TABLE 1.
Fractionsa
|
NAAb(x-ray)
|
Native MfpA
|
Dialysis-renatured MfpA
|
||||||
---|---|---|---|---|---|---|---|---|---|
Fractionc | RMSDd | NRMSDd | NAAb(CD) | Fraction | RMSD | NRMSD | NAA (CD) | ||
Htotal | 16 | 0.035 | 0.033 | 0.681 | 1–12 | 0.152 | 0.039 | 0.249 | 21–35 |
Stotal | 40 | 0.188 | 0.096 | 0.454 | 17–52 | 0.317 | 0.008 | 0.027 | 57–59 |
Turns | 40 | 0.221 | 0.026 | 0.118 | 36–45 | 0.216 | 0.011 | 0.049 | 38–42 |
Unordered | 87 | 0.574 | 0.179 | 0.298 | 72–138 | 0.312 | 0.039 | 0.125 | 50–64 |
Overalle | 0.104 | 0.307 | 0.029 | 0.11 |
Secondary structure types: Htotal, total helixes, Stotal, total strands, Turns, turns; Unordered, the remainder of the protein
Number of amino acids included in the given type the secondary structure calculated from DSSP assignment of the crystal structure, NAA (x-ray) or from the CD spectra of MfpA, NAA (CD)
Calculated fraction of each secondary structure type
The values of r.m.s.d. and n.r.m.s.d. in this table reflect the analysis of the CD spectrum by the different programs and protein reference sets as described under “Experimental Procedures”
The overall performance of the CD analysis determined by considering all secondary structures collectively