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. 2002 Jun;11(6):1415–1423. doi: 10.1110/ps.4890102

Table 2.

Refinement statistics of test protein structures with and without the hydrogen bond restraint

Refinement without a hydrogen-bond restrainta Refinement with optimized hydrogen bond restraintsb
PDB code Rfree (%) R (%) Rfree − R (%) Rfree (%) R (%) Rfree − R (%)
2CHR 26.18 17.94 8.24 24.35 19.46 4.89
1A7B 31.64 22.85 8.79 29.06 23.98 5.08
2BCT 28.16 21.13 7.03 26.78 21.58 5.20
1A9B 30.69 25.57 5.12 29.83 25.44 4.39
1A43 27.72 22.07 5.65 26.77 21.93 4.84
1AVC 27.11 19.64 7.47 26.44 19.63 6.81
6PFK 24.02 16.78 7.24 23.54 16.93 6.61
1AWU 35.24 33.58 1.66 34.19 32.62 1.57
1AS3 27.18 21.86 5.32 26.67 21.76 4.91
1AB4 31.16 23.13 8.03 30.65 22.82 7.83

PDB, Protein Data Bank.

a R-factors are calculated in a consistent manner in this table and differ slightly from those of Table 1, which were calculated in the original structure determinations by the original authors using a variety of scaling procedures and refinement protocols.

b Hydrogen bond restraint parameters were optimized against each of these training proteins individually.