Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.

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One additional, unobservable residue (His) was added to the N-terminus of the protein as a consequence of the removal of the His tag.

Nmr Solution Structure Of The Bacillus Subtilis Clpc N- Domain

Crystal Structure Of Clpc N-Terminal Domain

Structure Of Meca121 & Clpc N-Domain Complex

Structure Of Meca121 And Clpc1-485 Complex

ATP-dependent Clp protease ATP-binding subunit ClpC [Bacillus gobiensis]

NMR solution structure of the Bacillus subtilis ClpC N-domain

cryogenically cooled triple resonance probe

Rex @ 499.8824609 MHz; Rex units = s-1; protocol as described in d'Auvergne,
E.J., and Gooley, P.R. (2008). Optimisation of NMR dynamic models II. A new
methodology for the dual optimisation of the model-free parameters and the
Brownian rotational diffusion tensor. J Biomol NMR 40, 121-133.

isotropic data collected at 499.8824609 MHz; anisotropic data collected at 600.7904943 MHz.

d'Auvergne et al. Optimisation of NMR dynamic models I. Minimisation algorithms
and their performance within the model-free and Brownian rotational diffusion
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Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman
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