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Structure paper

TitleBackbone Modification in a Protein Hydrophobic Core.
Journal, issue, pagesChemistry, Page e202401890-e202401890, Year 2024
Publish dateApr 5, 2024 (structure data deposition date)
AuthorsLin, Y. / Horne, W.S.
External linksChemistry / PubMed:38753977
MethodsNMR (solution)
Structure data

PDB-9bb1:
Backbone Modification in the GA Module of Protein PAB: Wild-type Sequence
Method: SOLUTION NMR

PDB-9bb2:
Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 20 and 24
Method: SOLUTION NMR

PDB-9bb3:
Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 22 and 26
Method: SOLUTION NMR

PDB-9bb4:
Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 23 and 26
Method: SOLUTION NMR

PDB-9bb5:
Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 22 and 26
Method: SOLUTION NMR

PDB-9bb6:
Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 5 and 13, beta3 residue at position 9
Method: SOLUTION NMR

PDB-9bb7:
Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 5 and 39, beta3 residue at position 26
Method: SOLUTION NMR

Source
  • finegoldia magna (bacteria)
KeywordsPROTEIN BINDING / helix bundle / designed variant

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