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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
26506	2015-02-09	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	Anonino Polimeno, Eva Meirovitch, Liqun Zhang, Mariano Rech, Matthias Buck, Mirco Zerbetto, Ross Anderson, Sabine Bouguet-Bonnet
17223	2010-11-10	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	D F Hansen, Elliott Stollar, Eva Meirovitch, Lewis E Kay, Pramodh Vallurupalli
15677	2008-11-10	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	Anna Carnini, Dejian Ma, Eva Meirovitch, Pei Tang, Roderic Eckenhoff, Tommy S Tillman, Yan Xu
5720	2003-05-01	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	Edith Kahana, Eva Meirovitch, Jack H Freed, Vitali Tugarinov, Yury E Shapiro, Zhichun Liang
5746	2003-05-01	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	Edith Kahana, Eva Meirovitch, Jack H Freed, Vitali Tugarinov, Yury E Shapiro, Zhichun Liang
4193	1999-09-30	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	Elena V Sineva, Eva Meirovitch, Michael A Sinev