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/ Structural basis for the histone chaperone activity of Asf1. Structural basis for the histone chaperone activity of Asf1. Cell (0092-8674) 2006 imex curation English CM., Adkins MW., Carson JJ., Churchill ME., Tyler JK. Chromatin - Epigenetic interactions resulting in chromatin modulation N-terminal truncation of the histones and coexpression of the three proteins was necessary to obtain the crystals. The structure was solved by molecular replacement with the structures of Asf1 and the histone H3/H4 dimer from the nucleosome jessica.tyler@uchsc.edu,mair.churchill@uchsc.edu 08-DEC-2006: Contacted by JYOTI. Only protein-protein interactions 1 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined English CM., Adkins MW., Carson JJ., Churchill ME., Tyler JK. Chromatin - Epigenetic interactions resulting in chromatin modulation N-terminal truncation of the histones and coexpression of the three proteins was necessary to obtain the crystals. The structure was solved by molecular replacement with the structures of Asf1 and the histone H3/H4 dimer from the nucleosome jessica.tyler@uchsc.edu,mair.churchill@uchsc.edu Accepted 2006-NOV-24 by DAVET. 08-DEC-2006: Contacted by JYOTI. Cell (0092-8674) 2006 Only protein-protein interactions 1 imex curation h4_xenla Histone H4 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62799 original sequence version: 90 DIP protein P62799 original sequence version: 50 DIP protein P62799 original sequence version: 53 DIP protein P62799 original sequence version: 68 DIP protein P62799 original sequence version: 91 DIP protein P62799 original sequence version: 109 A9E5DFD3F8B97598 asf1_yeast Histone chaperone ASF1 ASF1 YJL115W J0755 CIA1 Anti-silencing function protein 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGDLYPPEQPGVDDEEEEDDEEEDDDEDDEDDEDDDQEDGEGEAEEAAEEEEEEEEKTEDNETNLEEEEEDIENSDGDEEEGEEEVGSVDKNEDGNDKKRRKIEGGSTDIESTPKDAARSTN 186E76075C0B1644 186E76075C0B1644 h32_xenla Histone H3.2 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P84233 original sequence version: 76 DIP protein P84233 original sequence version: 53 DIP protein P84233 original sequence version: 77 DIP protein P84233 original sequence version: 95 6FD8508EA50A0EEC asf1-h3 1 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 ecoli Escherichia coli (strain K12) 2 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 ecoli Escherichia coli (strain K12) 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 ecoli Escherichia coli (strain K12) 9 11 direct interaction direct interaction 1,2, Table S1 A single Asf1-H3/H4 complex formed the asymmetric unit in the crystals, which belong to space group P3121 The protein sequences for H3 proteins P84233 and Q6PI79 are identical. Here we have used P84233 1.7 A