PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20659345-14 2010 As expected, Cys55 modification reduced the strength of the interaction between Nef-His and CD4 tail peptide by 50%. Histidine 84-87 S100 calcium binding protein B Homo sapiens 80-83 20858440-6 2010 The conformation of Nef was probed upon binding to Langmuir monolayers through the interaction of an N-terminal His tag with a synthetic metal-chelating lipid, which models one of the possible limiting cases for myr-Nef. Histidine 112-115 S100 calcium binding protein B Homo sapiens 20-23 20858440-8 2010 Binding of Nef through the N-terminal His tag apparently facilitates insertion of residues, as no insertion occurred upon binding of Nef through weak electrostatic interactions in the absence of the specific interaction through the His tag. Histidine 38-41 S100 calcium binding protein B Homo sapiens 11-14 20858440-8 2010 Binding of Nef through the N-terminal His tag apparently facilitates insertion of residues, as no insertion occurred upon binding of Nef through weak electrostatic interactions in the absence of the specific interaction through the His tag. Histidine 232-235 S100 calcium binding protein B Homo sapiens 11-14 19469484-5 2009 The SBi279 binding site on Ca(2+)-S100B overlaps the SBi132 and SBi523 sites and contacts residues in both loop 2 (Ser-41, His-42, Phe-43, Leu-44, and Glu-45) and helix 4 (Ile-80, Ala-83, Cys-84, Phe-87, and Phe-88). Histidine 123-126 S100 calcium binding protein B Homo sapiens 34-39 14621986-4 2003 Thus, His-15, His-25, Cys-84, His-85, and perhaps His-90 of S100B are involved in coordinating Zn(2+), which was confirmed by NMR spectroscopy. Histidine 6-9 S100 calcium binding protein B Homo sapiens 60-65 14621986-4 2003 Thus, His-15, His-25, Cys-84, His-85, and perhaps His-90 of S100B are involved in coordinating Zn(2+), which was confirmed by NMR spectroscopy. Histidine 14-17 S100 calcium binding protein B Homo sapiens 60-65 14621986-4 2003 Thus, His-15, His-25, Cys-84, His-85, and perhaps His-90 of S100B are involved in coordinating Zn(2+), which was confirmed by NMR spectroscopy. Histidine 14-17 S100 calcium binding protein B Homo sapiens 60-65 14621986-4 2003 Thus, His-15, His-25, Cys-84, His-85, and perhaps His-90 of S100B are involved in coordinating Zn(2+), which was confirmed by NMR spectroscopy. Histidine 14-17 S100 calcium binding protein B Homo sapiens 60-65 12821199-3 2003 A two-step procedure that includes heparin and immobilized metal ion affinity chromatographies (IMACs) was developed to purify His-tagged Nef (His(6)-Nef) expressed in bacteria in native condition. Histidine 127-130 S100 calcium binding protein B Homo sapiens 138-141 12821199-3 2003 A two-step procedure that includes heparin and immobilized metal ion affinity chromatographies (IMACs) was developed to purify His-tagged Nef (His(6)-Nef) expressed in bacteria in native condition. Histidine 127-130 S100 calcium binding protein B Homo sapiens 143-153 27251136-11 2016 CONCLUSIONS: Our structures of Zn(2+)/Ca(2+)-bound hS100A8 demonstrate that S100A8 is a genuine His-Zn S100 protein. Histidine 96-99 S100 calcium binding protein B Homo sapiens 52-56