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1H Chemical Shift Assignments for fragments of Sticholysin protein
Authors
Oliveira, A.L., Cilli, E.M., Alvarez, C., Spisni, A., Pertinhez, T.A.
Assembly
St II fragments
Entity
1. St II fragments (polymer, Thiol state: not present), 30 monomers, 3128.659 Da Detail

ALAGTIIAGA SLTFQVLDKV LEELGKVSRK


Formula weight
3128.659 Da
Source organism
Stichodactyla helianthus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 78.6 %, Completeness (bb): 90.5 % Detail

Polymer type: polypeptide(L)

Total1H
All78.6 % (136 of 173)78.6 % (136 of 173)
Backbone90.5 % (57 of 63)90.5 % (57 of 63)
Sidechain71.8 % (79 of 110)71.8 % (79 of 110)
Aromatic40.0 % (2 of 5)40.0 % (2 of 5)
Methyl73.1 % (19 of 26)73.1 % (19 of 26)

1. St II (1-30) - synthetic fragment encompassing residues 1 to 30 of Sticholysin protein

ALAGTIIAGA SLTFQVLDKV LEELGKVSRK

Sample

Temperature 293 (±0.5) K, pH 4.0 (±0.5)


#NameIsotope labelingTypeConcentration
1St II (1-30)protein1 mM
2SDSlipid100 mM

Release date
2007-09-25
Citation 1
NMRView: A computer program for the visualization and analysis of NMR data
Johnson, B.A., Blevins, R.A.
J. Biomol. NMR (1994), 4, 603-614
Citation 2
NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 ,
Citation 3
Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II
Casallanovo, F., Oliveira, F.J.F., Souza, F.C., Ros, U., Martinez, Y., Penton, D., Tejuca, M., Martinez, D., Pazos, F., Pertinhez, T.A., Spisni, A., Cilli, E.M., Lanio, M.E., Alvarez, C., Schreier, S.
Biopolymers (2006), 84, 169-180, PubMed 16170802 , DOI 10.1002/bip.20374 ,
Related entities 1. St II fragments, : 1 : 4 : 1 : 28 entities Detail
Experiments performed 3 experiments Detail
Chemical shift validation 3 contents Detail
Keywords peptide-membrane interaction, sticholysin