BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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Entry ID Data summary Entry Title Citation Title Authors
4919 Chemical Shifts: 1 set
Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29. NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer Download bibtex for citation iamge Anatoly Sharipo, Edvards Liepinsh, Gottfried Otting, Magnus Ingelman-Sundberg, Michail Baryshev, Souren Mkrtchian
4920 Chemical Shifts: 1 set
Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer Download bibtex for citation iamge Anatoly Sharipo, Edvards Liepinsh, Gottfried Otting, Magnus Ingelman-Sundberg, Michail Baryshev, Souren Mkrtchian