BMRB: 17889

The polyserine tract of Nasonia vitripennis Vg residues 351-385

Authors

Havukainen, H., Halskau, O.

Assembly

NvVg

Entity

1. NvVg (polymer, Thiol state: not present), 35 monomers, 4040.143 Da Detail

EHKHSDESTS ESFESIADNN DDSYFQRKPK LTEAP

Formula weight

4040.143 Da

Source organism

Nasonia vitripennis

Exptl. method

solution NMR

Refine. method

simulated annealing, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 98.8 %, Completeness (bb): 100.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H	15N
All	98.8 % (242 of 245)	98.6 % (206 of 209)	100.0 % (36 of 36)
Backbone	100.0 % (101 of 101)	100.0 % (68 of 68)	100.0 % (33 of 33)
Sidechain	97.9 % (141 of 144)	97.9 % (138 of 141)	100.0 % (3 of 3)
Aromatic	100.0 % (18 of 18)	100.0 % (18 of 18)
Methyl	100.0 % (8 of 8)	100.0 % (8 of 8)

1. NvVg

EHKHSDESTS ESFESIADNN DDSYFQRKPK LTEAP

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	NvVg	[U-15N]-ILE		20 w/v
2	sodium phosphate	natural abundance		50 mM
3	sodium azide	natural abundance		0.02 %
4	H2O	natural abundance		95 %
5	D2O	natural abundance		5 %

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

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Release date

2012-05-21

Citation

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

Related entities 1. NvVg, : 1 : 3 entities Detail

Experiments performed 3 experiments Detail