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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 |
---|---|---|---|---|
51236 | Chemical Shifts: 1 set Heteronuclear NOE Values: 2 sets T1 Relaxation Values: 2 sets T2 Relaxation Values: 2 sets |
CI2 L49I/I57V backbone and methyl assignment |
Double Mutant of Chymotrypsin Inhibitor 2 Stabilized through Increased Conformational Entropy
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Andreas Prestel, Felix Kummerer, Kaare Teilum, Kresten Lindorff-Larsen, Simone Orioli, Yulian Gavrilov |
51235 | Chemical Shifts: 1 set Heteronuclear NOE Values: 2 sets T1 Relaxation Values: 2 sets T2 Relaxation Values: 2 sets |
CI2 L49I backbone and methyl assignment |
Double Mutant of Chymotrypsin Inhibitor 2 Stabilized through Increased Conformational Entropy
|
Andreas Prestel, Felix Kummerer, Kaare Teilum, Kresten Lindorff-Larsen, Simone Orioli, Yulian Gavrilov |
51234 | Chemical Shifts: 1 set Heteronuclear NOE Values: 2 sets T1 Relaxation Values: 2 sets T2 Relaxation Values: 2 sets |
CI2 I57V backbone and methyl assignment |
Double Mutant of Chymotrypsin Inhibitor 2 Stabilized through Increased Conformational Entropy
|
Andreas Prestel, Felix Kummerer, Kaare Teilum, Kresten Lindorff-Larsen, Simone Orioli, Yulian Gavrilov |
51230 | Chemical Shifts: 1 set Heteronuclear NOE Values: 2 sets T1 Relaxation Values: 2 sets T2 Relaxation Values: 2 sets |
CI2 backbone and methyl assignment |
Double Mutant of Chymotrypsin Inhibitor 2 Stabilized through Increased Conformational Entropy
|
Andreas Prestel, Felix Kummerer, Kaare Teilum, Kresten Lindorff-Larsen, Simone Orioli, Yulian Gavrilov |
51181 | Chemical Shifts: 4 sets |
1H/13C/15N Assignments for the transmembrane domains of Kv-like E71V mutant of the potassium channel KcsA |
A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V
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Ahmed Rohaim, Benoit Roux, Bram JA Vermeulen, Federico Napoli, Felix Kummerer, Jing Li, Joao Medeiros-Silva, Lydia Blachowicz, Markus Weingarth |
51180 | Chemical Shifts: 3 sets |
1H/13C/15N Assignments for the transmembrane domains of the potassium channel KcsA WT |
A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V
|
Ahmed Rohaim, Benoit Roux, Bram JA Vermeulen, Federico Napoli, Felix Kummerer, Jing Li, Joao Medeiros-Silva, Lydia Blachowicz, Markus Weingarth |
27680 | Chemical Shifts: 1 set |
1H/13C/15N Assignments for the TM domains of the KcsA potassium channel |
Shifts in the selectivity filter dynamics cause modal gating in K+ channels
|
Benoit Roux, Christoph Muller-Hermes, Felix Kummerer, Jing Li, Joao Medeiros-Silva, Marc Baldus, Markus Weingarth, Shehrazade Jekhmane |
27679 | Chemical Shifts: 1 set |
1H/13C/15N Assignments for the TM domains of the KcsA potassium channel |
Shifts in the selectivity filter dynamics cause modal gating in K+ channels
|
Benoit Roux, Christoph Muller-Hermes, Felix Kummerer, Jing Li, Joao Medeiros-Silva, Marc Baldus, Markus Weingarth, Shehrazade Jekhmane |
27678 | Chemical Shifts: 1 set |
1H/13C/15N Assignments for the TM domains of the KcsA potassium channel |
Shifts in the selectivity filter dynamics cause modal gating in K+ channels
|
Benoit Roux, Christoph Muller-Hermes, Felix Kummerer, Jing Li, Joao Medeiros-Silva, Marc Baldus, Markus Weingarth, Shehrazade Jekhmane |
27676 | Chemical Shifts: 1 set |
1H/13C/15N Assignments for the TM domains of the KcsA potassium channel |
Shifts in the selectivity filter dynamics cause modal gating in K+ channels
|
Benoit Roux, Christoph Muller-Hermes, Felix Kummerer, Jing Li, Joao Medeiros-Silva, Marc Baldus, Markus Weingarth, Shehrazade Jekhmane |