BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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Entry ID Data summary Entry Title Citation Title Authors
12039 Chemical Shifts: 1 set
Backbone assignment for the segmental-labeled basic region and HMG-box in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1 Ultrasensitive Change in Nucleosome Binding by Multiple Phosphorylations to the Intrinsically Disordered Region of the Histone Chaperone FACT. Download bibtex for citation iamge Akinori Awazu, Daisuke Aoki, Jun-ichi Uewaki, Manami Hashimoto, Masashi Fujii, Naoya Tochio, Shin-ichi Tate, Takashi Umehara
12038 Chemical Shifts: 1 set
Backbone assignment for the segmental-labeled acidic region in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1 Ultrasensitive Change in Nucleosome Binding by Multiple Phosphorylations to the Intrinsically Disordered Region of the Histone Chaperone FACT. Download bibtex for citation iamge Akinori Awazu, Daisuke Aoki, Jun-ichi Uewaki, Manami Hashimoto, Masashi Fujii, Naoya Tochio, Shin-ichi Tate, Takashi Umehara
12036 Chemical Shifts: 1 set
Backbone assignment for the segmental-labeled basic region and HMG-box in the DNA-binding domain of Drosophila melanogaster SSRP1 Ultrasensitive Change in Nucleosome Binding by Multiple Phosphorylations to the Intrinsically Disordered Region of the Histone Chaperone FACT. Download bibtex for citation iamge Akinori Awazu, Daisuke Aoki, Jun-ichi Uewaki, Manami Hashimoto, Masashi Fujii, Naoya Tochio, Shin-ichi Tate, Takashi Umehara
12035 Chemical Shifts: 1 set
Backbone assignment for the segmental-labeled acidic region in the DNA-binding domain of Drosophila melanogaster SSRP1 Ultrasensitive Change in Nucleosome Binding by Multiple Phosphorylations to the Intrinsically Disordered Region of the Histone Chaperone FACT. Download bibtex for citation iamge Akinori Awazu, Daisuke Aoki, Jun-ichi Uewaki, Manami Hashimoto, Masashi Fujii, Naoya Tochio, Shin-ichi Tate, Takashi Umehara
36014 Chemical Shifts: 1 set
Solution structure of the Pin1-PPIase (S138A) mutant Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1. Download bibtex for citation iamge Arif Rashid, Jing Wang, Jun-Ichi I Uewaki, Naoya Tochio, Ryosuke Kawasaki, Shin-Ichi I Tate
11588 Chemical Shifts: 1 set
Solution structure of Human Pin1 PPIase C113S mutant Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif in the Active Site of Human Pin1 PPIase Download bibtex for citation iamge Jing Wang, Jun-ichi Uewaki, Naoko Utsunomiya-Tate, Naoya Tochio, Ning Xu, Ryosuke Kawasaki, Shin-ichi Tate, Yu Tamari
11587 Chemical Shifts: 1 set
Solution structure of Human Pin1 PPIase mutant C113A Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif in the Active Site of Human Pin1 PPIase Download bibtex for citation iamge Jing Wang, Jun-ichi Uewaki, Naoko Utsunomiya-Tate, Naoya Tochio, Ning Xu, Ryosuke Kawasaki, Shin-ichi Tate, Yu Tamari
11560 Chemical Shifts: 1 set
Solution structure of the peptidyl prolyl cis-trans isomerase domain of C113D mutant with 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 Jing Wang, Jun-ichi Uewaki, Kazuhiko Igarashi, Naohiro Kobayashi, Naoko Utsunomiya-Tate, Naoya Tochio, Ning Xu, Shin-ichi Tate, Takuma Shiraki, Yu Tamari
11559 Chemical Shifts: 1 set
Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with 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 Jing Wang, Jun-ichi Uewaki, Kazuhiko Igarashi, Naohiro Kobayashi, Naoko Utsunomiya-Tate, Naoya Tochio, Ning Xu, Shin-ichi Tate, Takuma Shiraki, Yu Tamari
11557 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 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