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Entry ID	Data summary	Entry Title	Citation Title	Authors
50434	Chemical Shifts: 1 set	Backbone assignments of AEG12	The mosquito protein AEG12 displays both cytolytic and antiviral properties via a common lipid transfer mechanism.	Alexander Foo, Brianna Lupo, Eugene F DeRose, Geoffrey A Mueller, Lakshmanane Premkumar, Lalith Perera, Lars C Pedersen, Negin Martin, Peter M Thompson, Ramesh Jadi, Shih-Heng H Chen, Simrat Arora, Victoria C Placentra
34521	Chemical Shifts: 1 set Spectral_peak_list: 8 sets	Ternary complex of Calmodulin bound to 2 molecules of NHE1	Dynamic Na +/H + Exchanger 1 (NHE1):Calmodulin complexes of varying stoichiometry and structure regulate Ca 2+-dependent NHE1 activation	A Prestel, B B Kragelund, E S Pedersen, J G Olsen, L M Sjoegaard-Frich, M Severin, S F Pedersen
30520	Chemical Shifts: 1 set	A consensus human beta defensin	Antimicrobial Activity and Structure of a Consensus Human beta-Defensin and Its Comparison to a Novel Putative hBD10	A Rodriguez, B Rivas-Santiago, C Amero, E Villegas, G Corzo, J Villegas-Moreno, M O Pedersen, R S Norton
34012	Chemical Shifts: 1 set	In situ atomic-resolution structure of the baseplate antenna complex in Chlorobaculum tepidum obtained combining solid-state NMR spectroscopy, cryo electron microscopy and polarization spectroscopy	In situ high-resolution structure of the baseplate antenna complex in Chlorobaculum tepidum	C Jegerschold, G Garab, J M Linnanto, J T Nielsen, K Thomsen, M Bjerring, M Dorogi, M Lindahl, M Pedersen, M Ratsep, N C Nielsen, N U Frigaard, N V Kulminskaya, P H Lambrev
25292	Chemical Shifts: 1 set	HIV-1 reverse transcriptase N terminal 216 residues (Fingers and Palm subdomain)	Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation	Eugene F DeRose, Geoffrey A Mueller, Juno M Krahn, Lars C Pedersen, Matthew J Cuneo, Robert E London, Scott A Gabel, Xunhai Zheng
20074	Chemical Shifts: 1 set	Protein Fibril	Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR Spectroscopy	Daniel E Otzen, Jakob T Nielsen, Jan M Pedersen, Kim L Hein, Martin Jeppesen, Morten Bjerring, Niels Christian Nielsen, Ronnie O Pedersen, Thomas Vosegaard, Troels Skrydstrup
15566	Chemical Shifts: 1 set	POLYMERASE LAMBDA BRCT DOMAIN	A comparison of BRCT domains involved in nonhomologous end-joining: Introducing the solution structure of the BRCT domain of polymerase lambda	A F Moon, D A Ramsden, E F Derose, G A Mueller, J M Havener, L C Pedersen, R E London
4595	Chemical Shifts: 1 set	Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P25	Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation	A S Mildvan, M A Massiah, P L Pedersen, Y H Ko
4596	Chemical Shifts: 1 set	Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P26	Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P26	A S Mildvan, M A Massiah, P L Pedersen, Y H Ko
4597	Chemical Shifts: 1 set	Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation	Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation	A S Mildvan, M A Massiah, P L Pedersen, Y H Ko
4598	Chemical Shifts: 1 set	Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation	Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation	A S Mildvan, M A Massiah, P L Pedersen, Y H Ko