BMRB Entry 16514
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16514
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Title: NMR chemical shifts of soluble synaptobrevin (1-96) in buffer and in DPC micelle PubMed: 19918058
Deposition date: 2009-09-23 Original release date: 2009-11-20
Authors: Ellena, Jeffrey; Liang, Binyong; Wiktor, Maciej; Stein, Alexander; Cafiso, David; Jahn, Reinhard; Tamm, Lukas
Citation: Ellena, Jeffrey; Liang, Binyong; Wiktor, Maciej; Stein, Alexander; Cafiso, David; Jahn, Reinhard; Tamm, Lukas. "Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation." Proc. Natl. Acad. Sci. U.S.A. 106, 20306-20311 (2009).
Assembly members:
syb96, polymer, 96 residues, Formula weight is not available
Natural source: Common Name: Norway Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
syb96: MSATAATVPPAAPAGEGGPP
APPPNLTSNRRLQQTQAQVD
EVVDIMRVNVDKVLERDQKL
SELDDRADALQAGASQFETS
AAKLKRKYWWKNLKMM
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 543 |
| 15N chemical shifts | 174 |
| 1H chemical shifts | 174 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | syb96 | 1 |
Entities:
Entity 1, syb96 96 residues - Formula weight is not available
| 1 | MET | SER | ALA | THR | ALA | ALA | THR | VAL | PRO | PRO | ||||
| 2 | ALA | ALA | PRO | ALA | GLY | GLU | GLY | GLY | PRO | PRO | ||||
| 3 | ALA | PRO | PRO | PRO | ASN | LEU | THR | SER | ASN | ARG | ||||
| 4 | ARG | LEU | GLN | GLN | THR | GLN | ALA | GLN | VAL | ASP | ||||
| 5 | GLU | VAL | VAL | ASP | ILE | MET | ARG | VAL | ASN | VAL | ||||
| 6 | ASP | LYS | VAL | LEU | GLU | ARG | ASP | GLN | LYS | LEU | ||||
| 7 | SER | GLU | LEU | ASP | ASP | ARG | ALA | ASP | ALA | LEU | ||||
| 8 | GLN | ALA | GLY | ALA | SER | GLN | PHE | GLU | THR | SER | ||||
| 9 | ALA | ALA | LYS | LEU | LYS | ARG | LYS | TYR | TRP | TRP | ||||
| 10 | LYS | ASN | LEU | LYS | MET | MET |
Samples:
sample_1: syb96, [U-99% 13C; U-99% 15N], 0.2 mM; potassium phosphate 60 mM; NaCl 300 mM; DTT 5 mM; EDTA 1 mM; H2O 95%; D2O 5%
sample_2: syb96, [U-99% 13C; U-99% 15N], 0.5 mM; DPC 300 mM; potassium phosphate 60 mM; NaCl 300 mM; DTT 5 mM; EDTA 1 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 300 mM; pH: 6.1; pressure: 1 atm; temperature: 291 K
sample_conditions_2: ionic strength: 300 mM; pH: 6.1; pressure: 1 atm; temperature: 318 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_2 |
Software:
SPARKY, Goddard - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 16508 4272 |
| PDB | |
| DBJ | BAC41125 BAE90084 BAF82244 BAG73857 |
| EMBL | CAA12385 CAA53792 CAB43509 CDQ77958 |
| GB | AAA42321 AAA60604 AAB03463 AAB62931 AAB88138 |
| REF | NP_001027992 NP_001034578 NP_001080944 NP_001088233 NP_001272142 |
| SP | P47193 P63026 P63027 P63044 P63045 |
| TPG | DAA18807 |
| AlphaFold | P63044 P47193 P63045 P63026 P63027 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts