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- PDB-2v9n: L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2v9n | ||||||
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Title | L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A88F- E192A) | ||||||
![]() | RHAMNULOSE-1-PHOSPHATE ALDOLASE![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Grueninger, D. / Schulz, G.E. | ||||||
![]() | ![]() Title: Designed protein-protein association. Authors: Grueninger, D. / Treiber, N. / Ziegler, M.O. / Koetter, J.W. / Schulze, M.S. / Schulz, G.E. #1: ![]() Title: Structure and Catalytic Mechanism of L-Rhamnulose-1-Phosphate Aldolase Authors: Kroemer, M. / Merkel, I. / Schulz, G.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 488.6 KB | Display | ![]() |
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PDB format | ![]() | 401.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2uyuC ![]() 2uyvC ![]() 2v7gC ![]() 2v9eC ![]() 2v9fC ![]() 2v9gC ![]() 2v9iC ![]() 2v9lC ![]() 2v9mC ![]() 2v9oC ![]() 2v9uC ![]() 1ojrS 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 domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: 4 / Auth seq-ID: 1 - 274 / Label seq-ID: 1 - 274
NCS oper: (Code: given Matrix: (0.2614, 0.03225, 0.9647), Vector ![]() |
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Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | ![]() Mass: 30192.467 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() References: UniProt: P32169, ![]() |
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-Non-polymers , 6 types, 1241 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/CIT.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/PGO.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CIT.gif)
![](data/chem/img/PO4.gif)
![](data/chem/img/PGO.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-CIT / ![]() #4: Chemical | ChemComp-PO4 / ![]() #5: Chemical | ChemComp-PGO / ![]() #6: Chemical | ChemComp-GOL / ![]() #7: Water | ChemComp-HOH / | ![]() |
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-Details
Compound details | ENGINEERED RESIDUE IN CHAIN A, ALA 88 TO PHE ENGINEERED RESIDUE IN CHAIN A, GLU 192 TO ALA ...ENGINEERED |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.2 Å3/Da / Density % sol: 61 % / Description: NONE |
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Crystal grow![]() | pH: 4.9 Details: 25% (V/V) 1,2-PROPANEDIOL, 10% (V/V) GLYCEROL, 5% (W/V) PEG 3000, PHOSPHATE-CITRATE BUFFER (0.1M, PH 4.2) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 15, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.4→51 Å / Num. obs: 268317 / % possible obs: 91 % / Observed criterion σ(I): 2.88 / Redundancy: 2.3 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 7.25 |
Reflection shell | Highest resolution: 1.4 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 2.88 / % possible all: 94.4 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1OJR Resolution: 1.4→51.03 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.952 / SU B: 1.848 / SU ML: 0.033 / Cross valid method: THROUGHOUT / ESU R: 0.064 / ESU R Free: 0.057 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 7.11 Å2
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Refinement step | Cycle: LAST / Resolution: 1.4→51.03 Å
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Refine LS restraints |
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