BMRB: 15044

DPC micelle-bound NMR structures of Tritrp8

Authors

Schibli, D.J., Nguyen, L.T.

Assembly

none

Entity

1. none (polymer, Thiol state: not present), 14 monomers, 1874.224 Da Detail

VRRFPWWWAF LRRX

Formula weight

1874.224 Da

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.9 %, Completeness: 84.9 %, Completeness (bb): 92.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	84.9 % (90 of 106)	84.9 % (90 of 106)
Backbone	92.0 % (23 of 25)	92.0 % (23 of 25)
Sidechain	82.7 % (67 of 81)	82.7 % (67 of 81)
Aromatic	85.7 % (24 of 28)	85.7 % (24 of 28)
Methyl	60.0 % (3 of 5)	60.0 % (3 of 5)

1. 13-mer analogue of Prophenin-1 containing WWW

VRRFPWWWAF LRRX

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Sample

Solvent system 90% H2O, 10% D2O, Temperature 310 K, pH 4.7, Details 90% H2O, 10% D2O, 150 mM DPC-d38

#	Name	Isotope labeling	Type	Concentration
1	Tritrp8	natural abundance		1.0 ~ 3.0 mM
2	DPC-d38			150 mM
3	H2O			90 %
4	D2O			10 %

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Calculated from 20 models in PDB: 2I1I, Strand ID: A Detail

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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 , Abstract

Related entities 1. none, : 1 : 3 : 3 entities Detail

Experiments performed 3 experiments Detail