| Entry ID | Original Release date | Data summary | Entry Title | Citation Title | Authors | 
    
    
        | 30591 | 2019-06-07 | Chemical Shifts: 1 set 
 | Remarkable rigidity of the single alpha-helical domain of myosin-VI revealed by NMR spectroscopy | Remarkable rigidity of the single alpha-helical domain of myosin-VI revealed by NMR spectroscopy.   | A Bax, C A Barnes, D A Torchia, J R Sellers, J Ying, Y Shen, Y Takagi | 
    
        | 17187 | 2010-11-10 | Binding Constants: 1 set 
 | Elucidation of the poly-L-proline binding site in Acanthamoeba profilin I by NMR spectroscopy | Elucidation of the poly-L-proline binding site in Acanthamoeba profilin I by NMR spectroscopy   | Dennis A Torchia, Sharon J Archer, Thomas D Pollard, Valda K Vinson | 
    
        | 5967 | 2004-05-15 | Chemical Shifts: 1 set 
 | Solution structure of the mature HIV-1 protease monomer | Solution structure of the mature HIV-1 protease monomer: Insight into the tertiary fold and stability of a precursor   | A M Gronenborn, D A Torchia, J M Louis, R Ishima, S M Lynch | 
    
        | 4206 | 2000-03-10 | Chemical Shifts: 1 set 
 | Solution NMR Structure of Linked Cell Attachment Modules of Mouse Fibronectin Containing the RGD and Synergy Regions, 20 Structures | Solution Structure and Dynamics of Linked Cell Attachment Modules of Mouse Fibronectin Containing the RGD and Synergy Regions: Comparison with the Human Fibronectin Crystal Structure   | D A Torchia, K M Yamada, R M Venable, R W Pastor, S Aota, S K Akiyama, S Krueger, V Copie, Y Tomita | 
    
        | 1624 | 1995-07-31 | Chemical Shifts: 1 set 
 | Secondary structure of the phosphocarrier protein III(Glc), a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy | Secondary structure of the phosphocarrier protein III(Glc), a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy   | Cing-Yuen Wong, Dennis A Torchia, J G Pelton, Norman D Meadow, Saul Roseman |