PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25710635-3	2015	To assess potential feasibility of a radical-pair mechanism in DmCry1 and gwCry1a, formed by excitation and electron transfer between a Trp-triad and flavin adenine dinucleotide (FAD), further separated by electron transfer within the triad, we applied a combination of theoretical methods, including homology modeling and molecular dynamics (MD) for structure refinement, high-level ab initio theory, and MD simulations using a polarizable force-field for prediction of pKa and the electron transfer rate.	Tryptophan	136-139	cryptochrome	Drosophila melanogaster	63-69	
25710635-4	2015	Calculated excitation energies, followed by electron transfer in model compounds of DmCry1 that assume proton transfer in conjunction with electron transfer from Trp (W420) to FAD and the predicted pKa for the proximate residue to FAD (Cys416), support a radical-pair mechanism.	Tryptophan	162-165	cryptochrome	Drosophila melanogaster	84-90	
25710635-5	2015	Furthermore, free-energy and reorganization energies for the Trp-triad in DmCry1 demonstrate facile electron transfer, explained by the local protein environment and exposure to solvent, which in turn enables a large enough distance separation for the radical-pair partners.	Tryptophan	61-64	cryptochrome	Drosophila melanogaster	74-80	
11818067-6	2002	Two tryptophan residues in dCRY are critical for its function and are likely involved in an intramolecular redox reaction.	Tryptophan	4-14	cryptochrome	Drosophila melanogaster	27-31