Crimean Congo Hemorrhagic Fever Virus OTU domain in complex with ubiquitin-propargyl.

On Terminal Alkynes that Can React with Active-Site Cysteine Nucleophiles in Proteases.

GLY76 IS REPLACED WITH A PROPARGYL GROUP

OTU DOMAIN OF CRIMEAN CONGO HEMORRHAGIC FEVER VIRUS CCHFV

MDFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCFYHSIAELTMPNKTDHSYHYIKRLTESAARKYYQEEPEAR
LVGLSLEDYLKRMLSDNEWGSTLEASMLAKEMGITIIIWTVAASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQ
FETDTREALSLMDRVIAVDQLTS

20-30% PEG 8000, 100 MM NA CACODYLATE PH 6.5, 100 MM MG ACETATE, AND 2% N-OCTYL-BETA-D-GLUCOSIDE.

ALLYLAMINE (AYE): THIS IS THE PRODUCT OF COVALENT MODIFICATION FROM PROPARGYL UBIQUITIN WITH A CYS. THE ETHANAMINE IS COVALENTLY LINKED TO CYS40 OF MOLECULE A.

RESIDUES 1-183
RESIDUE 76 IS REPLACED WITH A PROPARGYL MOIETY, WHICH FORMS
A QUATERNARY VINYL THIOETHER WITH CYS40 OF MOLECULE A.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES REFINED INDIVIDUALLY. COVALENT LINKS BETWEEN MOLECULE B GLY75,ETHANAMINE76 AND MOLECULE A CYS40 HAVE BEEN REFINED IN REFMAC. DISORDERED RESIDUES WERE MODELLED WITH SIDE CHAINS REMOVED OR MUTATED TO ALA.

HYDROLASE-SIGNALING PROTEIN COMPLEX, DEUBIQUITINASE