MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint anonymous-2014z-1 The cytochrome c peroxidise and cytochrome c encounter complex: The other side of the story in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined m.ubbink@chem.leidenuniv.nl 2014 imex curation Schilder J., Löhr F., Schwalbe H., Ubbink M. FEBS Lett. (0014-5793) Only protein-protein interactions cyc1_yeast Cytochrome c isoform 1 CYC1 Cytochrome c aerobic isoform J1653 YJR048W protein protein yeast Saccharomyces cerevisiae Baker's yeast MTEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 1F8B6CB3B60C0BE8 ccpr_yeast Cytochrome c peroxidase, mitochondrial CCP1 CCP CPO YKR066C protein protein yeast Saccharomyces cerevisiae Baker's yeast MTTAVRLLPSLGRTAHKRSLYLFSAAAAAAAAATFAYSQSQKRSSSSPGGGSNHGWNNWGKAAALASTTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL A5D26385DA6F0A0B ccp1-cyc1-3 1531167 n/a Cc 1531168 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a CcP 1531169 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false f1 f2 f3 f4 Numerous resonances shifted in the spectrum, indicating a fast-exchange binding process. The KB values were determined for the WT or MTS-V28C complex by fitting the CSP curves to a 1:1 binding model (Fig. 1). The KB determined for the complex with WT Cc is KB = 2 ± 1 x 105 M-1, which is the same within error as previously reported. [39,40] The binding constant for the complex with MTSV28C was found to be the same within error, KB = 3 ± 1 x 105 M-1. These values were then used to extrapolate average amide shifts, Δδavg, for 100% bound CcP (Fig. S3). For the WT complex, the overall CSP pattern was similar to that described previously. [41] The CSPs for WT and MTS-V28C in this study were also identical within the error margins (±0.011 ppm) except for 20 peaks showing slightly larger differences (Table S2). The Δδavg values were used to create a CSP map (Fig. 2). For both WT and MTS-V28C Cc, the CSP effects on CcP were localized around the binding interface where Cc is expected to be in the stereospecific complex. The few peaks with significant differences in Δδavg for MTS-V28C (Table S2) are in the centre of the binding interface (square box in Fig. 2). However, overall the differences between the two CSP maps are small and the KB values (Fig. 1) are the same within error, indicating that the effects of the tag on complex formation are minimal.