Table II. Cross-links detected in helices 3–7 of APOA1 in human HDL.
| Cross-link | m/z | Charge state | Mass Error (ppm)a | Distance (Cα-Cα, Å)b | Orientation |
|---|---|---|---|---|---|
| K94-E125 | 595.984 | 3 | 1.7 | 60.08* | LL5/2 |
| K96-E91 | 459.447 | 5 | −1 | 9.90 | N/A |
| K96-E147 | 616.82 | 4 | 0 | 30.69* | LL5/4 |
| K96-D168 | 477.92 | 6 | 1.5 | 13.5 | LL5/5 |
| K96-E169 | 684.351 | 4 | −0.6 | 11.58 | LL5/5 |
| K106-E92 | 524.276 | 4 | 3.1 | 23.22* | N/A |
| K118-D102 | 526.538 | 4 | 2.1 | 25.46* | N/A |
| K118-E147 | 628.013 | 3 | 1.5 | 13.02 | LL5/5 |
| K133-E110 | 637.071 | 4 | −9.8 | 28.03* | LL5/4 |
| K140-E125 | 604.721 | 5 | 2.6 | 14.62 | LL5/5 |
a Relative to theoretical masses of cross-linked peptides.
b Distance between α-carbons of cross-linked amino acids in the crystal structure of lipid-free C-terminal truncated APOA1 dimer (Δ185–243, PDB ID 3R2P) (28).
* Distance between α-carbons in crystal structure > 15.1 Å.