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
5780 Chemical Shifts: 1 set
NMR structure of the PYRIN domain of human ASC The Death-domain Fold of the ASC PYRIN Domain, Presenting a Basis for PYRIN/PYRIN Recognition Download bibtex for citation iamge Anatoly Sharipo, Edgar Dahl, Edvards Liepinsh, Eike Staub, Gottfried Otting, Raitis Barbals
5535 Chemical Shifts: 1 set
NMR structure of R3H domain Solution Structure of the R3H Domain from Human Subp-2 Download bibtex for citation iamge Ainars Leonchiks, Anatoly Sharipo, Edvards Liepinsh, Gottfried Otting, Laurent Guignard
5121 Chemical Shifts: 1 set
In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein Download bibtex for citation iamge Anatoly Sharipo, Dene R Littler, Edvards Liepinsh, Gottfried Otting, Inara Line, Neal K Williams, Nicholas E Dixon, Paul MG Curmi, Pavel Prosselkov
5122 Chemical Shifts: 1 set
In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein Download bibtex for citation iamge Anatoly Sharipo, Dene R Littler, Edvards Liepinsh, Gottfried Otting, Inara Line, Neal K Williams, Nicholas E Dixon, Paul MG Curmi, Pavel Prosselkov
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