PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10215897-3 1999 Considerable changes were observed at both 20 : 1 and 10 : 1 ratios (AGA*IM : antithrombin) in 1H as well as 13C chemical shifts. Hydrogen 95-97 serpin family C member 1 Homo sapiens 78-90 9067613-8 1997 In particular, the observed hydrogen bonding of these residues to the body of the molecule in the latent form explains the mechanism for the release of newly formed antithrombin-protease complexes into the circulation for catabolic removal. Hydrogen 28-36 serpin family C member 1 Homo sapiens 165-177 9737884-9 1998 The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin. Hydrogen 235-243 serpin family C member 1 Homo sapiens 78-90 9784873-2 1998 1H NMR studies demonstrated that, as anticipated, such a modification induces a shift of the conformational equilibrium toward 1C4 (contribution to the conformational equilibrium rises from 37% to 65%) and a substantial decrease of the affinity for antithrombin III (Kd 0.154 microM versus 0.050 microM). Hydrogen 0-2 serpin family C member 1 Homo sapiens 249-265 7721817-9 1995 1H NMR difference spectroscopy of antithrombin complexes with LAH and HAH and competitive binding studies were consistent with LAH accelerating activity being mediated by binding to the same site on the inhibitor as HAH. Hydrogen 0-2 serpin family C member 1 Homo sapiens 34-46 1311598-0 1992 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments. Hydrogen 0-2 serpin family C member 1 Homo sapiens 70-86 7957907-0 1994 Antithrombin histidine variants 1H NMR resonance assignments and functional properties. Hydrogen 32-34 serpin family C member 1 Homo sapiens 0-12 1311598-4 1992 Perturbations to the 1H resonances in the NMR spectrum of antithrombin upon binding of the two series of heparin fragments are compared to those generated by intact heparin binding, as well as to the effects of binding of a synthetic high-affinity pentasaccharide. Hydrogen 21-23 serpin family C member 1 Homo sapiens 58-70 1311598-6 1992 Three of the heparin fragments (hexasaccharide-2, octasaccharide-2, and octasaccharide-1) produce almost identical perturbations in the antithrombin 1H NMR spectrum compared to binding of intact heparin, including perturbations of resonances from tryptophan 49. Hydrogen 149-151 serpin family C member 1 Homo sapiens 136-148 3663595-2 1987 The denaturation of human and bovine antithrombin III by guanidine hydrochloride has been followed by 1H NMR spectroscopy. Hydrogen 102-104 serpin family C member 1 Homo sapiens 37-53 3408716-3 1988 1H NMR spectroscopy has been used to characterize these proteins and to compare them to one another and to native antithrombin III. Hydrogen 0-2 serpin family C member 1 Homo sapiens 114-130 23152789-9 2012 Cavity analyses suggest the presence of a reasonably sized bifurcated cavity in antithrombin that facilitates a firm "hand-shake" with H/HS, but with thrombin, a weaker "high-five". Hydrogen 137-139 serpin family C member 1 Homo sapiens 80-92 3567176-2 1987 1H NMR has been used to characterize and compare the structures of antithrombin III from human, bovine, and porcine plasma as well as to investigate the interactions of each of these proteins with heparin fragments of defined length. Hydrogen 0-2 serpin family C member 1 Homo sapiens 67-83 27783482-0 2017 An Asymmetric Runaway Domain Swap Antithrombin Dimer as a Key Intermediate for Polymerization Revealed by Hydrogen/Deuterium-Exchange Mass Spectrometry. Hydrogen 106-114 serpin family C member 1 Homo sapiens 34-46 27783482-6 2017 Here, we show how hydrogen/deuterium-exchange mass spectrometry (HDX-MS) provides detailed insight into the structural dynamics of each subunit in a polymerization-competent antithrombin dimer. Hydrogen 18-26 serpin family C member 1 Homo sapiens 174-186 21875153-0 2011 Energetics of hydrogen bond switch, residue burial and cavity analysis reveals molecular basis of improved heparin binding to antithrombin. Hydrogen 14-22 serpin family C member 1 Homo sapiens 126-138 21875153-4 2011 Crystal structures and site directed mutagenesis studies have mapped the heparin binding site in ATIII, however the hydrogen bond switch and energetics of interaction during the course of heparin dependent conformational change remains largely unclear. Hydrogen 116-124 serpin family C member 1 Homo sapiens 97-102 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Hydrogen 163-171 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Hydrogen 254-262 serpin family C member 1 Homo sapiens 54-59 21875153-6 2011 In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions. Hydrogen 102-110 serpin family C member 1 Homo sapiens 22-34