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Solution structure of AS1p-Tar in 10% negatively charged bicelles
Authors
Unnerstale, S., von Heijne, G., Draheim, R.R., Maler, L.
Assembly
AS1p-TarEc
Entity
1. AS1p-TarEc (polymer, Thiol state: not present), 19 monomers, 2116.614 Da Detail

RMLLTPLAKI IAHIREIAG


Formula weight
2116.614 Da
Source organism
Escherichia coli
Exptl. method
solution NMR
Refine. method
molecular dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 94.7 %, Completeness: 68.1 %, Completeness (bb): 92.1 % Detail

Polymer type: polypeptide(L)

Total1H
All68.1 % (81 of 119)68.1 % (81 of 119)
Backbone92.1 % (35 of 38)92.1 % (35 of 38)
Sidechain56.8 % (46 of 81)56.8 % (46 of 81)
Aromatic 0.0 % (0 of 2) 0.0 % (0 of 2)
Methyl100.0 % (18 of 18)100.0 % (18 of 18)

1. AS1p-TarEc

RMLLTPLAKI IAHIREIAG

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.2, Details 2 mM AS1p-TarEc and 300 mM [DMPC/DMPG 9:1]/[DHPC] phospholipid bicelles, q-ratio 0.25, dissolved in 50 mM sodium phosphate buffer, pH 7.2.


#NameIsotope labelingTypeConcentration
1sodium phosphatenatural abundance50 mM
2DHPC[U-2H]240 mM
3DMPC[U-2H]54 mM
4DMPG[U-2H]6 mM
5H2Onatural abundance90 %
6D2Onatural abundance10 %
7AS1p-TarEcnatural abundance2 mM

Protein Blocks Logo
Calculated from 25 models in PDB: 2L9G, Strand ID: A Detail


Release date
2011-08-16
Citation
Structural characterization of AS1-membrane interactions from a subset of HAMP domains
Unnerstale, S., Maler, L., Draheim, R.R.
Biochim. Biophys. Acta (2011), 1808, 2403-2412, PubMed 21763270 , DOI 10.1016/j.bbamem.2011.06.018 ,
Related entities 1. AS1p-TarEc, : 1 : 2 : 1 entities Detail
Interaction partners 1. AS1p-TarEc, : 9 interactors Detail
Experiments performed 2 experiments Detail
NMR combined restraints 3 contents Detail
Keywords HAMP-domain, helicity of AS1, membrane-spanning receptors, signal transduction, transmembrane communication