HK853 is a transmembrane protein from Thermotoga maritime, which belongs to HK853/RR468 two-component signal transduction system (TCS) and acts as a sensor histidine kinase. HK853 is mainly composed of a transmembrane domain, dimerization and histidine-containing phosphotransfer domain (HK853), catalytic and ATP-binding domain (HK853) and several linkers. HK853 can be completely autophosphorylated, which is the first step for signal transduction of TCS. HK853 is an essential domain for its kinase function, since HK853 could bind with ATP and convert it to ADP. Here, we report the backbone and part of side chain assignments of HK853. By analyzing the chemical shifts of HN, N, CO, C and C, the secondary structure was predicted and contrasted with the published crystal structure of HK853. The result showed that our predicted structure could basically fit into the crystal structure. Thus, the chemical shift assignments of HK853 are the starting point for further structural and dynamics study.
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