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- PDB-5isv: Crystal structure of the ribosomal-protein-S18-alanine N-acetyltr... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5isv | ||||||
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Title | Crystal structure of the ribosomal-protein-S18-alanine N-acetyltransferase from Escherichia coli | ||||||
![]() | Ribosomal-protein-alanine acetyltransferase | ||||||
![]() | TRANSFERASE / RimI / AcCoA / GNAT / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID | ||||||
Function / homology | ![]() [ribosomal protein bS18]-alanine N-acetyltransferase / N-terminal peptidyl-alanine acetylation / peptide-alanine-alpha-N-acetyltransferase activity / N-terminal protein amino acid acetylation / protein modification process => GO:0036211 / internal peptidyl-lysine acetylation / N-acetyltransferase activity / acyltransferase activity, transferring groups other than amino-acyl groups / peptide-lysine-N-acetyltransferase activity / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Filippova, E.V. / Minasov, G. / Kiryukhina, O. / Shuvalova, L. / Grimshaw, S. / Wolfe, A.J. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID) | ||||||
![]() | ![]() Title: Crystal structure of the ribosomal-protein-S18-alanine N-acetyltransferase from Escherichia coli Authors: Filippova, E.V. / Minasov, G. / Kiryukhina, O. / Shuvalova, L. / Grimshaw, S. / Wolfe, A.J. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID) | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 157.7 KB | Display | ![]() |
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PDB format | ![]() | 126.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 431 KB | Display | ![]() |
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Full document | ![]() | 432.8 KB | Display | |
Data in XML | ![]() | 16.9 KB | Display | |
Data in CIF | ![]() | 25.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2cntS S: Starting model for refinement |
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Similar structure data | |
Other databases |
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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 domain:
NCS domain segments: Ens-ID: 1 / Refine code: 6
NCS oper:
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Components
#1: Protein | Mass: 18591.744 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A946, UniProt: P0A944*PLUS, ribosomal-protein-alanine N-acetyltransferase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.87 Å3/Da / Density % sol: 34.28 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.01 M tri-sodium citrate, 33% (w/v) PEG6000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 8, 2016 / Details: beryllium lenses |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97857 Å / Relative weight: 1 |
Reflection | Resolution: 1.35→30 Å / Num. obs: 56272 / % possible obs: 95 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.045 / Net I/σ(I): 38.05 |
Reflection shell | Resolution: 1.35→1.37 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.335 / Mean I/σ(I) obs: 3.3 / % possible all: 90 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2CNT Resolution: 1.35→30 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.962 / SU B: 3.731 / SU ML: 0.065 / Cross valid method: THROUGHOUT / ESU R: 0.072 / ESU R Free: 0.068 / 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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.192 Å2
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Refinement step | Cycle: LAST / Resolution: 1.35→30 Å
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Refine LS restraints |
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