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- PDB-2ixq: The solution structure of the invasive tip complex from Afa-Dr fibrils -

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Basic information

Entry
Database: PDB / ID: 2ixq
TitleThe solution structure of the invasive tip complex from Afa-Dr fibrils
Components
  • Afimbrial adhesin AFA-III
  • Protein AfaD
KeywordsCELL ADHESION / IG-LIKE DOMAIN / AFIMBRIAL SHEATH / STRUCTURAL PROTEIN / DONOR STRAND COMPLEMENTED / DAF / AFAE / UPEC / DAEC / FIMBRIA
Function / homology
Function and homology information


Enterobacteria AfaD invasin / Enterobacteria AfaD invasin protein / Adhesin, Dr-family / Adhesin, Dr family, signal peptide / Dr-family adhesin / Dr family adhesin / Dr adhesin / Dr-adhesin superfamily / Adhesion domain superfamily / Immunoglobulin-like ...Enterobacteria AfaD invasin / Enterobacteria AfaD invasin protein / Adhesin, Dr-family / Adhesin, Dr family, signal peptide / Dr-family adhesin / Dr family adhesin / Dr adhesin / Dr-adhesin superfamily / Adhesion domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Protein AfaD / Afimbrial adhesin AFA-III / AfaD
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR
Model type detailsMINIMIZED AVERAGE
AuthorsCota, E. / Jones, C. / Simpson, P. / Altroff, H. / Anderson, K.L. / du Merle, L. / Guignot, J. / Servin, A. / Le Bouguenec, C. / Mardon, H. / Matthews, S.
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
DepositionJul 10, 2006Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 20, 2006Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Dec 5, 2018Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Source and taxonomy / Structure summary
Category: atom_site / citation ...atom_site / citation / citation_author / entity / entity_name_com / entity_src_gen / pdbx_entity_src_syn / pdbx_nmr_spectrometer / pdbx_validate_close_contact / struct_ref / struct_ref_seq / struct_ref_seq_dif
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name / _entity.pdbx_description / _entity.src_method / _pdbx_validate_close_contact.auth_atom_id_2
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein AfaD
B: Afimbrial adhesin AFA-III


Theoretical massNumber of molelcules
Total (without water)30,7682
Polymers30,7682
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 / -
Representative

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Components

#1: Protein Protein AfaD


Mass: 15311.866 Da / Num. of mol.: 1 / Fragment: RESIDUES 26-147
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: afaD / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q47038, UniProt: Q7BG36*PLUS
#2: Protein Afimbrial adhesin AFA-III


Mass: 15456.051 Da / Num. of mol.: 1 / Fragment: RESIDUES 38-160
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: afaE3, afaE-3 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q57254

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: NONE

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Sample preparation

Sample conditionsTemperature: 303.0 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAvance5001
Bruker AvanceBrukerAvance8002

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Processing

NMR softwareName: CNS
Developer: BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARREN
Classification: refinement
NMR ensembleConformers submitted total number: 1

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