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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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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
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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 |
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 |
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 |
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
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Hiroaki Ishida, K-i Nakashima, Kunio Hikichi, Michio Yazawa, Mitsuo Nakata, Yasuhiro Kumaki |
4290 | Chemical Shifts: 1 set |
Sequence-specific 1H Assignment of Antimicrobial Protein Tachycitin. |
Chitin-binding Proteins in Invertebrates and Plants Comprise a Common Chitin-binding Structural Motif
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Katsutoshi Nitta, Kawano Keiichi, Kazunori Miura, Keiichi Kawano, Kunio Hikichi, Sadaaki Iwanaga, Sakae Tsuda, Shun-ichiro Kawabata, Tetsuya Suetake |
2440 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Michio Yazawa, Mitsuhiko Ikura, Toshiaki Mikuni, Toshifumi Hiraoki |
258 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Mikiharu Yoshida, Sakae Tsuda, Yasushi Hasegawa |
259 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Mikiharu Yoshida, Sakae Tsuda, Yasushi Hasegawa |
676 | Chemical Shifts: 1 set |
1H NMR Study of Rabbit Skeletal Muscle Troponin C: Mg2+-Induced Conformational Change |
1H NMR Study of Rabbit Skeletal Muscle Troponin C: Mg2+-Induced Conformational Change
|
Kenji Ogura, Koichi Yagi, Kunio Hikichi, Sakae Tsuda, Yasushi Hasegawa |
677 | Chemical Shifts: 1 set |
1H NMR Study of Rabbit Skeletal Muscle Troponin C: Mg2+-Induced Conformational Change |
1H NMR Study of Rabbit Skeletal Muscle Troponin C: Mg2+-Induced Conformational Change
|
Kenji Ogura, Koichi Yagi, Kunio Hikichi, Sakae Tsuda, Yasushi Hasegawa |
749 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Mikiharu Yoshida, Sakae Tsuda, Yasushi Hasegawa |
750 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Mikiharu Yoshida, Sakae Tsuda, Yasushi Hasegawa |
2435 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Michio Yazawa, Mitsuhiko Ikura, Toshiaki Mikuni, Toshifumi Hiraoki |
2436 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Michio Yazawa, Mitsuhiko Ikura, Toshiaki Mikuni, Toshifumi Hiraoki |
2437 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Michio Yazawa, Mitsuhiko Ikura, Toshiaki Mikuni, Toshifumi Hiraoki |
2438 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Michio Yazawa, Mitsuhiko Ikura, Toshiaki Mikuni, Toshifumi Hiraoki |
2439 | Chemical Shifts: 1 set |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change |
Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change
|
Koichi Yagi, Kunio Hikichi, Michio Yazawa, Mitsuhiko Ikura, Toshiaki Mikuni, Toshifumi Hiraoki |