BMRB Entry 30500
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30500
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Title: Structure of a protein complex
Deposition date: 2018-07-20 Original release date: 2019-11-12
Authors: Buel, G.; Walters, K.
Citation: Buel, G.; Walters, K.. "Structure of a protein complex" . ., .-..
Assembly members:
entity_1, polymer, 87 residues, 9991.648 Da.
entity_2, polymer, 24 residues, 2373.528 Da.
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
Entity Sequences (FASTA):
entity_1: GPLGSRPKMTPEQMAKEMSE
FLSRGPAVLATKAAAGTKKY
DLSKWKYAELRDTINTSCDI
ELLAACREEFHRRLKVYHAW
KSKNKKR
entity_2: GPLGSPEFIENDEAFAILDG
GAPG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 431 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 713 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 87 residues - 9991.648 Da.
| 1 | GLY | PRO | LEU | GLY | SER | ARG | PRO | LYS | MET | THR | ||||
| 2 | PRO | GLU | GLN | MET | ALA | LYS | GLU | MET | SER | GLU | ||||
| 3 | PHE | LEU | SER | ARG | GLY | PRO | ALA | VAL | LEU | ALA | ||||
| 4 | THR | LYS | ALA | ALA | ALA | GLY | THR | LYS | LYS | TYR | ||||
| 5 | ASP | LEU | SER | LYS | TRP | LYS | TYR | ALA | GLU | LEU | ||||
| 6 | ARG | ASP | THR | ILE | ASN | THR | SER | CYS | ASP | ILE | ||||
| 7 | GLU | LEU | LEU | ALA | ALA | CYS | ARG | GLU | GLU | PHE | ||||
| 8 | HIS | ARG | ARG | LEU | LYS | VAL | TYR | HIS | ALA | TRP | ||||
| 9 | LYS | SER | LYS | ASN | LYS | LYS | ARG |
Entity 2, entity_2 24 residues - 2373.528 Da.
| 1 | GLY | PRO | LEU | GLY | SER | PRO | GLU | PHE | ILE | GLU | ||||
| 2 | ASN | ASP | GLU | ALA | PHE | ALA | ILE | LEU | ASP | GLY | ||||
| 3 | GLY | ALA | PRO | GLY |
Samples:
sample_1: Myosin VI 1050-1131, [U-13C; U-15N], 0.36 mM; Clathrin Light Chain Alpha 46-61 0.36 mM; NaCl 50 mM; NaPO4 20 mM
sample_2: Myosin VI 1050-1131 0.4 mM; Clathrin Light Chain Alpha 46-61, [U-13C; U-15N], 0.4 mM; NaCl 50 mM; NaPO4 20 mM
sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 760 mmHg; temperature: 283.2 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 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| half-filtered 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| half-filtered 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment, peak picking
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AvanceIII 850 MHz
- Bruker AvanceIII 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts