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
34551 Chemical Shifts: 1 set
NMR structure of flagelliform spidroin (FlagSp) N-terminal domain from Trichonephila clavipes at pH 5.5 The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence Download bibtex for citation iamge Alessandro Mantese, Anna Rising, Dipen Shah, Jan Johansson, Kaspar Tars, Kellie-Ann A Walsh-White, Kristaps Jaudzems, Kristine Kitoka, Margit Kaldmae, Medoune Sarr, Michael Landreh, Nina Kronqvist, Rimants Metlans
34550 Chemical Shifts: 1 set
NMR structure of flagelliform spidroin (FlagSp) N-terminal domain from Trichonephila clavipes at pH 7.2 The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence Download bibtex for citation iamge Alessandro Mantese, Anna Rising, Dipen Shah, Jan Johansson, Kaspar Tars, Kellie-Ann A Walsh-White, Kristaps Jaudzems, Kristine Kitoka, Margit Kaldmae, Medoune Sarr, Michael Landreh, Nina Kronqvist, Rimants Metlans
18480 Chemical Shifts: 1 set
NMR structure of major ampullate spidroin 1 N-terminal domain at pH 5.5 Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation. Download bibtex for citation iamge Anna Rising, Daniel Otzen, Gefei Chen, Hans Jornvall, Jan Johansson, Jerker Widengren, Kerstin Nordling, Kristaps Jaudzems, Marlene Andersson, Martins Otikovs, Medoune Sarr, Michael Landreh, Nina Kronqvist, Qing Meng, Stefan D Knight, Stefan Wennmalm, Volodymyr Chmyrov