MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint mcdowall-2015-1 ecoli Escherichia coli (strain K12) affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom ms participant Identification by mass spectrometry ms participant McDowall JS., Hjersing MC., Palmer T., Sargent F. f.sargent@dundee.ac.uk FEBS letters 2015 Only protein-protein interactions imex curation imex curation hycg_ecoli Formate hydrogenlyase subunit 7 Hydrogenase-3 component G hycG hevG b2719 JW2689 protein protein ecoli Escherichia coli (strain K12) MSNLLGPRDANGIPVPMTVDESIASMKASLLKKIKRSAYVYRVDCGGCNGCEIEIFATLSPLFDAERFGIKVVPSPRHADILLFTGAVTRAMRSPALRAWQSAPDPKICISYGACGNSGGIFHDLYCVWGGTDKIVPVDVYIPGCPPTPAATLYGFAMALGLLEQKIHARGPGELDEQPAEILHGDMVQPLRVKVDREARRLAGYRYGRQIADDYLTQLGQGEEQVARWLEAENDPRLNEIVSHLNHVVEEARIR hycf_ecoli Formate hydrogenlyase subunit 6 hycF hevF b2720 JW2690 Hydrogenase-3 component F protein protein ecoli Escherichia coli (strain K12) MFTFIKKVIKTGTATSSYPLEPIAVDKNFRGKPEQNPQQCIGCAACVNACPSNALTVETDLATGELAWEFNLGHCIFCGRCEEVCPTAAIKLSQEYELAVWKKEDFLQQSRFALCNCRVCNRPFAVQKEIDYAIALLKHNGDSRAENHRESFETCPECKRQKCLVPSDRIELTRHMKEAI hycb_ecoli Formate hydrogenlyase subunit 2 hycB hevB b2724 JW2694 Hydrogenase-3 component B protein protein ecoli Escherichia coli (strain K12) MNRFVIADSTLCIGCHTCEAACSETHRQHGLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEFSGSRPLDIPANANTPKAPPAPPAPARVSTLLDWVPGIRAIAVKCDLCSFDEQGPACVRMCPTKALHLVDNTDIARVSKRKRELTFNTDFGDLTLFQQAQSGEAK hyce_ecoli Formate hydrogenlyase subunit 5 Hydrogenase-3 component E hycE hevE b2721 JW2691 protein protein ecoli Escherichia coli (strain K12) MSEEKLGQHYLAALNEAFPGVVLDHAWQTKDQLTVTVKVNYLPEVVEFLYYKQGGWLSVLFGNDERKLNGHYAVYYVLSMEKGTKCWITVRVEVDANKPEYPSVTPRVPAAVWGEREVRDMYGLIPVGLPDERRLVLPDDWPDELYPLRKDSMDYRQRPAPTTDAETYEFINELGDKKNNVVPIGPLHVTSDEPGHFRLFVDGENIIDADYRLFYVHRGMEKLAETRMGYNEVTFLSDRVCGICGFAHSTAYTTSVENAMGIQVPERAQMIRAILLEVERLHSHLLNLGLACHFTGFDSGFMQFFRVRETSMKMAEILTGARKTYGLNLIGGIRRDLLKDDMIQTRQLAQQMRREVQELVDVLLSTPNMEQRTVGIGRLDPEIARDFSNVGPMVRASGHARDTRADHPFVGYGLLPMEVHSEQGCDVISRLKVRINEVYTALNMIDYGLDNLPGGPLMVEGFTYIPHRFALGFAEAPRGDDIHWSMTGDNQKLYRWRCRAATYANWPTLRYMLRGNTVSDAPLIIGSLDPCYSCTDRMTVVDVRKKKSKVVPYKELERYSIERKNSPLK 1-89 1884850 N/A 1884851 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate N/A 1884852 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate N/A 1884853 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate N/A 1884854 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed cell lysate cell lysate his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false association association false false false f2 these experiments suggests that the most stable, minimal, core of the FHL complex comprises HycB, -E, -F,and -G, and that this 125kDa species may be formed in the absence of FdhF and/or HycC. these experiments suggests that the most stable, minimal, core of the FHL complex comprises HycB, -E, -F, and -G, and that this 125kDa species may be formed in the absence of FdhF and/or HycC.