mpidb The Microbial Protein Interaction Database Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride. Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride. J. Bacteriol. (ISSN:0021-9193) 2007 imex curation Bachhawat P, Stock AM 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecoli Escherichia coli (strain K12) molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Bachhawat P, Stock AM Accepted 2012-DEC-14 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (ISSN:0021-9193) 2007 Only protein-protein interactions imex curation Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride. Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride. J. Bacteriol. (ISSN:0021-9193) 2007 imex curation Bachhawat P, Stock AM 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions ecoli Escherichia coli (strain K12) x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bachhawat P, Stock AM Accepted 2012-DEC-14 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (ISSN:0021-9193) 2007 Only protein-protein interactions imex curation phop_ecoli Transcriptional regulatory protein PhoP phoP b1130 JW1116 protein protein ecoli Escherichia coli (strain K12) MRVLVVEDNALLRHHLKVQIQDAGHQVDDAEDAKEADYYLNEHIPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNSGLASQVISLPPFQVDLSRRELSINDEVIKLTAFEYTIMETLIRNNGKVVSKDSLMLQLYPDAELRESHTIDVLMGRLRKKIQAQYPQEVITTVRGQGYLFELR DIP protein P23836 original sequence version: 95 2EFF27E3923D43EF phop-phop 1 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 region phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig 5 phop-phop-1 2 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 2.54A Rworking = 0.21 Rfree = 0.25 Table 1