Table I

Cross-linked lysine residues in inactive Akt molecule

PH, the PH domain; kin, the kinase domain; reg, the regulatory domain; ND, not detected; NA, not applicable; mod., modified.

Cross-linked lysine pairs or end-capped lysine residues identified by MS/MSMass of the cross-linked tryptic peptidesType of cross-linkingBS3 -mod.DSS-mod.DSG-mod.Distance constraint of cross-linked α-carbonsα-Carbon distance in the crystal structure
Da Å Å
Lys111(PH)-Lys112(PH)3120a (3078)bIntradomain+++≤203.8c
Lys214(kin)-Lys284(kin)3623 (3581)Intradomain+++≤2017.9d
Lys158(kin)-Lys163(kin)1610 (1568)Intradomain+++≤204.0d
Lys30(PH)-Lys39(PH)2939 (2897)Intradomain+++≤2017.9c
Lys284(kin)-Lys426(reg)3465 (3423)Interdomain+++≤207.8d
Lys30(PH)-Lys389(kin)2458 (ND)Interdomain++20–24NA
Lys377(kin)-Lys385(kin)1792 (1750)Intradomain+++≤2012.1d
Lys20(PH)1617 (1575)Capping+++
Lys189(kin)2079 (2037)Capping+++
Lys268(kin)2728 (2686)Capping+++
Lys400(kin)1783 (1741)Capping+++
Lys420(reg)2086 (2044)Capping+++
  • a Using DSS or BS3.

  • b Using DSG.

  • c Obtained from the Protein Data Bank entry 1unp.

  • d Obtained from the equivalent lysine residues in inactive Akt2 (Protein Data Bank entry 1mrv).