BMRB Entry 19256

Title:
NMR assignments and backbone amide relaxation data (T1-T2) for the complex of the FimH adhesin carbohydrate-binding domain with heptyl-mannose
Deposition date:
2013-05-22
Original release date:
2014-02-13
Authors:
Vanwetswinkel, Sophie; Van Nuland, N.
Citation:

Citation: Vanwetswinkel, Sophie; Volkov, Alexander; Sterckx, Yann; Garcia-Pino, Abel; Buts, Lieven; Vranken, Wim; Bouckaert, Julie; Roy, Rene; Wyns, Lode; van Nuland, Nico. "Study of the Structural and Dynamic Effects in the FimH Adhesin upon alfa-D-Heptyl Mannose Binding"  J. Med. Chem. 57, 1416-1427 (2014).
PubMed: 24476493

Assembly members:

Assembly members:
FIMH, polymer, 158 residues, 16907.9118 Da.
Heptyl Alpha-D-mannopyrannoside, non-polymer, 278.342 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: pET24a

Data sets:
Data typeCount
13C chemical shifts622
15N chemical shifts171
1H chemical shifts1006
T1 relaxation values131
T2 relaxation values127

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FIMH1
2heptyl-mannose2

Entities:

Entity 1, FIMH 158 residues - 16907.9118 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   ASNASNASPVALVALVALPROTHR

Entity 2, heptyl-mannose - C13 H26 O6 - 278.342 Da.

1   KGM

Samples:

sample_1: FIMH, [U-13C; U-15N], 1 mM; sodium phosphate 0.02 M; sodium chloride 0.1 M; H2O 93%; D2O 7%; heptyl-mannose 1.3 mM

sample_2: FIMH, [U-100% 15N], 1.1 mM; heptyl alpha-D-mannopyranoside (heptyl-mannose) 1.3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.12 M; pH: 6.000; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1solutionsample_conditions_1
2D 1H-13C HSQCsample_1solutionsample_conditions_1
3D HNCAsample_1solutionsample_conditions_1
3D HNCOsample_1solutionsample_conditions_1
3D HNCOCAsample_1solutionsample_conditions_1
3D CCH-TOCSYsample_1solutionsample_conditions_1
2D (HB)CB(CGCD)HDsample_1solutionsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1solutionsample_conditions_1
3D 1H-15N NOESYsample_1solutionsample_conditions_1
3D 1H-13C NOESYsample_1solutionsample_conditions_1
2D 1H-1H NOESYsample_1solutionsample_conditions_1
2D 1H-15N HSQC (inversion recovery)sample_2solutionsample_conditions_1
2D 1H-15N HSQC (CPMG)sample_2solutionsample_conditions_1

Software:

ANALYSIS v2.1, CCPN - assignment and data analysis

NMRDraw vany - Spectrum analysis, Spectrum display

NMRPipe vany - Spectrum processing

NMR spectrometers:

  • Varian Direct-Drive 600 MHz
  • Varian Direct-Drive 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

UNP A2IC68_ECOLX
BMRB 19066 19254 19255 21033 26541
PDB
DBJ BAB38702 BAE78313 BAG80117 BAI28639 BAI33780
EMBL CAA12423 CAA29156 CAH55784 CAM92099 CAP78801
GB AAA97216 AAB29812 AAC35864 AAC77276 AAD44319
REF NP_313306 NP_418740 NP_709914 WP_000816510 WP_000816511
SP P08191
AlphaFold A2IC68 P08191

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