BMRB: 7011

Solution structure of 97-109 segment of staphylococcal nuclease

Authors

Wang, M., Shan, L., Wang, J.F.

Assembly

13-mer peptide from Thermonuclease (E.C.3.1.31.1)

Entity

1. 13-mer peptide from Thermonuclease (E.C.3.1.31.1) (polymer, Thiol state: not present), 13 monomers, 1428.698 Da Detail

KMVNEALVRQ GLA

Formula weight

1428.698 Da

Source organism

Staphylococcus aureus

Exptl. method

NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 77.9 %, Completeness (bb): 81.5 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C
All	77.9 % (106 of 136)	78.5 % (62 of 79)	77.2 % (44 of 57)
Backbone	81.5 % (53 of 65)	100.0 % (27 of 27)	68.4 % (26 of 38)
Sidechain	78.3 % (65 of 83)	67.3 % (35 of 52)	96.8 % (30 of 31)
Methyl	85.0 % (17 of 20)	70.0 % (7 of 10)	100.0 % (10 of 10)

1. 13-mer peptide from Thermonuclease (E.C.3.1.31.1)

KMVNEALVRQ GLA

Show sample condition

Sample

Pressure 1 atm, Temperature 298 K, pH 5.0

#	Name	Isotope labeling	Type	Concentration
1	13-mer peptide from Thermonuclease (E.C.3.1.31.1)			2.0 mM
2	DSS			0.02 mM
3	NaN3			0.02 mM
4	trifluoroethanol-d4			40 %
5	H2O			60 %

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Protein Blocks Logo

Calculated from 15 models in PDB: 2FXZ, Strand ID: A Detail

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Release date

2006-09-06

Citation

Two peptide fragments G55-I72 and K97-A109 from staphylococcal nuclease exhibit different behaviors in conformational preferences for helix formation
Wang, M., Shan, L., Wang, J.F.
Biopolymers (2006), 83, 268-279, PubMed 16767771 , DOI 10.1002/bip.20558 , Abstract

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. 13-mer peptide from Thermonuclease (E.C.3.1.31.1), : 1 : 105 entities Detail

Experiments performed 5 experiments Detail