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- PDB-1fsp: NMR SOLUTION STRUCTURE OF BACILLUS SUBTILIS SPO0F PROTEIN, 20 STR... -

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Basic information

Entry
Database: PDB / ID: 1fsp
TitleNMR SOLUTION STRUCTURE OF BACILLUS SUBTILIS SPO0F PROTEIN, 20 STRUCTURES
ComponentsSTAGE 0 SPORULATION PROTEIN F
KeywordsRESPONSE REGULATOR / SPORULATION / TWO-COMPONENT SYSTEMS / BACTERIAL SIGNAL TRANSDUCTION / PHOSPHO-RELAY / (BETA/ALPHA)5 PROTEIN
Function / homology
Function and homology information


Transferases; Transferring phosphorus-containing groups / sporulation resulting in formation of a cellular spore / phosphorelay signal transduction system / kinase activity / metal ion binding / cytoplasm
Similarity search - Function
: / Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / Response regulator / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Sporulation initiation phosphotransferase F
Similarity search - Component
Biological speciesBacillus subtilis (bacteria)
MethodSOLUTION NMR / DISTANCE GEOMETRY WITH SIMULATED ANNEALING REFINEMENT
AuthorsFeher, V.A. / Skelton, N.J. / Dahlquist, F.W. / Cavanagh, J.
Citation
Journal: Biochemistry / Year: 1997
Title: High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition.
Authors: Feher, V.A. / Zapf, J.W. / Hoch, J.A. / Whiteley, J.M. / McIntosh, L.P. / Rance, M. / Skelton, N.J. / Dahlquist, F.W. / Cavanagh, J.
#1: Journal: Protein Sci. / Year: 1995
Title: 1H, 15N, and 13C Backbone Chemical Shift Assignments, Secondary Structure, and Magnesium-Binding Characteristics of the Bacillus Subtilis Response Regulator, Spo0F, Determined by Heteronuclear High-Resolution NMR
Authors: Feher, V.A. / Zapf, J.W. / Hoch, J.A. / Dahlquist, F.W. / Whiteley, J.M. / Cavanagh, J.
History
DepositionJun 5, 1997Processing site: BNL
Revision 1.0Dec 10, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
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: STAGE 0 SPORULATION PROTEIN F


Theoretical massNumber of molelcules
Total (without water)14,2451
Polymers14,2451
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)20 / 60LEAST RESTRAINT VIOLATIONS
Representative

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Components

#1: Protein STAGE 0 SPORULATION PROTEIN F / SPO0F


Mass: 14244.660 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (bacteria) / Cell line: BL21 / Gene: SPO0F / Plasmid: PET0F / Species (production host): Escherichia coli / Gene (production host): SPO0F / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P06628

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: TPPI-STATES

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Sample preparation

Sample conditionspH: 6.8 / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker BRUKER AMX 600BrukerBRUKER AMX 6005001
Varian DMX 500VarianDMX 5006002
GE DMX 500GEDMX 5006003

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLOR3.1structure solution
RefinementMethod: DISTANCE GEOMETRY WITH SIMULATED ANNEALING REFINEMENT
Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN BIOCHEMISTRY CITATION.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATIONS / Conformers calculated total number: 60 / Conformers submitted total number: 20

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