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Entry ID Original Release date Data summary Entry Title Citation Title Authors
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. Download bibtex for citation iamge 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. Download bibtex for citation iamge 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. Download bibtex for citation iamge 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