BMRB Entry 15685
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15685
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Title: Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for the complex of Epidermal Growth Factor-like 2 domain from Microneme Protein 6 (Toxoplasma gondii) with the Galectin-like domain of Microneme protein 1 PubMed: 19636901
Deposition date: 2008-03-17 Original release date: 2008-10-03
Authors: Sawmynaden, Kovilen; Saouros, Savvas; Marchant, Jan; Simpson, Peter; Matthews, Stephen
Citation: Sawmynaden, Kovilen; Saouros, Savvas; Marchant, Jan; Simpson, Peter; Matthews, Stephen. "Complete NMR assignments for the second EGF domain of MIC6 from Toxoplasma gondii and re-assignment in complex with the galectin-like domain of MIC1" Biomol. NMR Assignments 2, 187-189 (2008).
Assembly members:
Epidermal_Growth_Factor-like_domain_2, polymer, 61 residues, 6362.06 Da.
Microneme_Protein_6, polymer, 138 residues, Formula weight is not available
Natural source: Common Name: Toxoplasma gondii Taxonomy ID: 5811 Superkingdom: Eukaryota Kingdom: not available Genus/species: Toxoplasma gondii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Epidermal_Growth_Factor-like_domain_2: MANFVQLSETPAACSSNPCG
PEAAGTCKETNSGYICRCNQ
GYRISLDGTGNVTCIVRQES
G
Microneme_Protein_6: MKTEIHGDSTKATLEEGQQL
TLTFISTKLDVAVGSCHSLV
ANFLDGFLKFQTGSNSAFDV
VEVEEPAGPAVLTIGLGHKG
RLAVVLDYTRLNAALGSAAY
VVEDSGCSSSEEVSFQGVGS
GATLVVTTLGESPTAVSA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 764 |
| 15N chemical shifts | 180 |
| 1H chemical shifts | 1169 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Epidermal Growth Factor-like domain 2 | 1 |
| 2 | Galectin-like domain (MIC1) | 2 |
Entities:
Entity 1, Epidermal Growth Factor-like domain 2 61 residues - 6362.06 Da.
| 1 | MET | ALA | ASN | PHE | VAL | GLN | LEU | SER | GLU | THR | ||||
| 2 | PRO | ALA | ALA | CYS | SER | SER | ASN | PRO | CYS | GLY | ||||
| 3 | PRO | GLU | ALA | ALA | GLY | THR | CYS | LYS | GLU | THR | ||||
| 4 | ASN | SER | GLY | TYR | ILE | CYS | ARG | CYS | ASN | GLN | ||||
| 5 | GLY | TYR | ARG | ILE | SER | LEU | ASP | GLY | THR | GLY | ||||
| 6 | ASN | VAL | THR | CYS | ILE | VAL | ARG | GLN | GLU | SER | ||||
| 7 | GLY |
Entity 2, Galectin-like domain (MIC1) 138 residues - Formula weight is not available
| 1 | MET | LYS | THR | GLU | ILE | HIS | GLY | ASP | SER | THR | ||||
| 2 | LYS | ALA | THR | LEU | GLU | GLU | GLY | GLN | GLN | LEU | ||||
| 3 | THR | LEU | THR | PHE | ILE | SER | THR | LYS | LEU | ASP | ||||
| 4 | VAL | ALA | VAL | GLY | SER | CYS | HIS | SER | LEU | VAL | ||||
| 5 | ALA | ASN | PHE | LEU | ASP | GLY | PHE | LEU | LYS | PHE | ||||
| 6 | GLN | THR | GLY | SER | ASN | SER | ALA | PHE | ASP | VAL | ||||
| 7 | VAL | GLU | VAL | GLU | GLU | PRO | ALA | GLY | PRO | ALA | ||||
| 8 | VAL | LEU | THR | ILE | GLY | LEU | GLY | HIS | LYS | GLY | ||||
| 9 | ARG | LEU | ALA | VAL | VAL | LEU | ASP | TYR | THR | ARG | ||||
| 10 | LEU | ASN | ALA | ALA | LEU | GLY | SER | ALA | ALA | TYR | ||||
| 11 | VAL | VAL | GLU | ASP | SER | GLY | CYS | SER | SER | SER | ||||
| 12 | GLU | GLU | VAL | SER | PHE | GLN | GLY | VAL | GLY | SER | ||||
| 13 | GLY | ALA | THR | LEU | VAL | VAL | THR | THR | LEU | GLY | ||||
| 14 | GLU | SER | PRO | THR | ALA | VAL | SER | ALA |
Samples:
sample_1: Epidermal Growth Factor-like domain 2 0.5 mM; Galectin-like domain (MIC1) 0.5 mM; potassium phosphate 25 mM; sodium chloride 50 mM
sample_2: Epidermal Growth Factor-like domain 2, [U-100% 13C; U-100% 15N], 1-1.3 mM; Galectin-like domain (MIC1) 0.5 mM; potassium phosphate 25 mM; sodium chloride 50 mM
sample_conditions_1: pH: 6.8; temperature: 308 K
sample_conditions_2: ionic strength: 0.1 M; pH: 6.9; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_2 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_2 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker DRX 500 MHz
Related Database Links:
| BMRB | 15682 15692 6376 |
| PDB | |
| EMBL | CAA96466 |
| GB | EPR59679 EPT28103 ESS33997 KFG30856 KFG41657 |
| REF | XP_002368531 |
| SP | O00834 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts