BMRB Entry 16259
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16259
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Beta7 Integrin Cytoplasmic Tail 1H and 15N Chemical Shift Assignments PubMed: 19843520
Deposition date: 2009-04-17 Original release date: 2009-12-11
Authors: Memo, Massimiliano; Anthis, Nicholas; Campbell, Iain
Citation: Anthis, Nicholas; Haling, Jacob; Oxley, Camilla; Memo, Massimiliano; Wegener, Kate; Lim, Chinten; Ginsberg, Mark; Campbell, Iain. "Beta integrin tyrosine phosphorylation is a conserved mechanism for regulating talin-induced integrin activation." J. Biol. Chem. 284, 36700-36710 (2009).
Assembly members:
beta7_integrin, polymer, 54 residues, 6446 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
Entity Sequences (FASTA):
beta7_integrin: GPRLSVEIYDRREYSRFEKE
QQQLNWKQDSNPLYKSAITT
TINPRFQEADSPTL
| Data type | Count |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 39 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | beta7 integrain tail | 1 |
Entities:
Entity 1, beta7 integrain tail 54 residues - 6446 Da.
| 1 | GLY | PRO | ARG | LEU | SER | VAL | GLU | ILE | TYR | ASP | ||||
| 2 | ARG | ARG | GLU | TYR | SER | ARG | PHE | GLU | LYS | GLU | ||||
| 3 | GLN | GLN | GLN | LEU | ASN | TRP | LYS | GLN | ASP | SER | ||||
| 4 | ASN | PRO | LEU | TYR | LYS | SER | ALA | ILE | THR | THR | ||||
| 5 | THR | ILE | ASN | PRO | ARG | PHE | GLN | GLU | ALA | ASP | ||||
| 6 | SER | PRO | THR | LEU |
Samples:
pH_6.1: D2O, [U-2H], 5%; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; beta7 integrin, [U-15N], 0.05 mM; H2O 95%
pH_4.5: D2O, [U-2H], 5%; sodium acetate 20 mM; sodium azide 0.02%; DSS 0.1 mM; beta7 integrin, [U-15N], 0.2 mM; H2O 95%
pH6.1: ionic strength: 200 mM; pH: 6.1; pressure: 1 atm; temperature: 298 K
pH4.5: ionic strength: 10 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | pH_6.1 | isotropic | pH6.1 |
| 3D 1H-15N NOESY | pH_4.5 | isotropic | pH4.5 |
| 3D 1H-15N TOCSY | pH_4.5 | isotropic | pH4.5 |
| 2D 1H-15N HSQC | pH_4.5 | isotropic | pH4.5 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
Omega Spectrometer Operating Software vBeta 6.0.3b2, GE - collection
ANALYSIS, Boucher and Stevens - chemical shift assignment
NMR spectrometers:
- GE OMEGA 600 MHz
- GE OMEGA 950 MHz
Related Database Links:
| PDB | |
| DBJ | BAG10580 BAH12742 |
| GB | AAA36118 AAA59184 AAA59185 AAB21332 AAB23688 |
| REF | NP_000880 XP_001087864 XP_001141622 XP_003831078 XP_004053261 |
| SP | P26010 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts