BMRB Entry 18506
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18506
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Saouros, Savvas; Dou, Zhicheng; Henry, Maud; Marchant, Jan; Carruthers, Vern; Matthews, Stephen. "Microneme protein 5 regulates the activity of Toxoplasma subtilisin 1 by mimicking a subtilisin prodomain." J. Biol. Chem. 287, 36029-36040 (2012).
PubMed: 22896704
Assembly members:
Tg_Micronemal_Protein_5, polymer, 29 residues, 8883.205 Da.
Natural source: Common Name: Toxoplasma gondii Taxonomy ID: 5811 Superkingdom: Bacteria Kingdom: not available Genus/species: Toxoplasma gondii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTYB2
Entity Sequences (FASTA):
Tg_Micronemal_Protein_5: CGETCVGGTCNTPGCTCSWP
VCGHFRWGV
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 156 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Tg Micronemal Protein 5 | 1 |
Entities:
Entity 1, Tg Micronemal Protein 5 29 residues - 8883.205 Da.
| 1 | CYS | GLY | GLU | THR | CYS | VAL | GLY | GLY | THR | CYS | ||||
| 2 | ASN | THR | PRO | GLY | CYS | THR | CYS | SER | TRP | PRO | ||||
| 3 | VAL | CYS | GLY | HIS | PHE | ARG | TRP | GLY | VAL |
Samples:
sample_1: Tg Micronemal Protein 5, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 25 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.2; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O'Donoghue and Nilges - refinement, structure solution
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - validation
TOPSPIN, Bruker Biospin - data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Bruker Avance II 800 MHz
- Bruker Avance III 600 MHz
- Varian INOVA 900 MHz