BMRB Entry 50309
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50309
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Citation: Rajak, Manoj; Sundd, Monica. "Chemical shift assignments of the biotin carboxyl carrier protein domain of L. major Methylcrotonyl-CoA carboxylase" Biomol. NMR Assignments 15, 249-253 (2021).
PubMed: 33751378
Assembly members:
entity_1, polymer, 87 residues, Formula weight is not available
Natural source: Common Name: Leishmania major Taxonomy ID: 5664 Superkingdom: Eukaryota Kingdom: not available Genus/species: Leishmania major
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity_1: MLTDGFGDASMAGGTSAKIV
SPMPGKVSKFLVNSGDFVEK
GQALMIVEAMKMEHPVKALQ
DGQVSFLVKEGEVVGSDHVL
ATVVQKE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 280 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 492 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Methylcrotonyl-CoA carboxylase's BCCP domain | 1 |
Entities:
Entity 1, Methylcrotonyl-CoA carboxylase's BCCP domain 87 residues - Formula weight is not available
| 1 | MET | LEU | THR | ASP | GLY | PHE | GLY | ASP | ALA | SER | ||||
| 2 | MET | ALA | GLY | GLY | THR | SER | ALA | LYS | ILE | VAL | ||||
| 3 | SER | PRO | MET | PRO | GLY | LYS | VAL | SER | LYS | PHE | ||||
| 4 | LEU | VAL | ASN | SER | GLY | ASP | PHE | VAL | GLU | LYS | ||||
| 5 | GLY | GLN | ALA | LEU | MET | ILE | VAL | GLU | ALA | MET | ||||
| 6 | LYS | MET | GLU | HIS | PRO | VAL | LYS | ALA | LEU | GLN | ||||
| 7 | ASP | GLY | GLN | VAL | SER | PHE | LEU | VAL | LYS | GLU | ||||
| 8 | GLY | GLU | VAL | VAL | GLY | SER | ASP | HIS | VAL | LEU | ||||
| 9 | ALA | THR | VAL | VAL | GLN | LYS | GLU |
Samples:
sample_1: Methylcrotonyl-CoA carboxylase's BCCP domain, [U-99% 13C; U-99% 15N], 650 uM; Tris HCl buffer 20 mM; soduim chloride 100 mM
sample_conditions_1: ionic strength: 0.2 M; pH: 8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D HSQC C13 | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CBCACO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 3D N15-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCCONH | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCE | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY - chemical shift assignment
CARA - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| NCBI | 5654253 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks