BMRB Entry 25303
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25303
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Title: Titin M10 bound to obscurin ig1 PubMed: 25739468
Deposition date: 2014-10-29 Original release date: 2015-08-25
Authors: Wright, Nathan; Rudloff, Michael; Woosley, Alec
Citation: Rudloff, Michael; Woosley, Alec; Wright, Nathan. "Biophysical characterization of naturally occurring titin M10 mutations" Protein Sci. 24, 946-955 (2015).
Assembly members:
titin_M10, polymer, 101 residues, Formula weight is not available
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: pET24a
Entity Sequences (FASTA):
titin_M10: GSRGIPPKIEALPSDISIDE
GKVLTVACAFTGEPTPEVTW
SCGGRKIHSQEQGRFHIENT
DDLTTLIIMDVQKQDGGLYT
LSLGNEFGSDSATVNIHIRS
I
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 79 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | titin M10 | 1 |
Entities:
Entity 1, titin M10 101 residues - Formula weight is not available
| 1 | GLY | SER | ARG | GLY | ILE | PRO | PRO | LYS | ILE | GLU | ||||
| 2 | ALA | LEU | PRO | SER | ASP | ILE | SER | ILE | ASP | GLU | ||||
| 3 | GLY | LYS | VAL | LEU | THR | VAL | ALA | CYS | ALA | PHE | ||||
| 4 | THR | GLY | GLU | PRO | THR | PRO | GLU | VAL | THR | TRP | ||||
| 5 | SER | CYS | GLY | GLY | ARG | LYS | ILE | HIS | SER | GLN | ||||
| 6 | GLU | GLN | GLY | ARG | PHE | HIS | ILE | GLU | ASN | THR | ||||
| 7 | ASP | ASP | LEU | THR | THR | LEU | ILE | ILE | MET | ASP | ||||
| 8 | VAL | GLN | LYS | GLN | ASP | GLY | GLY | LEU | TYR | THR | ||||
| 9 | LEU | SER | LEU | GLY | ASN | GLU | PHE | GLY | SER | ASP | ||||
| 10 | SER | ALA | THR | VAL | ASN | ILE | HIS | ILE | ARG | SER | ||||
| 11 | ILE |
Samples:
sample_1: titin M10, [U-99% 13C; U-99% 15N], 0.5 – 2.5 mM; Tris 20 mM; NaCl 20 mM; NaN3 0.35 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: .02 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts