BMRB: 5037

Solution structure of ovispirin-1

Authors

Sawai, M.V., Waring, A.J., Kearney, W.R., McCray, P.B., Forsyth, W.R., Lehrer, R.I., Tack, B.F.

Assembly

OVISPIRIN-1

Entity

1. OVISPIRIN-1 (polymer, Thiol state: not present), 18 monomers, 2262.831 Da Detail

KNLRRIIRKI IHIIKKYG

Formula weight

2262.831 Da

Exptl. method

NMR

Refine. method

simulated annealing, torsion angle dynamics

Data set

assigned_chemical_shifts, coupling_constants

Chem. Shift Complete

Sequence coverage: 94.4 %, Completeness: 89.9 %, Completeness (bb): 91.9 % Detail

Download

• NMR-STAR v3.1 (partial)
• BMRB/XML (partial)
• CSV
• TSV

Polymer type: polypeptide(L)

	Total	1H
All	89.9 % (125 of 139)	89.9 % (125 of 139)
Backbone	91.9 % (34 of 37)	91.9 % (34 of 37)
Sidechain	89.2 % (91 of 102)	89.2 % (91 of 102)
Aromatic	100.0 % (6 of 6)	100.0 % (6 of 6)
Methyl	100.0 % (14 of 14)	100.0 % (14 of 14)

1. OVISPIRIN-1

KNLRRIIRKI IHIIKKYG

Show sample condition

Sample

Pressure 1 atm, Temperature 298 K, pH 6.32

#	Name	Isotope labeling	Type	Concentration
1	OVISPIRIN-1			0.88 mM
2	sodium phosphate buffer			50 mM
3	TFE	[U-2H]		40 %
4	H2O			50 %
5	D2O			10 %

Hide sample codition

Protein Blocks Logo

Calculated from 20 models in PDB: 1HU5, Strand ID: A Detail

---

Coupling constant

8 J values in 1 lists
Field strength (¹H) 500 MHz, Pressure 1 atm, Temperature 298 K, pH 6.32 Detail

---

Pressure 1 atm, Temperature 298 K, pH 6.32

List #1 J-values_set_1, Field strength (¹H) 500 MHz

Release date

2002-09-22

Citation

Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides
Sawai, M.V., Waring, A.J., Kearney, W.R., McCray, P.B., Forsyth, W.R., Lehrer, R.I., Tack, B.F.
Protein Eng. (2002), 15, 225-232, PubMed 11932493 , DOI: , Abstract

Related entities 1. OVISPIRIN-1, : 1 : 2 : 3 entities Detail

Experiments performed 3 experiments Detail