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PDBsum entry 5b3z
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Isomerase,sugar binding protein
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PDB id
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5b3z
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PDB id:
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| Name: |
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Isomerase,sugar binding protein
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Title:
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Crystal structure of hpin1 ww domain (5-39) fused with maltose-binding protein
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Structure:
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Peptidyl-prolyl cis-trans isomerase nima-interacting 1, maltose-binding periplasmic protein. Chain: a, b, c, d. Fragment: unp(q13526) 5-39,unp(p0aex9) residues 27-393. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens, escherichia coli k-12. Human. Organism_taxid: 9606, 83333. Strain: k-12. Gene: pin1, male. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.30Å
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R-factor:
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0.183
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R-free:
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0.224
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Authors:
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Y.Hanazono,K.Takeda,K.Miki
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Key ref:
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Y.Hanazono
et al.
(2016).
Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein.
Sci Rep,
6,
34654.
PubMed id:
DOI:
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Date:
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17-Mar-16
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Release date:
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26-Oct-16
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PROCHECK
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Headers
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References
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Enzyme class 1:
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E.C.?
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Enzyme class 2:
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E.C.5.2.1.8
- peptidylprolyl isomerase.
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Reaction:
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[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
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Peptidylproline (omega=180)
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=
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peptidylproline (omega=0)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Sci Rep
6:34654
(2016)
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PubMed id:
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Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein.
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Y.Hanazono,
K.Takeda,
K.Miki.
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ABSTRACT
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');
}
}
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