The structure corresponds to the acidosis-resistant a162H mutant of the switch
region of troponin I bound to the regulatory domain of troponin C.
The relaxation data was obtained using cChimeraA162H, a chimera protein that
contains the acidosis-resistant a162H mutant of the switch region of troponin I
attached to the regulatory domain of troponin C through a flexible linker.
See Pineda-Sanabria et al (2014) ACS Chem. Biol. 9, 2121-2130 for reference on the
wildtype cChimera protein.

Contains the structure of the wild type cTnI peptide that is mutated in this study

Contains the structure of the wild type sTnI peptide that the cTnI peptide mimics in this study.

The structure of cNTnC bound to sTnI that resembles the cNTnC-cTnIA162H complex in this study.

Structure and Dynamics of the Acidosis-Resistant A162H Mutant of the Switch Region of Troponin I Bound to the Regulatory Domain of Troponin C.

The relaxation data was obtained using a chimera protein that contains the
acidosis-resistant a162H mutant of the switch region of troponin I attached to
the regulatory domain of troponin C through a flexible linker.
See Pineda-Sanabria et al (2014) ACS Chem. Biol. 9, 2121-2130 for reference.

Schwieters, Kuszewski, Tjandra and Clore

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax