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 |
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25368 | Chemical Shifts: 1 set |
Backbone 1H, 13C and 15N chemical shifts for Staphylococcus aureus EF-GC3, a truncated form of elongation factor G comprising domains III-V. | A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance | Alex J O'Neill, Anastasia Zhuravleva, Arnout P Kalverda, Gary S Thompson, Jennifer H Tomlinson |
18861 | Chemical Shifts: 1 set |
NMR Structure of Antiamoebin I (peptaibol antibiotic) bound to DMPC/DHPC bicelles | Peptaibol antiamoebin I: spatial structure, backbone dynamics, interaction with bicelles and lipid-protein nanodiscs, and pore formation in context of barrel-stave model. | Albina K Gizatullina, Alexander S Arseniev, Alexander S Paramonov, Anastasia V Zhuravleva, Andrey A Tagaev, Ekaterina N Lyukmanova, Irina N Telezhinskaya, Mikhail P Kirpichnikov, Tatiana V Ovchinnikova, Zakhar O Shenkarev, Zoya A Yakimenko |
7126 | Chemical Shifts: 1 set Order Parameters: 1 set |
1H,13C and 15N resonance assignments of barnase-barstar complex NMR deuterium methyl relaxation data for free barnase and barnase-barstar complex | Propagation of dynamic changes in barnase upon binding of barstar: an NMR and computational study | Alexander S Arseniev, Anastasia V Zhuravleva, Dmitry M Korzhnev, Lewis E Kay, Martin Billiter, Svetlana B Nolde, Vladislav Yu Orekhov |
7139 | Order Parameters: 1 set |
1H,13C and 15N resonance assignments of barnase-barstar complex NMR deuterium methyl relaxation data for free barnase and barnase-barstar complex | Propagation of Dynamic Changes in Barnase Upon Binding of Barstar: An NMR and Computational Study | Alexander S Arseniev, Anastasia V Zhuravleva, Dmitry M Korzhnev, Lewis E Kay, Martin Billiter, Svetlana B Nolde, Vladislav Yu Orekhov |
6243 | Heteronuclear NOE Values: 6 sets T1 Relaxation Values: 7 sets T2 Relaxation Values: 7 sets Order Parameters: 2 sets |
NMR Relaxation data for Protein Azurin from Pseudomonas aeruginosa | Gated electron transfers and electron pathways in azurin: a NMR dynamic study at multiple fields and temperatures | Alexander S Arseniev, Anastasia V Zhuravleva, Dmitry M Korzhnev, Eriks Kupce, Martin Billeter, Vladislav Yu Orekhov |