UBIQUITINTHIOESTERASE / OTU DOMAIN OF CRIMEAN CONGO HEMORRHAGIC FEVER VIRUS CCHFV
Mass: 20857.414 Da / Num. of mol.: 1 / Fragment: OTU DOMAIN, RESIDUES 1-183 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CRIMEAN-CONGO HEMORRHAGIC FEVER VIRUS / Strain: IBAR10200 / Description: DNA GENERATED BY GENE SYNTHESIS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): ROSETTA2 PLACI / References: UniProt: Q6TQR6, ubiquitinyl hydrolase 1
#2: Protein
POLYUBIQUITIN-B / UBIQUITIN PROPARGYL / UBIQUITIN
Mass: 8558.857 Da / Num. of mol.: 1 / Mutation: YES / Source method: obtained synthetically / Details: GLY76 IS REPLACED WITH A PROPARGYL GROUP / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P0CG47
Mass: 18.015 Da / Num. of mol.: 48 / Source method: isolated from a natural source / Formula: H2O
Has protein modification
Y
Nonpolymer details
ALLYLAMINE (AYE): THIS IS THE PRODUCT OF COVALENT MODIFICATION FROM PROPARGYL UBIQUITIN WITH A CYS. ...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.
Sequence details
RESIDUES 1-183 RESIDUE 76 IS REPLACED WITH A PROPARGYL MOIETY, WHICH FORMS A QUATERNARY VINYL ...RESIDUES 1-183 RESIDUE 76 IS REPLACED WITH A PROPARGYL MOIETY, WHICH FORMS A QUATERNARY VINYL THIOETHER WITH CYS40 OF MOLECULE A.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 3.1 Å3/Da / Density % sol: 60 % / Description: NONE
Crystal grow
pH: 6.5 Details: 20-30% PEG 8000, 100 MM NA CACODYLATE PH 6.5, 100 MM MG ACETATE, AND 2% N-OCTYL-BETA-D-GLUCOSIDE.
Resolution: 2.3→126.48 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.913 / SU B: 6.793 / SU ML: 0.161 / Cross valid method: THROUGHOUT / ESU R: 0.232 / ESU R Free: 0.221 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: 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 ...Details: 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.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.27465
838
5.1 %
RANDOM
Rwork
0.21076
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obs
0.21385
15629
97.73 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK