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
15276 Chemical Shifts: 1 set
1H, 13C and 15N resonance assignment of 6aJL2(R25G), a highly fibrillogenic lamdaVI light chain variable domain. 1H, 13C and 15N resonance assignment of 6aJL2(R25G), a highly fibrillogenic lamdaVI light chain variable domain. Download bibtex for citation iamge Baltazar Becerril, Christian Lucke, Leopoldo Guereca, Lucia Muresanu, Luis del Pozo-Yauner, Luis H Gutierrez-Gonzalez, Rosalba Sanchez
6966 Chemical Shifts: 1 set
1H and 15N assignment of cytochrome c552 from Thermus thermophilus in the reduced state The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach Download bibtex for citation iamge Bernd Ludwig, Christian Luecke, Frank Loehr, Heinz Rueterjans, Lucia Muresanu, Marco D Mukrasch, Oliver Maneg, Primoz Pristovsek
6967 Chemical Shifts: 1 set
1H and 15N assignment of cytochrome c552 from Thermus thermophilus in the oxidized state The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach Download bibtex for citation iamge Bernd Ludwig, Christian Luecke, Frank Loehr, Heinz Rueterjans, Lucia Muresanu, Marco D Mukrasch, Oliver Maneg, Primoz Pristovsek
6965 Chemical Shifts: 1 set
1H and 15N assignment of the soluble domain of the ba3 oxidase subunit II of Thermus thermophilus in the oxidized state The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach Download bibtex for citation iamge Bernd Ludwig, Christian Luecke, Frank Loehr, Heinz Rueterjans, Lucia Muresanu, Marco D Mukrasch, Oliver Maneg, Primoz Pristovsek
5539 Chemical Shifts: 1 set
Solution Structure and Stability of the Full-Length Excisionase (Xis) from Bacteriophage HK022 Solution Structure and Stability of the Full-Length Excisionase from Bacteriophage HK022 Download bibtex for citation iamge C Luecke, Frank Loehr, Hans Wienk, Heinz Rueterjans, Ioana Kleinhaus, Karla Werner, Lucia Muresanu, Primoz Pristovsek, Vladimir V Rogov