BMRB Entry 17237
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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/BMR17237
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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: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Pichia Pastoris Vector: N/A
Entity Sequences (FASTA):
Fn14: EQAPGTAPCSRGSSWSADLD
KCMDCASCRARPHSDFCLGC
AAAPPAPFRLLWP
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 33 |
| 1H chemical shifts | 180 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hFn14 | 1 |
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 | GLU | GLN | ALA | PRO | GLY | THR | ALA | PRO | CYS | SER | ||||
| 2 | ARG | GLY | SER | SER | TRP | SER | ALA | ASP | LEU | ASP | ||||
| 3 | LYS | CYS | MET | ASP | CYS | ALA | SER | CYS | ARG | ALA | ||||
| 4 | ARG | PRO | HIS | SER | ASP | PHE | CYS | LEU | GLY | CYS | ||||
| 5 | ALA | ALA | ALA | PRO | PRO | ALA | PRO | PHE | ARG | LEU | ||||
| 6 | LEU | TRP | PRO |
Samples:
sample: hFn14, [U-99% 15N], 700 uM; sodium phosphate 10 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; H2O 95%; D2O 5%
sample_2: hFn14 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 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_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 |
| AlphaFold | Q9NP84 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts