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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 |
|---|---|---|---|---|
| 30370 | Chemical Shifts: 1 set |
Solution NMR structure of uncharacterized protein YejG representing the first structure from PF13989 |
The uncharacterized bacterial protein YejG has the same architecture as domain III of elongation factor G.
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Biswaranjan Mohanty, Cecilia R Chambers, Ingrid Macindoe, James McKellar, Joel P Mackay, Paulina Hanson-Manful, Stephanie Helder, Surya Setiyaputra, Thomas J Finn, Wayne M Patrick, Yichen Zhong |
| 17765 | Chemical Shifts: 1 set |
Identification of the key regions that drive functional amyloid formation by the fungal hydrophobin EAS |
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.
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Ann H Kwan, Ingrid Macindoe, Joel P Mackay, Margaret Sunde, Qin Ren, Vanessa K Morris, Wenrong Yang |
| 15863 | Chemical Shifts: 1 set Spectral_peak_list: 2 sets |
Solution structure of EAS D15 truncation mutant |
The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity
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Alan E Mark, Ann H Kwan, Ingrid Macindoe, Itamar Kass, Joel P Mackay, Margaret Sunde, Matthew D Templeton, Rima Gupte, Vanessa K Morris, Vukasin V Paul |