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Biological Magnetic Resonance Data BankA 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 |
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34765 | Chemical Shifts: 1 set |
Solution structure of human apo/Calmodulin G113R (G114R) |
Building the Case against Calmodulin G113 - Circumstantial Evidence from Structure and Dynamics
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C V Holler, H Iwai, M B Brohus, M Niemelae, M T Overgaard, N M Petersson, R Wimmer |
34764 | Chemical Shifts: 1 set |
Calcium-bound Calmodulin variant G113R |
Calcium-bound Calmodulin variant G113R
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C V Holler, H Iwai, M A Niemelae, M Brohus, M T Overgaard, N M Petersson, R Wimmer |
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
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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
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A B Sorensen, C Holt, C Sommer, F V Petegem, K Lau, K T Larsen, L Hamborg, M Brohus, M T Overgaard, R Wimmer |
34262 | Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
Calcium bound form of human calmodulin mutant F141L |
Arrhythmia mutations in calmodulin cause conformational changes that affect interactions with the cardiac voltage-gated calcium channel
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C Holt, F van Petegem, J Lu, K T Larsen, K Wang, 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
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C Holt, F V Petegem, J Lu, K T Larsen, K Wang, M Brohus, M T Overgaard, R Wimmer |