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: 34360.336 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: THE DI-PEPTIDE LW IS BOUND TO THE PROTEIN Source: (gene. exp.) BACILLUS THERMOPROTEOLYTICUS (bacteria) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P00800, thermolysin
Resolution: 1.95→20 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.923 / SU B: 3.489 / SU ML: 0.102 / Cross valid method: THROUGHOUT / ESU R: 0.174 / ESU R Free: 0.159 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.21905
1995
8.4 %
RANDOM
Rwork
0.16553
-
-
-
obs
0.17002
21829
98.29 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK