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Entry ID	Data summary	Entry Title	Citation Title	Authors
34396	Chemical Shifts: 1 set	Structure of pore-forming amyloid-beta tetramers	Abeta(1-42) Tetramer and Octamer Structures Reveal Edge Conductivity Pores as a Mechanism for Membrane Damage	Andres S Arango, Benjamin Bardiaux, Eduard Puig, Emad Tajkhorshid, Giovanni Maglia, Jimmy Do, Mariam Bayoumi, Maxim Mayzel, Moeen Meigooni, Natalia Carulla, Sarah Cianferani, Sonia Ciudad, Stephane Chaignepain, Thomas Botzanowski, Vladislav Orekhov
27784	Chemical Shifts: 1 set	Backbone 1H, 15N, 13C Chemical Shift Assignment of the Pfr state of monomeric PAS-GAF-PHY from Deinococcus radiodurans	A photoactivated soft-to-rigid transition in the bacteriophytochrome PHY tongue - a solution NMR study of a 57 kDa protein	Cecilia Persson, Emil Gustavsson, Goran Karlsson, Janne Ihalainen, Lidija Vrhovac, Linnea Isaksson, Maxim Mayzel, Sebastian Westenhoff, Ulrika Brath, Vladislav Orekhov
27783	Chemical Shifts: 1 set	Backbone 1H, 15N, 13C Chemical Shift Assignment of the Pr state of monomeric PAS-GAF-PHY from Deinococcus radiodurans	A photoactivated soft-to-rigid transition in the bacteriophytochrome PHY tongue - a solution NMR study of a 57 kDa protein	Cecilia Persson, Emil Gustavsson, Goran Karlsson, Janne Ihalainen, Lidija Vrhovac, Linnea Isaksson, Maxim Mayzel, Sebastian Westenhoff, Ulrika Brath, Vladislav Orekhov
27586	Chemical Shifts: 1 set Spectral_peak_list: 3 sets	5 and 7 dimensional spectra of alpha-synuclein	XLSY: Extra-Large NMR Spectroscopy	Maxim Mayzel, Vladislav Orekhov, Yulia Pustovalova
25674	Chemical Shifts: 1 set	Backbone Assignment of the MALT1 Paracaspase by Solution NMR	Backbone Assignment of the MALT1 Paracaspase by Solution NMR	Gun Stenberg, Jimmy Lindberg, Maxim Mayzel, Michal Nowakowski, Sofia Unnerstaale, Tatiana Agback, Vera Baraznenok, Vladislav Orekhov
19876	Chemical Shifts: 1 set	3D structure of YmoB. A modulator of biofilm formation.	TomB/YmoB proteins: structure and function in biofilm regulation.	Irene Amata, Maxim Mayzel, Miquel Pons, Oriol Marimon, Thomas K Wood, Tiago N Cordeiro, Vladislav Y Orekhov
19656	Chemical Shifts: 1 set	CD79b cytosolic domain phosphorylated, denatured state	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.	Anders Pedersen, Bernhard Brutscher, B Goran Karlsson, Joakim Rosenlow, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Y Orekhov
19655	Chemical Shifts: 1 set	CD79b cytosolic domain phosphorylated	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.	Anders Pedersen, Bernhard Brutscher, B Goran Karlsson, Joakim Rosenlow, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Y Orekhov
19649	Chemical Shifts: 1 set	CD79a cytosolic domain phosphorylated, denatured state	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.	Anders Pedersen, Bernhard Brutscher, B Goran Karlsson, Joakim Rosenlow, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Y Orekhov
19648	Chemical Shifts: 1 set	CD79a cytosolic domain phosphorylated	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.	Anders Pedersen, Bernhard Brutscher, B Goran Karlsson, Joakim Rosenlow, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Y Orekhov
19650	Chemical Shifts: 1 set	CD79b cytosolic domain	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.	Anders Pedersen, Bernhard Brutscher, B Goran Karlsson, Joakim Rosenlow, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Y Orekhov
19651	Chemical Shifts: 1 set	CD79b cytosolic domain denatured	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.	Anders Pedersen, Bernhard Brutscher, B Goran Karlsson, Joakim Rosenlow, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Y Orekhov
19645	Chemical Shifts: 1 set	CD79a cytosolic domain denatured	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.	Anders Pedersen, Bernhard Brutscher, B Goran Karlsson, Joakim Rosenlow, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Y Orekhov
19644	Chemical Shifts: 1 set	CD79a cytosolic domain native	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.	Anders Pedersen, Bernhard Brutscher, B Goran Karlsson, Joakim Rosenlow, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Y Orekhov
19195	Chemical Shifts: 1 set	alfa-actinin from parasite Entamoeba histolytica	alfa-actinin from parasite Entamoeba histolytica	Cecilia K Persson, Goran B Karlsson, Lars Backman, Maxim L Mayzel
18890	Chemical Shifts: 1 set	CD3g cytosolic domain	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains	Anders Pedersen, Bernhard Brutscher, Goran Karlsson, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Orekhov
18889	Chemical Shifts: 2 sets	CD3e cyt	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains	Anders Pedersen, Bernhard Brutscher, Goran Karlsson, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Orekhov
18884	Chemical Shifts: 1 set	CD79b cytosolic domain	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains	Anders Pedersen, Bernhard Brutscher, Goran Karlsson, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Orekhov
18867	Chemical Shifts: 2 sets	CD79a cytosolic domain	Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains	Anders Pedersen, Bernhard Brutscher, Goran Karlsson, Linnea Isaksson, Maria Saline, Maxim Mayzel, Vladislav Orekhov
16005	Chemical Shifts: 1 set	EphA2 dimeric structure in the lipidic bicelle at pH 5.0	Left-handed dimer of EphA2 transmembrane domain: Helix packing diversity among receptor tyrosine kinases.	Alexander S Arseniev, Alexey A Schulga, Eduard V Bocharov, Elena N Tkach, Konstantin S Mineev, Maxim L Mayzel, Pavel E Volynsky, Roman G Efremov, Yaroslav S Ermolyuk
15728	Chemical Shifts: 1 set Coupling Constants: 2 sets Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set	NMR structures of dimeric transmembrane domain of the receptor tyrosine kinase EphA1 in lipid bicelles at pH 4.3	Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1	Alexander S Arseniev, Alexey A Schulga, Eduard V Bocharov, Elena O Artemenko, Marina V Goncharuk, Maxim L Mayzel, Pavel E Volynsky, Roman G Efremov, Yaroslav S Ermolyuk