Download MendeleyAntibody Switch Residue Engineering for Improved Crystallization Chaperones
Bailey, L.J., Kossiakoff, A.A.To be published.
5UEK
Structure of antigen-Fab 12E complex with Histone chaperone ASF1
- PDB DOI: https://doi.org/10.2210/pdb5UEK/pdb
- Classification: IMMUNE SYSTEM
- Organism(s): Saccharomyces cerevisiae S288C, Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2017-01-02 Released: 2018-01-10
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.212
- R-Value Work: 0.176
- R-Value Observed: 0.178
wwPDB Validation 3D Report Full Report
This is version 1.0 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Histone chaperone ASF1 | 154 | Saccharomyces cerevisiae S288C | Mutation(s): 0 Gene Names: ASF1, CIA1, YJL115W, J0755 |  | |
UniProt | |||||
Find proteins for P32447 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P32447 Go to UniProtKB: P32447 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P32447 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Fab 12E Heavy Chain | B [auth H] | 227 | Homo sapiens | Mutation(s): 0 |  |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Fab 12E Light Chain | C [auth L] | 215 | Homo sapiens | Mutation(s): 0 |  |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
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Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.212
- R-Value Work: 0.176
- R-Value Observed: 0.178
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 43.175 | α = 90 |
| b = 142.932 | β = 98.8 |
| c = 49.401 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-2000 | data reduction |
| SCALEPACK | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2018-01-10 Deposition Author(s): Bailey, L.J., Kossiakoff, A.A.
Revision History (Full details and data files)
- Version 1.0: 2018-01-10
Type: Initial release
