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.
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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
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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.
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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
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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.
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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.
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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
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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
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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.
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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
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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
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Andrzej Bierzynski, Andrzej Ejchart, Igor Zhukov |