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NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+ ligating residues
Authors
Nielsen, G., Malmendal, A., Meissner, A., Moller, J.V., Nielsen, N.
Assembly
fifth transmembrane segment (residue L758 to E785) of sarcoplasmic reticulum Ca2+-ATPase
Entity
1. fifth transmembrane segment (residue L758 to E785) of sarcoplasmic reticulum Ca2+-ATPase (polymer, Thiol state: not present), 28 monomers, 3065.560 Da Detail

KQFIRYLISS NVGEVVSIFL TAALGLPE


Formula weight
3065.56 Da
Source organism
Oryctolagus cuniculus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 95.9 %, Completeness (bb): 100.0 % Detail

Polymer type: polypeptide(L)

Total1H
All95.9 % (163 of 170)95.9 % (163 of 170)
Backbone100.0 % (57 of 57)100.0 % (57 of 57)
Sidechain93.8 % (106 of 113)93.8 % (106 of 113)
Aromatic92.9 % (13 of 14)92.9 % (13 of 14)
Methyl91.3 % (21 of 23)91.3 % (21 of 23)

1. fifth transmembrane segment (residue L758 to E785) of sarcoplasmic reticulum Ca2+-ATPase

KQFIRYLISS NVGEVVSIFL TAALGLPE

Sample

Temperature 313 (±1) K, pH 7.0 (±0.1)


#NameIsotope labelingTypeConcentration
1fifth transmembrane segment (residue L758 to E785) of sarcoplasmic reticulum Ca2+-ATPase2.4 mM
2SDS-d25400 mM
3NaCl100 mM
4sodium phosphate20 mM
5NaN31 mM
6D2O10 %

Release date
2003-08-07
Citation
NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+-ligating residues
Nielsen, G., Malmendal, A., Meissner, A., Moller, J.V., Nielsen, N.
FEBS Lett. (2003), 544, 50-56, PubMed 12782289 , DOI: ,
Related entities 1. fifth transmembrane segment (residue L758 to E785) of sarcoplasmic reticulum Ca2+-ATPase, : 1 : 5 : 91 : 35 entities Detail
Interaction partners 1. fifth transmembrane segment (residue L758 to E785) of sarcoplasmic reticulum Ca2+-ATPase, : 14 interactors Detail
Experiments performed 1 experiments Detail
nullKeywords Ca2+-ATPase, fifth transmembrane segment M5, membrane proteins, micelle, NMR, nuclear magnetic resonance, sarcoplasmic reticulum, SDS