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- PDB-11as: ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE -
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Open data
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Basic information
Entry | Database: PDB / ID: 11as | ||||||
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Title | ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE | ||||||
![]() | ASPARAGINE SYNTHETASE | ||||||
![]() | LIGASE / ASPARAGINE SYNTHETASE / NITROGEN FIXATION | ||||||
Function / homology | ![]() aspartate-ammonia ligase / aspartate-ammonia ligase activity / L-asparagine biosynthetic process / asparagine biosynthetic process / DNA damage response / protein homodimerization activity / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Nakatsu, T. / Kato, H. / Oda, J. | ||||||
![]() | ![]() Title: Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase. Authors: Nakatsu, T. / Kato, H. / Oda, J. #1: ![]() Title: Crystallization and Preliminary Crystallographic Study of Asparagine Synthetase from Escherichia Coli Authors: Nakatsu, T. / Kato, H. / Oda, J. #2: ![]() Title: Overexpression and Purification of Asparagine Synthetase from Escherichia Coli Authors: Sugiyama, A. / Kato, H. / Nishioka, T. / Oda, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 133.3 KB | Display | ![]() |
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PDB format | ![]() | 106.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 395.1 KB | Display | ![]() |
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Full document | ![]() | 422.7 KB | Display | |
Data in XML | ![]() | 17 KB | Display | |
Data in CIF | ![]() | 25.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 36633.367 Da / Num. of mol.: 2 / Mutation: C51A, C315A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: PROTEIN CRYSTALLIZED FROM 45% SATURATED AMMONIUM SULFATE, 22 MM ASPARAGINE, 88 MM MGCL2, 10 %(W/V) GLYCEROL 5 MM 2-MERCAPTOETHANOL, 50 MM HEPES, PH7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / Method: vapor diffusion, sitting dropDetails: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Apr 1, 1995 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.5 Å / Num. obs: 17805 / % possible obs: 73.8 % / Observed criterion σ(I): 1 / Redundancy: 2.9 % / Biso Wilson estimate: 11 Å2 / Rmerge(I) obs: 0.105 / Net I/σ(I): 5.3 |
Reflection shell | Resolution: 2.5→2.7 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 2.4 / % possible all: 54.5 |
Reflection | *PLUS Num. measured all: 50844 |
Reflection shell | *PLUS % possible obs: 54.5 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 13.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.21 Å / Luzzati d res low obs: 5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.61 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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