BMRB Entry 17247
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17247
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Title: Solution NMR Structure of xenopus Fn14 PubMed: 23438059
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: 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:
xeFn14, polymer, 66 residues, 5682.339 Da.
Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus laevis
Experimental source: Production method: recombinant technology Host organism: Pichia Pastoris Vector: N/A
Entity Sequences (FASTA):
xeFn14: SQGECPEGRAYSQDLGKCME
CSVCKNSEKSDFCQNCPSKT
EQPDFPWIWVEQKLISEEDL
HHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 36 |
| 1H chemical shifts | 211 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | xeFn14 | 1 |
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 | SER | GLN | GLY | GLU | CYS | PRO | GLU | GLY | ARG | ALA | ||||
| 2 | TYR | SER | GLN | ASP | LEU | GLY | LYS | CYS | MET | GLU | ||||
| 3 | CYS | SER | VAL | CYS | LYS | ASN | SER | GLU | LYS | SER | ||||
| 4 | ASP | PHE | CYS | GLN | ASN | CYS | PRO | SER | LYS | THR | ||||
| 5 | GLU | GLN | PRO | ASP | PHE | PRO | TRP | ILE | TRP | VAL | ||||
| 6 | GLU | GLN | LYS | LEU | ILE | SER | GLU | GLU | ASP | LEU | ||||
| 7 | HIS | HIS | HIS | HIS | HIS | HIS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample | isotropic | sample_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
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SPARKY: Backbone
or all simulated shifts