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Yorodumi- PDB-1ssk: Structure of the N-terminal RNA-binding Domain of the SARS CoV Nu... -
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-Basic information
Entry | Database: PDB / ID: 1ssk | ||||||
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Title | Structure of the N-terminal RNA-binding Domain of the SARS CoV Nucleocapsid Protein | ||||||
Components | Nucleocapsid proteinVirus | ||||||
Keywords | STRUCTURAL PROTEIN / nucleocapsid protein | ||||||
Function / homology | Function and homology information SARS-CoV-1-host interactions / Translation of Structural Proteins / Virion Assembly and Release / viral RNA genome packaging / Transcription of SARS-CoV-1 sgRNAs / negative regulation of interferon-beta production / Maturation of nucleoprotein / SARS-CoV-1 modulates host translation machinery / Attachment and Entry / SARS-CoV-1 targets host intracellular signalling and regulatory pathways ...SARS-CoV-1-host interactions / Translation of Structural Proteins / Virion Assembly and Release / viral RNA genome packaging / Transcription of SARS-CoV-1 sgRNAs / negative regulation of interferon-beta production / Maturation of nucleoprotein / SARS-CoV-1 modulates host translation machinery / Attachment and Entry / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / SARS-CoV-1 activates/modulates innate immune responses / viral capsid / host cell endoplasmic reticulum-Golgi intermediate compartment / host cell Golgi apparatus / viral nucleocapsid / host cell perinuclear region of cytoplasm / molecular adaptor activity / ribonucleoprotein complex / host cell nucleus / DNA binding / RNA binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | SARS coronavirus | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | Huang, Q. / Yu, L. / Petros, A.M. / Gunasekera, A. / Liu, Z. / Xu, N. / Hajduk, P. / Mack, J. / Fesik, S.W. / Olejniczak, E.T. | ||||||
Citation | Journal: Biochemistry / Year: 2004 Title: Structure of the N-Terminal RNA-Binding Domain of the SARS CoV Nucleocapsid Protein. Authors: Huang, Q. / Yu, L. / Petros, A.M. / Gunasekera, A. / Liu, Z. / Xu, N. / Hajduk, P. / Mack, J. / Fesik, S.W. / Olejniczak, E.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ssk.cif.gz | 59 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ssk.ent.gz | 48.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ssk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ss/1ssk ftp://data.pdbj.org/pub/pdb/validation_reports/ss/1ssk | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17179.035 Da / Num. of mol.: 1 / Fragment: N-terminal Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) SARS coronavirus / Genus: Coronavirus / Strain: SARS / Gene: N / Plasmid: pet21d+ / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P59595 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5 mM N-terminal SARS CoV NP, U-15N,90% H2O/10% 2H2O, 50 mM sodium phosphate (pH 6.8) and 100 mM sodium chloride. |
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Sample conditions | Ionic strength: 100mM Nacl / pH: 6.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software | Name: CNS / Version: 2000 / Developer: brunger / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR representative | Selection criteria: minimized average structure |
NMR ensemble | Conformers submitted total number: 1 |