| | Name | Initial Conc. (uM) | Volume (fL) | Buffered |
| 1 | 3kCaM*_ip3_cmplx | 0 | 1000 | No |
| | Enzyme complex exclusively modeled as M-M kinetics do not hold. Enzyme is reversible as per free energy calculations that yield a a significant back flux. |
| 2 | 3kCaM_ip3_cmplx | 0 | 1000 | No |
| | Enzyme complex exclusively modeled because enzymes is reversible, unlike M-M enzymes. Reversibility determined from dG calculations. |
| 3 | IP3(145) | 0.2 | 1000 | No |
| | Inositol (145)trisphosphate |
| 4 | IP3_3K | 0.3853 | 1000 | No |
| | from Johanson et al, JBC, 1988, Vol. 263, No.16, pp 7465-7471 this is the predominant isoform in brain ie IP3-3kinaseA: BiochemJ, 1995, 306, 429-435 |
| 5 | IP3_3K* | 0 | 1000 | No |
| | phosphorylation at thr311 Communi et al, EMBO J 16; 1997 |
| 6 | IP3_3K*1 | 0 | 1000 | No |
| | Sim et al; JBC 265(18) June 25; 1990: pp 10367-10372 Phos. at 2 major sites = Ser109 & Ser 175; but there is a possibility that inactivation is due to combined effect of multiple phosphorylations activity suppressed by 75% |
| 7 | IP3_3K_CaM | 0 | 1000 | No |
| | 2-2.5 fold increase in enzyme activity due to CaM binding CaM binding involves Trp165 Erneux et al; Biochem 214, 497-501 (1993) |
| 8 | IP3_3K_CaM* | 0 | 1000 | No |
| | 8-10 fold activation with both CaM bound and CaMKII phosphorylation (phos at thr311) Communi et al; EMBO J 16 (8), pp 1943-1952, 1997 |
| 9 | IP4(1345) | 1 | 1000 | No |
| | Inositol(1345)tetrakisphosphate |
