DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ froese-2013-1 ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253983X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-2 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253973X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-3 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253976X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-4 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253977X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-5 ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253974X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-6 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253980X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-7 ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253975X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-8 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253978X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-9 ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253981X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-10 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253982X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation froese-2013-11 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. DIP original experiment: DIP-253979X Structure (London, England : 1993) 2013 IMEx Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. Froese DS., Forouhar F., Tran TH., Vollmar M., Kim YS., Lew S., Neely H., Seetharaman J., Shen Y., Xiao R., Acton TB., Everett JK., Cannone G., Puranik S., Savitsky P., Krojer T., Pilka ES., Kiyani W., Lee WH., Marsden BD., von Delft F., Allerston CK., Spagnolo L., Gileadi O., Montelione GT., Oppermann U., Yue WW., Tong L. Only protein-protein interactions imex curation b9k0v9_agrvs Avi_5372 protein protein agrvs Agrobacterium vitis (strain S4 / ATCC BAA-846) Rhizobium vitis (strain S4) MAGTSFLSDLLSGVTERGRALLFSGSKARDRVVDTDIETLCEMLLSSRGEASGMAIAAEILDRWSRFNAAEAVQFLHMLSDRFGAEAAALDKAIDAYRTDKSPMAVIALHNAAEPRRQELLRRLNLAPNGTQKLVRMRERLLETKEDRADLGAVDTDFAHLFSSWFNRGFLTLQPIDWTTPAHILEKIIKYEAVHEIAGWEELRRRLAPADRRCFAFFHPRLRDDPLVFVEVALTRSIPSAIADVLDESRDHIGADTATTAVFYSISNCQDGLRGISFGNFLIKQVVEDLRRDLPGLKEFVTLSPVPGFARWISKIRDPKSGFPLSPEDRNTLVLLDDPTWPEDKARADAVERILLPLAARYFITERTPDNRPVDPVARFHLGNGARLERLNFLGDRSVKAMRQAHGLMVNYLYKLEDIETNHEALAQRGEVAASPAVKALQGKIEPILPEKPKDIKKAESLSGS dcmc_human Malonyl-CoA decarboxylase, mitochondrial MLYCD protein protein human Homo sapiens Human MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL q6ncb2_rhopa MCD MLYCD RPA0560 protein protein rhopa Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) MKLMPIATTADRASEFLGGLFNSLTERGRSLFGLTSSQPMSGDELIALSETLLSRRGEASGVALAASLLAGYEAADEDDKLAFLDALAEQFGPDLAELNTAIEAFRADASAEATGELLRAAEPRRQELIRRLNHAPGGTAALVKMREAVLARIAAHPQLRHVDDDFVHLFTSWFNRGFLVLQRIDWTTPANILEKIIRYEQVHTIHDWDDLRARLAPPDRRCYGFFHPRLVDEPLIFVEVALTKDSPAAIAPLLDLEREPIAASDATTAVFYSISNTQQGLAGISFGNFLIKQVVEEIKRELPNVQTFVTLSPVPGFAKWLKRERDNPDSTLLDASARTALEALDTPNWFDDADTADRLKPIVLQLAAAYFLQAKGPNGRPLDPVARFHLGNGARLDRLNFLGDRSPNGMRQSHGLMVNYLYALGDIEANHEALFERGQIAAASAVRKLVPTKPVTSEPRKGNGKTASAPQAAPTA q1ljk6_cupmc matA Rmet_2797 protein protein cupmc Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) Ralstonia metallidurans MTALDTSDQQKVSAPLDAAEPVSDTLLSRFGRWWNRKGDADATAAGPAKAQDTPALSTRATKRQRDQLRQCFDARLTDVAANAAAQAWQDEYEAAVEPLRQAMLGVLAEVAAVRDAAGGQPATASGLSQALSNARIRFFKRFAALHGQRGNSACGLHFLIQLRADMLRWHKRIPGLRELDEDLEALFSNWFDVGLLELQPITWDSPASLLEKLIRYEAVHEISSWTDLRNRLDSDRRCYAFFHPRIPREPLIFVEVAFVPEMAANVQALLDEAAPLEDLRRVKWAIFYSISNTQAGLRGVSFGNFLLKRVIEELQREHPKLKQFATLSPIPGFADWLRKRDGESIDRVLGVKRLARWREQHGEVPADGAAWFSALSADTEDTVIRDTAMTLAAHYLVREGGKGVPADPVARFHLGNGACVERVNWGADMSRKGRAQSCGMMVNYLYVPDALDDNLARLGDGNPRISRAVAKLL b9k0v9_agrvs-1 3255161 N/A 3255172 unspecified role unspecified role unspecified role unspecified role Region 1-448 Region 1-448 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mlycd-1 3255162 N/A 3255173 unspecified role unspecified role unspecified role unspecified role Region 40-491 Region 40-491 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mlycd-2 3255163 N/A 3255173 unspecified role unspecified role unspecified role unspecified role Region 40-491 Region 40-491 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mcd-1 3255164 N/A 3255174 unspecified role unspecified role unspecified role unspecified role Region 8-451 Region 8-451 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mlycd-3 3255165 N/A 3255173 unspecified role unspecified role unspecified role unspecified role Region 40-491 Region 40-491 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mcd-2 3255166 N/A 3255174 unspecified role unspecified role unspecified role unspecified role Region 8-451 Region 8-451 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mlycd-4 3255167 N/A 3255173 unspecified role unspecified role unspecified role unspecified role Region 40-491 Region 40-491 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false b9k0v9_agrvs-2 3255168 N/A 3255172 unspecified role unspecified role unspecified role unspecified role Region 1-448 Region 1-448 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mcd-3 3255169 N/A 3255174 unspecified role unspecified role unspecified role unspecified role Region 8-451 Region 8-451 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false b9k0v9_agrvs-3 3255170 N/A 3255172 unspecified role unspecified role unspecified role unspecified role Region 1-448 Region 1-448 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mata-1 3255171 N/A 3255175 unspecified role unspecified role unspecified role unspecified role Region 57-473 Region 57-473 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false