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- PDB-4baa: Redesign of a Phenylalanine Aminomutase into a beta-Phenylalanine... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4baa | |||||||||
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Title | Redesign of a Phenylalanine Aminomutase into a beta-Phenylalanine Ammonia Lyase | |||||||||
![]() | PHENYLALANINE AMMONIA-LYASE | |||||||||
![]() | LYASE / MIO | |||||||||
Function / homology | ![]() phenylalanine aminomutase (L-beta-phenylalanine forming) / intramolecular aminotransferase activity / paclitaxel biosynthetic process / phenylalanine ammonia-lyase / L-phenylalanine metabolic process / cinnamic acid biosynthetic process / alkaloid biosynthetic process / phenylalanine ammonia-lyase activity / L-phenylalanine catabolic process / protein homotetramerization / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Bartsch, S. / Wybenga, G.G. / Jansen, M. / Heberling, M.M. / Wu, B. / Dijkstra, B.W. / Janssen, D.B. | |||||||||
![]() | ![]() Title: Redesign of a Phenylalanine Aminomutase Into a Phenylalanine Ammonia Lyase Authors: Bartsch, S. / Wybenga, G.G. / Jansen, M. / Heberling, M.M. / Wu, B. / Dijkstra, B.W. / Janssen, D.B. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 480.1 KB | Display | ![]() |
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PDB format | ![]() | 394.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 475 KB | Display | ![]() |
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Full document | ![]() | 493.6 KB | Display | |
Data in XML | ![]() | 83 KB | Display | |
Data in CIF | ![]() | 113.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4babC ![]() 2yiiS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 77483.516 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() #2: Water | ChemComp-HOH / | Sequence details | SEQUENCE INCLUDES AN N-TERMINAL LINKER OF 20 AMINO ACIDS AND INCLUDES AN R92S AND R93S MUTATION | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.2 % / Description: NONE |
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Crystal grow | Details: 4 % TACSISMATE, 12 % W/V PEG 3350, 2 MM DTT |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Aug 28, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97934 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→48.9 Å / Num. obs: 94431 / % possible obs: 98.1 % / Observed criterion σ(I): 0 / Redundancy: 2.3 % / Biso Wilson estimate: 36.7 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 6.2 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.38 / Mean I/σ(I) obs: 2.4 / % possible all: 97.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2YII Resolution: 2.5→48.9 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.898 / SU B: 9.745 / SU ML: 0.216 / Cross valid method: THROUGHOUT / ESU R: 0.765 / ESU R Free: 0.298 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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 / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.459 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→48.9 Å
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Refine LS restraints |
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