CASP4 Target Toll 1. Protein name Example of a CASP target 2. Ors Name Escherichia coli 3. Number of amino acids(approx) 4. Accession number P08324 5. Sequence Database -pr 6. Amino acid sequence SKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALEL RDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTE NKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGKYSMPVPMM NIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHLAK VLKAKG MNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASE FYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDGF AYQTKVLGDKIQL VGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTE TLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSD RVAKYNQLIRIEEALGEKAPYNGRKEIKGQA 7. Additional Information oligomerization state: dimer in the presence of magnesium by dynamic light scattering and small angle x-ray solution scattering and in the recently solved crystal structure 8. Homologous Sequence of known structure 9. Current state of the experimental work Structure solved by molecular replacement. Currently the refinement to 2. 5 a resolution is near completion Current Rfree 27 %. R 22CASP4 Target T0111 1. Protein Name Example of a CASP target enolase 2. Organism Name Escherichia coli 3. Number of amino acids (approx) 431 4. Accession number P08324 5. Sequence Database Swiss-prot 6. Amino acid sequence SKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALEL RDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTE NKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGKYSMPVPMM NIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHLAKVLKAKG MNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASE FYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDGF AYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTE TLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSD RVAKYNQLIRIEEALGEKAPYNGRKEIKGQA 7. Additional Information oligomerization state: dimer in the presence of magnesium by dynamic light scattering and small angle x-ray solution scattering and in the recently solved crystal structure. 8. Homologous Sequence of known structure yes 9. Current state of the experimental work Structure solved by molecular replacement. Currently, the refinement to 2.5 A resolution is near completion. Current Rfree 27 % ; R 22 %