// DOQCS : http://doqcs.ncbs.res.in/ // Accession Name = Chemotaxis // Accession Number = 57 // Transcriber = Sharat J. Vayttaden, NCBS // Developer = Dennis Bray, Robert B. Bourret and, Melvin I. Simon, Cambridge and Caltech // Species = E. Coli // Tissue = - // Cell Compartment = Cell membrane + cytosol // Notes = Reactions feeding into TnWa, TaWA and TWA are scaled by 10 Binding reaction of Tar with Aspartate has been scaled by 10 Phosphotransfer from CheAp to CheY has Kb = 0.263/sec/uM instead of 0.2/sec/uM used in BCT1.1.
All remaining parameters are from the .BCT files for BCT1.1 provided by Matthew Levin from the Computational Biology Group in the Department of Zoology at the University of Cambridge.
The June 2003 version of the BCT program is BCT4.3 and is available at the computational biology site of the Zoology department at Cambridge University.
Citation: Bray et al. 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\ 0 simundump doqcsinfo /kinetics/doqcsinfo 0 db57.g Chemotaxis pathway \ " Sharat J. Vayttaden, NCBS" \ " Dennis Bray, Robert B. Bourret and, Melvin I. Simon, Cambridge and Caltech" \ "citation here" "E. Coli-" - " Cell membrane + cytosol" Qualitative \ "Bray et al. Mol.Biol.Cell (1993) 4(5): 469-482. ( peer-reviewed publication )" \ "Mathematically equivalent" "Replicates original data " 148 91 0 simundump xgraph /graphs/conc1 0 0 45 0.68 1 0 simundump xgraph /graphs/conc2 0 0 45 0.00073069 0.054934 0 simundump xplot /graphs/conc1/Bias.Co 0 0 nil 0 0 0 1 simundump xplot /graphs/conc1/Bias.Co[1] 0 0 nil 0 1.1248e-07 0 1 simundump xplot /graphs/conc1/Bias.Co[2] 0 0 nil 0 0 0 1 simundump xplot /graphs/conc1/Bias.Co[3] 0 0 nil 0 0 0 1 simundump xplot /graphs/conc1/Bias.Co[4] 0 0 nil 0 0 0 1 simundump xplot /graphs/conc2/Motor.Co 3 524288 \ "delete_plot.w ; edit_plot.D " 18 0 0 1 simundump xgraph /moregraphs/conc3 0 0 45 9.789 9.9067 0 simundump xgraph /moregraphs/conc4 0 0 45 0.016921 3.1898 0 simundump xplot /moregraphs/conc3/MYpYp.Co 3 524288 \ "delete_plot.w ; edit_plot.D " 23 0 0 1 simundump xplot /moregraphs/conc3/MYp.Co 3 524288 \ "delete_plot.w ; edit_plot.D " 56 0 0 1 simundump xplot /moregraphs/conc4/MYpYpYpYp.Co 3 524288 \ "delete_plot.w ; edit_plot.D " 62 0 0 1 simundump xplot /moregraphs/conc4/MYpYpYp.Co 3 524288 \ "delete_plot.w ; edit_plot.D " 18 0 0 1 simundump xcoredraw /edit/draw 0 -349 210 -486 130 simundump xtree /edit/draw/tree 0 \ /kinetics/#[],/kinetics/#[]/#[],/kinetics/#[]/#[]/#[][TYPE!=proto],/kinetics/#[]/#[]/#[][TYPE!=linkinfo]/##[] \ "edit_elm.D ; drag_from_edit.w " auto 0.6 simundump xtext /file/notes 0 1 xtextload /file/notes \ "Reactions feeding into TnWA, TaWA and TWA scaled by 10" \ "Binding reaction of Tar with Aspartate scaled by 10" \ "Motor and Yp reactions scaled by 10" \ "Phosphotransfer from CheAp to CheY has Kb = 0.263/sec/uM " \ "instead of 0.2/sec/uM used in BCT1.1 All remaining parameters" \ "as in .BCT files for BCT1.1 provided by Matthew Levin" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "" \ "The current version of the BCT program is BCT4.3 and is available" \ "at http://www.zoo.cam.ac.uk/comp-cell/Chemotaxis.html" addmsg /kinetics/Phosphotransfer /kinetics/CheA REAC B A addmsg /kinetics/Phosphotransfer[1] 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/kinetics/CheA /kinetics/Binding[7] SUBSTRATE n addmsg /kinetics/TaA /kinetics/Binding[7] PRODUCT n addmsg /kinetics/Binding[7] /kinetics/TaA REAC B A addmsg /kinetics/Complexing[9] /kinetics/TaA REAC A B addmsg /kinetics/TaA /kinetics/Complexing[9] SUBSTRATE n addmsg /kinetics/TaWA /kinetics/Complexing[9] PRODUCT n addmsg /kinetics/CheW /kinetics/Complexing[9] SUBSTRATE n addmsg /kinetics/MYpYp /kinetics/Denominator SUMTOTAL n nInit addmsg /kinetics/MYpYpYp /kinetics/Denominator SUMTOTAL n nInit addmsg /kinetics/MYpYpYpYp /kinetics/Denominator SUMTOTAL n nInit addmsg /kinetics/MYp /kinetics/Denominator SUMTOTAL n nInit addmsg /kinetics/Motor /kinetics/Denominator SUMTOTAL n nInit addmsg /kinetics/Binding[1] /kinetics/Aspartate REAC A B addmsg /kinetics/Complexing[3] /kinetics/MYp REAC B A addmsg /kinetics/Complexing[4] /kinetics/MYp REAC A B addmsg /kinetics/Complexing[3] /kinetics/Motor REAC A B addmsg /kinetics/MYp /kinetics/Numerator SUMTOTAL n nInit addmsg /kinetics/Motor /kinetics/Numerator SUMTOTAL n nInit addmsg /kinetics/MYpYpYpYp /kinetics/CW_rotation SUMTOTAL n nInit addmsg /kinetics/MYpYpYp /kinetics/CW_rotation SUMTOTAL n nInit addmsg /kinetics/Complexing[10] /kinetics/WA REAC B A addmsg /kinetics/Binding[9] /kinetics/WA REAC A B addmsg /kinetics/Binding[10] /kinetics/WA REAC A B addmsg /kinetics/Binding[11] /kinetics/WA REAC A B addmsg /kinetics/Complexing /kinetics/Tar REAC A B addmsg /kinetics/Binding[3] /kinetics/Tar REAC A B addmsg /kinetics/Binding[9] /kinetics/Tar REAC A B addmsg /kinetics/Binding /kinetics/Tar REAC A B addmsg /kinetics/Binding[1] /kinetics/Tar REAC A B addmsg /kinetics/WA /kinetics/Binding[9] SUBSTRATE n addmsg /kinetics/Tar /kinetics/Binding[9] SUBSTRATE n addmsg /kinetics/TWA /kinetics/Binding[9] PRODUCT n addmsg /kinetics/Tn /kinetics/Binding[10] SUBSTRATE n addmsg /kinetics/TnWA /kinetics/Binding[10] PRODUCT n addmsg /kinetics/WA /kinetics/Binding[10] SUBSTRATE n addmsg /kinetics/Ta /kinetics/Binding[11] SUBSTRATE n addmsg /kinetics/TaWA /kinetics/Binding[11] PRODUCT n addmsg /kinetics/WA /kinetics/Binding[11] SUBSTRATE n addmsg /kinetics/Denominator /kinetics/Division DIVIDE Co addmsg /kinetics/Numerator /kinetics/Division MULTIPLY Co addmsg /kinetics/CheW /kinetics/Complexing[10] SUBSTRATE n addmsg /kinetics/CheA /kinetics/Complexing[10] SUBSTRATE n addmsg /kinetics/WA /kinetics/Complexing[10] PRODUCT n addmsg /kinetics/Division /graphs/conc1 PLOT output *Bias.Co *0 addmsg /kinetics/Division /graphs/conc1/Bias.Co PLOT output *Bias.Co *0 addmsg /kinetics/Division /graphs/conc1/Bias.Co[1] PLOT output *Bias.Co *0 addmsg /kinetics/Division /graphs/conc1/Bias.Co[2] PLOT output *Bias.Co *0 addmsg /kinetics/Division /graphs/conc1/Bias.Co[3] PLOT output *Bias.Co *0 addmsg /kinetics/Division /graphs/conc1/Bias.Co[4] PLOT output *Bias.Co *0 addmsg /kinetics/Motor /graphs/conc2/Motor.Co PLOT Co *Motor.Co *18 addmsg /kinetics/MYpYp /moregraphs/conc3/MYpYp.Co PLOT Co *MYpYp.Co *23 addmsg /kinetics/MYp /moregraphs/conc3/MYp.Co PLOT Co *MYp.Co *56 addmsg /kinetics/MYpYpYpYp /moregraphs/conc4/MYpYpYpYp.Co PLOT Co *MYpYpYpYp.Co *62 addmsg /kinetics/MYpYpYp /moregraphs/conc4/MYpYpYp.Co PLOT Co *MYpYpYp.Co *18 enddump // End of dump call /kinetics/CheA/notes LOAD \ "CheA = 1.13e-06 M = 1.13 uM" \ "As per Signal in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "CheA = 4250 molecules per cell" \ "As per Enzyme entry 4 in 1ENZ.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/CheAp/notes LOAD \ "CheAp = 5.69e-07 M = 5.69e-1 uM" \ "As per Signal entry 17 in 1SIG_B.BCT" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/CheB/notes LOAD \ "CheB = 1.62e-06 M = 1.62 uM" \ "As per Signal 18 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "CheB = 1700 molecules per cell" \ "As per Enzyme entry 2 in 1ENZ.BCT provided by " \ "" \ "Cell volume = 1.41e-15 L" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 1 pp.474" call /kinetics/CheBp/notes LOAD \ "CheBp = 3.81e-07 M = 3.81e-1 uM" \ "As per Signal entry 19 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Phosphotransfer/notes LOAD \ "Phosphotransfer from CheAp to CheB" \ "" \ "Kf = 1 * 10e6 /sec/M = 1 /sec/uM" \ "Kb = 0 /sec/M" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475 Reaction Scheme 9" call /kinetics/CheYp/notes LOAD \ "CheYp = 1.24e-07 M = 1.24e-01 uM" \ "As per Signal 22 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "CheYp = 1e-08 M = 1e-2 uM" \ "As per Set_Yp configuration in 1CONFIG.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/CheY/notes LOAD \ "CheY = 9.88e-06 M = 9.88 uM" \ "As per Signal 21 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "CheY = 8500 molecules per cell" \ "As per Enzyme entry 5 in 1ENZ.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Phosphotransfer[1]/notes LOAD \ "Phosphotransfer from CheAp to CheY" \ "" \ "Kf = 2 * 10e+05 /sec/M = 0.2 /sec/uM" \ "Kb = 0 /sec/M" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475 Reaction Scheme 5" call /kinetics/CheW/notes LOAD \ "CheW = 1.37 uM " \ "As per Signal 5 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "CheW = 4250 molecules per cell" \ "As per Enzyme entry 3 in 1ENZ.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Complexing/notes LOAD \ "Tar and CheW complex formation" \ "" \ "Kf = 1 * 10e5 /sec/M = 0.1 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 3" call /kinetics/TW/notes LOAD \ "Tar-CheW complex" \ "TW = 1.88e-06 M = 1.88 uM" \ "As per Signal entry 3 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/CheZ/notes LOAD \ "CheZ = 2.00e-05 M = 20 uM" \ "As per Signal 20 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "CheZ = 17000 molecules per cell" \ "As per Enzyme entry 6 in 1ENZ.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Autophosphorylation/notes LOAD \ "Autophosphorylation of CheA by ATP" \ "" \ "Kf = 0.001 /sec" \ "Kb = 0 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475 Reaction Scheme 1" call /kinetics/Autodephosphorylation/notes LOAD \ "Autodephosphorylation of CheBp" \ "" \ "Kf = 1 /sec" \ "Kb = 0 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475 Reaction Scheme 10" call /kinetics/Autodephosphorylation[1]/notes LOAD \ "Autodephosphorylation of CheYp" \ "" \ "Kf = 3.7*10e-02 /sec" \ "Kb = 0 /sec" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475 Reaction Scheme 7 " call /kinetics/Autophosphorylation[1]/notes LOAD \ "TWA stimulated autophosphorylation of CheA " \ "TWA is complex of Tar, CheW and CheA" \ "Kf = 7.57*10e+04 /sec/M = 0.0757 /sec/uM" \ "As per Reaction 9 in 1REACT.BCT provided by Matthew Levin" \ "" \ "Kf = 5.9*10e+4 /sec/M = 0.059 /sec/uM" \ "Kb = 0 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475 Reaction Scheme 2" call /kinetics/Autophosphorylation[2]/notes LOAD \ "Autophosphorylation of CheY" \ "Paper says reaction not applicable " \ "Table 2 pp.475 Reaction Scheme 6" \ "" \ "kf = 0/sec" \ "kb = 0/sec " \ "As per Reaction 14 in 1REACT.BCT provided by Matthew Levin" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Dephosphorylation/notes LOAD \ "CheZ stimulated dephosphorylation of CheYp" \ "" \ "Kf = 5*10e+05 /sec/M = 0.5 /sec/uM" \ "Kb = 0 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475 Reaction Scheme 8" call /kinetics/Complexing[1]/notes LOAD \ "Complex formation of Ni bound Tar and CheW" \ "Kf = 1 * 10e5 /sec/M = 0.1 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482; " \ "Table 3 pp.476 Reaction Scheme 3 " \ " " \ "Footnote states that ligands do not have any effect" \ "on the formation of the Tar-Chew-CheA complex so same rates" \ "are used for Aspartate or Ni associated Tar complexes." call /kinetics/Ni/notes LOAD \ "Ni = 0.0 uM" \ "As per Signal 1 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Binding/notes LOAD \ "Binding of Tar and Ni" \ "" \ "Kf = 1 * 10e+03 /sec/M = 0.001 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 2" call /kinetics/Tn/notes LOAD \ "Ni bound Tar" \ "Ni-Tar = 0 M" \ "As per Signal 4 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/TnW/notes LOAD \ "Nickel bound Tar and CheW complex" \ "TnW = 0.0 uM" \ "As per Signal 8 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Autophosphorylation[3]/notes LOAD \ "TnWA stimulated autophosphorylation of CheA " \ "TnWA is complex of Tar, CheW, CheA and Ni" \ "Kf = 1*10e+06 /sec/M = 1 /sec/uM" \ "Kb = 0 /sec" \ "As per Reaction 10 in 1REACT.BCT provided by Matthew Levin" \ " " \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475, Reaction scheme 3" call /kinetics/Binding[1]/notes LOAD \ "Binding of Aspartate with Tar" \ "Kd = 0.78 uM Dunten and Koshland, 1991" \ "" \ "Kf = 1.28e+06 /sec/M = 1.28 /sec/uM here scaled by 5" \ "As per Reaction 0 in 1REACT.BCT provided by Matthew Levin" \ "" \ "Kf = 1.0e+06 /sec/M = 1 /sec/uM; Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 1" call /kinetics/Ta/notes LOAD \ "Aspartate bound Tar" \ "Ta = 0.0 M" \ "As per Signal 3 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Complexing[2]/notes LOAD \ "Complex formation of aspartate bound Tar and CheW" \ "Kf = 1 * 10e+05 /sec/M = 0.1 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482;" \ "Table 3 pp.476 Reaction Scheme 3" \ "" \ "Footnote states that ligands do not have any effect" \ "on the formation of complexes so same rates are used for" \ "Aspartate or Ni associated Tar complexes." call /kinetics/TaW/notes LOAD \ "Aspartate bound Tar and CheW complex" \ "TaW = 0 M" \ "As per Signal 7 in 1SIG_B.BCT" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Dephosphorylation[1]/notes LOAD \ "TWA-aspartate stimulated dephosphorylation of CheYp" \ "" \ "Kf = 1 * 10e08 /sec/M = 100 /sec/uM" \ "Kb = 0 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 2 pp.475 Reaction Scheme 4" call /kinetics/Binding[2]/notes LOAD \ "Binding of TW and CheA" \ "Kd = 0.3 uM and therefore Kf also suggested as 0.3 /sec/uM" \ "Kf = 4*10e5 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 6" \ "Rates used here are 10 times that stated, to allow for " \ "faster time courses seen during the drop of bias" \ "on removal of stimulus." call /kinetics/TWA/notes LOAD \ "Tar-CheW-CheA complex" \ "TWA = 2.12e-07 M = 2.12e-1 uM" \ "As per Signal entry 13 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Complexing[3]/notes LOAD \ "CheYp complexes with Flagellar Motor (M)" \ "" \ "Kf = 0.88/Set_Yp = 0.88/1e-08 /sec/M " \ " = 0.88e+2/sec/uM" \ "Kb = 5.5 /sec" \ "" \ "As per EXEC.C provided by Matthew Levin" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/MYpYp/notes LOAD \ "MYpYp = 3.66e-10 M = 3.66e-4 uM" \ "As per Signal 25 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "MYpYp is responsible for pause in rotation of flagella" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/MYpYpYp/notes LOAD \ "MYpYpYp = 4.47e-10 M = 4.47e-4 uM" \ "As per Signal 26 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/MYpYpYpYp/notes LOAD \ "MYpYpYpYp = 1.51e-09 M = 1.51e-3 uM" \ "As per Signal 27 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Complexing[4]/notes LOAD \ "CheYp complexes with MYp" \ "" \ "Kf = 2.85/Set_Yp = 2.85/1e-08 /sec/M " \ " = 2.85e+2/sec/uM" \ "Kb = 6.64 /sec" \ "" \ "As per EXEC.C provided by Matthew Levin" \ " " \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Complexing[5]/notes LOAD \ "CheYp complexes with MYpYp" \ "" \ "Kf = 6.94/Set_Yp = 6.94/1e-08 /sec/M " \ " = 6.94e+2 /sec/uM" \ "Kb = 5.1 /sec" \ "" \ "As per EXEC.C provided by Matthew Levin " \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Complexing[6]/notes LOAD \ "CheYp complexes with MYpYpYp" \ "" \ "Kf = 20.07/Set_Yp = 20.07/1e-08 /sec/M " \ " = 20.07e+2 /sec/uM" \ "Kb = 5.5 /sec" \ "" \ "As per EXEC.C provided by Matthew Levin" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Binding[3]/notes LOAD \ "Binding of T and CheA" \ "" \ "Kf = 0.05 /sec/uM as per Reaction 3 in 1REACT.BCT" \ "" \ "Kf = 1*10e+04 /sec/M = 0.01 /sec/uM " \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 4" call /kinetics/TA/notes LOAD \ "Tar-CheA complex" \ "TA = 1.55e-06 M = 1.55 uM" \ "" \ "As per Signal entry 9 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ " " \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Complexing[7]/notes LOAD \ "TA and CheW complex formation" \ "" \ "Kf = 4*10e+05 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Table 3 pp.476 Reaction Scheme 7" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Rates used here are 10 times that stated, to allow for" \ "faster time courses seen during the drop of bias " \ "on removal of stimulus." call /kinetics/TnA/notes LOAD \ "Tar-Ni-CheA complex" \ "TnA = 0 M" \ "As per Signal 11 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ " " \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Binding[4]/notes LOAD \ "Binding of T-Ni and CheA" \ "Kf = 0.05 /sec/uM as per Reaction 3 in 1REACT.BCT" \ "Kf = 1*10e+04 /sec/M = 0.01 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 4" \ "Footnote states that ligands do not have any effect on the " \ "formation of complexes so same rates are used for " \ "Aspartate or Ni associated Tar complexes." call /kinetics/Complexing[8]/notes LOAD \ "TnA and CheW complex formation" \ "Kf = 4*10e+05 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 7" \ "Rates used here are 10 times that stated, to allow for" \ "faster time courses seen during the drop of bias on" \ "removal of stimulus. " \ "Footnote states that ligands do not have any effect " \ "on the formation of Tar-CheW-CheA complex so same rates" \ "are used for Aspartate or Ni associated Tar complexes." call /kinetics/TnWA/notes LOAD \ "Tar-Ni-CheW-CheA complex" \ "TnWA = 0 M" \ "As per Signal 15 in 1SIG.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Binding[5]/notes LOAD \ "Binding of TnW and CheA" \ "Kf = 4*10e+05 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 6" \ "" \ "Footnote states that ligands do not have any effect on the" \ "formation of complexes so same rates are used for" \ "Aspartate or Ni associated tar complexes." call /kinetics/Binding[6]/notes LOAD \ "Binding of TaW and CheA" \ "Kf = 4*10e+05 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 6" \ "Rates used here are 10 times that stated, to allow for" \ "faster time courses seen during the drop of bias" \ "on removal of stimulus." \ "Footnote states that ligands do not have any effect on " \ "the formation of the Tar-CheW-CheA complex so same rates" \ "are used for Aspartate or Ni associated Tar complexes." call /kinetics/TaWA/notes LOAD \ "Tar-CheW-CheA-Aspartate complex" \ "TaWA = 0 M" \ "As per Signal 14 in 1SIG_B.BCT provided by Matthew Levin" \ " " \ "Cell volume = 1.41e-15 L" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 1. pp.474" call /kinetics/Binding[7]/notes LOAD \ "Binding of Tar-Aspartate and CheA" \ "Kf = 0.05 /sec/uM as per Reaction 3 in 1REACT.BCT" \ "Kf = 1e+04 /sec/M = 0.01 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 4" \ "Footnote states that ligands do not have any effect" \ "on the formation of complexes so same rates are " \ "used for Aspartate or Ni associated Tar complexes." call /kinetics/TaA/notes LOAD \ "Tar-Asp-CheA complex" \ "TaA = 0 M" \ "As per Signal 10 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ " " \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Complexing[9]/notes LOAD \ "TaA and CheW complex formation" \ "Kf = 4*10e+05 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 7" \ "Rates used here are 10 time that stated, to allow for" \ "faster time courses seen during the drop of bias" \ "on removal of stimulus." \ "Footnote states that ligands do not have any effect on " \ "the formation of the Tar-CheW-CheA complex so same rates" \ "are used for Aspartate or Ni associated Tar complexes" call /kinetics/Denominator/notes LOAD \ "Denominator value to calculate bias as stated on pp.471" \ "" \ " M + MYp" \ "Bias = ----------------------------------------" \ " M + MYp + MYpYp + MYpYpYp + MYpYpYpYp" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Bias/notes LOAD \ "Bias calculated as per formula stated on pp.471" \ "" \ " M + MYp" \ "Bias = ----------------------------------------" \ " M + MYp + MYpYp + MYpYpYp + MYpYpYpYp" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Initialy set to 0.7" call /kinetics/Aspartate/notes LOAD \ "Aspartate = 0.0 uM" \ "As per Signal 0 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/MYp/notes LOAD \ "MYp = 9.53*e-10 M = 9.53*e-4 uM" \ "As per Signal 24 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Motor/notes LOAD \ "Motor = 8.5 molecules per cell" \ "As per Enzyme entry 7 in 1ENZ.BCT provided by Matthew Levin" \ "" \ "Motor = 6.73e-9 M = 6.73e-3 uM" \ "As per Signal 23 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Numerator/notes LOAD \ "Numerator value to calculate bias as stated on pp.471" \ "" \ " M + MYp" \ "Bias = ----------------------------------------" \ " M + MYp + MYpYp + MYpYpYp + MYpYpYpYp" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/CW_rotation/notes LOAD \ "Sum total of MYpYpYp and MYpYpYpYp which is responsible for " \ "CW rotation of the flagella" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/WA/notes LOAD \ "CheW-CheA complex" \ "WA = 1.55e-6 M = 1.55 uM" \ "As per Signal 12 in 1SIG_B.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Tar/notes LOAD \ "Tar = 1.37e-06 M = 1.37 uM" \ "As per Signal 2 in 1SIG_B.BCT provided by Matthew Levin " \ "" \ "Tar = 4250 molecules per cell" \ "As per Enzyme entry 0 in 1ENZ.BCT provided by Matthew Levin" \ "" \ "Cell volume = 1.41e-15 L" \ "Table 1 pp.474" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" call /kinetics/Binding[9]/notes LOAD \ "Binding of Tar and CheW-CheA complex" \ "Kd = 2 uM and therefore Kf also suggested as 0.5 /sec/uM" \ "Kf = 4e+05 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 8" \ "Rates used here are 10 times that stated, to allow for " \ "faster time courses seen during the drop of bias " \ "on removal of stimulus." call /kinetics/Binding[10]/notes LOAD \ "Binding of Tn and CheW-CheA complex" \ "Kf = 4e+05 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 8" \ "Rates used here are 10 times that stated, to allow for" \ "faster time courses seen during the drop of bias on" \ "removal of stimulus." \ "Footnote states that ligands do not have any effect on" \ "the formation of complexes so same rates are used for" \ "Aspartate or Ni associated Tar complexes." call /kinetics/Binding[11]/notes LOAD \ "Binding of Ta and CheW-CheA complex" \ "Kf = 4e+05 /sec/M = 0.4 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 8" \ "Rates used here are 10 times that stated, to allow for" \ "faster time courses seen during the drop of bias on " \ "removal of stimulus." \ "Footnote states that ligands do not have any effect on the" \ "the formation of complexes so same rates are used for " \ "Aspartate or Ni associated Tar complexes." call /kinetics/Complexing[10]/notes LOAD \ "CheA and CheW complex formation" \ "Kf = 5*10e+04 /sec/M = 0.05 /sec/uM" \ "As per Reaction 4 in 1REACT.BCT provided by Matthew Levin" \ "" \ "Kf = 0.01 /sec/uM" \ "Kb = 1 /sec" \ "Bray et al 1993, Mol.Biol.Cell 4: 469-482" \ "Table 3 pp.476 Reaction Scheme 5" call /kinetics/doqcsinfo/notes LOAD \ "Reactions feeding into TnWa, TaWA and TWA are scaled by 10 Binding reaction of Tar with Aspartate has been scaled by 10\ Phosphotransfer from CheAp to CheY has Kb = 0.263/sec/uM instead of 0.2/sec/uM used in BCT1.1.
All remaining parameters are\ from the .BCT files for BCT1.1. All remaining parameters are from the .BCT files for BCT1.1 provided by Matthew Levin from the Computational Biology Group in the Department of Zoology at the University of Cambridge. The June 2003 version of the BCT program is BCT4.3 and is available at the computational biology site of the Zoology department at Cambridge University.
Citation: Bray et al. Mol.Biol.Cell (1993) 4(5): 469-482." complete_loading