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 15753

Title: Structure of a Glycosylphosphatidylinositol-anchored Domain from a Trypanosome Variant Surface Glycoprotein   PubMed: 18003615

Deposition date: 2008-05-05 Original release date: 2008-11-12

Authors: Jones, Nicola; Nietlispach, Daniel; Sharma, Reuben; Burke, David; Eyres, Isobel; Mues, Marsilius; Mott, Helen; Carrington, Mark

Citation: Jones, Nicola; Nietlispach, Daniel; Sharma, Reuben; Burke, David; Eyres, Isobel; Mues, Marsilius; Mott, Helen; Carrington, Mark. "Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein"  J. Biol. Chem. 283, 3584-3593 (2008).

Assembly members:
Variant_Surface_Glycoprotein_ILTat1.24, polymer, 46 residues, 5141.820 Da.

Natural source:   Common Name: not available   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Variant_Surface_Glycoprotein_ILTat1.24: GKSPEAECNKITEEPKCSEE KICSWHKEVKAGEKNCQFNS TKASKS

Data sets:
Data typeCount
1H chemical shifts298

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 46 residues - 5141.820 Da.

This is the first C-terminal subdomain of the Variant Surface Glycoprotein ILTat1.24

1   GLYLYSSERPROGLUALAGLUCYSASNLYS
2   ILETHRGLUGLUPROLYSCYSSERGLUGLU
3   LYSILECYSSERTRPHISLYSGLUVALLYS
4   ALAGLYGLULYSASNCYSGLNPHEASNSER
5   THRLYSALASERLYSSER

Samples:

sample_1: ILTat1.24 C1-domain 0.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.05%; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

AZARA, Boucher - processing

ANSIG, Kraulis - data analysis

ARIA, Linge, O, . - structure solution

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
EMBL CAA40086
GB AGH61239
SP P26329