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Entry ID Original Release date Data summary Entry Title Citation Title Authors
34240 2019-03-28 Chemical Shifts: 1 set
Protein environment affects the water-tryptophan binding mode. Molecular dynamics simulations of Engrailed homeodomain mutants Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutants. Download bibtex for citation iamge F Sebesta, J Kozelka, J V Burda, L Zidek, M Zachrdla, N Spackova, P Srb, S Jansen, Z Trosanova
30401 2018-08-20 Chemical Shifts: 1 set
NMR data-driven model of GTPase KRas-GMPPNP tethered to a nanodisc (E3 state) Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site Download bibtex for citation iamge A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang
30403 2018-08-20 Chemical Shifts: 1 set
NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site Download bibtex for citation iamge A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang
30400 2018-08-31 Chemical Shifts: 1 set
NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc Inhibition of K-RAS4B by a Unique Mechanism of Action: Stabilizing Membrane-Dependent Occlusion of the Effector-Binding Site Download bibtex for citation iamge A D Gossert, C B Marshall, J M Jansen, M Ikura, T Nishikawa, W Jahnke, Z Fang