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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 |
|---|---|---|---|---|
| 26336 | Chemical Shifts: 1 set |
Solution Structure of the Corynebacterium diphtheriae SpaB |
The basal and major pilins in the Corynebacterium diphtheriae SpaA pilus adopt similar structures that competitively react with the pilin polymerase
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Brendan J Mahoney, Christopher K Sue, Chungyu Chang, Hung Ton-That, Jack M Scully, Janine Y Fu, Joseph A Loo, Nicole A Cheung, Robert T Clubb, Scott A McConnell |
| 34617 | Chemical Shifts: 1 set |
Solution NMR Structure of the Neh1 Domain of Human Nuclear factor erythroid 2-related factor 2 (NRF2) |
A Step toward NRF2-DNA Interaction Inhibitors by Fragment-Based NMR Methods
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Darryl B McConnell, Gerd Bader, Julian E Fuchs, Moriz Mayer, Robert Konrat, Sven Bruschweiler |
| 30821 | Chemical Shifts: 1 set Spectral_peak_list: 3 sets |
Solution Structure of the R2ab Repeat Domain from Staph. epidermidis Autolysin (AtlE) |
Solution Structure of the R2ab Repeat Domain from Staph. epidermidis Autolysin (AtlE)
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K D McConnell, N C Fitzkee, R Yadav, T M South, Y R Perera |
| 30800 | Chemical Shifts: 1 set Spectral_peak_list: 6 sets |
Solution Structure of the Corynebacterium diphtheriae SpaA Pilin-Signal Peptide Complex |
Sortase-assembled pili in Corynebacterium diphtheriae are built using a latch mechanism
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B A Amer, B J Mahoney, C Chang, C K Sue, H Ton-That, R A McAllister, R T Clubb, S A McConnell |
| 27635 | T1rho Relaxation Values: 27 sets |
Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance R1rho Relaxation-Dispersion MAS NMR |
Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance R1rho Relaxation-Dispersion MAS NMR
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Diego F Gauto, Dominique Marion, Isabel Ayala, Karine Giandoreggio-Barranco, Paul Schanda |
| 26745 | Chemical Shifts: 1 set |
Backbone 1H, 13C, and 15N assignments for Sortase C1 (SrtC1) from Streptococcus pneumoniae |
The "Lid" in the Streptococcus pneumoniae SrtC1 Sortase Adopts a Rigid Structure that Regulates Substrate Access to the Active Site
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Alex W Jacobitz, Emmanuel B Naziga, Jeff Wereszczynski, Michael E Jung, Robert Peterson, Robert T Clubb, Scott A McConnell, Yi Sung Wook |