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
27746 Chemical Shifts: 1 set
The conduction pathway of potassium channels is water-free under physiological conditions The conduction pathway of potassium channels is water free under physiological conditions Download bibtex for citation iamge Adam Lange, Bert L de Groot, Carl Oester, Chaowei Shi, Dagmar Michl, Han Sun, Kitty Hendriks, Sascha Lange, Veniamin Chevelkov, Wojciech Kopec
27219 Chemical Shifts: 1 set
ssNMR assignment of membrane embedded NaK channel (ion-free conformer) A single NaK channel conformation is not enough for non-selective ion conduction Download bibtex for citation iamge Adam Lange, Bert L de Groot, Changlin Tian, Chaowei Shi, Han Sun, Kitty Hendriks, Xiaoying Cai, Yao He
27220 Chemical Shifts: 1 set
ssNMR assignment of membrane embedded NaK channel (ion-favored conformer) A single NaK channel conformation is not enough for non-selective ion conduction Download bibtex for citation iamge Adam Lange, Bert L de Groot, Changlin Tian, Chaowei Shi, Han Sun, Kitty Hendriks, Xiaoying Cai, Yao He
4639 Chemical Shifts: 1 set
NMR structure of the hRap1 Myb motif reveals a canonical three helix bundle lacking the positive surface charge typical of Myb DNA binding domains NMR structure of the hRap1 Myb motif reveals a canonical three helix bundle lacking the positive surface charge typical of Myb DNA binding domains Download bibtex for citation iamge A Nagadoi, B Li, S Aimoto, S Hanaoka, S Yoshimura, T de Lange, Y Nishimura