Table 2

Structure refinement and validation statistics
Parameter Form-I (unliganded) Form-II (citrate-bound)
Resolution range (Å) a 50.0-2.70 (2.80-2.70) 50.0-1.90 (1.97-1.90)
No. of atoms
   Protein / Water / EDO / CIT b 11748 / 204 / 16 / - 5838 / 442 / 16 / 13
R-factors (%) c
   Rwork / Rfree 22.1 / 28.3 18.9 / 22.4
Correlation coefficient (%) d 85.4 94.1
Wilson B-factor (Å2) 53.4 41.9
Average B-factor (Å2)
   Protein / Water / EDO / CIT 44.7 / 10.4 / 45.8 / - 36.1 / 44.2 / 56.4 / 33.9
RMS deviation
   Bond length (Å) 0.006 0.014
   Bond angle (°) 0.977 1.414
   Dihedral angle (°) 5.024 5.908
   Chiral-center restraints (Å3) 0.066 0.098
   General planes (Å) 0.003 0.006
Coordinate error: Luzzati (Å) 0.412 0.237
Residues in Ramachandran map (% / number)
   Most favoured region 89.1 / 1,228 90.9 / 610
   Allowed region 10.9 / 150 8.8 / 59
   Generously allowed region 0 / 0 0.3 / 2
   Disallowed region 0 / 0 0 / 0

Refinement and validation statistics are from REFMAC5 [19] and PROCHECK [37].

a Values for the highest resolution shell are given in parentheses.

b EDO and CIT refer to ethylene glycol and citrate, respectively.

c Rwork = <a onClick="popup('http://www.biomedcentral.com/1472-6807/12/24/mathml/M1','MathML',630,470);return false;" target="_blank" href="http://www.biomedcentral.com/1472-6807/12/24/mathml/M1">View MathML</a>; Rfree was calculated similarly by using 5% of the reflections that were excluded from the refinement.

d Correlation coefficient = <a onClick="popup('http://www.biomedcentral.com/1472-6807/12/24/mathml/M2','MathML',630,470);return false;" target="_blank" href="http://www.biomedcentral.com/1472-6807/12/24/mathml/M2">View MathML</a>.

Chittori et al.

Chittori et al. BMC Structural Biology 2012 12:24   doi:10.1186/1472-6807-12-24

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