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 34055

Title: C-terminal domain structure of VSG M1.1   PubMed: 28894098

Authors: Jones, N.; Mott, H.; Carrington, M.

Citation: Bartossek, Thomas; Jones, Nicola; Schafer, Christin; Cvitkovic, Mislav; Glogger, Marius; Mott, Helen; Kuper, Jochen; Brennich, Martha; Carrington, Mark; Smith, Ana-Suncana; Fenz, Susanne; Kisker, Caroline; Engstler, Markus. "Structural basis for the shielding function of the dynamic trypanosome variant surface glycoprotein coat"  Nat. Microbiol. ., .-. (2017).

Assembly members:
Variant surface glycoprotein MITAT 1.1, polymer, 73 residues, 8156.062 Da.

Natural source:   Common Name: kinetoplastids   Taxonomy ID: 5702   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 MITAT 1.1: GSKKQQTESAENKEKICNAA KDNQKACENLKEKGCVFNTE SNKCELKKDVKEKLEKESKE TEGKDEKANTTGS

Data sets:
Data typeCount
15N chemical shifts81
1H chemical shifts490

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 73 residues - 8156.062 Da.

1   GLYSERLYSLYSGLNGLNTHRGLUSERALA
2   GLUASNLYSGLULYSILECYSASNALAALA
3   LYSASPASNGLNLYSALACYSGLUASNLEU
4   LYSGLULYSGLYCYSVALPHEASNTHRGLU
5   SERASNLYSCYSGLULEULYSLYSASPVAL
6   LYSGLULYSLEUGLULYSGLUSERLYSGLU
7   THRGLUGLYLYSASPGLULYSALAASNTHR
8   THRGLYSER

Samples:

sample_1: Variant surface glycoprotein MITat1.1, [U-15N], 0.5 mM; sodium chloride 150 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%

sample_2: Variant surface glycoprotein MITat1.1 0.5 mM; sodium chloride 150 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 200 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

ANSIG, Kraulis - chemical shift assignment

AZARA, Boucher - processing

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

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