BMRB Entry 15759
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15759
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Title: 1H, 13C and 15N backbone chemical shift assignments of the 3FNIII module from human fibronectin PubMed: 19366708
Deposition date: 2008-05-06 Original release date: 2009-04-15
Authors: Vakonakis, Ioannis; Campbell, Iain
Citation: Vakonakis, Ioannis; Staunton, David; Ellis, Ian; Sarkies, Peter; Flanagan, Aleksandra; Schor, Ana; Schor, Seth; Campbell, Iain. "Motogenic sites in human fibronectin are masked by long range interactions" J. Biol. Chem. 284, 15668-15675 (2009).
Assembly members:
3F3, polymer, 96 residues, 10256.2 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: Escherichia coli Vector: pGEX-6P-2
Entity Sequences (FASTA):
3F3: GPLGSAPDAPPDPTVDQVDD
TSIVVRWSRPQAPITGYRIV
YSPSVEGSSTELNLPETANS
VTLSDLQPGVQYNITIYAVE
ENQESTPVVIQQETTG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 178 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 80 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protein | 1 |
Entities:
Entity 1, protein 96 residues - 10256.2 Da.
| 1 | GLY | PRO | LEU | GLY | SER | ALA | PRO | ASP | ALA | PRO | ||||
| 2 | PRO | ASP | PRO | THR | VAL | ASP | GLN | VAL | ASP | ASP | ||||
| 3 | THR | SER | ILE | VAL | VAL | ARG | TRP | SER | ARG | PRO | ||||
| 4 | GLN | ALA | PRO | ILE | THR | GLY | TYR | ARG | ILE | VAL | ||||
| 5 | TYR | SER | PRO | SER | VAL | GLU | GLY | SER | SER | THR | ||||
| 6 | GLU | LEU | ASN | LEU | PRO | GLU | THR | ALA | ASN | SER | ||||
| 7 | VAL | THR | LEU | SER | ASP | LEU | GLN | PRO | GLY | VAL | ||||
| 8 | GLN | TYR | ASN | ILE | THR | ILE | TYR | ALA | VAL | GLU | ||||
| 9 | GLU | ASN | GLN | GLU | SER | THR | PRO | VAL | VAL | ILE | ||||
| 10 | GLN | GLN | GLU | THR | THR | GLY |
Samples:
sample_1: 3F3 0.7 mM; D2O 5%; DSS 0.1 mM; sodium chloride 20 mM; sodium phosphate 20 mM; sodium azide 0.01%
sample_conditions_1: ionic strength: 115 mM; pH: 6; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP v4.3.7, Garrett - data analysis
TOPSPIN v1.3, Bruker Biospin - collection
NMR spectrometers:
- Bruker DMX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts