Table 2b.

Structure refinement and final model statistics

GH 12 homolog	H. grisea WT	T. reesei P201C
PDB access codes	1olr	1olq
Resolution used in refinement (Å)	30–1.22	20–1.70
Reflections in
Working set	56,977	40,981
Test set	1793	1331
R & Rfree factor (%)	13.5; 15.1	20.9; 25.1
Protein molecules in AU	1	2
Residues in protein	224	218
Protein atoms	1832	3320
Waters	300	286
Residues with double conformations	17	—
N-glycosylation (NAG) residues	—	2
〈B〉 (Å2)	13.1	15.4
Protein 〈B〉 (Å2)	11.4	14.8
Water 〈B〉 (Å2)	23.3	23.0
RMSD bond lengths (Å)a	0.013	0.015
RMSD bond angles (°)a	1.6	1.7
RMSD ΔB on bonded atoms (Å2)	1.5	1.3
Average RMSD NCS Cα (Å)	—	0.5
Average RMSD NCS all atoms (Å)	—	0.6
Stringent Ramachandran outliersb (%)	1.0	0.7

Values were calculated with O (Jones et al. 1991; Jones and Kjeldgaard 1997), CNS (Brünger et al. 1998), MOLEMAN (Kleywegt and Jones 1996b), LSQMAN (Kleywegt and Jones 1997), and Refmac 5.0 (Murshudov et al. 1997).

^a From Engh and Huber 1991.

^b According to the stringent boundary definition (Kleywegt and Jones 1996a).