PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11063571-0	2000	Removal of the four C-terminal glycine-rich repeats enhances the thermostability and substrate binding affinity of barley beta-amylase.	Glycine	31-38	1,4-alpha-D-glucan maltohydrolase	Hordeum vulgare	122-134	
11063571-7	2000	The possible reasons for the increased thermostability and substrate binding affinity, due to the removal of the four C-terminal glycine-rich repeats, are discussed in terms of the three-dimensional structure of beta-amylase.	Glycine	129-136	1,4-alpha-D-glucan maltohydrolase	Hordeum vulgare	212-224