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Structure paper

TitleStructural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein
Journal, issue, pagesSci Rep, Vol. 6, Page 34654-34654, Year 2016
Publish dateMar 17, 2016 (structure data deposition date)
AuthorsHanazono, Y. / Takeda, K. / Miki, K.
External linksSci Rep / PubMed:27698466
MethodsX-ray diffraction
Resolution1.901 - 2.4 Å
Structure data

PDB-5b3w:
Crystal structure of hPin1 WW domain (5-15) fused with maltose-binding protein in C2221 form
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-5b3x:
Crystal structure of hPin1 WW domain (5-15) fused with maltose-binding protein in P41212 form
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-5b3y:
Crystal structure of hPin1 WW domain (5-23) fused with maltose-binding protein
Method: X-RAY DIFFRACTION / Resolution: 1.901 Å

PDB-5b3z:
Crystal structure of hPin1 WW domain (5-39) fused with maltose-binding protein
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5bmy:
Crystal structure of hPin1 WW domain (5-21) fused with maltose-binding protein
Method: X-RAY DIFFRACTION / Resolution: 2.001 Å

Chemicals

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • escherichia coli k-12 (bacteria)
  • escherichia coli o157:h7 (bacteria)
KeywordsISOMERASE / SUGAR BINDING PROTEIN / WW domain / maltose-binding protein

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