TABLE 1.
Data collection and refinement statistics for the structures of the complexes of peptidoglycan recognition protein (CPGRP-S) with MDP, GlcNAc, and maltose
The values in parentheses correspond to the values in the highest resolution shell.
| Parameters | CPGRP-S+MDP | CPGRP-S+GlcNAc and maltose |
|---|---|---|
| PDB code | 3NW3 | 3NG4 |
| Space group | I222 | I222 |
| Unit cell dimensions | a = 87.1, b = 102.0, and c = 161.6 Å | a = 87.1, b = 100.8, and c = 161.8 Å |
| Number of molecules in the asymmetric unit | 4 | 4 |
| Resolution range (Å) | 50–2.5 | 85.5–1.7 |
| Total number of measured reflections | 717,180 | 1,562,425 |
| Number of unique reflections | 24,772 | 70,076 |
| Rsym (%)a | 6.5 (25.2) | 4.7 (48.4) |
| I/σ(I) | 31.2 (3.4) | 32.7 (2.4) |
| Overall completeness of data (%) | 97.9 (98.1) | 99.1 (99.0) |
| Rcryst (%)b | 23.6 | 20.2 |
| Rfree (%) | 24.9 | 24.4 |
| Protein atoms | 5348 | 5348 |
| Water oxygen atoms | 400 | 735 |
| Atoms of glycerol | 6 | 6 |
| Atoms of tartrate | 10 | 10 |
| Atoms of ligands (MDP and GlcNAc/maltose) | 34 | 23/15 |
| R.m.s.d in bond lengths (Å) | 0.02 | 0.02 |
| R.m.s.d in bond angles | 1.9° | 1.9° |
| R.m.s.d in torsion angles | 15.3° | 15.0° |
| Wilson B-factor | 52.8 | 20.7 |
| Mean B-factor for main chain atoms (Å2) | 48.9 | 21.3 |
| Mean B-factor for side chain atoms (Å2) | 51.3 | 26.8 |
| Mean B-factor for all atoms(Å2) | 50.2 | 24.3 |
| Ramachandran ϕ, ψ map | ||
| Residues in most favored regions (%) | 89.4 | 88.7 |
| Residues in additionally allowed regions (%) | 10.6 | 11.3 |
a Rsym = ΣhklΣi|Ii(hkl) − 〈I(hkl)〉|/ΣhklΣiIi(hkl-).
b Rcryst = Σhkl|Fo(hkl) − Fc(hkl)|/Σhkl|Fo(hkl)|, where Fo and Fc are observed and calculated structure factors, respectively.