Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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Entry ID | Data summary | Entry Title | Citation Title | Authors |
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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- |
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 |