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 nils-2013-1 Structural differences between the closed and open states of channelrhodopsin-2 as observed by EPR spectroscopy in vitro In vitro electron resonance electron resonance predetermined predetermined participant predetermined Krause N., Engelhard C., Heberle J., Schlesinger R., Bittl R. robert.bittl@fu-berlin.de FEBS Lett. (0014-5793) 2013 Only protein-protein interactions imex curation q8rut8_chlre CHLRE_02g085257v5 acop2 COP4 CSOB CHLREDRAFT_182032 cop4 protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MDYGGALSAVGRELLFVTNPVVVNGSVLVPEDQCYCAGWIESRGTNGAQTASNVLQWLAAGFSILLLMFYAYQTWKSTCGWEEIYVCAIEMVKVILEFFFEFKNPSMLYLATGHRVQWLRYAEWLLTCPVILIHLSNLTGLSNDYSRRTMGLLVSDIGTIVWGATSAMATGYVKVIFFCLGLCYGANTFFHAAKAYIEGYHTVPKGRCRQVVTGMAWLFFVSWGMFPILFILGPEGFGVLSVYGSTVGHTIIDLMSKNCWGLLGHYLRVLIHEHILIHGDIRKTTKLNIGGTEIEVETLVEDEAEAGAVNKGTGKYASRESFLVMRDKMKEKGIDVRASLDNSKEVEQEQAARAAMMMMNGNGMGMGMGMNGMNGMGGMNGMAGGAKPGLELTPQLQPGRVILAVPDISMVDFFREQFAQLSVTYELVPALGADNTLALVTQAQNLGGVDFVLIHPEFLRDRSSTSILSRLRGAGQRVAAFGWAQLGPMRDLIESANLDGWLEGPSFGQGILPAHIVALVAKMQQMRKMQQMQQIGMMTGGMNGMGGGMGGGMNGMGGGNGMNNMGNGMGGGMGNGMGGNGMNGMGGGNGMNNMGGNGMAGNGMGGGMGGNGMGGSMNGMSSGVVANVTPSAAGGMGGMMNGGMAAPQSPGMNGGRLGTNPLFNAAPSPLSSQLGAEAGMGSMGGMGGMSGMGGMGGMGGMGGAGAATTQAAGGNAEAEMLQNLMNEINRLKRELGE cop4 1436659 n/a ChR2 1436660 unspecified role unspecified role unspecified role unspecified role purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f3 The pELDOR time trace of the spin-labeled ChR2-C79 variant (Fig. 3a) shows a fast decay of the signal intensity within the first 500 ns, which is unexpected for a monomeric protein with a single spin-label. The distance distribution derived from the time trace displays a sharp peak at 3.7 nm (Fig. 3b) proving that this ChR2 mutant forms a dimer under our conditions The ChR2 variant containing mutations C34,36,87,179,183,259A and C128T but retaining wild-type cysteines 79 and 208 is abbreviated as ChR2-C79/208. A variant further reduced in cysteine 208 is named ChR2-C79.