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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
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
19186	2013-08-16	Chemical Shifts: 1 set	Chemical shift assignments of a S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP)	The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein.	Eugenia Polverini, George Harauz, Kenrick A Vassall, Kyrylo Bessonov, Miguel De Avila