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Solution structure of 55-72 segment of staphylococcal nuclease
Authors
Wang, M., Shan, L., Wang, J.F.
Assembly
18-mer peptide from Thermonuclease (E.C.3.1.31.1)
Entity
1. 18-mer peptide from Thermonuclease (E.C.3.1.31.1) (polymer, Thiol state: not present), 18 monomers, 1949.271 Da Detail

GPEASAFTKK MVENAKKI


Formula weight
1949.271 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: 77.4 %, Completeness (bb): 80.7 % Detail

Polymer type: polypeptide(L)

Total1H13C
All77.4 % (151 of 195)82.3 % (93 of 113)70.7 % (58 of 82)
Backbone80.7 % (71 of 88)100.0 % (35 of 35)67.9 % (36 of 53)
Sidechain78.2 % (97 of 124)74.4 % (58 of 78)84.8 % (39 of 46)
Aromatic30.0 % (3 of 10)60.0 % (3 of 5) 0.0 % (0 of 5)
Methyl87.5 % (14 of 16)87.5 % (7 of 8)87.5 % (7 of 8)

1. 18-mer peptide from Thermonuclease (E.C.3.1.31.1)

GPEASAFTKK MVENAKKI

Sample

Pressure 1 atm, Temperature 298 K, pH 5.0


#NameIsotope labelingTypeConcentration
118-mer peptide from Thermonuclease (E.C.3.1.31.1)2.0 mM
2DSS0.02 mM
3NaN30.01 mM
4trifluoroethanol-d440 %
5H2O60 %

Protein Blocks Logo
Calculated from 15 models in PDB: 2FXY, Strand ID: A Detail


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 ,
Related entities 1. 18-mer peptide from Thermonuclease (E.C.3.1.31.1), : 1 : 103 : 1 entities Detail
Keywords SNase(55-72), solution structure