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
34496 Chemical Shifts: 1 set
Heteronuclear NOE Values: 1 set
T1 Relaxation Values: 1 set
T2 Relaxation Values: 1 set
Ca2+-bound Calmodulin mutant N53I The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-domain, altering its interaction with the cardiac ryanodine receptor Download bibtex for citation iamge A B Sorensen, C Holt, C Sommer, F V Petegem, K Lau, K T Larsen, L Hamborg, M Brohus, M T Overgaard, R Wimmer
34497 Chemical Shifts: 1 set
Heteronuclear NOE Values: 1 set
T1 Relaxation Values: 1 set
T2 Relaxation Values: 1 set
Ca2+-free Calmodulin mutant N53I The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-domain, altering its interaction with the cardiac ryanodine receptor Download bibtex for citation iamge A B Sorensen, C Holt, C Sommer, F V Petegem, K Lau, K T Larsen, L Hamborg, M Brohus, M T Overgaard, R Wimmer
34263 Chemical Shifts: 1 set
Calmodulin mutant - F141L apo-form Unstructured C-domain Arrhythmia mutations in calmodulin cause conformational changes that affect interactions with the cardiac voltage-gated calcium channel Download bibtex for citation iamge C Holt, F V Petegem, J Lu, K T Larsen, K Wang, M Brohus, M T Overgaard, R Wimmer