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
26506 Heteronuclear NOE Values: 2 sets
T1 Relaxation Values: 2 sets
T2 Relaxation Values: 2 sets
Order Parameters: 1 set
Analysis of 15N-1H NMR Relaxation in Proteins by a Combined Experimental and Molecular Dynamics Simulation Approach: Picosecond-Nanosecond Dynamics of the Rho GTPase Binding Domain of Plexin-B1 in the Dimeric State Indicates Allosteric Pathways Analysis of 15N-1H NMR Relaxation in Proteins by a Combined Experimental and Molecular Dynamics Simulation Approach: Picosecond-Nanosecond Dynamics of the Rho GTPase Binding Domain of Plexin-B1 in the Dimeric State Indicates Allosteric Pathways Download bibtex for citation iamge Anonino Polimeno, Eva Meirovitch, Liqun Zhang, Mariano Rech, Matthias Buck, Mirco Zerbetto, Ross Anderson, Sabine Bouguet-Bonnet
17223 Chemical Rates: 1 set
Measurement of bond vector orientations in invisible excited states of proteins Measurement of bond vector orientations in invisible excited states of proteins Download bibtex for citation iamge D F Hansen, Elliott Stollar, Eva Meirovitch, Lewis E Kay, Pramodh Vallurupalli
15677 Chemical Shifts: 1 set
Solubilization of transmembrane proteins in water: structural studies of a water-soluble analogue of the potassium channel KcsA NMR studies of a channel protein without membranes: structure and dynamics of water-solubilized KcsA Download bibtex for citation iamge Anna Carnini, Dejian Ma, Eva Meirovitch, Pei Tang, Roderic Eckenhoff, Tommy S Tillman, Yan Xu
5720 Chemical Shifts: 1 set
Heteronuclear NOE Values: 2 sets
T1 Relaxation Values: 2 sets
T2 Relaxation Values: 2 sets
15N Relaxation Data of Escherichia coli Adenylate Kinase in Ligand-Free Form Obtained at Magnetic Fields of 14.10 and 18.79 T Domain Flexibility in Ligand-Free and Inhibitor-Bound Escherichia coli Adenylate Kinase Based on a Mode-Coupling Analysis of 15N Spin Relaxation Download bibtex for citation iamge Edith Kahana, Eva Meirovitch, Jack H Freed, Vitali Tugarinov, Yury E Shapiro, Zhichun Liang
5746 Chemical Shifts: 1 set
Heteronuclear NOE Values: 2 sets
T1 Relaxation Values: 2 sets
T2 Relaxation Values: 2 sets
15N Relaxation Data of Escherichia coli Adenylate Kinase in Complex with Inhibitor Ap5A Obtained at Magnetic Fields of 14.10 and 18.79 T Domain Flexibility in Ligand-Free and Inhibitor-Bound Escherichia coli Adenylate Kinase Based on a Mode-Coupling Analysis of 15N Spin Relaxation Download bibtex for citation iamge Edith Kahana, Eva Meirovitch, Jack H Freed, Vitali Tugarinov, Yury E Shapiro, Zhichun Liang
4193 Chemical Shifts: 1 set
Sequence-Specific 1H, 15N and 13C Assignment of Adenylate Kinase from Escherichia coli in Complex with the Inhibitor AP5A Letter to the Editor: Sequence-Specific 1H, 15N and 13C Assignment of Adenylate Kinase from Escherichia coli in Complex with the Inhibitor AP5A Download bibtex for citation iamge Elena V Sineva, Eva Meirovitch, Michael A Sinev