PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8891161-2	1996	A novel hydrogen bond between the hydroxyl of Thr-182 and the carbonyl of Glu-64 was expected to be responsible for the increase in the catalytic activity of the IST-T182 and IRT-3 enzymes compared with those of TEM-1 and IRT-169, respectively.	Glutamic Acid	74-77	CD248 molecule	Homo sapiens	212-217	
17070843-10	2007	Here, a double mutation replacing the wild-type Glu,Tyr to Tyr,Asn on TEM1 (res id 104,105) caused a major backbone structural rearrangement of BLIP, changing the composition of two modules but not of other modules within the interface.	Glutamic Acid	48-51	CD248 molecule	Homo sapiens	70-74	
16809340-6	2006	Comparison of the SHV-1.BLIP structure with the published TEM-1.BLIP structure suggests that the increased volume of Glu-104 stabilizes a key binding loop in the interface.	Glutamic Acid	117-120	CD248 molecule	Homo sapiens	58-63	
3116487-2	1987	Titration curves of TEM-1 (pI 5.4) and TEM-2 (pI 5.6) together were consistent with the known substitution of a glutamic acid in the former by a lysin in the latter.	Glutamic Acid	112-125	CD248 molecule	Homo sapiens	20-25	
8964456-5	1996	Molecular modelling of TEM-2, when compared to that of TEM-1, showed an additional ionic bond between Lys-39 and Glu-281.	Glutamic Acid	113-116	CD248 molecule	Homo sapiens	55-60