PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29109150-5	2018	Furthermore, hydrogen-deuterium exchange coupled with mass spectrometry showed that mutation of Asp21 promoted disorder in the N-terminal helices of 14-3-3zeta, suggesting that this residue plays an important role in maintaining structure across the dimer interface.	Deuterium	22-31	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta	Homo sapiens	149-159	
22027839-4	2011	We have used small angle x-ray scattering, hydrogen/deuterium exchange kinetics, and Forster resonance energy transfer measurements to determine the low-resolution solution structure of the 14-3-3zeta RGS3 complex.	Deuterium	52-61	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta	Homo sapiens	190-200	
22580067-0	2012	The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: mapping of human 14-3-3zeta homodimer interface.	Deuterium	28-37	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta	Homo sapiens	125-135