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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 |
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6779 | Chemical Shifts: 1 set |
Solution Structure of the type 1 pilus assembly platform FimD(25-125) |
Structural basis of chaperone-subunit complex recognition by type 1 pilus assembly platform FimD
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G Capitani, K Wuthrich, M Grutter, M Nishiyama, M Vetsch, O Ignatov, P Bettendorff, R Glockshuber, R Herrmann, R Horst |
6629 | Chemical Shifts: 1 set |
Solution Structure of the type 1 pilus assembly platform FimD(25-139) |
Structural basis of chaperone-subunit complex recognition by type 1 pilus assembly platform FimD
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G Capitani, K Wuthrich, M Grutter, M Nishiyama, M Vetsch, O Ignatov, P Bettendorff, R Glockshuber, R Horst, T Hermann |
5204 | Chemical Shifts: 1 set |
1H, 13C and 15N chemical shift assignments for CRT(189-261) |
NMR Structures of 36 and 73-residue Fragments of the Calreticulin P-domain
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Ari Helenius, Daniel Braun, Francesco Fiorito, Ilian Jelesarov, Kurt Wuethrich, Lars Ellgaard, Pascal Bettendorff, Peter Guentert, Torsten Herrmann |
5205 | Chemical Shifts: 1 set Coupling Constants: 1 set |
1H chemical shift assignemnts and coupling constants for CRT(221-256) |
NMR Structures of 36 and 73-residue Fragments of the Calreticulin P-domain
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Ari Helenius, Daniel Braun, Francesco Fiorito, Ilian Jelesarov, Kurt Wuethrich, Lars Ellgaard, Pascal Bettendorff, Peter Guentert, Torsten Herrmann |