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Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin
Authors
Chandrasekhar, K., Krause, G., Holmgren, A., Dyson, H.JANE.
Assembly
thioredoxin
Entity
1. thioredoxin (polymer), 108 monomers, 11675.28 Da Detail

SDKIIHLTDD SFDTDVLKAD GAILVDFWAE WCGPCKMIAP ILDEIADEYQ GKLTVAKLNI DQNPGTAPKY GIRGIPTLLL FKNGEVAATK VGALSKGQLK EFLDANLA


Formula weight
11675.28 Da
Source organism
Escherichia coli
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 93.5 %, Completeness: 90.3 %, Completeness (bb): 98.1 % Detail

Polymer type: polypeptide(L)

Total15N
All90.3 % (102 of 113)90.3 % (102 of 113)
Backbone98.1 % (101 of 103)98.1 % (101 of 103)
Sidechain10.0 % (1 of 10)10.0 % (1 of 10)
Aromatic 0.0 % (0 of 2) 0.0 % (0 of 2)

1. thioredoxin

SDKIIHLTDD SFDTDVLKAD GAILVDFWAE WCGPCKMIAP ILDEIADEYQ GKLTVAKLNI DQNPGTAPKY GIRGIPTLLL FKNGEVAATK VGALSKGQLK EFLDANLA

Sample

Temperature 308 K, pH 5.7



Release date
1995-07-30
Citation
Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin
Chandrasekhar, K., Krause, G., Holmgren, A., Dyson, H.JANE.
FEBS Lett. (1991), 284, 178-183, PubMed 2060637 , DOI http://dx.doi.org/10.1016/0014-5793(91)80679-w ,
Related entities 1. thioredoxin, : 1 : 28 : 11 : 27 : 128 entities Detail
Interaction partners 1. thioredoxin, : 23 interactors Detail