BMRB Entry 25304
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25304
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Citation: Rudloff, Michael; Woosley, Alec; Wright, Nathan. "Biophysical characterization of naturally occurring titin M10 mutations" Protein Sci. 24, 946-955 (2015).
PubMed: 25739468
Assembly members:
Ig1_bound_to_M10, polymer, 112 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):
Ig1_bound_to_M10: MDQPQFSGAPRFLTRPKAFV
VSVGKDATLSCQIVGNPTPQ
VSWEKDQQPVTAGARFRLAQ
DGDLYRLTILDLALGDSGQY
VCRARNAIGEAFAAVGLQVD
AEAALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 76 |
| 1H chemical shifts | 76 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ig1 | 1 |
Entities:
Entity 1, Ig1 112 residues - Formula weight is not available
| 1 | MET | ASP | GLN | PRO | GLN | PHE | SER | GLY | ALA | PRO | ||||
| 2 | ARG | PHE | LEU | THR | ARG | PRO | LYS | ALA | PHE | VAL | ||||
| 3 | VAL | SER | VAL | GLY | LYS | ASP | ALA | THR | LEU | SER | ||||
| 4 | CYS | GLN | ILE | VAL | GLY | ASN | PRO | THR | PRO | GLN | ||||
| 5 | VAL | SER | TRP | GLU | LYS | ASP | GLN | GLN | PRO | VAL | ||||
| 6 | THR | ALA | GLY | ALA | ARG | PHE | ARG | LEU | ALA | GLN | ||||
| 7 | ASP | GLY | ASP | LEU | TYR | ARG | LEU | THR | ILE | LEU | ||||
| 8 | ASP | LEU | ALA | LEU | GLY | ASP | SER | GLY | GLN | TYR | ||||
| 9 | VAL | CYS | ARG | ALA | ARG | ASN | ALA | ILE | GLY | GLU | ||||
| 10 | ALA | PHE | ALA | ALA | VAL | GLY | LEU | GLN | VAL | ASP | ||||
| 11 | ALA | GLU | ALA | ALA | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 12 | HIS | HIS |
Samples:
sample_1: Ig1 bound to 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | 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 peaks
SPARKY: Backbone
or all simulated peaks