Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations
Table 1
Data collection and refinement statistics/PDB code 4EB4. Values in parentheses are for the highest resolution shell.
Data collection
Space group
P212121
Cell dimensions
Å, Å, Å
Beamline
Bessy 14.1
Wavelength [Å]
0.918
Resolution [Å]
20.04–1.74 (1.76–1.74)
0.054 (0.556)
Unique reflections
148229
Completeness [%]
99.9 (100)
Redundancy
3.6 (3.5)
21
Refinement
Resolution [Å]
1.74 (1.78–1.74)
Number of reflections
148148 (9725)
0.19 (0.31)
0.24 (37)
Average B factor [Å2]:
Overall
31
Polypeptide chain A
24
Polypeptide chain B
24
Polypeptide chain C
35
Polypeptide chain D
36
RMS deviations from ideal values for refined atoms
Bond lengths [Å]
0.022
Bond angles [°]
1.967
Ramachandran’s plot assignments
The most favored
936 (92.0%)
Additionally allowed
77 (7.6%)
Generously allowed
4 (0.4%)
Disallowed
0 (0.0%)
, where is the integrated intensity of a given reflection and is the mean intensity of multiple corresponding symmetry-related reflections. , where and are the observed and calculated structure factors, respectively. is calculated using a randomly chosen 1000 reflections that were excluded from the refinement.