UniProt UniProt http://www.uniprot.org noble-2007-2 Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor. in vitro In vitro chromatography chromatography technology column chromatography chromatography weight identificat confirmation by molecular weight weight identificat Noble CG., Beuth B., Taylor IA. fig 1 itaylor@nimr.mrc.ac.uk Nucleic Acids Res. (0305-1048) 2007 Only protein-protein interactions imex curation noble-2007-1 Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Noble CG., Beuth B., Taylor IA. itaylor@nimr.mrc.ac.uk Nucleic Acids Res. (0305-1048) 2007 Only protein-protein interactions imex curation atp ATP Adenosine 5'-triphosphate Adenosine triphosphate ADENOSINE-5'-TRIPHOSPHATE Adephos Adetol Adynol Atipi ATP Atriphos Cardenosine Fosfobion Glucobasin H4atp Myotriphos Triadenyl Triphosphaden adenosine 5'-(tetrahydrogen triphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) clp1_yeast mRNA cleavage and polyadenylation factor CLP1 CLP1 YOR250C protein protein yeast Saccharomyces cerevisiae Baker's yeast MASLPGIDEHTTSEELITGDNEWHKLVIPKGSDWQIDLKAEGKLIVKVNSGIVEIFGTELAVDDEYTFQNWKFPIYAVEETELLWKCPDLTTNTITVKPNHTMKYIYNLHFMLEKIRMSNFEGPRVVIVGGSQTGKTSLSRTLCSYALKFNAYQPLYINLDPQQPIFTVPGCISATPISDILDAQLPTWGQSLTSGATLLHNKQPMVKNFGLERINENKDLYLECISQLGQVVGQRLHLDPQVRRSGCIVDTPSISQLDENLAELHHIIEKLNVNIMLVLCSETDPLWEKVKKTFGPELGNNNIFFIPKLDGVSAVDDVYKRSLQRTSIREYFYGSLDTALSPYAIGVDYEDLTIWKPSNVFDNEVGRVELFPVTITPSNLQHAIIAITFAERRADQATVIKSPILGFALITEVNEKRRKLRVLLPVPGRLPSKAMILTSYRYLE B00F7659E83090DA pcf11_yeast Protein PCF11 PCF11 YDR228C YD9934.13C protein 1 of CF I protein protein yeast Saccharomyces cerevisiae Baker's yeast MDHDTEVIVKDFNSILEELTFNSRPIITTLTKLAEENISCAQYFVDAIESRIEKCMPKQKLYAFYALDSICKNVGSPYTIYFSRNLFNLYKRTYLLVDNTTRTKLINMFKLWLNPNDTGLPLFEGSALEKIEQFLIKASALHQKNLQAMLPTPTVPLLLRDIDKLTCLTSERLKNQPNDEKLKMKLLVLSQLKQELKREKLTLNALKQVQMQLRQVFSQDQQVLQERMRYHELQQQQQQQQQQQQQQQQQQQQYHETKDMVGSYTQNSNSAIPLFGNNSDTTNQQNSLSSSLFGNISGVESFQEIEKKKSLNKINNLYASLKAEGLIYTPPKESIVTLYKKLNGHSNYSLDSHEKQLMKNLPKIPLLNDILSDCKAYFATVNIDVLNNPSLQLSEQTLLQENPIVQNNLIHLLYRSKPNKCSVCGKRFGNSESEKLLQNEHLDWHFRINTRIKGSQNTANTGISNSNLNTTTTRKNIQSRNWYLSDSQWAAFKDDEITSTKHKNDYTDPHANKNIDKSALNIHADENDEGSVDNTLGSDRSNELEIRGKYVVVPETSQDMAFKCPICKETVTGVYDEESGEWVWKNTIEVNGKYFHSTCYHETSQNSSKSNSGKVGLDDLKKLVTK 66F91BA9577E82F1 atp-clp1 1022395 n/a 1022397 unspecified role unspecified role neutral component neutral component Stoichiometry: 1.0 n/a 1022398 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 direct interaction direct interaction false false false fig 1 atp-clp1-1 1022395 n/a 1022397 unspecified role unspecified role neutral component neutral component Stoichiometry: 1.0 n/a 1022399 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 n/a 1022398 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 physical association physical association false false false fig 1 pcf11-clp1 1022396 n/a 1022399 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 n/a 1022398 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 direct interaction direct interaction false false false 2.95 A R-value 0.250 R-free 0.303