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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
34044	2017-10-19	Chemical Shifts: 1 set	Solution structure of bacteriocin BacSp222 from Staphylococcus pseudintermedius 222	Spatial attributes of the four-helix bundle group of bacteriocins-the high-resolution structure of BacSp222 in solution.	Andrzej Ejchart, Benedykt Wladyka, Grzegorz Dubin, Lukasz Jaremko, Michal Nowakowski, Pawel Mak
18864	2013-12-02	Chemical Shifts: 1 set Heteronuclear NOE Values: 6 sets T1 Relaxation Values: 4 sets T2 Relaxation Values: 4 sets	High resolution structure and dynamics of CsPinA parvulin at physiological temperature	High resolution structure and dynamics of CsPinA parvulin at physiological temperature	Andrzej Ejchart, Lukasz Jaremko, Mariusz Jaremko, Markus Zweckstetter, Peter Bayer
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
18545	2013-06-24	Chemical Shifts: 1 set Heteronuclear NOE Values: 3 sets T1 Relaxation Values: 3 sets T2 Relaxation Values: 3 sets	Calcium saturated form of human C85M S100A1 mutant	Solution structure of human holo-S100A1 C85M mutant	Andrzej Ejchart, Katarzyna Ruszczynska-Bartnik, Konrad Zdanowski, Monika Budzinska
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
18087	2013-01-08	Chemical Shifts: 1 set Heteronuclear NOE Values: 3 sets T1 Relaxation Values: 3 sets T2 Relaxation Values: 3 sets	solution structure of human apo-S100A1 C85M	Chemical Shift Assignments and solution structure of human apo-S100A1 C85M mutant	Andrzej Bierzynski, Andrzej Ejchart, Igor Zhukov, Konrad Zdanowski, Lukasz Jaremko, Mariusz Jaremko, Monika Budzinska
17857	2012-08-01	Chemical Shifts: 1 set Heteronuclear NOE Values: 3 sets T1 Relaxation Values: 3 sets T2 Relaxation Values: 3 sets	Chemical Shift Assignments and solution structure of human apo-S100A1 E32Q mutant	Chemical Shift Assignments and solution structure of human apo-S100A1 E32Q mutant	Andrzej Bierzynski, Andrzej Ejchart, Igor Zhukov, Katarzyna Ruszczynska-Bartnik, Konrad Zdanowski
11080	2011-06-03	Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 2 sets T2 Relaxation Values: 2 sets Order Parameters: 1 set	3D structure of Pin from the psychrophilic archeon Cenarcheaum symbiosum (CsPin)	Structure and dynamics of the first archaeal parvulin reveal a new functionally important loop in parvulin-type prolyl isomerases.	Andrzej Ejchart, Igor Zhukov, Imadeldin Elfaki, Jonathan W Mueller, Mariusz Jaremko, Peter Bayer, ukasz Jaremko
16360	2010-01-07	Chemical Shifts: 2 sets Heteronuclear NOE Values: 3 sets T1 Relaxation Values: 4 sets T2 Relaxation Values: 4 sets	1H, 13C and 15N NMR sequence-specific resonance assignments and relaxation parameters for human apo-S100A1(aa) in the reduced form	1H, 13C and 15N NMR sequence-specific resonance assignments and relaxation parameters for human apo-S100A1(aa) in the reduced form	Andrzej Bierzynski, Andrzej Ejchart, Igor Zhukov, Lukasz Jaremko, Michal Nowakowski
4982	2008-07-01	Chemical Shifts: 3 sets	1H, 13C and 15N NMR sequence-specific resonance assignments for bovine apo-S100A1(aa) in oxidized form	Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol	Andrzej Bierzynski, Andrzej Ejchart, Igor Zhukov