement
CYANA2.1structure solution
RefinementMethod: torsion angle dynamics, SIMULATED ANNEALING / Software ordinal: 1
NMR constraintsNOE constraints total: 2124 / NOE intraresidue total count: 694 / NOE long range total count: 388 / NOE medium range total count: 379 / NOE sequential total count: 663
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers submitted total number: 20

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