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 15685

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

Data sets:
Data typeCount
13C chemical shifts764
15N chemical shifts180
1H chemical shifts1169

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Epidermal Growth Factor-like domain 21
2Galectin-like domain (MIC1)2

Entities:

Entity 1, Epidermal Growth Factor-like domain 2 61 residues - 6362.06 Da.

1   METALAASNPHEVALGLNLEUSERGLUTHR
2   PROALAALACYSSERSERASNPROCYSGLY
3   PROGLUALAALAGLYTHRCYSLYSGLUTHR
4   ASNSERGLYTYRILECYSARGCYSASNGLN
5   GLYTYRARGILESERLEUASPGLYTHRGLY
6   ASNVALTHRCYSILEVALARGGLNGLUSER
7   GLY

Entity 2, Galectin-like domain (MIC1) 138 residues - Formula weight is not available

1   METLYSTHRGLUILEHISGLYASPSERTHR
2   LYSALATHRLEUGLUGLUGLYGLNGLNLEU
3   THRLEUTHRPHEILESERTHRLYSLEUASP
4   VALALAVALGLYSERCYSHISSERLEUVAL
5   ALAASNPHELEUASPGLYPHELEULYSPHE
6   GLNTHRGLYSERASNSERALAPHEASPVAL
7   VALGLUVALGLUGLUPROALAGLYPROALA
8   VALLEUTHRILEGLYLEUGLYHISLYSGLY
9   ARGLEUALAVALVALLEUASPTYRTHRARG
10   LEUASNALAALALEUGLYSERALAALATYR
11   VALVALGLUASPSERGLYCYSSERSERSER
12   GLUGLUVALSERPHEGLNGLYVALGLYSER
13   GLYALATHRLEUVALVALTHRTHRLEUGLY
14   GLUSERPROTHRALAVALSERALA

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_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