BMRB: 5034

Solution structure of novispirin-2

Authors

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

Assembly

NOVISPIRIN-2

Entity

1. NOVISPIRIN-2 (polymer, Thiol state: not present), 18 monomers, 2250.777 Da Detail

KNLRRITRKI IHIIKKYG

Formula weight

2250.777 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: 89.7 %, Completeness (bb): 91.9 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	89.7 % (122 of 136)	89.7 % (122 of 136)
Backbone	91.9 % (34 of 37)	91.9 % (34 of 37)
Sidechain	88.9 % (88 of 99)	88.9 % (88 of 99)
Aromatic	100.0 % (6 of 6)	100.0 % (6 of 6)
Methyl	100.0 % (13 of 13)	100.0 % (13 of 13)

1. NOVISPIRIN-2

KNLRRITRKI IHIIKKYG

Show sample condition

Sample

Pressure 1 atm, Temperature 298 K, pH 6.38

#	Name	Isotope labeling	Type	Concentration
1	NOVISPIRIN-2			1.89 mM
2	sodium phosphate buffer			50 mM
3	TFE	[U-2H]		40 %
4	H2O			50 %
5	D2O			10 %

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Calculated from 20 models in PDB: 1HU7, Strand ID: A Detail

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Coupling constant

7 J values in 1 lists
Field strength (¹H) 500 MHz, Pressure 1 atm, Temperature 298 K, pH 6.38 Detail

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Pressure 1 atm, Temperature 298 K, pH 6.38

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. NOVISPIRIN-2, : 1 : 1 : 5 entities Detail

Experiments performed 3 experiments Detail