wwPDB validation report of PDB entry 3SUE

NS4A (UNP residues 1674-1688), NS3 (UNP residues 1027-1208)

Crystal structure of NS3/4A protease in complex with vaniprevir

Crystal structure of NS3/4A protease variant R155K in complex with vaniprevir

Crystal structure of NS3/4A protease variant D168A in complex with vaniprevir

Crystal structure of NS3/4A protease variant A156T in complex with vaniprevir

Crystal structure of NS3/4A protease in complex with MK-5172

Crystal structure of NS3/4A protease variant D168A in complex with MK-5172

Crystal structure of NS3/4A protease variant A156T in complex with MK-5172

Crystal structure of NS3/4A protease in complex with Telaprevir

Crystal structure of NS3/4A protease variant R155K in complex with Telaprevir

Crystal structure of NS3/4A protease variant D168A in complex with Telaprevir

Crystal structure of NS3/4A protease variant A156T in complex with Telaprevir

MK-5172 IS A MACROCYCLIC, PEPTIDOMIMETIC HCV NS3/4A PROTEASE INHIBITOR FROM MERCK. THE DRUG MIMICS THE PEPTIDE BACKBONE OF PROTEINS, ALTHOUGH THE DRUG MOIETIES CANNOT BE SEQUENCED USING AMINO ACID NOMENCLATURE.
THE COFACTOR 4A RESIDUES 990-1000 (GLY SER VAL VAL ILE VAL GLY ARG ILE ASN LEU) IN THIS ENTRY CORRESPOND TO RESIDUES NUMBERING 1678-1688 OF DATABASE SEQUENCE REFERENCE (UNP A8DG50). THIS PEPTIDE IS COVALENTLY LINKED TO THE N-TERMINUS OF NS3. C1679S MUTATION WAS ENGINEERED TO PREVENT DISULFIDE FORMATION. THE V1686I AND I1687N WERE ENGINEERED TO OPTIMIZE THE LINKER BETWEEN THE COFACTOR 4A AND NS3.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Crystal structure of NS3/4A protease variant R155K in complex with MK-5172

The largest off-origin peak in the Patterson function is 4.40% of the height of the origin peak. No significant pseudotranslation is detected.

20191225.v01 (using entries in the PDB archive December 25th 2019)

structure factor analysis and validation

geometric validation package for ligand chemistry in protein x-ray structures