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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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17777 | Chemical Shifts: 1 set |
Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG |
Structural and functional studies on the N-terminal domain of the Shigella type III secretion protein MxiG.
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A Dorothea Roehrich, Ariel J Blocker, James M McDonnell, Janet E Deane, Martin Cheung, Melanie A McDowell, Steven Johnson, Susan M Lea |
6438 | Chemical Shifts: 1 set |
Sequence-specific resonance assignments of the C-terminal, 137-residue pseudo-receiver domain of circadian input kinase (CikA) that resets the circadian clock in Synechococcus elongatus |
1H, 13C and 15N Chemical Shift Assignments of the C-Terminal, 133-Residue Pseudo-Receiver Domain of Circadian Input Kinase (CikA) in Synechococcus elongatus
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Andy C LiWang, James C Sacchettini, Susan S Golden, Tiyu Gao, Xiaofan Zhang, Yoonsang Cho, Youlin Xia |
4351 | Chemical Shifts: 1 set Coupling Constants: 1 set |
A 30-residue Fragment of the Carp Granulin-1 Protein Folds into a Stack of two Beta-hairpins Similar to that found in the Native Protein |
A 30-residue Fragment of the Carp Granulin-1 Protein Folds into a Stack of two Beta-hairpins Similar to that found in the Native Protein
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Feng Ni, Hugh PJ Bennett, Ping Xu, Susan James, Wim F Vranken, Z G Chen |
4345 | Chemical Shifts: 2 sets |
1H, 13C, and 15N Chemical Shift Assignments for Yeast Ribosomal Protein L30 in Complex with Its mRNA in Solution |
A Novel Loop-loop Recognition Motif in the Yeast Ribosomal Protein L30 Autoregulatory RNA Complex
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Hongyuan Mao, james R Williamson, Susan A White |
4346 | Chemical Shifts: 1 set |
1H, 13C, and 15N Chemical Shift Assignments for the Regulatory mRNA of the Yeast Ribosomal Protein L30 |
A Novel Loop-loop Recognition Motif in the Yeast Ribosomal Protein L30 Autoregulatory RNA Complex
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Hongyuan Mao, james R Williamson, Susan A White |
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 |
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 |
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 |
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 |
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 |
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 |
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 |
2488 | Chemical Shifts: 1 set |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
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Daina Z Avizonis, James D Satterlee, Susan J Moench |
2489 | Chemical Shifts: 1 set |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
|
Daina Z Avizonis, James D Satterlee, Susan J Moench |
330 | Chemical Shifts: 1 set |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer
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James D Satterlee, Susan J Moench |
331 | Chemical Shifts: 1 set |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer
|
James D Satterlee, Susan J Moench |
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 |
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 |
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 |
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 |
499 | Chemical Shifts: 1 set |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c
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James D Satterlee, Susan J Moench |
500 | Chemical Shifts: 1 set |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c
|
James D Satterlee, Susan J Moench |
1192 | Chemical Shifts: 1 set |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c
|
James D Satterlee, Scott C Busse, Susan J Moench |
1194 | Chemical Shifts: 1 set |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c
|
James D Satterlee, Scott C Busse, Susan J Moench |