BMRB: 15043

DPC micelle-bound NMR structures of Tritrp7

Authors

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

Assembly

none

Entity

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

VRRFAWWWPF 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: 82.1 %, Completeness (bb): 92.0 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	82.1 % (87 of 106)	82.1 % (87 of 106)
Backbone	92.0 % (23 of 25)	92.0 % (23 of 25)
Sidechain	79.0 % (64 of 81)	79.0 % (64 of 81)
Aromatic	82.1 % (23 of 28)	82.1 % (23 of 28)
Methyl	80.0 % (4 of 5)	80.0 % (4 of 5)

1. Tritrp7

VRRFAWWWPF LRRX

Show sample condition

Sample

Solvent system 90% H2O, 10% D2O, Temperature 310 K, pH 4.7, Details 90% H2O, 10% D2O, 200 mM DPC-d38

#	Name	Isotope labeling	Type	Concentration
1	Tritrp7	natural abundance		1.0 ~ 3.0 mM
2	DPC-d38			200 mM
3	H2O			90 %
4	D2O			10 %

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Protein Blocks Logo

Calculated from 20 models in PDB: 2I1H, 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

Entries sharing articles BMRB: 5, Swiss-Prot: 1 entries Detail

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

Experiments performed 3 experiments Detail