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Paramagnetic relaxation enhancements of the amide protons in HHP-tagged thioredoxin
Authors
Jensen, M.R., Lauritzen, C., Dahl, S.W., Pedersen, J., Led, J.J.
Assembly
HHP-tagged E. coli Thioredoxin
Entity
1. HHP-tagged E. coli Thioredoxin (polymer, Thiol state: not reported), 111 monomers, 12046.67 × 3 Da Detail

HHPSDKIIHL TDDSFDTDVL KADGAILVDF WAEWCGPCKM IAPILDEIAD EYQGKLTVAK LNIDQNPGTA PKYGIRGIPT LLLFKNGEVA ATKVGALSKG QLKEFLDANL A


2. NI (non-polymer), 58.693 Da
Total weight
36198.7 Da
Max. entity weight
12046.67 Da
Source organism
Escherichia coli
Exptl. method
NMR
Data set
heteronucl_T1_relaxation
Heteronucl. T1
84 T1 values in 1 lists
Coherence Sz, Field strength (1H) 500 MHz, Temperature 298 (±0.1) K, pH 7.0 (±0.1) Detail
Release date
2004-03-22
Citation
Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR relaxation: the possibility of obtaining long-range structure information
Jensen, M.R., Lauritzen, C., Dahl, S.W., Pedersen, J., Led, J.J.
J. Biomol. NMR (2004), 29, 175-185, PubMed 15014231 , DOI 10.1023/B:JNMR.0000019251.09648.c4 ,
Related entities 1. HHP-tagged E. coli Thioredoxin, : 1 : 53 : 136 entities Detail
Interaction partners 1. HHP-tagged E. coli Thioredoxin, : 23 interactors Detail
Experiments performed 1 experiments Detail