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. 2010 Jul 13;10:20. doi: 10.1186/1472-6807-10-20

Table 2.

List of the large conformation change proteins

Protein name Free Partner protein name Complex RMSD (Å) (overall) Conformational change region RMSD (Å) (local)
Staphylococcus A 1BDD_A Human Fc fragment 1FC2_C 3.07 41-45 3.05

Ran GTPase 1QG4_A RCC1 1I2M_A 2.62 73-75, 126-130, 137-140 3.74

14-3-3 1QJB_AB Serotonin N-acetylase 1IB1_AB 3.34 129-140, 201-212 8.65

Actin 1IJJ_B Profilin 2BTF_A 2.71 37-54 5.68

Erythropoietin 1BUY_A EPO receptor 1EER_A 4.08 112-130 5.46

Fab fragment 1GIG_LH Flu virus hemagglutinin 2VIS_AB 4.97 105-114 3.85

96-104, 119-124

TGF-beta 1TGK_A TGF-beta receptor 1KTZ_A 2.19 47-76 3.12

Actin 1IJJ_B Dnase I 1ATN_A 2.71 37-54 6.14

Coagulation factor Vlla 1QFK_HL Soluble tissue factor 1FAK_HL 6.23 153-165 5.16

35-41

Ran GTPase 1QG4_A Importin-beta 1IBR_A 3.90 30-34, 39-42 8.56

HPr kinase C-ter domain 1JB1_A HPr 1KKL_A 2.32 119-146 3.08

HIV1 reverse transcriptase 1S6P_AB Fab28 2HMI_AB 3.62 69-71, 87-90, 132-134
213-224, 244-252, 291-293
3.65

81-94, 217-231, 352-359

Ecotin 1ECZ_AB D102N trypsin 1EZU_AB 2.29 84-93 1.43

EPO receptor 1ERN_AB Erythropoietin 1EER_BC 2.72 118-123, 125-130 3.59

Vitamin D binding 1KW2_B Actin 1KXP_D 2.12 83-114, 247-258, 310-325 2.33

Nitrogenase Fe 2NIP_AB Nitrogenase Mo-Fe protein 1N2C_EF 4.10 47-53, 85-88, 124-128 1.50

CDK2 kinase 1B39_A CDK inhibitor 3 1FQ1_B 3.41 55-57, 144-165 4.33

Gelsolin 1D0N_B Actin 1H1V_G 14.06 109-120, 210-223, 300-302 12.33

Importin-beta 1F59_A Ran GTPase 1IBR_B 2.95 294-310, 331-338, 398-408 3.59

Hirustatin 1BX8_A Kallikrein 1HIA_I 2.05 18-20 1.98

Proteins that undergo large conformational change upon protein-protein interaction are listed in the first column. The following information is given: PDB ID code of the free-state, partner protein name, PDB ID code of the complex-state with a partner protein, RMSD (in Å) between free-state and complex-state, observed conformational change region upon protein-protein interaction, and average RMSD (in Å) of the observed conformational change region. When a protein forms heterodimers, the observed conformational change regions were investigated in each chain.