| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 51949 |
2024-05-28 |
Chemical Shifts: 1 set
|
Assignments of mature MepS peptidoglycan hydrolase (residues 1-162) |
Structural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI
|
Chung-I I Chang, Chun-Hsiang H Huang, Hsi-Ching C Tseng, Shen Wang, Shing-Jong J Huang, Shiou-Ru R Tzeng, Si-Wei W Wang, Te-Sheng S Lin, U-Ser S Jeng, Yi-Qi Q Yeh, Yun-Sheng S Fan, Yu-Yang Y Chang |
| 11557 |
2018-12-18 |
Chemical Shifts: 1 set
|
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of human Pin1 without sulfate ion |
The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif.
|
Jong Wang, Jun-ichi Uewaki, Kazuhiko Igarashi, Naohiro Kobayashi, Naoko Utsunomiya-Tate, Naoya Tochio, Ning Xu, Shin-ichi Tate, Takuma Shiraki, Yu Tamari |
| 11558 |
2018-12-18 |
Chemical Shifts: 1 set
|
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the peptidyl prolyl cis-trans isomerase domain of C113D mutant human Pin1 without sulfate ion |
The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif.
|
Jong Wang, Jun-ichi Uewaki, Kazuhiko Igarashi, Naohiro Kobayashi, Naoko Utsunomiya-Tate, Naoya Tochio, Ning Xu, Shin-ichi Tate, Takuma Shiraki, Yu Tamari |
| 19206 |
2014-02-13 |
Chemical Shifts: 1 set
|
1H, 13C and 15N backbone and side-chain resonance assignments of a family 36 carbohydrate binding module of Xylanase from Paenibacillus campinasensis |
(1)H, (13)C and (15)N backbone and side-chain resonance assignments of a family 36 carbohydrate binding module of xylanase from Paenibacillus campinasensis.
|
Chi-Fon Chang, Chun-Han Ko, Der-Lii M Tzou, Hao-Ting Chang, Kai-Jay Yang, Pei-Ju Fang, Shing-Jong Huang, Yu-Jen Chen, Yu-Sheng Wang |
