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 15752

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

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, 48 residues, 5141.820 Da.

Natural source:   Common Name: Trypanosoma brucei   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: GTKASKSGVPVTQTQTAGAD TTAEKCKGKGEKDCKSPDCK WEGGTCKD

Data sets:
Data typeCount
1H chemical shifts276

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 48 residues - 5141.820 Da.

Residue G1 represents a residual non-native residue from affinity tag cleavage. This is the second C-terminal subdomain of the Variant Surface Glycoprotein ILTat1.24

1   GLYTHRLYSALASERLYSSERGLYVALPRO
2   VALTHRGLNTHRGLNTHRALAGLYALAASP
3   THRTHRALAGLULYSCYSLYSGLYLYSGLY
4   GLULYSASPCYSLYSSERPROASPCYSLYS
5   TRPGLUGLYGLYTHRCYSLYSASP

Samples:

sample_1: ILTat1.24 C2-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 500 MHz

Related Database Links:

PDB
EMBL CAA39964 CAA40086
SP P26329