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
50985 Chemical Shifts: 1 set
1H, 13C and 15N Chemical Shift Assignments of the R957C mutant from Arkadia (RNF111) E3 RING domain in solution Impact of a Single Nucleotide Polymorphism on the 3D Protein Structure and Ubiquitination Activity of E3 Ubiquitin Ligase Arkadia Download bibtex for citation iamge Athanasios Tsevis, Detlef Bentrop, Georgios A Spyroulias, Konstantinos D Marousis, Kyriakos Bourikas, Maria Birkou, Vasilios Raptis, Vasso Episkopou
28028 Chemical Shifts: 1 set
1H, 13C, 15N backbone and side-chain assignment of the native form of UbcH7 (UBE2L3) 1H, 13C, 15N backbone and side-chain resonance assignment of the native form of UbcH7 (UBE2L3) through solution NMR spectroscopy Download bibtex for citation iamge Antonia Asimakopoulou, Georgios A Spyroulias, Konstantinos D Marousis, Maria Birkou
26753 Chemical Shifts: 1 set
NMR study of non-structural proteins - 1H, 13C, 15N resonance assignment of macro domain of Venezuelan equine encephalitis virus (VEEV) in complex with ADP-ribose NMR study of non-structural proteins: 1H, 13C, 15N backbone and side-chain resonance assignment of macro domain of Venezuelan equine encephalitis virus (VEEV) in complex with ADP-ribose Download bibtex for citation iamge Detlef Bentrop, Dioni Ntonti, Garyfallia I Makrynitsa, Georgios A Spyroulias, Konstantinos D Marousis
25351 Chemical Shifts: 1 set
1H, 13C and 15N Chemical Shift Assignments of the H962C mutant from Arkadia (RNF111) E3 RING domain A Residue Specific Insight into the Arkadia E3 Ubiquitin Ligase Activity and Conformational Plasticity Download bibtex for citation iamge Ariadni K Loutsidou, Christos T Chasapis, Detlef Bentrop, Georgios A Spyroulias, Jonathon M Carthy, Konstantinos D Marousis, Maria Birkou, Moreno Lelli, Torsten Herrmann, Vasso Episkopou
25132 Chemical Shifts: 1 set
NMR study of non-structural proteins - 1H, 13C, 15N resonance assigment of macro domain of Venezuelan equine encephalitis virus (VEEV) NMR study of non-structural proteins Part II: 1H, 13C, 15N backbone & side-chain resonance assignment of macro domain of Venezuelan equine encephalitis virus (VEEV) Download bibtex for citation iamge Detlef Bentrop, Dioni I Ntonti, Garyfallia I Makrynitsa, Georgios A Spyroulias, Konstantinos D Marousis