SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
Mass: 18.015 Da / Num. of mol.: 409 / Source method: isolated from a natural source / Formula: H2O
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Details
Sequence details
THE FIRST 26 RESIDUES CORRESPOND TO THE PEPTIDE SEQUENCE OF THE PROTEIN, WHICH ARE CLEAVED. RESIDUE ...THE FIRST 26 RESIDUES CORRESPOND TO THE PEPTIDE SEQUENCE OF THE PROTEIN, WHICH ARE CLEAVED. RESIDUE 1 IN THE PDB CORRESPONDS TO RESIDUE 27 IN THE SEQUENCE FILE. ONLY THE CATALYTIC DOMAIN WAS CRYSTALLISED, CORRESPONDING TO RESIDUES 1-305 OF MATURE PROTEIN (27-331 IN SEQUENCE FILE).
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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: 2.2 Å3/Da / Density % sol: 43 % / Description: STRUCTURE ISOMORPHOUS WITH STARTING MODEL
Crystal grow
Details: 10 MG/ML PROTEIN. 1.5-1.8 M AMMONIUM SULPHATE. 25% GLYCEROL AS CRYO.
Resolution: 1.5→51.57 Å / Cor.coef. Fo:Fc: 0.98 / Cor.coef. Fo:Fc free: 0.972 / SU B: 1.876 / SU ML: 0.032 / Cross valid method: THROUGHOUT / ESU R: 0.068 / ESU R Free: 0.056 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.143
2416
5.1 %
RANDOM
Rwork
0.111
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obs
0.113
45273
99.7 %
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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: MASK