Properties of the disulfide bonds of the C domain of crossveinless 225 *
| Chain . | Cys1 residue† . | Cys1 solvent‡ . | Cys2 residue . | Cys2 solvent‡ . | Cα-Cα, ŧ . | Configuration . |
|---|---|---|---|---|---|---|
| 1 | 9 (1) | 17 | 31 (4) | 0 | 6.04 | +/−RHSpiral |
| 26 (2) | 26 | 60 (8) | 4 | 4.89 | +/−RHHook | |
| 29 (3) | 4 | 38 (5) | 16 | 3.98 | −RHStaple | |
| 43 (6) | 46 | 61 (9) | 35 | 5.39 | −LHSpiral | |
| 50 (7) | 37 | 64 (10) | 48 | 6.03 | −LHHook | |
| 2 | 9 (1) | 21 | 31 (4) | 0 | 5.96 | +/−RHSpiral |
| 26 (2) | 31 | 60 (8) | 12 | 5.08 | +/−RHHook | |
| 29 (3) | 9 | 38 (5) | 12 | 4.04 | −RHStaple | |
| 43 (6) | 54 | 61 (9) | 34 | 5.51 | −LHSpiral | |
| 50 (7) | 36 | 64 (10) | 57 | 6.12 | −RHSpiral |
| Chain . | Cys1 residue† . | Cys1 solvent‡ . | Cys2 residue . | Cys2 solvent‡ . | Cα-Cα, ŧ . | Configuration . |
|---|---|---|---|---|---|---|
| 1 | 9 (1) | 17 | 31 (4) | 0 | 6.04 | +/−RHSpiral |
| 26 (2) | 26 | 60 (8) | 4 | 4.89 | +/−RHHook | |
| 29 (3) | 4 | 38 (5) | 16 | 3.98 | −RHStaple | |
| 43 (6) | 46 | 61 (9) | 35 | 5.39 | −LHSpiral | |
| 50 (7) | 37 | 64 (10) | 48 | 6.03 | −LHHook | |
| 2 | 9 (1) | 21 | 31 (4) | 0 | 5.96 | +/−RHSpiral |
| 26 (2) | 31 | 60 (8) | 12 | 5.08 | +/−RHHook | |
| 29 (3) | 9 | 38 (5) | 12 | 4.04 | −RHStaple | |
| 43 (6) | 54 | 61 (9) | 34 | 5.51 | −LHSpiral | |
| 50 (7) | 36 | 64 (10) | 57 | 6.12 | −RHSpiral |
Calculated using the disulfide bond analysis tool.40 The protein crystallized as a dimer and the analysis of both chains (1 and 2) is shown.
The number in the bracket is the order of the cysteine in the primary sequence from 1-10.
Solvent accessibility is the area of the cysteine residue exposed to solvent in approximately Å2.
Distance between the α carbon atoms of the 2 cysteine residues.