PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12939144-0	2003	Introduction of a mutation in the shutter region of antithrombin (Phe77 --> Leu) increases affinity for heparin and decreases thermal stability.	Leucine	79-82	serpin family C member 1	Homo sapiens	52-64	
11159540-4	2001	Preincubation in vitro of neutrophils with Kybernin P or immune-adsorbed AT III significantly deactivated migration toward fMet-Leu-Phe, or interleukin-8 (IL-8), in a concentration-dependent manner.	Leucine	128-131	serpin family C member 1	Homo sapiens	73-79	
11380262-4	2001	As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)).	Leucine	67-74	serpin family C member 1	Homo sapiens	120-132	
7512382-7	1994	However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B.	Leucine	143-146	serpin family C member 1	Homo sapiens	37-49	
8037658-8	1994	Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin.	Leucine	81-88	serpin family C member 1	Homo sapiens	200-216	
7730349-2	1995	To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated.	Leucine	163-166	serpin family C member 1	Homo sapiens	56-68	
7730349-2	1995	To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated.	Leucine	163-166	serpin family C member 1	Homo sapiens	70-72	
3305015-14	1987	The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin.	Leucine	83-86	serpin family C member 1	Homo sapiens	255-271	
8429008-8	1993	A three-dimensional molecular model of the Quick II active site compared to alpha-thrombin suggested that the heparin cofactor II Leu-Ser-reactive site sequence (P1-P1") is a compatible "pseudosubstrate" in contrast to the Arg-Ser sequence found in antithrombin.	Leucine	130-133	serpin family C member 1	Homo sapiens	249-261	
8392392-4	1993	Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser).	Leucine	200-203	serpin family C member 1	Homo sapiens	111-123	
3305015-14	1987	The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin.	Leucine	213-216	serpin family C member 1	Homo sapiens	255-271	
16940049-8	2006	Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity.	Leucine	34-37	serpin family C member 1	Homo sapiens	114-126	
16940049-8	2006	Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity.	Leucine	34-37	serpin family C member 1	Homo sapiens	305-310	
16940049-8	2006	Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity.	Leucine	43-46	serpin family C member 1	Homo sapiens	114-126	
16940049-8	2006	Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity.	Leucine	43-46	serpin family C member 1	Homo sapiens	305-310	
3080419-5	1986	The amino acid sequence of the peptide from antithrombin III Basel had a single substitution of Pro (normal) by Leu (abnormal) at position 41.	Leucine	112-115	serpin family C member 1	Homo sapiens	44-56