BMRB: 17888

NMR Structure of the Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392

Authors

Halskau, H., Halskau, O.

Assembly

Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392

Entity

1. Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392 (polymer, Thiol state: not present), 35 monomers, 4062.255 Da Detail

EKLKQDILNL RTDISTSXSS ISSSEENDFW QPKPT

Formula weight

4062.255 Da

Source organism

Apis mellifera

Exptl. method

solution NMR

Refine. method

simulated annealing, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 91.4 %, Completeness: 89.2 %, Completeness (bb): 93.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	89.2 % (189 of 212)	89.2 % (189 of 212)
Backbone	93.9 % (62 of 66)	93.9 % (62 of 66)
Sidechain	87.0 % (127 of 146)	87.0 % (127 of 146)
Aromatic	90.9 % (10 of 11)	90.9 % (10 of 11)
Methyl	100.0 % (15 of 15)	100.0 % (15 of 15)

1. Vg

EKLKQDILNL RTDISTSXSS ISSSEENDFW QPKPT

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 273 K, pH 6.7

#	Name	Isotope labeling	Type	Concentration
1	Vg	[U-15N]-ILE		7.8 w/v
2	sodium azide	natural abundance		0.02 %
3	sodium phosphate	natural abundance		50 mM
4	DSS	natural abundance		5 %

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Calculated from 20 models in PDB: 2LIC, Strand ID: A Detail

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Release date

2012-08-16

Citation

A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation
Havukainen, H., Underhaug, J., Wolschin, F., Amdam, G.V., Halskau, O.
J. Exp. Biol. (2012), 215, 1837-1846, PubMed 22573762 , DOI 10.1242/jeb.065623 , Abstract

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392, : 1 : 5 entities Detail

Experiments performed 3 experiments Detail