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Yorodumi- PDB-3ne1: Mycobacterium tuberculosis Acyl Carrier Protein Synthase in compl... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3ne1 | ||||||
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Title | Mycobacterium tuberculosis Acyl Carrier Protein Synthase in complex with sulfate ion | ||||||
Components | Holo-[acyl-carrier-protein] synthase | ||||||
Keywords | TRANSFERASE / acyl carrier protein synthase / acyl carrier protein / fatty acid synthase / ACPS / Mycobacterium Tuberculosis Structural Proteomics Project | ||||||
Function / homology | Function and homology information holo-[acyl-carrier-protein] synthase / holo-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Mycobacterium tuberculosis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.51 Å | ||||||
Authors | Gokulan, K. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2011 Title: Mycobacterium tuberculosis acyl carrier protein synthase adopts two different pH-dependent structural conformations. Authors: Gokulan, K. / Aggarwal, A. / Shipman, L. / Besra, G.S. / Sacchettini, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ne1.cif.gz | 87.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ne1.ent.gz | 67.6 KB | Display | PDB format |
PDBx/mmJSON format | 3ne1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3ne1_validation.pdf.gz | 457.9 KB | Display | wwPDB validaton report |
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Full document | 3ne1_full_validation.pdf.gz | 500.8 KB | Display | |
Data in XML | 3ne1_validation.xml.gz | 22.1 KB | Display | |
Data in CIF | 3ne1_validation.cif.gz | 28.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ne/3ne1 ftp://data.pdbj.org/pub/pdb/validation_reports/ne/3ne1 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14019.756 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Strain: H37RV Gene: acpS, MT2599, MTV009.08c, Mycobacterium Tuberculosis, Rv2523c Production host: Escherichia coli (E. coli) / Strain (production host): BL21 DE3 References: UniProt: P0A4W8, UniProt: P9WQD3*PLUS, holo-[acyl-carrier-protein] synthase #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.73 Å3/Da / Density % sol: 54.87 % |
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Crystal grow | Method: evaporation Details: 5.6% PEG 4K, 0.07 M sodium acetate pH 4.6 to 5.5, 50 mM ammonium sulfate, 30% glycerol., EVAPORATION PH range: 4 to 6 |
-Data collection
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 Å |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.51→30 Å / Num. all: 15471 / Num. obs: 15471 / % possible obs: 95.7 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 13.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.51→20.07 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.911 / SU B: 14.034 / SU ML: 0.294 / Cross valid method: THROUGHOUT / ESU R Free: 0.353 / 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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 74.144 Å2
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Refinement step | Cycle: LAST / Resolution: 2.51→20.07 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.51→2.57 Å / Total num. of bins used: 20
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