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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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| Entry ID | Data summary | Entry Title | Citation Title | Authors |
|---|---|---|---|---|
| 18545 | 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 | 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 | 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 | 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 | 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 |