BMRB Entry 51258
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51258
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Title: Backbone and sidechain assignments of Actophorin protein from Entamoeba histolytica PubMed: 35281106
Deposition date: 2022-01-05 Original release date: 2022-01-14
Authors: Aggarwal, Priyanka; Kumar, Nitesh; Samudrala, Gourinath; Bhavesh, Neel
Citation: Kumar, Nitesh; Rath, Pragyan Parimita; Aggarwal, Priyanka; Maiti, Sankar; Bhavesh, Neel Sarovar; Gourinath, Samudrala. "Unravelling the Biology of EhActo as the First Cofilin From Entamoeba histolytica" Front. Cell Dev. Biol. 10, 785680-785680 (2022).
Assembly members:
entity_1, polymer, 146 residues, Formula weight is not available
Natural source: Common Name: Entamoeba histolytica Taxonomy ID: 5759 Superkingdom: Eukaryota Kingdom: not available Genus/species: Entamoeba histolytica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
Entity Sequences (FASTA):
entity_1: MAMAGIQLADEVTSVYNDFK
LSHKYRYIVFKMNDGMTEVV
VEKTAEKNATYDDFLKDLPE
KSARYAVYDLEYDTPEGLRQ
KIIFYLWTPEGCKIREKMLY
SATKATIKQALVGLSAEIQA
TDAGELNLDEVIAKVKTILE
HHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 534 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 130 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Actophorin | 1 |
Entities:
Entity 1, Actophorin 146 residues - Formula weight is not available
| 1 | MET | ALA | MET | ALA | GLY | ILE | GLN | LEU | ALA | ASP | ||||
| 2 | GLU | VAL | THR | SER | VAL | TYR | ASN | ASP | PHE | LYS | ||||
| 3 | LEU | SER | HIS | LYS | TYR | ARG | TYR | ILE | VAL | PHE | ||||
| 4 | LYS | MET | ASN | ASP | GLY | MET | THR | GLU | VAL | VAL | ||||
| 5 | VAL | GLU | LYS | THR | ALA | GLU | LYS | ASN | ALA | THR | ||||
| 6 | TYR | ASP | ASP | PHE | LEU | LYS | ASP | LEU | PRO | GLU | ||||
| 7 | LYS | SER | ALA | ARG | TYR | ALA | VAL | TYR | ASP | LEU | ||||
| 8 | GLU | TYR | ASP | THR | PRO | GLU | GLY | LEU | ARG | GLN | ||||
| 9 | LYS | ILE | ILE | PHE | TYR | LEU | TRP | THR | PRO | GLU | ||||
| 10 | GLY | CYS | LYS | ILE | ARG | GLU | LYS | MET | LEU | TYR | ||||
| 11 | SER | ALA | THR | LYS | ALA | THR | ILE | LYS | GLN | ALA | ||||
| 12 | LEU | VAL | GLY | LEU | SER | ALA | GLU | ILE | GLN | ALA | ||||
| 13 | THR | ASP | ALA | GLY | GLU | LEU | ASN | LEU | ASP | GLU | ||||
| 14 | VAL | ILE | ALA | LYS | VAL | LYS | THR | ILE | LEU | GLU | ||||
| 15 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Actophorin, [U-99% 13C; U-99% 15N], 1 ± 0.01 mM; sodium phosphate 10 mM; potassium phosphate 1.8 mM; NaCl 60 mM; KCl 2.7 mM
sample_conditions_1: ionic strength: 60 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.5pl6 - collection, processing
CARA - chemical shift assignment, data analysis
CS-Rosetta - structure solution
NMR spectrometers:
- Bruker AVANCE III 500.15 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts