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
51132 Chemical Shifts: 1 set
1H, 15N and 13C sequence-specific backbone assignment of RRP1B PP1 binding domain The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs Download bibtex for citation iamge Antoine Gaudreau-Lapierre, Dale Kreitler, Delphine Chamousset, Ganesan Senthil S Kumar, Gautam Srivastava, Hannah Nicolas, Laura Trinkle-Mulcahy, Rakhi Bajaj, Rebecca Page, Wolfgang Peti
27464 Chemical Shifts: 1 set
C-terminal tail of Protein Phosphatase 1, alpha isoform. ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail Download bibtex for citation iamge Audrey van Drogen, Federico Uliana, Ganesan Senthil S Kumar, Jennifer J Banerjee, Matthias Gstaiger, M Teresa T Bertran, Nicola O'Reilly, Nicolas Tapon, Rakhi Bajaj, Rebecca Lee, Rebecca Page, Simon Hauri, Stephane Mouilleron, Wolfgang Peti, Yanxiang Zhou
27066 Chemical Shifts: 1 set
Chemical Shift Assignment of the PP1 and Microtubule binding domain of phosphorylated human KNL-1 KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive. Download bibtex for citation iamge Mathieu Bollen, Rakhi Bajaj, Rebecca Page, Wolfgang Peti
27057 Chemical Shifts: 1 set
Chemical Shift Assignment of the PP1 and Microtubule binding domain of human KNL-1 KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive. Download bibtex for citation iamge Mathieu Bollen, Rakhi Bajaj, Rebecca Page, Wolfgang Peti