BMRB Entry 26541

Title:
Backbone Chemical Shift Assignment of the FimH lectin domain from Escherichia coli
Deposition date:
2015-03-13
Original release date:
2015-05-11
Authors:
Fiege, Brigitte; Ernst, Beat
Citation:

Citation: Fiege, Brigitte; Rabbani, Said; Preston, Roland; Jakob, Roman; Zihlmann, Pascal; Schwardt, Oliver; Jiang, Xiaohua; Maier, Timm; Ernst, Beat. "he Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography"  Chembiochem 16, 1235-1246 (2015).
PubMed: 25940742

Assembly members:

Assembly members:
FimH-CRD, polymer, 173 residues, 18643.8386 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   Vector: pDsbA3

Data sets:
Data typeCount
13C chemical shifts510
15N chemical shifts173
1H chemical shifts191

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FimH-CRD1

Entities:

Entity 1, FimH-CRD 173 residues - 18643.8386 Da.

1   PHEALACYSLYSTHRALAASNGLYTHRALA
2   ILEPROILEGLYGLYGLYSERALAASNVAL
3   TYRVALASNLEUALAPROVALVALASNVAL
4   GLYGLNASNLEUVALVALASPLEUSERTHR
5   GLNILEPHECYSHISASNASPTYRPROGLU
6   THRILETHRASPTYRVALTHRLEUGLNARG
7   GLYSERALATYRGLYGLYVALLEUSERASN
8   PHESERGLYTHRVALLYSTYRSERGLYSER
9   SERTYRPROPHEPROTHRTHRSERGLUTHR
10   PROARGVALVALTYRASNSERARGTHRASP
11   LYSPROTRPPROVALALALEUTYRLEUTHR
12   PROVALSERSERALAGLYGLYVALALAILE
13   LYSALAGLYSERLEUILEALAVALLEUILE
14   LEUARGGLNTHRASNASNTYRASNSERASP
15   ASPPHEGLNPHEVALTRPASNILETYRALA
16   ASNASNASPVALVALVALPROTHRGLYLEU
17   VALPROARGGLYSERLEUGLUHISHISHIS
18   HISHISHIS

Samples:

sample_1: FimH-CRD, [U-100% 13C; U-100% 15N], 0.6 mM; sodium phosphate 25.0 mM; TSP-d4 0.1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 0.025 M; pH: 6.800; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropiccondition_1
3D HNCAsample_1isotropiccondition_1
3D HN(CO)CAsample_1isotropiccondition_1
3D HN(CA)COsample_1isotropiccondition_1
3D HNCOsample_1isotropiccondition_1
3D HNCACBsample_1isotropiccondition_1
3D CBCA(CO)NHsample_1isotropiccondition_1

Software:

CcpNmr_Analysis v2.3, CCPN - chemical shift assignment

Sparta vany, Yang Shen, Ad Bax - chemical shift calculation

Topspin v3.2, Bruker - data acquisition, processing

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

UniProt A2IC68_ECOLX
PDB
BMRB 19066
GB CAM92099.1
AlphaFold A2IC68

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