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Yorodumi- PDB-2kii: NMR structure of the SO2144 H-NOX domain from Shewanella oneidens... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2kii | ||||||
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Title | NMR structure of the SO2144 H-NOX domain from Shewanella oneidensis in the Fe(II)CO ligation state | ||||||
Components | Putative uncharacterized protein | ||||||
Keywords | UNKNOWN FUNCTION / H-NOX | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Shewanella oneidensis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Erbil, W.K. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2009 Title: A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation. Authors: Erbil, W.K. / Price, M.S. / Wemmer, D.E. / Marletta, M.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kii.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2kii.ent.gz | 982.9 KB | Display | PDB format |
PDBx/mmJSON format | 2kii.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ki/2kii ftp://data.pdbj.org/pub/pdb/validation_reports/ki/2kii | HTTPS FTP |
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-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: 20534.594 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Shewanella oneidensis (bacteria) / Gene: SO2144, SO_2144 / Plasmid: pET20b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)PLysS / References: UniProt: Q8EF49 |
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#2: Chemical | ChemComp-HEM / |
#3: Chemical | ChemComp-CMO / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 50 / pH: 7.4 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software | Name: X-PLOR NIH / Developer: Schwieters, C.D. et al. / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR constraints | NOE constraints total: 3262 / NOE intraresidue total count: 941 / NOE long range total count: 717 / NOE medium range total count: 678 / NOE sequential total count: 706 |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |