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.: 279 / Source method: isolated from a natural source / Formula: H2O
Compound details
RESIDUES 56 AND 57 MUTATED TO LYS FROM ARGININE. THE MUTATION IS NOT VISIBLE IN THE STRUCTURE ...RESIDUES 56 AND 57 MUTATED TO LYS FROM ARGININE. THE MUTATION IS NOT VISIBLE IN THE STRUCTURE DEPOSITED. FUNCTION: RESPONSIBLE FOR THE PROTEOLYTIC PROCESSING OF THE AMYLOID PRECURSOR PROTEIN (APP).
Sequence details
RESIDUES 56 AND 57 FROM THE UNIPROT REFERENCE BELOW HAVE HAVE BEEN MUTATED TO LYS FROM ARG. SINCE ...RESIDUES 56 AND 57 FROM THE UNIPROT REFERENCE BELOW HAVE HAVE BEEN MUTATED TO LYS FROM ARG. SINCE THIS MUTATION IS NOT VISIBLE IN THE STRUCTURE, THERE ARE NO SEQADV RECORDS GIVEN BELOW.
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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: 2.86 Å3/Da / Density % sol: 56.65 %
Resolution: 1.75→39.52 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.915 / SU B: 3.063 / SU ML: 0.098 / Cross valid method: THROUGHOUT / ESU R: 0.132 / ESU R Free: 0.131 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THIS ENTRY CONTAINS SOME ATOMS WHICH HAVE BEEN REFINED WITH AN OCCUPANCY OF 0.00. RESIDUES BETWEEN 157 AND 169 WERE NOT VISIBLE IN THE ELECTRON DENSITY MAPS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.283
2624
5.1 %
RANDOM
Rwork
0.244
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obs
0.245
48964
95.1 %
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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