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Entry ID	Data summary	Entry Title	Citation Title	Authors
52152	Chemical Shifts: 1 set	Endo-b-1,4-xylanase (Xylanase A) WT peak assignments from Bacillus subtilis	Effects of Xylanase A double mutation on substrate specificity and structural dynamics	Bakar A Hassan, Colin A Smith, Dmitry M Korzhnev, James M Aramini, Joshua A Dudley, Kylie J Walters, Meagan E MacDonald, Nicholas Wells
52155	Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T1rho Relaxation Values: 1 set Order Parameters: 1 set T2 Relaxation Values: 1 set	Endo-b-1,4-xylanase (Xylanase A) D11F/R122D double mutant from Bacillus subtilis Lipari-Szabo order parameters and relaxation data	Effects of Xylanase A double mutation on substrate specificity and structural dynamics	Bakar A Hassan, Colin A Smith, Dmitry M Korzhnev, James M Aramini, Joshua A Dudley, Kylie J Walters, Meagan E MacDonald, Nicholas Wells
52154	Heteronuclear NOE Values: 1 set T1 Relaxation Values: 1 set T1rho Relaxation Values: 1 set Order Parameters: 1 set T2 Relaxation Values: 1 set	Endo-b-1,4-xylanase (Xylanase A) WT from Bacillus subtilis Lipari-Szabo order parameters and relaxation data	Effects of Xylanase A double mutation on substrate specificity and structural dynamics	Bakar A Hassan, Colin A Smith, Dmitry M Korzhnev, James M Aramini, Joshua A Dudley, Kylie J Walters, Meagan E MacDonald, Nicholas Wells
52153	Chemical Shifts: 1 set	Endo-b-1,4-xylanase (Xylanase A) D11F/R122D mutant from Bacillus subtilis	Effects of Xylanase A double mutation on substrate specificity and structural dynamics	Bakar A Hassan, Colin A Smith, Dmitry M Korzhnev, James M Aramini, Joshua A Dudley, Kylie J Walters, Meagan E MacDonald, Nicholas Wells
25437	Chemical Shifts: 1 set	Endo T5-ZN+2	Structure and dynamics of the retro-form of the bacteriophage T5 endolysin	Dmitry A Prokhorov, Galina V Mikoulinskaia, Nikolai V Molochkov, Sergei A Taran, Victor P Kutyshenko, Vladimir N Uversky
11542	Chemical Shifts: 1 set	Backbone 1H, 13C, and 15N Chemical Shift Assignments for yeast Tim50 PBD domain	NMR analyses on the interactions of the yeast Tim50 C-terminal region with the presequence and Tim50 core domain.	Bytul M Rahman, Kaori Esaki, Shin Kawano, Takahiro Anzai, Toshiya Endo
16481	Chemical Shifts: 2 sets	1H, 13C and 15N resonance assignments of the hyperthermostable 264-residue endo--1,3-glucanase LamA at 62 C	NMR characterization of a 264-residue hyperthermostable endo-beta-1,3-glucanase.	Carlo PM van Mierlo, Johannes H Ippel, John van der Oost, Sanne M Nabuurs, Sotirios Koutsopoulos, Willem JH van Berkel
5161	Chemical Shifts: 1 set	Characterization of the ATP-binding Domain of the Sarco(endo)plasmic Reticulum Ca (2+) -ATPase: Probing Nucleotide Binding By Multidimensional NMR	Characterization of the ATP-binding Domain of the Sarco(endo)plasmic Reticulum Ca(2+)-ATPase: Probing Nucleotide Binding By Multidimensional NMR	David H MacLennan, Masatsune Kainosho, Mitsuhiko Ikura, Mona Abu-Abed, Tapas Mal
4916	Chemical Shifts: 1 set	RECEPTOR-BOUND CONFORMATION OF PACAP21	Conformation of a Peptide Ligand bound to its G-protein Coupled Receptor	C Kitada, H Inooka, H Onda, K Ogi, M Fujino, M Shirakawa, O Kitahara, S Endo, T Ikegami, T Ohtaki
4496	Chemical Shifts: 1 set	Solution nmr structure of the mitochondrial protein import receptor Tom20 from rat in a complex with a presequence peptide derived from rat aldehyde dehydrogenase (ALDH)	Structure Basis of Presequence Recognition by the Mitochondrial Protein Import Receptor Tom20	D Kohda, H Torii, K Mihara, S Nishikawa, T Endo, T Muto, T Shodai, Y Abe
1201	Chemical Shifts: 1 set	Conformation in solution of porcine brain natriuretic peptide determined by combined use of nuclear magnetic resonance and distance geometry	Conformation in solution of porcine brain natriuretic peptide determined by combined use of nuclear magnetic resonance and distance geometry	Eiji Mizuta, Hiroshi Inooka, Mitsuhiro Wakimasu, Satoshi Endo, Takashi Kikuchi, Yoshihiro Ishibashi
306	Chemical Shifts: 1 set	N-Terminal Half of a Mitochondrial Presequence Peptide Takes a Helical Conformation When Bound to Dodecylphosphocholine Micelles: A Proton Nuclear Magnetic Resonance Study	N-Terminal Half of a Mitochondrial Presequence Peptide Takes a Helical Conformation When Bound to Dodecylphosphocholine Micelles: A Proton Nuclear Magnetic Resonance Study	David Roise, Fuyuhiko Inagaki, Ichio Shimada, Toshiya Endo
193	Chemical Shifts: 1 set	Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry.	Solution conformation of endothelin determined by nuclear magnetic resonance and distance geometry.	Chieko Kitada, Eiji Mizuta, Hiroshi Inooka, Masahiko Fujino, Satoshi Endo, Yoshihiro Ishibashi
307	Chemical Shifts: 1 set	N-Terminal Half of a Mitochondrial Presequence Peptide Takes a Helical Conformation When Bound to Dodecylphosphocholine Micelles: A Proton Nuclear Magnetic Resonance Study	N-Terminal Half of a Mitochondrial Presequence Peptide Takes a Helical Conformation When Bound to Dodecylphosphocholine Micelles: A Proton Nuclear Magnetic Resonance Study	David Roise, Fuyuhiko Inagaki, Ichio Shimada, Toshiya Endo