BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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Entry ID Data summary Entry Title Citation Title Authors
27199 Chemical Shifts: 1 set
1H and 15N chemical shift assignments of human S100B The neuronal S100B protein is a calcium-tuned suppressor of amyloid-beta aggregation. Download bibtex for citation iamge Bernd Reif, Christoph Gobl, Claudio M Gomes, Gunter Fritz, Hugo M Botelho, Isabel Cardoso, Javier Martinez, Joana S Cristovao, Katrin Kierdorf, Mobina Alemi, Rodrigo David, Sonia S Leal, Tobias Madl, Vanessa K Morris
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. Download bibtex for citation iamge Ann H Kwan, Ingrid Macindoe, Joel P Mackay, Margaret Sunde, Qin Ren, Vanessa K Morris, Wenrong Yang
17596 Chemical Shifts: 2 sets
Backbone and sidechain 1H, 13C and 15N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans Backbone and sidechain (1)H, (13)C and (15)N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans. Download bibtex for citation iamge Ann H Kwan, Joel P Mackay, Margaret Sunde, Vanessa K Morris
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 Download bibtex for citation iamge 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