IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J. Biol. Chem. (0021-9258) 2003 imex curation Gaboriaud C., Juanhuix J., Gruez A., Lacroix M., Darnault C., Pignol D., Verger D., Fontecilla-Camps J.C., Arlaud G.J. I have included the Edman sequencing data, despite lack of figure, as it proves they have the correct proteins. Sequence has been mapped to current UniProt. For the crystal, the PDB header file give a slightly different set of coordinates so have gone with them in that case. C-terminal globular domain of C1q was obtained after digestion of the collagenous part of the protein with collagenase, treated with sialidase, and purified by ion-exchange chromatography. The length of the polypeptide chains were calculated from analysis by mass spectrometry. arlaud@ibs.fr 19-Sept-2012: Contacted by IntAct-Help. Only protein-protein interactions human-serum Homo sapiens serum Serum x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Gaboriaud C., Juanhuix J., Gruez A., Lacroix M., Darnault C., Pignol D., Verger D., Fontecilla-Camps J.C., Arlaud G.J. I have included the Edman sequencing data, despite lack of figure, as it proves they have the correct proteins. Sequence has been mapped to current UniProt. For the crystal, the PDB header file give a slightly different set of coordinates so have gone with them in that case. C-terminal globular domain of C1q was obtained after digestion of the collagenous part of the protein with collagenase, treated with sialidase, and purified by ion-exchange chromatography. The length of the polypeptide chains were calculated from analysis by mass spectrometry. arlaud@ibs.fr Accepted 2012-AUG-13 by MGT 19-Sept-2012: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 2003 Only protein-protein interactions imex curation The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J. Biol. Chem. (0021-9258) 2003 imex curation Gaboriaud C., Juanhuix J., Gruez A., Lacroix M., Darnault C., Pignol D., Verger D., Fontecilla-Camps J.C., Arlaud G.J. I have included the Edman sequencing data, despite lack of figure, as it proves they have the correct proteins. Sequence has been mapped to current UniProt. For the crystal, the PDB header file give a slightly different set of coordinates so have gone with them in that case. C-terminal globular domain of C1q was obtained after digestion of the collagenous part of the protein with collagenase, treated with sialidase, and purified by ion-exchange chromatography. The length of the polypeptide chains were calculated from analysis by mass spectrometry. arlaud@ibs.fr 19-Sept-2012: Contacted by IntAct-Help. Only protein-protein interactions human-serum Homo sapiens serum Serum affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom edman degradation edman degradation Gaboriaud C., Juanhuix J., Gruez A., Lacroix M., Darnault C., Pignol D., Verger D., Fontecilla-Camps J.C., Arlaud G.J. I have included the Edman sequencing data, despite lack of figure, as it proves they have the correct proteins. Sequence has been mapped to current UniProt. For the crystal, the PDB header file give a slightly different set of coordinates so have gone with them in that case. C-terminal globular domain of C1q was obtained after digestion of the collagenous part of the protein with collagenase, treated with sialidase, and purified by ion-exchange chromatography. The length of the polypeptide chains were calculated from analysis by mass spectrometry. arlaud@ibs.fr Accepted 2012-AUG-13 by MGT 19-Sept-2012: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 2003 Only protein-protein interactions imex curation c1qb_human Complement C1q subcomponent subunit B C1QB protein protein human Homo sapiens Human MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA D80C753C0D430EDC c1qc_human Complement C1q subcomponent subunit C C1QC C1QG protein protein human Homo sapiens Human MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEPGIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQSVFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCVLLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGFLLFPD FA17117EB7ABFC12 c1qa_human Complement C1q subcomponent subunit A C1QA protein protein human Homo sapiens Human MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFLIFPSA DIP protein P02745 original sequence version: null 8FF6B6AE02D49C4C c1qa-c1qb 2 3 unspecified role unspecified role unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain association association c1qa-c1qb-2 1 5 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 4 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 3 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 physical association physical association Table 1 1.85A Rworking = 0.2 Rfree = 0.24