Mass: 18.015 Da / Num. of mol.: 192 / Source method: isolated from a natural source / Formula: H2O
Compound details
ENGINEERED RESIDUE IN CHAIN A, GLU 69 TO ALA ENGINEERED RESIDUE IN CHAIN A, GLU 70 TO ALA ...ENGINEERED RESIDUE IN CHAIN A, GLU 69 TO ALA ENGINEERED RESIDUE IN CHAIN A, GLU 70 TO ALA ENGINEERED RESIDUE IN CHAIN A, ARG 73 TO ALA
Sequence details
THE SEQUENCE DISCREPANCIES ARE BECAUSE THE DATABASE SEQUENCE IS FROM E.COLI STRAIN O157-H7. THE ...THE SEQUENCE DISCREPANCIES ARE BECAUSE THE DATABASE SEQUENCE IS FROM E.COLI STRAIN O157-H7. THE GENE WHICH WAS USED FOR PROTEIN EXPRESSION AND STRUCTURE DETERMINATION WAS ISOLATED FROM E.COLI BL21 (DE3).
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
Resolution: 1.88→79 Å / Num. obs: 61818 / % possible obs: 95.8 % / Observed criterion σ(I): 0 / Redundancy: 5.2 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 16.7
Reflection shell
Resolution: 1.88→1.93 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 3.9 / % possible all: 72.9
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Processing
Software
Name
Version
Classification
autoSHARP
modelbuilding
XSCALE
datascaling
SHELXD
phasing
SHELXE
phasing
SHARP
phasing
autoSHARP
phasing
REFMAC
5.2.0005
refinement
Refinement
Method to determine structure: MAD / Resolution: 1.88→48.34 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.941 / SU B: 5.812 / SU ML: 0.094 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.164 / ESU R Free: 0.144 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. A THEORETICAL GAMMA PHOSPHATE WAS MODELLED IN THE FINAL STRUCTURE WITH AN OCCUPANCY OF 0.00. THIS WAS NOT USED IN REFINEMENT.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.209
1644
5 %
RANDOM
Rwork
0.167
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obs
0.169
31242
95.9 %
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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