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=STRUCTURE= | =STRUCTURE= | ||
'''Quality of YlqF protein model and overall structure''' | '''Quality of YlqF protein model and overall structure''' | ||
The asymmetric unit of Bacillus subtilis YlqF protein consists of a polymer containing 282 amino acids (Figure 1). The protein has been refined at 2 angstroms to a crystallographic R factor of 21.6% and free R factor of 25%. Table 1 summarizes the refinement statistics including protein quality parameters. MolProbity Ramachandran analysis of YlqF in shows that 96.5% of all residues lie in the favoured regions and 98.8% of all residues lie in the allowed regions. | The asymmetric unit of Bacillus subtilis YlqF protein consists of a polymer containing 282 amino acids (Figure 1). The protein has been refined at 2 angstroms to a crystallographic R factor of 21.6% and free R factor of 25%. Table 1 summarizes the refinement statistics including protein quality parameters. MolProbity Ramachandran analysis of YlqF in shows that 96.5% of all residues lie in the favoured regions and 98.8% of all residues lie in the allowed regions. | ||
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Revision as of 02:49, 11 June 2007
STRUCTURE
Quality of YlqF protein model and overall structure
The asymmetric unit of Bacillus subtilis YlqF protein consists of a polymer containing 282 amino acids (Figure 1). The protein has been refined at 2 angstroms to a crystallographic R factor of 21.6% and free R factor of 25%. Table 1 summarizes the refinement statistics including protein quality parameters. MolProbity Ramachandran analysis of YlqF in shows that 96.5% of all residues lie in the favoured regions and 98.8% of all residues lie in the allowed regions.
