Table 1. Overview of cross-links within the nidogen-1 G3/laminin γ1 LEb2–4 complex.
Cα–Cα distances (Å) | |||
model | model | ||
cross-linked lysines | 1NPE | (best atom-pair constraint score) | (best total score) |
K-948 × K-953 | 10.4 | 10.9 | 11.1 |
K-1128 × K-1165 | 13.3 | 12.3 | 16.0 |
K-1072 × K-1128 | 16.7 | 19.1 | 16.2 |
K-948 × K-1144 | 17.9 | 16.4 | 17.6 |
K-850 (laminin) × K-1072 (nidogen-1) | 20.9 | 17.5 | 16.9 |
K-948 × K-1152 | 22.2 | 21.2 | 22.2 |
K-1032 × K-1072 | 27.1 | 27.1 | 27.0 |
K-961 × K-1072 | 28.7 | 28.0 | 28.2 |
K-864 (laminin) × K-1152 (nidogen-1) | 32.2 | 22.4 | 27.1 |
K-850 (laminin) × K-953 (nidogen-1) | 33.0 | 29.5 | 29.4 |
K-1032 × K-1152 | 35.8 | 35.4 | 35.4 |
Photo-L-990 × Arg-1038 | 24.7 | 23.4 | 23.5 |
Photo-L-844 (laminin) × K-1072 (nidogen-1) | 33.8 | 19.4 | 20.8 |
Cα–Cα distances of cross-linked residues were determined for the unmodified crystal structure (PDB entry 1NPE) as well as for the Rosetta models with the best Rosetta total score and atom-pair constraint score, respectively (shown in Figure 6). For intermolecular contacts, residues are assigned to the respective protein. All other cross-links are located within nidogen-1.