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- PDB-1rfo: Trimeric Foldon of the T4 phagehead fibritin -

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Basic information

Entry
Database: PDB / ID: 1rfo
TitleTrimeric Foldon of the T4 phagehead fibritin
Componentswhisker antigen control protein
KeywordsVIRAL PROTEIN / BETA HAIRPIN / TRIMER
Function / homologyFibritin C-terminal / Fibritin C-terminal region / virion component / Fibritin
Function and homology information
Biological speciesEnterobacteria phage T4 (virus)
MethodSOLUTION NMR / simulated annealing with torsion angle dynamics
AuthorsGuthe, S. / Kapinos, L. / Moglich, A. / Meier, S. / Kiefhaber, T. / Grzesiek, S.
CitationJournal: J.Mol.Biol. / Year: 2004
Title: Very fast folding and association of a trimerization domain from bacteriophage t4 fibritin.
Authors: Guthe, S. / Kapinos, L. / Moglich, A. / Meier, S. / Grzesiek, S. / Kiefhaber, T.
History
DepositionNov 10, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 30, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 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: whisker antigen control protein
B: whisker antigen control protein
C: whisker antigen control protein


Theoretical massNumber of molelcules
Total (without water)9,2533
Polymers9,2533
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide whisker antigen control protein


Mass: 3084.461 Da / Num. of mol.: 3 / Fragment: trimerization domain (residues 457-483)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Enterobacteria phage T4 (virus) / Genus: T4-like viruses / Species: Enterobacteria phage T4 sensu lato / Gene: wac / Plasmid: pET32a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P10104

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: STANDARD TRIPLE AND DOUBLE RESONANCE EXPERIMENTS WERE CONDUCTED AS DESCRIBED IN KAHMANN ET AL. (2003),EMBO J. 1824-1834

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Sample preparation

DetailsContents: 0.3 mM Foldon 15N,13C; 5mM phosphate buffer pH 7.1
Solvent system: 95% H2O/5% D2O
Sample conditionsIonic strength: 10 mM / pH: 7.1 / Pressure: 1013 mbar / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CNS1Brungerstructure solution
NMRPipe2.1Delaglioprocessing
PIPP4.3.2Garrettdata analysis
XwinNMR2.6BRUKERcollection
CNS1Brungerrefinement
RefinementMethod: simulated annealing with torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 10

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