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Open data
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Basic information
Entry | Database: PDB / ID: 5ypy | ||||||
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Title | Crystal structure of IlvN. Val-1c | ||||||
![]() | Acetolactate synthase isozyme 1 small subunit | ||||||
![]() | TRANSFERASE / Transferase subunit / Regulatory subunit / ACT protein / amino acid binding | ||||||
Function / homology | ![]() acetolactate synthase regulator activity / acetolactate synthase / acetolactate synthase complex / branched-chain amino acid biosynthetic process / acetolactate synthase activity / valine biosynthetic process / isoleucine biosynthetic process / amino acid biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sarma, S.P. / Bansal, A. / Schindelin, H. / Demeler, B. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Crystallographic Structures of IlvN·Val/Ile Complexes: Conformational Selectivity for Feedback Inhibition of Aceto Hydroxy Acid Synthases. Authors: Bansal, A. / Karanth, N.M. / Demeler, B. / Schindelin, H. / Sarma, S.P. #1: ![]() Title: The coil-to-helix transition in IlvN regulates the allosteric control of Escherichia coli acetohydroxyacid synthase I. Authors: Karanth, N.M. / Sarma, S.P. #2: Journal: Biochemistry / Year: 2008 Title: Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme. Authors: Mitra, A. / Sarma, S.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 163.2 KB | Display | ![]() |
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PDB format | ![]() | 129.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 469.3 KB | Display | ![]() |
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Full document | ![]() | 473.5 KB | Display | |
Data in XML | ![]() | 15.4 KB | Display | |
Data in CIF | ![]() | 21.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5yppC ![]() 5ypwC ![]() 5yumC ![]() 2lvwS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 11262.869 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: ilvN, b3670, JW3645 / Production host: ![]() ![]() #2: Chemical | ChemComp-VAL / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 58.11 % |
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Crystal grow | Temperature: 288 K / Method: microbatch / pH: 6.5 / Details: 1.6M Sodium citrate tribasic dihydrate, pH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 30, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 1.966→62.72 Å / Num. obs: 36151 / % possible obs: 99.7 % / Redundancy: 4 % / CC1/2: 0.993 / Rmerge(I) obs: 0.107 / Rpim(I) all: 0.096 / Net I/σ(I): 5.2 |
Reflection shell | Resolution: 1.97→2.01 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.666 / Mean I/σ(I) obs: 1.1 / Num. unique obs: 2421 / CC1/2: 0.764 / Rpim(I) all: 0.589 / Rrim(I) all: 0.893 / % possible all: 95.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2LVW Resolution: 1.966→44.25 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 31.46
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.966→44.25 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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