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
36018 Chemical Shifts: 1 set
Solution structure of the first RRM domain of human spliceosomal protein SF3b49 Solution structure of the first RNA recognition motif domain of human spliceosomal protein SF3b49 and its mode of interaction with a SF3b145 fragment Download bibtex for citation iamge Atsuko Sato, Kanako Kuwasako, Kaori Wakamatsu, Kengo Tsuda, Makoto Inoue, Mari Takahashi, Mikako Shirouzu, Naohiro Kobayashi, Naoya Tochio, Nobukazu Nameki, Peter Guntert, Seizo Takahashi, Shigeyuki Yokoyama, Taiichi Sakamoto, Takaho Terada, Takanori Kigawa, Takuhiro Ito, Yutaka Muto
11068 Chemical Shifts: 1 set
solution structure of 1-23 GBP (growth-blocking peptide) C-terminal elongation of growth-blocking peptide enhances its biological activity and micelle binding affinity. Download bibtex for citation iamge Hiroko Yamamoto, Kaori Muto, Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Mineyuki Mizuguchi, Tomoyasu Aizawa, Yasuhiro Kumaki, Yoichi Hayakawa, Yoshitaka Umetsu
11069 Chemical Shifts: 1 set
solution structure of 1-28 GBP (growth-blocking peptide) C-terminal elongation of growth-blocking peptide enhances its biological activity and micelle binding affinity. Download bibtex for citation iamge Hiroko Yamamoto, Kaori Muto, Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Mineyuki Mizuguchi, Tomoyasu Aizawa, Yasuhiro Kumaki, Yoichi Hayakawa, Yoshitaka Umetsu
11070 Chemical Shifts: 1 set
DPC micelle bound structure of 1-28 GBP (growth-blocking peptide) C-terminal elongation of growth-blocking peptide enhances its biological activity and micelle binding affinity. Download bibtex for citation iamge Hiroko Yamamoto, Kaori Muto, Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Mineyuki Mizuguchi, Tomoyasu Aizawa, Yasuhiro Kumaki, Yoichi Hayakawa, Yoshitaka Umetsu