| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 51541 |
2023-06-30 |
Chemical Shifts: 1 set
|
Staphylococcus Aureus Protein A, Immunoglobulin-binidng B domain |
The B domain of protein A retains residual structures in 6 M guanidinium chloride as revealed by hydrogen/deuterium-exchange NMR spectroscopy
|
Koichi Kato, Kunihiro Kuwajima, Maho Yagi-Utsumi, Saeko Yanaka |
| 30304 |
2017-09-15 |
Chemical Shifts: 1 set
|
Molecular structure of FUS low sequence complexity domain protein fibrils |
Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains
|
D T Murray, I Hung, K Thurber, M Kato, R Tycko, S McKnight, Y Lin |
| 11057 |
2012-07-19 |
Chemical Shifts: 1 set
|
MICROTUBULE BINDING DOMAIN OF DYNEIN-C |
Structure of the Microtubule-Binding Domain of Flagellar Dynein
|
K Yura, M Tanokura, R Kamiya, S Burgess, S Harris, S Honda, S Ohki, T Yagi, Y Kato, Y Shimizu |
| 15607 |
2008-11-25 |
Chemical Shifts: 1 set
|
Putative 32 kDa myrosinase binding protein At3g16450.1 from Arabidopsis |
Structure of the putative 32 kDa myrosinase-binding protein from Arabidopsis (At3g16450.1) determined by SAIL-NMR.
|
Akira M Ono, David J Aceti, Hirokazu Yagi, John L Markley, Jungoo Jee, Koichi Kato, Masatsune Kainosho, Mitsuhiro Takeda, Nozomi Sugimori, Peter Guntert, Takuya Torizawa, Teppei Ikeya, Tsutomu Terauchi, Yoshiki Yamaguchi |
| 6721 |
2006-04-24 |
Chemical Shifts: 1 set
|
Solution structure of the first WW domain of FBP11 |
Solution structure and binding specificity of FBP11/HYPA WW domain as Group-II/III
|
K Nagata, M Tanokura, Y Hino, Y Kato |
| 6719 |
2007-01-29 |
Chemical Shifts: 2 sets
|
Complex structure of the first WW domain of FBP11/HYPA and a -Pro-Pro-Leu-Pro- ligand reveals mechanism of Pro-rich ligand recognition by Group-II/III WW domains |
Solution structure and binding specificity of FBP11/HYPA WW domain as Group-II/III
|
K Nagata, M Tanokura, Y Hino, Y Kato |
| 6649 |
2005-12-05 |
Chemical Shifts: 1 set
|
Solution structure of the peptidoglycan binding domain of B. subtilis cell wall lytic enzyme CwlC: Characterization of the sporulation-related repeats by NMR |
Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
|
C Kojima, J Sekiguchi, K Kato, K Yabuki, M Mishima, T Shida |
