BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17237

Title: NMR Structure of hFn14   PubMed: 23438059

Deposition date: 2010-10-05 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: 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).

Assembly members:
Fn14, polymer, 53 residues, 5615.414 Da.

Natural source:   Common Name: not available   Taxonomy ID: 9606   Superkingdom: not available   Kingdom: 17237   Genus/species: not available not available

Experimental source:   Production method: recombinant technology' 'Pichia Pastoris

Entity Sequences (FASTA):
Fn14: EQAPGTAPCSRGSSWSADLD KCMDCASCRARPHSDFCLGC AAAPPAPFRLLWP

Data sets:
Data typeCount
15N chemical shifts33
1H chemical shifts180

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hFn141

Entities:

Entity 1, hFn14 53 residues - 5615.414 Da.

Extracellular Cys-rich domain of human Fn14, the recombinant protein contained a C-terminal Myc-His tag.

1   GLUGLNALAPROGLYTHRALAPROCYSSER
2   ARGGLYSERSERTRPSERALAASPLEUASP
3   LYSCYSMETASPCYSALASERCYSARGALA
4   ARGPROHISSERASPPHECYSLEUGLYCYS
5   ALAALAALAPROPROALAPROPHEARGLEU
6   LEUTRPPRO

Samples:

sample: hFn14, [U-99% 15N], 700 uM; sodium phosphate' 'natural abundance; .; . mM; . %; . %

sample_2: hFn14 700 uM; sodium phosphate' 'natural abundance; .; . mM; . %; . %

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
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

SPARKY v3.11, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz MHz

Related Database Links:

BMRB 11346
PDB
DBJ BAA94792 BAJ20302
GB AAF69108 AAH02718 ABM83894 ABM87215 EAW85429
REF NP_057723 XP_001089176 XP_001165479 XP_002826080 XP_003269240
SP Q9NP84

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts