Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: A potential clock input mechanism -- Data Supplement - Supporting Information -- Proceedings of the National Academy of Sciences

Supporting information for Williams et al. (2002) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.232517099

Table 1. Restraints and structural statistics of KaiA135N

Total experimental restraints	2,034
Total distance restraints	1,847
Intraresidue (i = j)	424
Sequential (\|i - j\| = 1)	522
Short range (1 £ \|i - j\| £ 4)	375
Long range ( \|i - j\| > 4)	485
Hydrogen bond	31*
Total dihedral restraints	187
j	67
y	63
c (56 c ¹, 1 c ²)	57
NOE violations >0.3 Å	0
Dihedral violations >3º	0
Mean RMSDs from experimental restraints
Distance, Å	0.02 ± 0.001
Dihedral angle, º	0.22 ± 0.06
Deviations from idealized geometry
Bonds, Å	0.0029 ± 0.0002
Angles, º	0.63 ± 0.01
Impropers, º	0.51 ± 0.02
PROCHECK Ramachandran analysis
Most favored regions, %	85.7 (88.3) ^†
Additional allows regions, %	12.0 (9.9) ^†
Generously allowed regions, %	2.0 (1.8) ^†
Disallowed regions, %	0.3 (0.0) ^†
Atomic RMS deviations from the mean structure
Backbone heavy atoms of residues 4–83 and 98–135, Å	0.38 ± 0.04
Non-hydrogen atoms of residues 4–83 and 98–135, Å	0.78 ± 0.05

*Distance restraints were applied between amide proton and oxygen atoms, and between amide nitrogen and oxygen atoms for each hydrogen bond restraint.

^†Values in parenthesis correspond to residues 4–83 and 98–135.