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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
50746	2021-04-06	Chemical Shifts: 1 set	1H, 13C and 15N assignment of the flexible C-terminus of alpha-synuclein bound to lipid vesicles	Partial magic angle spinning NMR 1H, 13C, 15N resonance assignments of the flexible regions of a monomeric alpha-synuclein: conformation of C-terminus in the lipid-bound and amyloid fibril states	Carla Coackley, Catherine Jany, George Harauz, Justin Medeiros, Meaghan Ward, Scott D Ryan, Vladimir Ladizhansky, Vladimir V Bamm
19972	2019-07-11	Chemical Shifts: 1 set	The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn	The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro	George Harauz, Graham Smith, Kenrick A Vassall, Miguel De Avila, Vladimir V Bamm
19949	2019-07-11	Chemical Shifts: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set	The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn	The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro	George Harauz, Graham Smith, Kenrick A Vassall, Miguel De Avila, Vladimir V Bamm
19948	2019-07-11	Chemical Shifts: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set	The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn	The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro	George Harauz, Graham Smith, Kenrick A Vassall, Miguel De Avila, Vladimir V Bamm
18520	2012-09-17	Chemical Shifts: 1 set	Chemical shift assignments of a S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP) in association with dodecylphosphocholine micelles	Solution Nuclear Magnetic Resonance Structure and Molecular Dynamics Simulations of a Murine 18.5 kDa Myelin Basic Protein Segment (S72-S107) in Association with Dodecylphosphocholine Micelles.	Eugenia Polverini, George Harauz, Kyrylo Bessonov, Miguel De Avila, Mumdooh AM Ahmed, Vladimir V Bamm
7358	2007-03-06	Chemical Shifts: 1 set	Backbone 1H, 13C, and 15N Chemical Shift Assignments for the golli myelin basic protein isoform BG21	The BG21 Isoform of Golli Myelin Basic Protein Is Intrinsically Disordered with a Highly Flexible Amino-Terminal Domain	George Harauz, Mumdooh A M Ahmed, Vladimir Ladizhansky, Vladimir V Bamm