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Entry ID Original Release date Data summary Entry Title Citation Title Authors
30734 2020-04-08 Chemical Shifts: 1 set
NMR-driven structure of KRAS4B-GTP homodimer on a lipid bilayer nanodisc Two Distinct Structures of Membrane-associated Homodimers of GTP- and GDP-bound KRAS4B Revealed by Paramagnetic Relaxation Enhancement. Download bibtex for citation iamge C B Marshall, G G Seabrook, K Y Lee, L Zheng, M Enomoto, M Ikura, S Koide, Z Fang
30735 2020-04-27 Chemical Shifts: 1 set
NMR-driven structure of KRAS4B-GDP homodimer on a lipid bilayer nanodisc Two Distinct Structures of Membrane-associated Homodimers of GTP- and GDP-bound KRAS4B Revealed by Paramagnetic Relaxation Enhancement. Download bibtex for citation iamge C B Marshall, G G Seabrook, K Y Lee, L Zheng, M Enomoto, M Ikura, S Koide, Z Fang
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
30019 2016-04-12 Chemical Shifts: 2 sets
NMR structure of UHRF1 Tandem Tudor Domains in a complex with Spacer peptide Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition Download bibtex for citation iamge C Cao, C Tang, H Yang, J Cheng, J Fang, J Wang, J Wong, M Liu, P Wang, Q Zhang, R Gong, W Lan, X Zhang, Y Feng, Y Xu, Z Gong