PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21210651-4	2011	This peptide, designated AMP-IBP5 (antimicrobial peptide derived from insulin-like growth factor-binding protein 5), showed antimicrobial activity against six of the eight microorganisms tested at concentrations comparable to or lower than those for well-characterized AMPs cathelicidin and beta-defensin-2.	Adenosine Monophosphate	25-28	insulin like growth factor binding protein 5	Homo sapiens	29-33	
21210651-4	2011	This peptide, designated AMP-IBP5 (antimicrobial peptide derived from insulin-like growth factor-binding protein 5), showed antimicrobial activity against six of the eight microorganisms tested at concentrations comparable to or lower than those for well-characterized AMPs cathelicidin and beta-defensin-2.	Adenosine Monophosphate	25-28	insulin-like growth factor binding protein 5	Rattus norvegicus	70-114	
21210651-4	2011	This peptide, designated AMP-IBP5 (antimicrobial peptide derived from insulin-like growth factor-binding protein 5), showed antimicrobial activity against six of the eight microorganisms tested at concentrations comparable to or lower than those for well-characterized AMPs cathelicidin and beta-defensin-2.	Adenosine Monophosphate	25-28	defensin beta 2	Rattus norvegicus	291-306	
21210651-4	2011	This peptide, designated AMP-IBP5 (antimicrobial peptide derived from insulin-like growth factor-binding protein 5), showed antimicrobial activity against six of the eight microorganisms tested at concentrations comparable to or lower than those for well-characterized AMPs cathelicidin and beta-defensin-2.	Adenylyl sulfate	269-273	insulin like growth factor binding protein 5	Homo sapiens	29-33	
21210651-5	2011	AMP-IBP5 is identical at the amino acid level between human, mouse, rat, pig, and cow.	Adenosine Monophosphate	0-3	insulin like growth factor binding protein 5	Homo sapiens	4-8	
21210651-7	2011	The peptide is flanked N-terminally by a single arginine and C-terminally by a common amidation signal, indicating that insulin-like growth factor-binding protein 5 (IGFBP-5) undergoes specific cleavage by a defined set of processing proteases.	Arginine	48-56	insulin-like growth factor binding protein 5	Rattus norvegicus	120-164	
21210651-7	2011	The peptide is flanked N-terminally by a single arginine and C-terminally by a common amidation signal, indicating that insulin-like growth factor-binding protein 5 (IGFBP-5) undergoes specific cleavage by a defined set of processing proteases.	Arginine	48-56	insulin-like growth factor binding protein 5	Rattus norvegicus	166-173	
21210651-8	2011	Furthermore, the intramolecular linkage C199-C210 reveals itself as a correct disulfide pairing in the precursor protein, the finding not inferred from closely related family members IGFBP-4 and -6.	Disulfides	78-87	insulin-like growth factor binding protein 4	Rattus norvegicus	183-197