BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19066

Title: Solution structure of the FimH adhesin carbohydrate-binding domain   PubMed: 24476493

Authors: Van nuland, N.; VANWETSWINKEL, SOPHIE; Vranken, W.; Buts, L.

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).

Assembly members:
FIMH, polymer, 158 residues, 16904.8881 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
FIMH: FACKTANGTAIPIGGGSANV YVNLAPVVNVGQNLVVDLST QIFCHNDYPETITDYVTLQR GSAYGGVLSNFSGTVKYSGS SYPFPTTSETPRVVYNSRTD KPWPVALYLTPVSSAGGVAI KAGSLIAVLILRQTNNYNSD DFQFVWNIYANNDVVVPT

Data sets:
Data typeCount
13C chemical shifts694
15N chemical shifts171
1H chemical shifts1074
T1 relaxation values132
T2 relaxation values133

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FIMH1

Entities:

Entity 1, FIMH 158 residues - 16904.8881 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

Samples:

sample_1: FIMH, [U-13C,15N], 0.001 M; sodium phosphate 0.02 M; sodium chloride 0.1 M; H2O 93%; D2O 7%

sample_2: FIMH, [U-15N], 0.0011 M; sodium phosphate 0.02 M; sodium chloride 0.1 M; 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 CBCA(CO)NHsample_1solutionsample_conditions_1
3D HNCACBsample_1solutionsample_conditions_1
3D HNCOsample_1solutionsample_conditions_1
3D HBHA(CO)NHsample_1solutionsample_conditions_1
3D C(CO)NHsample_1solutionsample_conditions_1
3D HCCH-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-15N HSQC CPMGsample_2solutionsample_conditions_1
2D 1H-15N HSQCsample_2solutionsample_conditions_1

Software:

CING_any vany - chemical shift assignment

CNS vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN -

ANALYSIS v2.1 -

CYANA v2.1 -

DANGLE v1.1 -

Talosplus_any vany -

ccpNmr_any vany -

NMRDraw vany -

NMRPipe vany -

NMR spectrometers:

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

Related Database Links:

UNP A2IC68_ECOLX
BMRB 19254 19255 19256 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