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Yorodumi- PDB-5kr5: Directed Evolution of Transaminases By Ancestral Reconstruction. ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5kr5 | ||||||
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Title | Directed Evolution of Transaminases By Ancestral Reconstruction. Using Old Proteins for New Chemistries | ||||||
Components | 4-aminobutyrate transaminase | ||||||
Keywords | TRANSFERASE / phylogenetics / directed evolution / transaminase / protein engineering | ||||||
Function / homology | Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / 3-Layer(aba) Sandwich / Alpha Beta / DI(HYDROXYETHYL)ETHER / PYRIDOXAL-5'-PHOSPHATE Function and homology information | ||||||
Biological species | Pseudomonas (RNA similarity group I) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Wilding, M. / Newman, J. / Peat, T.S. / Scott, C. | ||||||
Citation | Journal: Green Chemistry / Year: 2017 Title: Reverse engineering: transaminase biocatalyst development using ancestral sequence reconstruction Authors: Wilding, M. / Peat, T.S. / Kalyaanamoorthy, S. / Newman, J. / Scott, C. / Jermiin, L.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5kr5.cif.gz | 195.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5kr5.ent.gz | 152.6 KB | Display | PDB format |
PDBx/mmJSON format | 5kr5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kr/5kr5 ftp://data.pdbj.org/pub/pdb/validation_reports/kr/5kr5 | HTTPS FTP |
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-Related structure data
Related structure data | 5kqtSC 5kquC 5kqwC 5kr3C 5kr4C 5kr6C S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / Ens-ID: 1 / Beg auth comp-ID: SER / Beg label comp-ID: SER / End auth comp-ID: ALA / End label comp-ID: ALA / Refine code: 0 / Auth seq-ID: 3 - 455 / Label seq-ID: 23 - 475
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-Components
#1: Protein | Mass: 52033.895 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas (RNA similarity group I) / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: beta-alanine-pyruvate transaminase #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.22 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 150 plus 150 nL drops with protein at 4 mg/mL and reservoir conditions of 15% PEG 8000, 11 mM calcium acetate, 100 mM Tris pH 7.1. Microcrystals were used as nucleating agents to obtain full size crystals. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 1, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→48.6 Å / Num. obs: 59261 / % possible obs: 99.6 % / Redundancy: 7.3 % / CC1/2: 0.994 / Rmerge(I) obs: 0.17 / Net I/σ(I): 9.5 |
Reflection shell | Resolution: 2.1→2.15 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.899 / Mean I/σ(I) obs: 2.2 / CC1/2: 0.67 / % possible all: 97.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5kqt Resolution: 2.1→48.6 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.908 / SU B: 6.161 / SU ML: 0.155 / Cross valid method: THROUGHOUT / ESU R: 0.23 / ESU R Free: 0.186 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.309 Å2
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Refinement step | Cycle: 1 / Resolution: 2.1→48.6 Å
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Refine LS restraints |
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