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- PDB-2fvn: The fibrillar tip complex of the Afa/Dr adhesins from pathogen E.... -

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Basic information

Entry
Database: PDB / ID: 2fvn
TitleThe fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins
ComponentsProtein afaD
KeywordsCELL ADHESION / afaD / afaE / fibrillar / afimbrial / integrin-binding / DAEC / DAF / CEACAM
Function / homologyEnterobacteria AfaD invasin / Enterobacteria AfaD invasin protein / Dr adhesin / Dr-adhesin superfamily / Adhesion domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta / Protein AfaD
Function and homology information
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / Aria-implemented distance geometry, simulated annealing
AuthorsCota, E. / Simpson, P. / Anderson, K.L. / Matthews, S.J.
CitationJournal: Mol.Microbiol. / Year: 2006
Title: The solution structure of the invasive tip complex from Afa/Dr fibrils
Authors: Cota, E. / Jones, C. / Simpson, P. / Altroff, H. / Anderson, K.L. / du Merle, L. / Guignot, J. / Servin, A. / Le Bouguenec, C. / Mardon, H. / Matthews, S.
History
DepositionJan 31, 2006Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Feb 27, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.4Oct 23, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein afaD


Theoretical massNumber of molelcules
Total (without water)16,6301
Polymers16,6301
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)1 / -REGULARIZED MEAN STRUCTURE
Representative

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Components

#1: Protein Protein afaD


Mass: 16630.320 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: Q47038
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1213D 15N-separated NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
10.5mM afaD-dsc, U-15N, 13C; 50mM Na phosphate buffer(pH 7.0); 50mM NaCl; 90% H2O, 10% D2O90% H2O/10% D2O
20.5mM afaDE-dsc, U-15N, 13C, D2O; 50mM Na phosphate buffer(pH 7.0); 50mM NaCl; 90% H2O, 10% D2O90% H2O/10% D2O
Sample conditionsIonic strength: 50mM phosphate / pH: 7 / Pressure: ambient / Temperature: 303 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMXBrukerAMX5001
Varian INOVAVarianINOVA8002

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Processing

NMR software
NameVersionDeveloperClassification
ARIA1.2Linge, O'Donoghue, Nilgesrefinement
ARIA1.2Linge, O'Donoghue, Nilgesstructure solution
NMRView4Johnson, Blevinsdata analysis
NMRPipe2.1Delaglio, Grzesiek, Vuister, Zhu, Pfeifer, Baxprocessing
XwinNMR3.1Bruker Biospincollection
RefinementMethod: Aria-implemented distance geometry, simulated annealing
Software ordinal: 1
Details: Structure based on 3839 noe-based restraints (2951 unambiguous, 1423 ambiguous) and 116 torsion angles (talos)
NMR ensembleConformer selection criteria: REGULARIZED MEAN STRUCTURE / Conformers submitted total number: 1

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