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 18039

Title: Solution structure ensemble of the two N-terminal apple domains (residues 58-231) of Toxoplasma gondii microneme protein 4   PubMed: 22399295

Deposition date: 2011-11-01 Original release date: 2012-03-09

Authors: Marchant, J.; Cowper, B.; Liu, Y.; Lai, L.; Pinzan, C.; Marq, J.; Friedrich, N.; Sawmynaden, K.; Chai, W.; Childs, R.; Saouros, S.; Simpson, P.; Barreira, M.; Feizi, T.; Soldati-favre, D.; Matthews, Stephen

Citation: Marchant, Jan; Cowper, Ben; Liu, Yan; Lai, Livia; Pinzan, Camila; Marq, Jean Baptiste; Friedrich, Nikolas; Sawmynaden, Kovilen; Liew, Lloyd; Chai, Wengang; Childs, Robert; Saouros, Savvas; Simpson, Peter; Roque Barreira, Maria Cristina; Feizi, Ten; Soldati-Favre, Dominique; Matthews, Stephen. "Galactose recognition by the apicomplexan parasite Toxoplasma gondii."  J. Biol. Chem. 287, 16720-16733 (2012).

Assembly members:
MICRONEMAL_PROTEIN_4, polymer, 161 residues, 17154.4701 Da.

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):
MICRONEMAL_PROTEIN_4: SSEPAKLDLSCVHSDNKGSR APTIGEPVPDVSLEQCAAQC KAVDGCTHFTYNDDSKMCHV KEGKPDLYDLTGGKTASRSC DRSCFEQHVSYEGAPDVMTA MVTSQSADCQAACAADPSCE IFTYNEHDQKCTFKGRGFSA FKERGVLGVTSGPKQFCDEG G

Data sets:
Data typeCount
1H chemical shifts970
13C chemical shifts641
15N chemical shifts161

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MICRONEMAL PROTEIN 41

Entities:

Entity 1, MICRONEMAL PROTEIN 4 161 residues - 17154.4701 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   GLY

Samples:

sample_1: MICRONEMAL PROTEIN 4, [U-13C; U-15N], 0.3 mM

sample_2: MICRONEMAL PROTEIN 4, [U-13C; U-15N], 0.3 mM

sample_conditions_1: ionic strength: 100.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 303.000 K

Experiments:

NameSampleSample stateSample conditions
CBCA(CO)NHsample_1solutionsample_conditions_1
HNCACBsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HN(CA)COsample_1solutionsample_conditions_1
(H)CC(CO)NH-TOCSYsample_1solutionsample_conditions_1
H(C)CH-TOCSYsample_1solutionsample_conditions_1
(H)CCH-TOCSYsample_1solutionsample_conditions_1
C-NOESY-HSQCsample_1solutionsample_conditions_1
N-NOESY-HSQCsample_1solutionsample_conditions_1
C-NOESY-HSQCsample_2solutionsample_conditions_1

Software:

ARIA vany, Linge, O, . - chemical shift assignment

CNS vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN - chemical shift assignment

NMRView vany, Johnson, One Moon Scientific - chemical shift assignment

TALOS vany, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker DRX 500.20 MHz
  • Varian UnityInova 800.23 MHz

Related Database Links:

UNP MIC4_TOXGO
BMRB 15694
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts