The protein stromal interaction molecule 1 (STIM1) plays a pivotal role in mediating store-operated calcium entry (SOCE) into cells, which is essential for adaptive immunity. It acts as a calcium sensor in the endoplasmic reticulum (ER) and extends into the cytosol, where it changes from an inactive (tight) to an active (extended) oligomeric form upon calcium store depletion. NMR studies of this protein are challenging due to its membrane-spanning and aggregation properties. Therefore follow the divide-and-conquer approach, focusing on individual domains first is in order. The cytosolic part is predicted to have a large content of coiled-coil (CC) structure. We report the 1H, 13C, 15N chemical shift assignments of the CC3 domain. This domain is crucial for the stabilisation of the tight quiescent form of STIM1 as well as for activating the ORAI calcium channel by direct contact, in the extended active form.

Faculty of Science University of South Bohemia Branišovská 1645 31A 370 05 České Budějovice Czech Republic

Institute of Analytical Chemistry University of Vienna Währingerstrasse 38 1090 Vienna Austria

Institute of Biophysics Johannes Kepler University Linz Gruberstrasse 40 4020 Linz Austria

Institute of Inorganic Chemistry Johannes Kepler University Linz Altenbergerstrasse 69 4040 Linz Austria

Institute of Organic Chemistry Johannes Kepler University Linz Altenbergerstrasse 69 4040 Linz Austria

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