@article{
 title = {1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis},
 type = {article},
 year = {2010},
 keywords = {Bacillus subtilis,Bacterial signal transduction,Histidine kinase inhibition,KipI},
 pages = {167-169},
 volume = {4},
 websites = {http://link.springer.com/10.1007/s12104-010-9237-6},
 month = {10},
 day = {4},
 id = {48c78b62-9179-35cb-ae9d-83d16d7e9f3b},
 created = {2020-12-17T05:29:56.688Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2020-12-17T05:29:56.688Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {Hynson2010},
 source_type = {ARTICLE},
 notes = {cited By 2},
 private_publication = {false},
 abstract = {KipI is a sporulation inhibitor in Bacillus subtilis which acts by binding to the dimerisation and histidine phosphotransfer (DHp) domain of KinA, the principle input kinase in the phosphorelay responsible for sporulation. The 15N, 13C and 1H chemical shift assignments of the N-terminal domain of KipI were determined using multidimensional, multinuclear NMR experiments. The N-terminal domain has two conformers and resonance assignments have been made for both conformers. © 2010 Springer Science+Business Media B.V.},
 bibtype = {article},
 author = {Hynson, Robert M. G. and Kwan, Ann H. and Jacques, David A. and Mackay, Joel P. and Trewhella, Jill},
 doi = {10.1007/s12104-010-9237-6},
 journal = {Biomolecular NMR Assignments},
 number = {2}
}

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