Molecular contacts at the FVa-APC interface
| FVa . | APC . | Distance∗ (Å) . |
|---|---|---|
| H-bonds | ||
| R316 H318 H318 H379 V381 N382 R400 R501 D504 R506 R506 R506 R506 R506 Q509 D513 T579 D660 E662 E669 | S332(c169) E333(c170) H388(c224) K308(c149) K308(c149) K311(c149c) S252(c97) T254(c99) G381(c216) H211(c57) D354(c189) S379(c214) W380(c215) G383(c219) R306(c147) K193(c39) K191(c37) R230(c75) D227(c72) R177(c23) | 2.9 3.2 3.7 2.8 2.9 2.9 2.9-3.7 2.7 3.1 2.7 2.8-3.0 3.5 3.0 2.7 2.9 2.7 2.7 2.9 3.5-3.6 3.9 |
| Salt bridges | ||
| H318 R506 R510 D513 E669 | E333(c170) D354(c189) E215(c60a) K193(c39) R177(c23) | 3.7 2.8-3.9 2.9-3.8 2.7 3.9 |
| Hydrophobic | ||
| H318 H318 M319 R321 R321 V381 N382 M385 D504 D504 R505 R505 R506 R506 R506 R506 R506 G507 G507 I508 I508 I508 R510 T626 D660 | M319(c157) V334(c171) H388(c224) E382(c217) S336(c173) K308(c149) E309(c149a) K311(c149c) G381(c216) E382(c217) W380(c215) H211(c57) A360(c195) C356(c191) G381(c216) V378(c213) W380(c215) A360(c195) G358(c193) A195(c41) G358(c193) Y302(c143) E215(c60a) K191(c37) R229(c74) | 3.9 4.0 3.7-3.8 3.6-4.0 3.5 3.7-3.9 4.0 3.8 3.8 3.8 4.1 3.4-3.8 3.6 3.8-4.0 3.6 3.8-4.1 3.6-3.9 3.7 4.0 3.9 3.5 3.5 3.7 4.0 3.7-4.0 |
| FVa . | APC . | Distance∗ (Å) . |
|---|---|---|
| H-bonds | ||
| R316 H318 H318 H379 V381 N382 R400 R501 D504 R506 R506 R506 R506 R506 Q509 D513 T579 D660 E662 E669 | S332(c169) E333(c170) H388(c224) K308(c149) K308(c149) K311(c149c) S252(c97) T254(c99) G381(c216) H211(c57) D354(c189) S379(c214) W380(c215) G383(c219) R306(c147) K193(c39) K191(c37) R230(c75) D227(c72) R177(c23) | 2.9 3.2 3.7 2.8 2.9 2.9 2.9-3.7 2.7 3.1 2.7 2.8-3.0 3.5 3.0 2.7 2.9 2.7 2.7 2.9 3.5-3.6 3.9 |
| Salt bridges | ||
| H318 R506 R510 D513 E669 | E333(c170) D354(c189) E215(c60a) K193(c39) R177(c23) | 3.7 2.8-3.9 2.9-3.8 2.7 3.9 |
| Hydrophobic | ||
| H318 H318 M319 R321 R321 V381 N382 M385 D504 D504 R505 R505 R506 R506 R506 R506 R506 G507 G507 I508 I508 I508 R510 T626 D660 | M319(c157) V334(c171) H388(c224) E382(c217) S336(c173) K308(c149) E309(c149a) K311(c149c) G381(c216) E382(c217) W380(c215) H211(c57) A360(c195) C356(c191) G381(c216) V378(c213) W380(c215) A360(c195) G358(c193) A195(c41) G358(c193) Y302(c143) E215(c60a) K191(c37) R229(c74) | 3.9 4.0 3.7-3.8 3.6-4.0 3.5 3.7-3.9 4.0 3.8 3.8 3.8 4.1 3.4-3.8 3.6 3.8-4.0 3.6 3.8-4.1 3.6-3.9 3.7 4.0 3.9 3.5 3.5 3.7 4.0 3.7-4.0 |
UCSF, University of California San Francisco.
Multiple entries indicate the range of distinct contacts between the same pair of residues. Residues are numbered sequentially and according to chymotrypsin (by parentheses) for the PD of APC. Contacts were derived from application of UCSF ChimeraX49 and the Protein Interfaces, Surfaces, and Assemblies service at the European Bioinformatics Institute.72 A graphical representation of the interface is given in Figure 4.