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Yorodumi- PDB-2l15: Solution Structure of Cold Shock Protein CspA Using Combined NMR ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2l15 | ||||||
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Title | Solution Structure of Cold Shock Protein CspA Using Combined NMR and CS-Rosetta method | ||||||
Components | Cold shock protein CspACold shock response | ||||||
Keywords | TRANSCRIPTION / CspA / CS-Rosetta | ||||||
Function / homology | Function and homology information negative regulation of termination of DNA-templated transcription / transcription antitermination factor activity, RNA binding / response to cold / single-stranded DNA binding / regulation of gene expression / nucleic acid binding / single-stranded RNA binding / positive regulation of DNA-templated transcription / DNA binding / RNA binding ...negative regulation of termination of DNA-templated transcription / transcription antitermination factor activity, RNA binding / response to cold / single-stranded DNA binding / regulation of gene expression / nucleic acid binding / single-stranded RNA binding / positive regulation of DNA-templated transcription / DNA binding / RNA binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Tang, Y. / Schneider, W.M. / Shen, Y. / Raman, S. / Inouye, M. / Baker, D. / Roth, M.J. / Montelione, G.T. | ||||||
Citation | Journal: J Struct Funct Genomics / Year: 2010 Title: Fully automated high-quality NMR structure determination of small (2)H-enriched proteins. Authors: Tang, Y. / Schneider, W.M. / Shen, Y. / Raman, S. / Inouye, M. / Baker, D. / Roth, M.J. / Montelione, G.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l15.cif.gz | 215.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l15.ent.gz | 173.9 KB | Display | PDB format |
PDBx/mmJSON format | 2l15.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l1/2l15 ftp://data.pdbj.org/pub/pdb/validation_reports/l1/2l15 | 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: 7411.253 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: ECP_3659 / Production host: Escherichia coli (E. coli) / References: UniProt: Q0TBP6, UniProt: P0A9X9*PLUS |
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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: 0.2 mM [U-100% 2H; 100% 13C; U-100% 15N] ILV Methyl 1H CspA-1, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O |
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Sample | Conc.: 0.2 mM / Component: CspA-1 Isotopic labeling: [U-100% 2H; 100% 13C; U-100% 15N] ILV Methyl 1H |
Sample conditions | Ionic strength: 50 / pH: 6.0 / Pressure: ambient / Temperature: 20 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 | |||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the best score calculted by CS-Rosetta Conformers calculated total number: 10000 / Conformers submitted total number: 10 |