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
26309 Chemical Shifts: 1 set
Backbone 1H, 15N, and 13C resonance assignments of the Phafin2 PH domain Backbone 1 H, 15 N, and 13 C resonance assignments of the Phafin2 pleckstrin homology domain Download bibtex for citation iamge Daniel GS Capelluto, Jeffrey F Ellena, Narasimhamurthy Shanaiah, Tuo-Xian Tang
26806 Chemical Shifts: 1 set
Chemical Shift Assignment of Tom1 VHS Domain Backbone 1H, 15N, and 13C resonance assignments of the Tom1 VHS domain Download bibtex for citation iamge Daniel Capelluto, Jeffrey Ellena, Narasimhamurthy Shanaiah, Wen Xiong, Xiaolin Zhao
25632 Chemical Shifts: 1 set
Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism Download bibtex for citation iamge Carla V Finkielstein, Daniel GS Capelluto, Geoffrey S Armstrong, Jeffrey F Ellena, John H Bushweller, Kristen I Fread, Mary K Brannon, Shuyan Xiao, Xiaolin Zhao
25602 Chemical Shifts: 1 set
Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism Download bibtex for citation iamge Carla V Finkielstein, Daniel GS Capelluto, Geoffrey S Armstrong, Jeffrey F Ellena, John H Bushweller, Kristen I Fread, Mary K Brannon, Shuyan Xiao, Xiaolin Zhao
26573 Chemical Shifts: 1 set
Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism Download bibtex for citation iamge Carla V Finkielstein, Daniel GS Capelluto, Geoffrey S Armstrong, Jeffrey F Ellena, John H Bushweller, Kristen I Fread, Mary K Brannon, Shuyan Xiao, Xiaolin Zhao
26574 Chemical Shifts: 1 set
Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism Download bibtex for citation iamge Carla V Finkielstein, Daniel GS Capelluto, Geoffrey S Armstrong, Jeffrey F Ellena, John H Bushweller, Kristen I Fread, Mary K Brannon, Shuyan Xiao, Xiaolin Zhao
19584 Chemical Shifts: 1 set
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Dvl-2 DEP domain Biophysical and Molecular-Dynamics Studies of Phosphatidic Acid Binding by the Dvl-2 DEP Domain. Download bibtex for citation iamge Andrew Lucas, Carla V Finkielstein, Daniel GS Capelluto, David R Bevan, Furong Sun, Justin A Lemkul, Shuyan Xiao, Xiangping Fu, Xiaolin Zhao
18449 Chemical Shifts: 1 set
Structure, sulfatide-binding properties, and inhibition of platelet aggregation by a Disabled-2-derived peptide Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide. Download bibtex for citation iamge Alireza Salmanzadeh, Carla V Finkielstein, Daniel GS Capelluto, John J Charonko, Pavlos P Vlachos, Rafael V Davalos, Shuyan Xiao, Xiangping Fu
18157 Chemical Shifts: 1 set
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Avirulence homolog-5 Structural basis for interactions of the Phytophthora sojae RxLR effector Avh5 with phosphatidylinositol 3-phosphate and for host cell entry. Download bibtex for citation iamge Brett M Tyler, Daniel GS Capelluto, Dan Li, Furong Sun, Hugo F Azurmendi, Shiv D Kale
5515 Chemical Shifts: 1 set
1H, 13C and 15N resonance assignment of the Dishevelled DIX domain 1H, 13C and 15N resonance assignment of the Dishevelled DIX domain Download bibtex for citation iamge Daniel GS Capelluto, Michael Overduin, Tatiana G Kutateladze