BMRB Entry 15694

Title:
Apple Domains 1 and 2 from Toxoplasma gondii microneme protein 4
Deposition date:
2008-03-26
Original release date:
2008-07-08
Authors:
Marchant, Jan; Sawmynaden, Kovilen; Saouros, Savvas; Simpson, Peter; Matthews, Steve
Citation:

Citation: Marchant, Jan; Sawmynaden, Kovilen; Saouros, Savvas; Simpson, Peter; Matthews, Stephen. "Complete resonance assignment of the first and second apple domains of MIC4 from Toxoplasma gondii, using a new NMRView-based assignment aid"  Biomol. NMR Assignments 2, 119-121 (2008).
PubMed: 19636884

Assembly members:

Assembly members:
MIC4_Ap12, polymer, 174 residues, 18711.6 Da.

Natural source:

Natural source:   Common Name: Toxoplasma gondii   Taxonomy ID: 5811   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Toxoplasma gondii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-32 Xa/LIC

Data sets:
Data typeCount
13C chemical shifts649
15N chemical shifts168
1H chemical shifts989

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1

Entities:

Entity 1, protein 174 residues - 18711.6 Da.

1   SERSERGLUPROALALYSLEUASPLEUSER
2   CYSVALHISSERASPASNLYSGLYSERARG
3   ALAPROTHRILEGLYGLUPROVALPROASP
4   VALSERLEUGLUGLNCYSALAALAGLNCYS
5   LYSALAVALASPGLYCYSTHRHISPHETHR
6   TYRASNASPASPSERLYSMETCYSHISVAL
7   LYSGLUGLYLYSPROASPLEUTYRASPLEU
8   THRGLYGLYLYSTHRALASERARGSERCYS
9   ASPARGSERCYSPHEGLUGLNHISVALSER
10   TYRGLUGLYALAPROASPVALMETTHRALA
11   METVALTHRSERGLNSERALAASPCYSGLN
12   ALAALACYSALAALAASPPROSERCYSGLU
13   ILEPHETHRTYRASNGLUHISASPGLNLYS
14   CYSTHRPHELYSGLYARGGLYPHESERALA
15   PHELYSGLUARGGLYVALLEUGLYVALTHR
16   SERGLYPROLYSGLNPHECYSASPGLUGLY
17   GLYLYSLEUTHRGLNGLUGLUMETGLUASP
18   GLNILESERGLY

Samples:

sample_1: MIC4_Ap12, [U-100% 13C; U-100% 15N], 300 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking, structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 18039
PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks