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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25877 | Chemical Shifts: 1 set |
Solution structure of cecropin P1 with LPS | Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy | Chiharu Abe, Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Mihwa Baek, Satoshi Tomisawa, Taichi Nakazumi, Takahiro Kushibiki, Takashi Kikukawa, Tomoyasu Aizawa, Yasuhiro Kumaki |
11538 | Chemical Shifts: 1 set |
Tachyplesin I in the presence of lipopolysaccharide | Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide. | Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Mineyuki Mizuguchi, Syun-ichiro Kawabata, Takahiro Kushibiki, Takashi Kikukawa, Tomoyasu Aizawa, Yasuhiro Kumaki |
11539 | Chemical Shifts: 1 set |
Tachyplesin I in water | Interaction between tachyplesin I, an antimicrobial peptide derived from horseshoe crab, and lipopolysaccharide. | Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Mineyuki Mizuguchi, Syun-ichiro Kawabata, Takahiro Kushibiki, Takashi Kikukawa, Tomoyasu Aizawa, Yasuhiro Kumaki |
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. | 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. | 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. | Hiroko Yamamoto, Kaori Muto, Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Mineyuki Mizuguchi, Tomoyasu Aizawa, Yasuhiro Kumaki, Yoichi Hayakawa, Yoshitaka Umetsu |
20010 | Conformer_family_coord_set: 1 set |
Superimposed fifteen structures of 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris | A circular loop of the 16-residue repeating unit in ice nucleation protein | Keiichi Kawano, Kunio Hikichi, Norio Matsushima, Takeshi Matsumoto, Yasuhiro Kumaki |
15641 | Chemical Shifts: 1 set Coupling Constants: 1 set |
1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 24-residue peptide corresponding to the segment within ice nucleation protein of Erwinia uredovora, Erwinia herbicola | A circular loop of the sixteen-residue repeating unit in ice nucleation protein | Keiichi Kawano, Kunio Hikichi, Norio Matsushima, Takeshi Matsumoto, Yasuhiro Kumaki |
15640 | Chemical Shifts: 1 set Coupling Constants: 1 set |
1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris | A circular loop of the sixteen-residue repeating unit in ice nucleation protein | Keiichi Kawano, Kunio Hikichi, Norio Matsushima, Takeshi Matsumoto, Yasuhiro Kumaki |
15639 | Chemical Shifts: 1 set Coupling Constants: 1 set |
1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris | A circular loop of the sixteen-residue repeating unit in ice nucleation protein | Keiichi Kawano, Kunio Hikichi, Norio Matsushima, Takeshi Matsumoto, Yasuhiro Kumaki |
7051 | Chemical Shifts: 1 set |
Solution structure of growth-blocking peptide of the tobacco cutworm, Spodoptera litura | Solution structure of growth-blocking peptide of the cabbage armyworm, Mamestra brassicae | Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Tomoyasu Aizawa, Yasuhiro Kumaki, Yoshitaka Umetsu |
7050 | Chemical Shifts: 1 set |
Solution structure of growth-blocking peptide of the cabbage armyworm, Mamestra brassicae | Solution structure of growth-blocking peptide of the cabbage armyworm, Mamestra brassicae | Keiichi Kawano, Makoto Demura, Masakatsu Kamiya, Tomoyasu Aizawa, Yasuhiro Kumaki, Yoshitaka Umetsu |
5986 | Chemical Shifts: 1 set |
Solution structure of paralytic peptide of the wild Silkmoth, Antheraea yamamai | Solution structure of paralytic peptide of the wild Silkmoth, Antheraea yamamai | An Ying, Katsutoshi Nitta, Koichi Suzuki, Kyosuke Kawaguchi, Makoto Demura, Yasuhiro Kumaki |
5811 | Chemical Shifts: 1 set Coupling Constants: 1 set |
1H Chemical Shift Assignments for quasi-repetitive arginine/glycine/ tyrosine-rich domains within glycine-rich RNA binding proteins | Side chain-side chain interactions of arginine with tyrosine and aspartic acid in Arg/Gly/Tyr-rich domains within plant glycine-rich RNA binding proteins | K Hikichi, K Nitta, N Matsushima, T Matsumoto, Yasuhiro Kumaki |
5812 | Chemical Shifts: 1 set Coupling Constants: 1 set |
1H Chemical Shift Assignments for quasi-repetitive arginine/glycine/ tyrosine-rich domains within glycine-rich RNA binding proteins | Side chain-side chain interactions of arginine with tyrosine and aspartic acid in Arg/Gly/Tyr-rich domains within plant glycine-rich RNA binding proteins | K Hikichi, K Nitta, N Matsushima, T Matsumoto, Yasuhiro Kumaki |
5353 | Chemical Shifts: 1 set |
1H, 15N and 13C resonance assignments of yeast Saccharomyces cerevisiae calmodulin in the Ca2+-free state | Letter to the Editor: 1H, 15N and 13C resonance assignments of yeast Saccharomyces cerevisiae calmodulin in the Ca2+-free state | Hiroaki Ishida, K-i Nakashima, Kunio Hikichi, Michio Yazawa, Mitsuo Nakata, Yasuhiro Kumaki |
5268 | Chemical Shifts: 1 set |
Structure of the Antimicrobial Peptide Tachystatin A | Structure of the Antimicrobial Peptide Tachystatin A | Katsutoshi Nitta, Keiichi Kawano, Makoto Demura, Naoki Fujitani, Shun-ichiro Kawabata, Tsukasa Osaki, Yasuhiro Kumaki |