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The NMR solution structure of octyl-tridecaptin A1 in DPC micelles
Authors
Cochrane, S.A., Findlay, B., Bakhtiary, A., Rodriguez-Lopez, E.M., Vederas, J.C.
Assembly
octyl-tridecaptin A1
Entity
1. octyl-tridecaptin A1 (polymer, Thiol state: not present), 13 monomers, 1394.573 Da Detail

XXGXXSXXFE VXA


Formula weight
1394.573 Da
Source organism
Paenibacillus terrae
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 46.2 %, Completeness: 100.0 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

Total1H
All100.0 % (30 of 30)100.0 % (30 of 30)
Backbone100.0 % (13 of 13)100.0 % (13 of 13)
Sidechain100.0 % (17 of 17)100.0 % (17 of 17)
Aromatic100.0 % (5 of 5)100.0 % (5 of 5)
Methyl100.0 % (3 of 3)100.0 % (3 of 3)

1. entity

XXGXXSXXFE VXA

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 273 K, pH 6


#NameIsotope labelingTypeConcentration
1entitynatural abundance0.0 ~ 0.0 mM
2D2Onatural abundance10 %
3H2Onatural abundance90 %
4DPCnatural abundance180 mM

Release date
2016-09-21
Citation
Antimicrobial lipopeptide tridecaptin A1 selectively binds to Gram-negative lipid II
Cochrane, S.A., Findlay, B., Bakhtiary, A., Acedo, J.Z., Rodriguez-Lopez, E.M., Mercier, P., Vederas, J.C.
Proc. Natl. Acad. Sci. U. S. A. (2016), 113, 11561-11566, PubMed 27688760 , DOI 10.1073/pnas.1608623113 ,
Experiments performed 2 experiments Detail
nullKeywords Antibiotic, Antimicrobial, Lipopeptide, Non-ribosomal, Tridecaptin A1