BMRB Entry 17247

Title:
Solution NMR Structure of xenopus Fn14
Deposition date:
2010-10-11
Original release date:
2013-06-04
Authors:
Pellegrini, M.; Willen, L.; Perroud, M.; Krushinskie, D.; Strauch, K.; Cuervo, H.; Sun, Y.; Day, E.; Schneider, P.; Zheng, T.
Citation:

Citation: Pellegrini, Maria; Willen, Laure; Perroud, Mai; Krushinskie, Dennis; Strauch, Kathy; Cuervo, Hernan; Day, Eric; Schneider, Pascal; Zheng, Timothy. "Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions."  FEBS J. 280, 1818-1829 (2013).
PubMed: 23438059

Assembly members:

Assembly members:
xeFn14, polymer, 66 residues, 5682.339 Da.

Natural source:

Natural source:   Common Name: African clawed frog   Taxonomy ID: 8355   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Xenopus laevis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Pichia Pastoris   Vector: N/A

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts36
1H chemical shifts211

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1xeFn141

Entities:

Entity 1, xeFn14 66 residues - 5682.339 Da.

the recombinant protein fragment contained a C-terminal Myc-His tag, the tag residues were not included in the structure calculations

1   SERGLNGLYGLUCYSPROGLUGLYARGALA
2   TYRSERGLNASPLEUGLYLYSCYSMETGLU
3   CYSSERVALCYSLYSASNSERGLULYSSER
4   ASPPHECYSGLNASNCYSPROSERLYSTHR
5   GLUGLNPROASPPHEPROTRPILETRPVAL
6   GLUGLNLYSLEUILESERGLUGLUASPLEU
7   HISHISHISHISHISHIS

Samples:

sample: xeFn14, [U-99% 15N], 500 – 700 uM; sodium phosphate 10 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 140 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsampleisotropicsample_conditions_1

Software:

CNS v1.1, Brunger A. T. et.al. - structure solution

SPARKY v3.11, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAI69735 AAI69737 AAR21225
REF NP_001083640

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