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The solution NMR structure of brevinin-1BYa in sodium dodecyl sulphate micelles
Authors
Timmons, P.B., O'Flynn, D.P., Conlon, J.M., Hewage, C.M.
Assembly
Brevinin-1BYa
Entity
1. Brevinin-1BYa (polymer), 24 monomers, 2609.282 Da Detail

FLPILASLAA KFGPKLFCLV TKKC


Formula weight
2609.282 Da
Source organism
Rana boylii
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 85.3 %, Completeness (bb): 97.9 % Detail

Polymer type: polypeptide(L)

Total1H
All85.3 % (133 of 156)85.3 % (133 of 156)
Backbone97.9 % (46 of 47)97.9 % (46 of 47)
Sidechain79.8 % (87 of 109)79.8 % (87 of 109)
Aromatic40.0 % (6 of 15)40.0 % (6 of 15)
Methyl94.4 % (17 of 18)94.4 % (17 of 18)

1. entity 1

FLPILASLAA KFGPKLFCLV TKKC

Sample

Solvent system 90% H2O/10% D2O, Pressure 100000 Pa, Temperature 298 K, pH 7, Details 1.5 mM NA- Brevinin-1BYa, 90% H2O/10% D2O


#NameIsotope labelingTypeConcentration
1Brevinin-1BYanatural abundance1.5 mM

Protein Blocks Logo
Calculated from 20 models in PDB: 6G4K, Strand ID: A Detail


Release date
2019-06-30
Citation 1
Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii
Conlon, J.M., Sonnevend, A., Patel, M., Davidson, C., Nielsen, P.F., Pal, T., Rollins-Smith, L.A.
J. Pept. Res. (2003), 62, 207-213, PubMed 14531844 ,
Citation 2
Structural and positional studies of the antimicrobial peptide brevinin-1BYa in membrane-mimetic environments
Timmons, P.B., O'Flynn, D.P., Conlon, J.M., Hewage, C.M.
J. Pept. Sci. (2019), 25, e3208-e3208, PubMed 31721374 , DOI 10.1002/psc.3208 ,
Related entities 1. Brevinin-1BYa, : 1 : 1 : 50 entities Detail
Experiments performed 2 experiments Detail
Chemical shift validation 3 contents Detail
Keywords ANTIMICROBIAL PROTEIN, antimicrobial peptide, cationic, rana-box