BMRB Entry 34042

Title:
Structural studies of the Aggregative Adherence Fimbriae of Enteroaggregative Escherichia coli
Deposition date:
2016-09-14
Original release date:
2017-10-13
Authors:
Liu, B.; Matthews, S.
Citation:

Citation: Jnsson, R.; Liu, B.; Struve, C.; Yang, Y.; Jrgensen, R.; Xu, Y.; Jenssen, H.; Krogfelt, K.; Matthews, S.. "Structural and functional studies of Escherichia coli aggregative adherence fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding."  Biochim. Biophys. Acta 1865, 304-311 (2017).
PubMed: 27939608

Assembly members:

Assembly members:
entity_1, polymer, 154 residues, 16493.498 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli-Pichia pastoris shuttle vector pPpARG4

Data sets:
Data typeCount
13C chemical shifts614
15N chemical shifts130
1H chemical shifts917

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 154 residues - 16493.498 Da.

1   ASNSERCYSSERLEUSERILESERSERPRO
2   ASPPROVALTHRTYRTHRILEPROTHRASP
3   LYSGLYASPLYSTYRILEASNPHELYSLEU
4   ASPVALPROASPPROARGCYSLYSALALEU
5   GLYGLYTHRVALTYRPHETRPGLYALAASP
6   THRARGASPGLYLYSLEUVALMETLYSLYS
7   GLYGLNASPLYSTYRTHRLEUMETTHRTHR
8   TYRGLYGLYALAVALGLNGLNGLNLEUGLY
9   GLYGLYTYRGLYTYRTYRHISVALSERGLN
10   LYSTHRPROPROGLNTHRILESERGLYVAL
11   VALSERLYSASNVALGLYTYRLYSPROGLY
12   GLNTYRTHRVALGLULEUTHRGLYPHEPHE
13   SERLEUASNASPASNLYSGLNALAASNPRO
14   THRPROSERSERLEUTHRSERLYSALAALA
15   GLYLYSASNILEVALSERSERTHRGLYTHR
16   ILETHRILESER

Samples:

sample_1: entity_1, na, mM; sodium acetate 50 ± 0.2 mM; sodium chloride 50 ± 0.2 nM

sample_conditions_1: ionic strength: 100 mM; pH: 5.0; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks