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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
50243	2020-05-15	Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set	Backbone (1H, 13C and 15N) Chemical Shift Assignments and 15N Relaxation Parameters for protein kinase Inhibitor alpha (PKIa) bound to cAMP-dependent protein kinase A	Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A	Benjamin R Stultz, Cristina Olivieri, David D Thomas, Donald K Blumenthal, Fernando Porcelli, Geoffrey C Li, Gianluigi Veglia, Jiali Gao, Jonggul Kim, Joseph M Muretta, Manu Veliparambil Subrahmanian, Matthew Neibergall, Susan S Taylor, Yingjie Wang
50238	2020-05-15	Chemical Shifts: 1 set Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set Residual Dipolar Couplings: 2 sets	Backbone (1H, 13C and 15N) Chemical Shift Assignments and 15N Relaxation Parameters for protein kinase Inhibitor alpha (PKIa) free state	Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A	Benjamin R Stultz, Cristina Olivieri, David D Thomas, Donald K Blumenthal, Fernando Porcelli, Geoffrey C Li, Gianluigi Veglia, Jiali Gao, Jonggul Kim, Joseph M Muretta, Manu Veliparambil Subrahmanian, Matthew Neibergall, Susan S Taylor, Yingjie Wang
25468	2016-02-15	Chemical Shifts: 1 set	Solution NMR Structure of PDFL2.1 from Arabidopsis thaliana	NMR structure and conformational dynamics of AtPDFL2.1, a defensin-like peptide from Arabidopsis thaliana.	Fernando Porcelli, Gianluigi Veglia, Holger Bohlmann, Reza Omidvar, Youlin Xia
17119	2010-11-10	Binding_constants: 1 set	Defining the Intramembrane Binding Mechanism of Sarcolipin to Calcium ATPase USing Solution NMR Spectroscopy	Defining the Intramembrane Binding Mechanism of Sarcolipin to Calcium ATPase USing Solution NMR Spectroscopy	Bethany A Buck-Koehntop, David D Thomas, Fernando Porcelli, Gianluigi Veglia, Jarrod J Buffy, Nathaniel J Traaseth