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 17888

Title: NMR Structure of the Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392   PubMed: 22573762

Deposition date: 2011-08-29 Original release date: 2012-08-17

Authors: Halskau, Heli; Halskau, Oyvind

Citation: Havukainen, Heli; Underhaug, Jarl; Wolschin, Florian; Amdam, Gro; Halskau, Oyvind. "A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation"  J. Exp. Biol. 215, 1837-1846 (2012).

Assembly members:
Vg, polymer, 35 residues, 3986.349 Da.

Natural source:   Common Name: honey bee   Taxonomy ID: 7460   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Apis mellifera

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
Vg: EKLKQDILNLRTDISTSXSS ISSSEENDFWQPKPT

Data sets:
Data typeCount
1H chemical shifts223

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Polyserine Tract of Apis mellifera Vitellogenin1

Entities:

Entity 1, Polyserine Tract of Apis mellifera Vitellogenin 35 residues - 3986.349 Da.

1   GLULYSLEULYSGLNASPILELEUASNLEU
2   ARGTHRASPILESERTHRSERSEPSERSER
3   ILESERSERSERGLUGLUASNASPPHETRP
4   GLNPROLYSPROTHR

Samples:

sample_1: Vg, [U-15N]-ILE, 7.8 w/v; sodium azide 0.02%; sodium phosphate 50 mM; DSS 5%

sample_conditions_1: ionic strength: 0.06 M; pH: 6.7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O, . - data analysis

NMR spectrometers:

  • Bruker AV600 600 MHz

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