BIOMOLECULE: 1 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON BURIED SURFACE AREA. COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. BIOMOLECULE: 1 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC SOFTWARE USED: PISA TOTAL BURIED SURFACE AREA: 2990 ANGSTROM**2 SURFACE AREA OF THE COMPLEX: 34680 ANGSTROM**2 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL APPLY THE FOLLOWING TO CHAINS: A, B BIOMT1 1 1.000000 0.000000 0.000000 0.00000 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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Components
#1: Protein
AminopeptidasePepS
Mass: 45274.816 Da / Num. of mol.: 2 / Mutation: E343D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Strain: ATCC BAA-334 / TIGR4 / Gene: pepS, SP_0278 / Plasmid: PVFT1S-PEPS / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q97SP8, UniProt: A0A0H2UN95*PLUS, Hydrolases; Acting on peptide bonds (peptidases); Aminopeptidases
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