BMRB Entry 51281
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51281
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Title: Salp15 NMR backbone assignment
Deposition date: 2022-01-14 Original release date: 2022-03-22
Authors: Persson, Cecilia; Chaves-Arquero, Belen; Blanco, Francisco
Citation: Belen, Chaves-Arquero; Persson, Cecilia; Merino, Nekane; Tomas-Cortazar, Julen; Rojas, Adriana; Anguita, Juan; Blanco, Francisco. "Structural Analysis of the Black-Legged Tick Saliva Protein Salp15" Int. J. Mol. Sci. 23, 3134-3134 (2022).
Assembly members:
entity_1, polymer, 117 residues, 12668.2 Da.
Natural source: Common Name: black-legged tick Taxonomy ID: 6945 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Ixodes scapularis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHIS-Parallel2
Entity Sequences (FASTA):
entity_1: GAMGESGPTKADASTADKDT
KKNNVQLRFPNYISNHQKLA
LKLLKICKDSKSSHNSLSSR
SSDVINDKYVDFKNCTFLCK
HGNDVNVTLNLPEDTPCGPN
GQTCAEKNKCVGHIPGC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 299 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 96 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | salp15 | 1 |
Entities:
Entity 1, salp15 117 residues - 12668.2 Da.
The initial 4 residues are non-native ones. The first native residue is E5, which corresponds to residue number 23 in the sequence of the full-length protein.
| 1 | GLY | ALA | MET | GLY | GLU | SER | GLY | PRO | THR | LYS | ||||
| 2 | ALA | ASP | ALA | SER | THR | ALA | ASP | LYS | ASP | THR | ||||
| 3 | LYS | LYS | ASN | ASN | VAL | GLN | LEU | ARG | PHE | PRO | ||||
| 4 | ASN | TYR | ILE | SER | ASN | HIS | GLN | LYS | LEU | ALA | ||||
| 5 | LEU | LYS | LEU | LEU | LYS | ILE | CYS | LYS | ASP | SER | ||||
| 6 | LYS | SER | SER | HIS | ASN | SER | LEU | SER | SER | ARG | ||||
| 7 | SER | SER | ASP | VAL | ILE | ASN | ASP | LYS | TYR | VAL | ||||
| 8 | ASP | PHE | LYS | ASN | CYS | THR | PHE | LEU | CYS | LYS | ||||
| 9 | HIS | GLY | ASN | ASP | VAL | ASN | VAL | THR | LEU | ASN | ||||
| 10 | LEU | PRO | GLU | ASP | THR | PRO | CYS | GLY | PRO | ASN | ||||
| 11 | GLY | GLN | THR | CYS | ALA | GLU | LYS | ASN | LYS | CYS | ||||
| 12 | VAL | GLY | HIS | ILE | PRO | GLY | CYS |
Samples:
sample_1: salp15, [U-98% 13C; U-98% 15N], 0.14 ± 0.01 mM; D2O, [U-2H], 5 ± 1 %; H2O 95 ± 1 5; DSS 30 ± 3 uM; sodium phosphate 10 ± 1 mM; sodium azide 0.01 ± 0.001 %; sodium chloride 50 ± 5 mM
sample_conditions_1: ionic strength: 75 mM; pH: 5.5; 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 HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCOCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCOCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts