Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27626
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NMR-STAR v3 text file.
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Citation: Batchelor, Matthew; Wolny, Marcin; Baker, Emily; Paci, Emanuele; Kalverda, Arnout; Peckham, Michelle. "Dynamic ion pair behavior stabilizes single alpha-helices in proteins" J. Biol. Chem. 294, 3219-3234 (2019).
PubMed: 30593502
Assembly members:
M7A_SAH, polymer, 80 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
M7A_SAH: SRLRVEYQRRLEAERMRLAE
EEKLRKEMSAKKAKEEAERK
HQERLAQLAREDAERELKEK
EEARRKKELLEQMEKARHEW
Data type | Count |
13C chemical shifts | 391 |
15N chemical shifts | 83 |
1H chemical shifts | 552 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | M7A SAH, 1 | 1 |
2 | M7A SAH, 2 | 1 |
Entity 1, M7A SAH, 1 80 residues - Formula weight is not available
1 | SER | ARG | LEU | ARG | VAL | GLU | TYR | GLN | ARG | ARG | |
2 | LEU | GLU | ALA | GLU | ARG | MET | ARG | LEU | ALA | GLU | |
3 | GLU | GLU | LYS | LEU | ARG | LYS | GLU | MET | SER | ALA | |
4 | LYS | LYS | ALA | LYS | GLU | GLU | ALA | GLU | ARG | LYS | |
5 | HIS | GLN | GLU | ARG | LEU | ALA | GLN | LEU | ALA | ARG | |
6 | GLU | ASP | ALA | GLU | ARG | GLU | LEU | LYS | GLU | LYS | |
7 | GLU | GLU | ALA | ARG | ARG | LYS | LYS | GLU | LEU | LEU | |
8 | GLU | GLN | MET | GLU | LYS | ALA | ARG | HIS | GLU | TRP |
sample_1: M7A SAH, [U-100% 13C; U-100% 15N], 0.4 mM
sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 23.4 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D H(C)CH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
3D HCACO | sample_1 | isotropic | sample_conditions_1 |
3D (HC)CO(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Analysis, CCPN - chemical shift assignment, peak picking
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks