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- PDB-2m5g: Solution structure of FimA wt -

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Basic information

Entry
Database: PDB / ID: 2m5g
TitleSolution structure of FimA wt
ComponentsType-1 fimbrial protein, A chain
KeywordsSTRUCTURAL PROTEIN / FimA / Pili / pilus
Function / homologyFimbrial-type adhesion domain / Fimbrial protein / Fimbrial-type adhesion domain superfamily / cell adhesion involved in single-species biofilm formation / Adhesion domain superfamily / pilus / cell adhesion / identical protein binding / Type-1 fimbrial protein, A chain
Function and homology information
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / simulated annealing
Model detailsminimized average structure, model1
Model type detailsminimized average
AuthorsWalczak, M.J. / Puorger, C. / Glockshuber, R. / Wider, G.
CitationJournal: J.Mol.Biol. / Year: 2014
Title: Intramolecular donor strand complementation in the E. coli type 1 pilus subunit FimA explains the existence of FimA monomers as off-pathway products of pilus assembly that inhibit host cell apoptosis.
Authors: Walczak, M.J. / Puorger, C. / Glockshuber, R. / Wider, G.
History
DepositionFeb 24, 2013Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Nov 13, 2013Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2022Group: Data collection / Database references
Category: citation / database_2 ...citation / database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.2Jun 14, 2023Group: Other / Category: pdbx_database_status / Item: _pdbx_database_status.status_code_nmr_data

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Type-1 fimbrial protein, A chain


Theoretical massNumber of molelcules
Total (without water)15,8351
Polymers15,8351
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 / 100structures with the lowest energy
RepresentativeModel #1minimized average structure

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Components

#1: Protein Type-1 fimbrial protein, A chain / Type-1A pilin


Mass: 15835.243 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: fimA / Production host: Escherichia coli (E. coli) / References: UniProt: P04128

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1212D 1H-13C HSQC
1313D HNCA
1413D HN(CO)CA
1513D HN(CA)CB
1613D (H)CCH-TOCSY
1713D 1H-15N TOCSY
1813D 1H-15N NOESY
1913D 1H-13C NOESY

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Sample preparation

DetailsContents: 2 mM [U-99% 13C; U-99% 15N] FimA-1, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
SampleConc.: 2 mM / Component: FimA-1 / Isotopic labeling: [U-99% 13C; U-99% 15N]
Sample conditionsIonic strength: 0.08 / pH: 7 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE7501
Bruker AvanceBrukerAVANCE9002

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Processing

NMR software
NameDeveloperClassification
SparkyGoddard, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich, Brunger, Adams, Clore, Gros, Nilges and Readchemical shift assignment
SparkyGoddard, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich, Brunger, Adams, Clore, Gros, Nilges and Readstructure solution
SparkyGoddard, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich, Brunger, Adams, Clore, Gros, Nilges and Readrefinement
CNSrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1

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