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DPC micelle-bound NMR structures of Tritrp5
Authors
Schibli, D.J., Nguyen, L.T.
Assembly
Tritrp5
Entity
1. Tritrp5 (polymer, Thiol state: not present), 14 monomers, 1932.261 Da Detail

VRRYPWWWPY LRRX


Formula weight
1932.261 Da
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 92.9 %, Completeness: 88.9 %, Completeness (bb): 95.8 % Detail

Polymer type: polypeptide(L)

Total1H
All88.9 % (96 of 108)88.9 % (96 of 108)
Backbone95.8 % (23 of 24)95.8 % (23 of 24)
Sidechain86.9 % (73 of 84)86.9 % (73 of 84)
Aromatic84.6 % (22 of 26)84.6 % (22 of 26)
Methyl50.0 % (2 of 4)50.0 % (2 of 4)

1. Tritrp5

VRRYPWWWPY LRRX

Sample

Solvent system 90% H2O, 10% D2O, Temperature 310 K, pH 4.8, Details 90% H2O, 10% D2O, 150 mM DPC-d38


#NameIsotope labelingTypeConcentration
1Tritrp5natural abundance1.0 ~ 2.0 mM
2DPC-d38150 mM
3H2O90 %
4D2O10 %

Protein Blocks Logo
Calculated from 20 models in PDB: 2I1G, Strand ID: A Detail


Release date
2007-10-29
Citation
Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures
Schibli, D.J., Nguyen, L.T., Kernaghan, S.D., Rekdal, O., Vogel, H.J.
Biophys. J. (2006), 91, 4413-4426, PubMed 16997878 , DOI 10.1529/biophysj.106.085837 ,
Related entities 1. Tritrp5, : 1 : 6 entities Detail
Experiments performed 3 experiments Detail
nullKeywords antimicrobial peptide, micelle-bound peptide, turn