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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
18758	2013-09-16	Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set Order Parameters: 1 set	Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme	NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme.	Andrzej Ejchart, Igor Zhukov, Marek Wojciechowski, Mariusz Jaremko, Matthias Bochtler, Micha Nowakowski, Renata Panecka, Roman H Szczepanowski, ukasz Jaremko
18230	2013-02-18	Chemical Shifts: 1 set Heteronuclear NOE Values: 3 sets T1 Relaxation Values: 3 sets T2 Relaxation Values: 3 sets	Solution structure and dynamics of human S100A1 protein modified at cysteine 85 with homocysteine disulfide bond formation in calcium saturated form.	Impact of calcium binding and thionylation of S100A1 protein on its nuclear magnetic resonance-derived structure and backbone dynamics.	Andrzej Bierzyski, Andrzej Ejchart, Katarzyna Ruszczyska-Bartnik, Konrad Zdanowski, Lukasz Jaremko, Mariusz Jaremko, Micha Nowakowski, Monika Budziska
18231	2013-02-18	Chemical Shifts: 1 set Heteronuclear NOE Values: 3 sets T1 Relaxation Values: 3 sets T2 Relaxation Values: 3 sets	Solution structure of S100A1 Ca2+	Impact of calcium binding and thionylation of S100A1 protein on its nuclear magnetic resonance-derived structure and backbone dynamics.	Andrzej Bierzyski, Andrzej Ejchart, Katarzyna Ruszczyska-Bartnik, Konrad Zdanowski, Lukasz Jaremko, Mariusz Jaremko, Micha Nowakowski, Monika Budziska