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- PDB-3zo8: Wild-type chorismate mutase of Bacillus subtilis at 1.6 A resolution -
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Open data
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Basic information
Entry | Database: PDB / ID: 3zo8 | ||||||
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Title | Wild-type chorismate mutase of Bacillus subtilis at 1.6 A resolution | ||||||
![]() | CHORISMATE MUTASE AROH | ||||||
![]() | ISOMERASE / PSEUDO-ALPHA BETA-BARREL | ||||||
Function / homology | ![]() chorismate metabolic process / chorismate mutase / chorismate mutase activity / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Burschowsky, D. / vanEerde, A. / Okvist, M. / Kienhofer, A. / Kast, P. / Hilvert, D. / Krengel, U. | ||||||
![]() | ![]() Title: Electrostatic Transition State Stabilization Rather Than Reactant Destabilization Provides the Chemical Basis for Efficient Chorismate Mutase Catalysis. Authors: Burschowsky, D. / Van Eerde, A. / Okvist, M. / Kienhofer, A. / Kast, P. / Hilvert, D. / Krengel, U. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 282.6 KB | Display | ![]() |
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PDB format | ![]() | 232.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 463.8 KB | Display | ![]() |
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Full document | ![]() | 473.2 KB | Display | |
Data in XML | ![]() | 28.2 KB | Display | |
Data in CIF | ![]() | 39.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3zopC ![]() 3zp4C ![]() 3zp7C ![]() 1dbfS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given / Matrix: (1), |
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Components
#1: Protein | Mass: 14507.915 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.9 % / Description: NONE |
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Crystal grow | pH: 6 Details: 100 MM MMT BUFFER ---MALIC ACID, MES, TRIS, IN MOLAR RATIOS OF 1:2:2, RESPECTIVELY--- PH 6.0, 100 MM MAGNESIUM CHLORIDE, 25% W/V PEG 1000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU IMAGE PLATE / Detector: IMAGE PLATE / Date: Nov 2, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54187 Å / Relative weight: 1 |
Reflection | Resolution: 1.59→82.58 Å / Num. obs: 93148 / % possible obs: 85 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 1.59→1.69 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 4.4 / % possible all: 59.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1DBF Resolution: 1.59→82.6 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.958 / SU B: 3.465 / SU ML: 0.051 / Cross valid method: THROUGHOUT / ESU R: 0.022 / ESU R Free: 0.016 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 118-127 ARE DISORDERED.
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.774 Å2
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Refinement step | Cycle: LAST / Resolution: 1.59→82.6 Å
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Refine LS restraints |
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