SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.
Mass: 18.015 Da / Num. of mol.: 521 / Source method: isolated from a natural source / Formula: H2O
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Details
Compound details
ENGINEERED MUTATION ASP 416 ALA CHAIN A
Sequence details
THIS MUTANT HAS BEEN PRODUCED BY SITE-DIRECTED MUTAGENESIS. THE CLONING WAS PERFORMED SUCH HAS ONLY ...THIS MUTANT HAS BEEN PRODUCED BY SITE-DIRECTED MUTAGENESIS. THE CLONING WAS PERFORMED SUCH HAS ONLY THE PRO-SEQUENCE AND THE CATALYTIC DOMAIN WERE EXPRESSED. THE CELLULOSE BINDING DOMAIN HAS BEEN REMOVED.THE CONSTRUCT IS POST-TRANSLATIONALLY CLEAVED TO YIELD TO A MATURE PROTEIN OF 450 RESIDUES WHICH COMMENCES AT RESIDUE TYR 89. THIS PROTEIN IS CLOSELY RELATED TO AVICELASE 2 (SWISS-PROT ACCESSION ID:Q9C1S9) WITH WHICH IT HAS 96% SEQUENCE IDENTITY.
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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: 2.01 Å3/Da / Density % sol: 42 % / Description: MOLECULE A
Crystal grow
pH: 7.5 Details: PROTEIN WAS CONCENTRATED TO 10MG/ML IN WATER.CRYSTALLISATION IN 200MM CALCIUM ACETATE, 100MM HEPES PH 7.5 AND 21% POLYETHYLENE GLYCOL 5KMME.20 % GLYCEROL WAS ADDED FOR CRYOPROTECTION
Resolution: 1.31→15 Å / Cor.coef. Fo:Fc: 0.979 / Cor.coef. Fo:Fc free: 0.973 / SU B: 0.638 / SU ML: 0.028 / Cross valid method: THROUGHOUT / ESU R: 0.056 / ESU R Free: 0.051 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.162
3485
5 %
RANDOM
Rwork
0.13
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obs
0.132
65959
90.2 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK