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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	Anonino Polimeno, Eva Meirovitch, Liqun Zhang, Mariano Rech, Matthias Buck, Mirco Zerbetto, Ross Anderson, Sabine Bouguet-Bonnet
6970	Chemical Shifts: 1 set	1H, 15N, 13C assignments for the activated form of the small Rho-GTPase Rac1	1H, 15N, 13C assignments for the activated form of the small Rho-GTPase Rac1	Matthias Buck, Sabine Bouguet-Bonnet
6346	Chemical Shifts: 1 set	1H, 15N and 13C Resonance Assignments and Secondary Structure Determination Reveal that the Minimal Rac1 GTPase Binding Domain of Plexin-B1 Has a Ubiquitin Fold	Letter to the Editor: 1H, 15N and 13C Resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold	Matthias Buck, Yufeng Tong
4831	Chemical Shifts: 1 set Residual Dipolar Couplings: 2 sets	Backbone 1H, 13C, and 15N Chemical Shift Assignments for Lysozyme	A Refined Solution Structure of Hen Lysozyme Determined Using Residual Dipolar Coupling Data	Andrew Spencer, Christina Redfield, Christopher M Dobson, Harald Schwalbe, Jonathan Boyd, Lorna J Smith, Matthias Buck, Shaun Grimshaw