BMRB Entry 16622
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16622
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Title: Bergerac-SH3: frustation induced by stabilizing the folding nucleus PubMed: 21290828
Deposition date: 2009-12-03 Original release date: 2012-08-03
Authors: Khristoforov, Vladimir; Prokhorov, Dmitry; Timchenko, Maria; Kudrevatykh, Yuri; Gushchina, Lyubov; Filimonov, Vladimir; Kutyshenko, Viktor
Citation: Kutyshenko, V.; Gushchina, L.; Khristoforov, V.; Prokhorov, D.; Timchenko, M.; Kudrevatykh, Iu.; Fediukina, D.; Filimonov, V.. "NMR structure and dynamics of the chimeric protein SH3-F2" Mol. Biol. (Mosk). 44, 1064-1074 (2010).
Assembly members:
SHA-D, polymer, 70 residues, 8124.332 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SHA-D: MDETGKELVLALYDYQEKSP
REVTMKKGDILTLLNSTNKD
WWKVEVKATANDKTYERQGF
VPAAYVKKLD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 323 |
15N chemical shifts | 74 |
1H chemical shifts | 501 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SH3 monomer | 1 |
Entities:
Entity 1, SH3 monomer 70 residues - 8124.332 Da.
1 | MET | ASP | GLU | THR | GLY | LYS | GLU | LEU | VAL | LEU | |
2 | ALA | LEU | TYR | ASP | TYR | GLN | GLU | LYS | SER | PRO | |
3 | ARG | GLU | VAL | THR | MET | LYS | LYS | GLY | ASP | ILE | |
4 | LEU | THR | LEU | LEU | ASN | SER | THR | ASN | LYS | ASP | |
5 | TRP | TRP | LYS | VAL | GLU | VAL | LYS | ALA | THR | ALA | |
6 | ASN | ASP | LYS | THR | TYR | GLU | ARG | GLN | GLY | PHE | |
7 | VAL | PRO | ALA | ALA | TYR | VAL | LYS | LYS | LEU | ASP |
Samples:
sample_1: SHA-D, [U-98% 13C; U-98% 15N], 1,5 mM; sodium acetate, [U-99% 2H], 20 mM; sodium azide 0.03%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 20 mM; pH: 3.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY-ali | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY-aro | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY-ali | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY-aro | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
xwinnmr v3.5, Bruker Biospin, Bruker Biospin, Cornilescu, Delaglio and Bax, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich, Koradi, Billeter and Wuthrich - chemical shift assignment, collection, data analysis, dihedral angle prediction, processing, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts