BMRB Entry 51960
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51960
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Title: 1H, 13C and 15N backbone and side-chain resonance assignments of BMSA1 PubMed: 37452919
Deposition date: 2023-05-11 Original release date: 2023-08-30
Authors: Mouhand, Assia; Pissarra, Joana; Delbecq, Stephane; Roumestand, Christian; Barthe, Philippe
Citation: Mouhand, Assia; Pissarra, Joana; Delbecq, Stephane; Roumestand, Christian; Barthe, Philippe. "1H, 13C and 15N backbone and side-chain resonance assignments of BmSA1, the surface antigen of Babesia microti" Biomol. NMR Assign. 17, 217-221 (2023).
Assembly members:
entity_1, polymer, 254 residues, Formula weight is not available
Natural source: Common Name: Babesia microti Taxonomy ID: 5868 Superkingdom: Eukaryota Kingdom: not available Genus/species: Babesia microti
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pDB-his-TEV
Entity Sequences (FASTA):
entity_1: GHMQPNNESKKKAVKLDLDL
MKETKNVCTTVNTKLVGKAK
SKLNKLEGESHKEYVAEKTK
EIDEKNKKFNENLVKIEKRK
KIKVPADTGAEVDAVDDGVA
GALSDLSSDISAIKTLTDDV
SEKVSENLKDDEASATEHTD
IKEKATLLQESCNGIGTILD
KLAEYLNNDTTQNIKKEFDE
RKKNLTSLKTKVENKDEDYV
THFRDMATEAQNAVGEVKKA
IDAVVAHRKAENLDVDDTLF
SNLSTLLDTIIETS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 748 |
15N chemical shifts | 272 |
1H chemical shifts | 1714 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | BmSA1 | 1 |
Entities:
Entity 1, BmSA1 254 residues - Formula weight is not available
1 | GLY | HIS | MET | GLN | PRO | ASN | ASN | GLU | SER | LYS | ||||
2 | LYS | LYS | ALA | VAL | LYS | LEU | ASP | LEU | ASP | LEU | ||||
3 | MET | LYS | GLU | THR | LYS | ASN | VAL | CYS | THR | THR | ||||
4 | VAL | ASN | THR | LYS | LEU | VAL | GLY | LYS | ALA | LYS | ||||
5 | SER | LYS | LEU | ASN | LYS | LEU | GLU | GLY | GLU | SER | ||||
6 | HIS | LYS | GLU | TYR | VAL | ALA | GLU | LYS | THR | LYS | ||||
7 | GLU | ILE | ASP | GLU | LYS | ASN | LYS | LYS | PHE | ASN | ||||
8 | GLU | ASN | LEU | VAL | LYS | ILE | GLU | LYS | ARG | LYS | ||||
9 | LYS | ILE | LYS | VAL | PRO | ALA | ASP | THR | GLY | ALA | ||||
10 | GLU | VAL | ASP | ALA | VAL | ASP | ASP | GLY | VAL | ALA | ||||
11 | GLY | ALA | LEU | SER | ASP | LEU | SER | SER | ASP | ILE | ||||
12 | SER | ALA | ILE | LYS | THR | LEU | THR | ASP | ASP | VAL | ||||
13 | SER | GLU | LYS | VAL | SER | GLU | ASN | LEU | LYS | ASP | ||||
14 | ASP | GLU | ALA | SER | ALA | THR | GLU | HIS | THR | ASP | ||||
15 | ILE | LYS | GLU | LYS | ALA | THR | LEU | LEU | GLN | GLU | ||||
16 | SER | CYS | ASN | GLY | ILE | GLY | THR | ILE | LEU | ASP | ||||
17 | LYS | LEU | ALA | GLU | TYR | LEU | ASN | ASN | ASP | THR | ||||
18 | THR | GLN | ASN | ILE | LYS | LYS | GLU | PHE | ASP | GLU | ||||
19 | ARG | LYS | LYS | ASN | LEU | THR | SER | LEU | LYS | THR | ||||
20 | LYS | VAL | GLU | ASN | LYS | ASP | GLU | ASP | TYR | VAL | ||||
21 | THR | HIS | PHE | ARG | ASP | MET | ALA | THR | GLU | ALA | ||||
22 | GLN | ASN | ALA | VAL | GLY | GLU | VAL | LYS | LYS | ALA | ||||
23 | ILE | ASP | ALA | VAL | VAL | ALA | HIS | ARG | LYS | ALA | ||||
24 | GLU | ASN | LEU | ASP | VAL | ASP | ASP | THR | LEU | PHE | ||||
25 | SER | ASN | LEU | SER | THR | LEU | LEU | ASP | THR | ILE | ||||
26 | ILE | GLU | THR | SER |
Samples:
sample_1: BmSA1, [U-100% 15N], 0.9 mM; sodium phosphate 20 mM; sodium chloride 50 mM
sample_2: BmSA1, [U-100% 13C; U-100% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM
sample_3: BmSA1, [U-100% 15N], 0.9 mM; sodium phosphate 20 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.2; pressure: 1 atm; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_3 | isotropic | sample_conditions_1 |
3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
3D HNCO | sample_3 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
Software:
CINDY v2.1 - 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