PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7574684-3	1995	Six disulfide linkages were determined to be Cys1-Cys7, Cys5-Cys14, Cys121-Cys145, Cys123-Cys163, Cys187-Cys235, and Cys271-Cys314, respectively.	CYS7	50-54	cystin 1	Homo sapiens	45-49	
7568208-6	1995	On the basis of these comparisons, the LAP domain consensus sequence is Cys1-Xaa1-2-Cys2-Xaa9-21-Cys3-Xaa2-4 -Cys4-Xaa4-5-His5-Xaa2-Cys6-Xaa12-46 - Cys7-Xaa2-Cys8, where subscripted numbers represent the number of amino acid residues.	CYS7	148-152	cystin 1	Homo sapiens	72-76	
7547953-6	1995	Peaks of residues in the N-terminal (Cys1-Cys7) and central (Met 8-Pro23) regions broadened and disappeared faster during the gradual broadening than those in the C-terminal region (Gln24-Pro32).	CYS7	42-46	cystin 1	Homo sapiens	37-41	
8020504-1	1994	The conformational characteristics of elcatonin, an analogue of eel calcitonin having a disulfide bond Cys1-Cys7 replaced by an ethylene linkage between residues 1 and 7, have been analyzed in aqueous trifluoroethanol solutions.	CYS7	108-112	cystin 1	Homo sapiens	103-107	
1931969-5	1991	In SDS, at both pHs, the main conformational feature of the hormone is an alpha-helix from Thr6 through Tyr22, thus including the amphipathic 8-22 segment and two residues of the Cys1-Cys7 N-terminal loop.	CYS7	184-188	cystin 1	Homo sapiens	179-183	
8454613-3	1993	CD experiments reveal that for both peptides, the ordering of the Cys1-Cys7 disulfide link and the alpha-helix formation can be distinguished.	CYS7	71-75	cystin 1	Homo sapiens	66-70	
25702411-1	2013	Linear hepta-peptide Cys-Lys-Gly-Asp-Trp-Asp-Cys was synthesized first and then disulfide bond was formed between the Cys1 and Cys7 to develop cyclo-heptapeptide containing Lys-Gly-Asp-sequence.	CYS7	127-131	cystin 1	Homo sapiens	118-122	
33220304-9	2021	Reduction of the Cys1-Cys7 disulfide bond resulted in faster fibrillation with involvement of different hCT residues as indicated by pulsed HDX-MS.	CYS7	22-26	cystin 1	Homo sapiens	17-21