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- PDB-2c0s: NMR Solution Structure of a protein aspartic acid phosphate phosp... -

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Basic information

Entry
Database: PDB / ID: 2c0s
TitleNMR Solution Structure of a protein aspartic acid phosphate phosphatase from Bacillus Anthracis
ComponentsCONSERVED DOMAIN PROTEIN
KeywordsTRANSFERASE / PHOSPHATASE / PHOSPHORYLATION / SPORULATION / BACILLUS ANTHRACIS / ANTITHETICAL / NEGATIVE REGULATOR / SPINE
Function / homology
Function and homology information


regulation of sporulation / protein dimerization activity
Similarity search - Function
Aspartyl-phosphate phosphatase Spo0E-like / Aspartyl-phosphate phosphatase Spo0E-like superfamily / : / Spo0E like sporulation regulatory protein / Helix-loop-helix DNA-binding domain / MYOD Basic-Helix-Loop-Helix Domain, subunit B / Helix-loop-helix DNA-binding domain superfamily / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Stage 0 sporulation regulatory protein / Aspartyl-phosphate phosphatase Spo0E family protein
Similarity search - Component
Biological speciesBacillus anthracis str. Ames (bacteria)
MethodSOLUTION NMR / CANDID
AuthorsGrenha, R. / Rzechorzek, N.J. / Brannigan, J.A. / Ab, E. / Folkers, G.E. / De Jong, R.N. / Diercks, T. / Wilkinson, A.J. / Kaptein, R. / Wilson, K.S.
CitationJournal: J. Biol. Chem. / Year: 2006
Title: Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli.
Authors: Grenha, R. / Rzechorzek, N.J. / Brannigan, J.A. / de Jong, R.N. / Ab, E. / Diercks, T. / Truffault, V. / Ladds, J.C. / Fogg, M.J. / Bongiorni, C. / Perego, M. / Kaptein, R. / Wilson, K.S. / ...Authors: Grenha, R. / Rzechorzek, N.J. / Brannigan, J.A. / de Jong, R.N. / Ab, E. / Diercks, T. / Truffault, V. / Ladds, J.C. / Fogg, M.J. / Bongiorni, C. / Perego, M. / Kaptein, R. / Wilson, K.S. / Folkers, G.E. / Wilkinson, A.J.
History
DepositionSep 7, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 25, 2006Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 9, 2018Group: Data collection / Database references / Source and taxonomy
Category: citation / citation_author ...citation / citation_author / entity_src_gen / pdbx_nmr_spectrometer
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name / _entity_src_gen.gene_src_strain / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain
Revision 1.4May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CONSERVED DOMAIN PROTEIN


Theoretical massNumber of molelcules
Total (without water)7,8261
Polymers7,8261
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)25 / 95LOWEST ENERGY
RepresentativeModel #1

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Components

#1: Protein CONSERVED DOMAIN PROTEIN


Mass: 7826.213 Da / Num. of mol.: 1
Fragment: SMALL ASPARTIC ACID PHOSPHATE PHOSPHATASE, RESIDUES 52-108
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus anthracis str. Ames (bacteria)
Plasmid: PET28A / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q81XQ9, UniProt: A0A6L7H8X9*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HNCO
121HN(CA)CO
131HN(CA)CB
141CBCA(CO)NH
151HNCA
161HBHA(CO)NH
171HNCAHA
181CCH-COSY
191(H)CCH-TOCSY
1101CC(CO)NH
1111HNH-NOESY
1121HCH-NOESY
1131CNH-NOESY
1141HH-NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR ON 15N- AND 13C- LABELED HIS-TAGGED SAMPLE

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Sample preparation

DetailsContents: 90% WATER/10% D2O
Sample conditionsIonic strength: 150 mM / pH: 6 / Pressure: 1.0 atm / Temperature: 278.0 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE7001
Bruker AVANCEBrukerAVANCE9002

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Processing

NMR software
NameDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARRENrefinement
Sparkystructure solution
CYANAstructure solution
RefinementMethod: CANDID / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 95 / Conformers submitted total number: 25

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