Table 2. Main-chain torsion angles (φ/ψ) of the phosphopeptide bound to the Grb2 SH2 domain and their amino acid sequencesa.
| PDB ID | Resolution (Å) | pY+1 | pY+2 [N] | pY+3 | O–N distanceb (Å) |
| 1BMB | 1.8 | –52.9/–33.4 [V] | –99.6/14.2 | [V] | 3.03 |
| 1BM2 | 2.1 | –58.9/–44.5 [V] | –83.0/–12.6 | [V] | 3.22 |
| 1JYR | 1.55 | –59.0/–32.3 [V] | –103.8/14.9 | [V] | 3.11 |
| 1TZE | 2.1 | –54.9/–28.9 [V] | –103.2/12.8 | [V] | 3.02 |
| 1ZFP | 1.8 | –61.8/–43.4 [I] | –88.0/19.8 | [Q] | 3.37 |
| 3N8M | 2.0 | –52.4/–35.0 [V] | –100.7/10.9 | [V] | 3.07 |
| CD28 c | 1.35 | –72.7/–21.5 [M] | –103.6/39.8 | [M] | 3.71 |
| β-turnd | – | –60/–30 | –90/0 | – | − |
| 3MXC | 2.0 | –67.3/–32.9 [E] | –99.2/127.0 | [P] | 5.10 |
| 3MXY | 2.3 | –60.6/–40.3 [V] | –92.8/142.8 | [P] | 5.11 |
a
The angles are given in degree. The residues in the pY+1 and pY+3 positions are shown as one-letter codes in square brackets.
b
The distance between the main-chain O of pY and the main-chain N of pY+3, which form a hydrogen bond in type-I β-turn.
c
The structure reported in this work.
d
Theoretically idealized values for type-I β-turn.