BMRB Entry 25406
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25406
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NMR-STAR v3 text file.
XML gzip file.
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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:
H56P, polymer, 107 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):
H56P: HHHHHHGSRGIPPKIEALPS
DISIDEGKVLTVACAFTGEP
TPEVTWSCGGRKIHSQEQGR
FPIENTDDLTTLIIMDVQKQ
DGGLYTLSLGNEFGSDSATV
NIHIRSI
- 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 | H56P | 1 |
Entities:
Entity 1, H56P 107 residues - Formula weight is not available
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | GLY | SER | ARG | GLY | ||||
| 2 | ILE | PRO | PRO | LYS | ILE | GLU | ALA | LEU | PRO | SER | ||||
| 3 | ASP | ILE | SER | ILE | ASP | GLU | GLY | LYS | VAL | LEU | ||||
| 4 | THR | VAL | ALA | CYS | ALA | PHE | THR | GLY | GLU | PRO | ||||
| 5 | THR | PRO | GLU | VAL | THR | TRP | SER | CYS | GLY | GLY | ||||
| 6 | ARG | LYS | ILE | HIS | SER | GLN | GLU | GLN | GLY | ARG | ||||
| 7 | PHE | PRO | ILE | GLU | ASN | THR | ASP | ASP | LEU | THR | ||||
| 8 | THR | LEU | ILE | ILE | MET | ASP | VAL | GLN | LYS | GLN | ||||
| 9 | ASP | GLY | GLY | LEU | TYR | THR | LEU | SER | LEU | GLY | ||||
| 10 | ASN | GLU | PHE | GLY | SER | ASP | SER | ALA | THR | VAL | ||||
| 11 | ASN | ILE | HIS | ILE | ARG | SER | ILE |
Samples:
sample_1: H56P, [U-99% 15N], 1 mM; D2O, [U-2H], 10%; sodium phosphate 10 mM; sodim fluoride 50 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment
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