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Entry ID	Data summary	Entry Title	Citation Title	Authors
51008	Chemical Shifts: 2 sets	A novel in vitro Ab40 polymorph, which was used to study the PET agent flutemetamol binding to Ab40.	Binding Sites of a Positron Emission Tomography Imaging Agent in Alzheimer's beta-Amyloid Fibrils Studied Using 19 F Solid-State NMR	Aurelio J Dregni, Gayani Wijegunawardena, Haifan Wu, Harrison K Wang, Kelly J Chen, Mei Hong, Pu Duan
51009	Chemical Shifts: 2 sets	A novel in vitro Ab40 polymorph, which was used to study the PET agent flutemetamol binding to Ab40.	Binding Sites of a Positron Emission Tomography Imaging Agent in Alzheimer's beta-Amyloid Fibrils Studied Using 19 F Solid-State NMR	Aurelio J Dregni, Gayani Wijegunawardena, Haifan Wu, Harrison K Wang, Kelly J Chen, Mei Hong, Pu Duan
50785	Chemical Shifts: 1 set	In Vitro Fibrillized 0N3R Tau	Inclusion of the C-Terminal Domain in the beta-Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy	Aurelio J Dregni, Haifan Wu, Harrison K Wang, Jia Jin, Mei Hong, Pu Duan, William F DeGrado
30795	Chemical Shifts: 1 set	SARS-CoV-2 Envelope Protein Transmembrane Domain: Pentameric Structure Determined by Solid-State NMR	Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers	Alexander A Shcherbakov, Antonios Kolocouris, Aurelio J Dregni, Matthew J McKay, Mei Hong, Venkata S Mandala
26536	Chemical Shifts: 1 set	Short hydrophobic peptides with cyclic constraints are po-tent GLP-1R agonists.	Short hydrophobic peptides with cyclic constraints are potent glucagon-like peptide-1 receptor (GLP-1R) agonists	Alan M Mathiowetz, Chris Limberakis, David A Griffith, David A Price, David J Edmonds, David P Fairlie, David R Derksen, David W Piotrowski, Huy N Hoang, Jacky Y Suen, Jane M Withka, Justin M Mitchell, Kun Song, Paula M Loria, Robert V Stanton, Spiros Liras, Timothy A Hill, Vincent Mascitti, W Mei Kok
26538	Chemical Shifts: 1 set	Short hydrophobic peptides with cyclic constraints are po-tent GLP-1R agonists.	Short hydrophobic peptides with cyclic constraints are potent glucagon-like peptide-1 receptor (GLP-1R) agonists	Alan M Mathiowetz, Chris Limberakis, David A Griffith, David A Price, David J Edmonds, David P Fairlie, David R Derksen, David W Piotrowski, Huy N Hoang, Jacky Y Suen, Jane M Withka, Justin M Mitchell, Kun Song, Paula M Loria, Robert V Stanton, Spiros Liras, Timothy A Hill, Vincent Mascitti, W Mei Kok
26537	Chemical Shifts: 1 set	Short hydrophobic peptides with cyclic constraints are po-tent GLP-1R agonists.	Short hydrophobic peptides with cyclic constraints are potent glucagon-like peptide-1 receptor (GLP-1R) agonists	Alan M Mathiowetz, Chris Limberakis, David A Griffith, David A Price, David J Edmonds, David P Fairlie, David R Derksen, David W Piotrowski, Huy N Hoang, Jacky Y Suen, Jane M Withka, Justin M Mitchell, Kun Song, Paula M Loria, Robert V Stanton, Spiros Liras, Timothy A Hill, Vincent Mascitti, W Mei Kok
25517	Chemical Shifts: 1 set	Short hydrophobic peptide, 11mer	Short hydrophobic peptides with cyclic constraints are potent glucagon-like peptide-1 receptor (GLP-1R) agonists	Alan M Mathiowetz, Chris Limberakis, David A Griffith, David A Price, David J Edmonds, David P Fairlie, David R Derksen, David W Piotrowski, Huy N Hoang, Jacky Y Suen, Jane M Withka, Justin M Mitchell, Kun Song, Paula M Loria, Robert V Stanton, Spiros Liras, Timothy A Hill, Vincent Mascitti, W Mei Kok
15603	Chemical Shifts: 1 set Spectral_peak_list: 4 sets	SOLUTION NMR STRUCTURE OF LIPOPROTEIN SPR FROM ESCHERICHIA COLI K12. NORTHEAST STRUCTURAL GENOMICS TARGET ER541-37-162	Solution NMR Structure of the NlpC/P60 Domain of Lipoprotein Spr from Escherichia coli: Structural Evidence for a Novel Cysteine Peptidase Catalytic Triad	Burkhard Rost, Gaetano T Montelione, James M Aramini, Jessica Locke, Li Zhao, Masayori Inouye, Mei Jiang, Melissa Maglaqui, Paolo Rossi, Rajesh Nair, Rong Xiao, Thomas B Acton, Yuanpeng J Huang
15476	Chemical Shifts: 1 set	Solution NMR structure of the folded N-terminal fragment of UPF0291 protein ynzC from Bacillus subtilis. Northeast Structural Genomics target SR384-1-46.	Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis	Burkhard Rost, Chi Kent Ho, Gaetano T Montelione, Gurla VT Swapna, James M Aramini, Jinfeng Liu, Karishma Shetty, Kellie Cunningham, Leah A Owens, Li-Chung Ma, Li Zhao, Mei Jiang, Micheal C Baran, Rong Xiao, Seema Sharma, Thomas B Acton, Yuanpeng J Huang
7180	Chemical Shifts: 1 set	NMR structure of UPF0301 PROTEIN SO3346 from Shewanella oneidensis: Northeast Structural Genomics Consortium target SOR39	NMR structure of UPF0301 PROTEIN SO3346 from Shewanella oneidensis: Northeast Structural Genomics Consortium target SOR39	A Eletsky, B Rost, D K Sukumaran, D Xu, G Liu, G T Montelione, J Mei, K Cunningham, K K Singarapu, L C Ma, R Xiao, S Ritu, T B Acton, T Szyperski
6953	Chemical Shifts: 1 set	NMR solution of rabbit Prion Protein (91-228)	1H, 13C and 15N resonance assignments of rabbit prion protein (91-228)	D H Lin, F H Mei, G F Xiao, J Li
4064	Chemical Shifts: 1 set	Assignments, Secondary Structure and Dynamics of the Inhibitor-Free Catalytic Fragment of Human Fibroblast Collagenase	Assignments, Secondary Structure and Dynamics of the Inhibitor-Free Catalytic Fragment of Human Fibroblast Collagenase	Charlotte Urbano, Franklin J Moy, Loran M Killar, Mei-Li Sung, Michael R Pisano, Pranab K Chanda, Robert Powers
1797	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1791	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1789	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1787	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1785	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1783	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1781	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1779	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1777	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1793	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1775	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi
1795	Chemical Shifts: 1 set	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c	James D Satterlee, Susan J Moench, Ting-Mei Shi