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. Author manuscript; available in PMC: 2010 Jan 23.
Published in final edited form as: J Mol Biol. 2008 Oct 19;385(3):867–888. doi: 10.1016/j.jmb.2008.10.037

Table 4.

Overall RMSD Comparisions. Values are in Ångstroms (Å)

Apo Structure NaMN-Bound Structure NaAD-Bound Structure
Chain A Chain B Dimer Chain A Chain B Dimer Chain A Chain B Chain C Dimer
Apo Structure Chain A X 0.603 (184) 0.596 (185) 0.652 (186) 1.127 (175) 0.998 (175) 1.148 (175)
Chain B 0.603 (184) X 0.605 (188) 0.667 (188) 0.974 (174) 0.832 (174) 1.025 (175)
Dimer X 0.583 (374) 2.074 (353)
NaMN-Bound Structure Chain A 0.596 (185) 0.605 (188) X 0.772 (186) 1.134 (175) 1.00 (175) 1.094 (174)
Chain B 0.652 (186) 0.667 (188) 0.772 (186) X 1.076 (178) 0.810 (175) 0.912 (174)
Dimer 0.583 (374) X 2.054 (350)
NaAD-Bound Structure Chain A 1.127 (175) 0.974 (174) 1.134 (175) 1.076 (178) X 0.505 (185) 0.347 (188)
Chain B 0.998 (175) 0.832 (174) 1.00 (175) 0.810 (175) X 0.499 (185)
Chain C 1.148 (175) 1.025 (175) 1.094 (174) 0.912 (174) X
Dimer 2.074 (353) 2.054 (350) X

Boxes marked with an X implies there is no RMSD associated with the two chains.

Values in parentheses indicate the number of residues used in the comparision.

Secondary structure matching (SSM) was used in the program Superpose to make pairwise aligments of the NMAT crystal structures.