A: ENGINEERED VERSION OF TRANSMEMBRANE RECEPTOR AF1503 B: ENGINEERED VERSION OF TRANSMEMBRANE RECEPTOR AF1503 C: ENGINEERED VERSION OF TRANSMEMBRANE RECEPTOR AF1503 D: ENGINEERED VERSION OF TRANSMEMBRANE RECEPTOR AF1503
Mass: 34496.090 Da / Num. of mol.: 4 Fragment: C-TERMINAL PROTEOLYTIC FRAGMENT WITH UNKNOWN CLEAVAGE SITE Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ARCHAEOGLOBUS FULGIDUS (archaea) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O28769
Mass: 18.015 Da / Num. of mol.: 382 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE STRUCTURE CONTAINS ONLY A C-TERMINAL PROTEOLYTIC FRAGMENT OF THE DEPOSITED SEQUENCE WITH ...THE STRUCTURE CONTAINS ONLY A C-TERMINAL PROTEOLYTIC FRAGMENT OF THE DEPOSITED SEQUENCE WITH UNKNOWN CLEAVAGE SITE
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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 Å3/Da / Density % sol: 40 % / Description: NONE
Resolution: 1.7→37.67 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.93 / SU B: 5.471 / SU ML: 0.092 / Cross valid method: THROUGHOUT / ESU R: 0.119 / ESU R Free: 0.122 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES U VALUES
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.24303
2187
5 %
RANDOM
Rwork
0.19286
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obs
0.19538
41246
99.15 %
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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