BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18506

Title: MIC5 regulates the activity of Toxoplasma subtilisin 1 by mimicking a subtilisin prodomain   PubMed: 22896704

Deposition date: 2012-06-07 Original release date: 2012-08-21

Authors: Saouros, Savvas; Dou, Zhicheng; Henry, Maud; Marchant, Jan; Carruthers, Vern; Matthews, Stephen

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).

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

Data sets:
Data typeCount
1H chemical shifts156

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tg Micronemal Protein 51

Entities:

Entity 1, Tg Micronemal Protein 5 29 residues - 8883.205 Da.

1   CYSGLYGLUTHRCYSVALGLYGLYTHRCYS
2   ASNTHRPROGLYCYSTHRCYSSERTRPPRO
3   VALCYSGLYHISPHEARGTRPGLYVAL

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D (H)CC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_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

Related Database Links:

BMRB 16235 18536 19611
PDB
GB AAL05477 ACI29319 ADJ17473
PIR A56283
SP P56254 P83938 P85185