5MP3

Crystal structure of DC8E8 Fab in the complex with a 30-mer tau peptide at pH 6.5

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.75 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.201 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history. 


Literature

Crystal structure of DC8E8 Fab in the complex with a 30-mer tau peptide at pH 6.5

Skrabana, R., Novak, M.

To be published.

Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Igh proteinA [auth H],
C [auth A]		220Mus musculusMutation(s): 0 
UniProt
Find proteins for Q99LC4 (Mus musculus)
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Go to UniProtKB:  Q99LC4
Entity Groups  
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UniProt GroupQ99LC4
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ENSMUSG00000076577 proteinB [auth L],
D [auth B]		218Mus musculusMutation(s): 0 
UniProt
Find proteins for Q52L64 (Mus musculus)
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UniProt GroupQ52L64
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Microtubule-associated proteinE [auth C],
F [auth D]		30Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P10636 (Homo sapiens)
Explore P10636 
Go to UniProtKB:  P10636
PHAROS:  P10636
GTEx:  ENSG00000186868 
Entity Groups  
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UniProt GroupP10636
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
PCA
Query on PCA		A [auth H],
C [auth A]		L-PEPTIDE LINKINGC5 H7 N O3GLN
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.75 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.201 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 61.85α = 90
b = 89.89β = 90.11
c = 83.6γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-05-02
    Type: Initial release
  • Version 1.1: 2018-11-21
    Changes: Data collection, Derived calculations
  • Version 1.2: 2019-07-10
    Changes: Data collection
  • Version 1.3: 2019-07-17
    Changes: Data collection
  • Version 2.0: 2020-03-11
    Changes: Polymer sequence
  • Version 2.1: 2024-01-17
    Changes: Data collection, Database references, Refinement description