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Yorodumi- PDB-2kos: NMR solution structures of octanoyl-ACP from Streptomyces coelico... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2kos | ||||||
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Title | NMR solution structures of octanoyl-ACP from Streptomyces coelicolor Fatty Acid Synthase | ||||||
Components | Acyl carrier protein | ||||||
Keywords | TRANSPORT PROTEIN / acyl carrier protein / intermediate binding / fatty acid synthase | ||||||
Function / homology | Function and homology information lipid A biosynthetic process / acyl binding / acyl carrier activity / cytosol Similarity search - Function | ||||||
Biological species | Streptomyces coelicolor (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | closest to the average, model 1 | ||||||
Authors | Ploskon, E. / Arthur, C. / Crump, M.P. | ||||||
Citation | Journal: Chem.Biol. / Year: 2010 Title: Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis Authors: Ploskon, E. / Arthur, C.J. / Kanari, A.L. / Wattana-amorn, P. / Williams, C. / Crosby, J. / Simpson, T.J. / Willis, C.L. / Crump, M.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kos.cif.gz | 549.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kos.ent.gz | 485 KB | Display | PDB format |
PDBx/mmJSON format | 2kos.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2kos_validation.pdf.gz | 420.8 KB | Display | wwPDB validaton report |
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Full document | 2kos_full_validation.pdf.gz | 542.6 KB | Display | |
Data in XML | 2kos_validation.xml.gz | 31.8 KB | Display | |
Data in CIF | 2kos_validation.cif.gz | 50.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ko/2kos ftp://data.pdbj.org/pub/pdb/validation_reports/ko/2kos | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8793.774 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces coelicolor (bacteria) / Gene: acpP, SCO2389, SC4A7.17 / Plasmid: Sc-apoFAS-pET21 / Production host: Escherichia coli (E. coli) / References: UniProt: P72393 |
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#2: Chemical | ChemComp-SXO / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 50mM potassium phosphate-1, 0.5mM sodium azide-2, 1mM octanoyl phosphopantetheine-3, 1mM [U-99% 13C; U-99% 15N] ACP-4, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 50 / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: 20 best structures from last iteration were selected for water refinement. Water refined structures were calculated using the slightly modified refinement script applied to the RECOORD database. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |