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- PDB-3mef: MAJOR COLD-SHOCK PROTEIN FROM ESCHERICHIA COLI SOLUTION NMR STRUCTURE -
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Open data
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Basic information
Entry | Database: PDB / ID: 3mef | |||||||||
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Title | MAJOR COLD-SHOCK PROTEIN FROM ESCHERICHIA COLI SOLUTION NMR STRUCTURE | |||||||||
![]() | PROTEIN (COLD-SHOCK PROTEIN A) | |||||||||
![]() | GENE REGULATION / COLD-SHOCK PROTEIN / TRANSCRIPTION REGULATION / SINGLE-STRANDED RNA/DNA BINDING / OB FOLD / GREEK-KEY TOPOLOGY / RNA CHAPERONE / AROMATIC-BASE STACKING INTERACTIONS | |||||||||
Function / homology | ![]() 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 Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | SOLUTION NMR / CONSTRAINT-VIOLATION MINIMIZATION IN DIHEDRAL ANGLE SPACE | |||||||||
![]() | Feng, W. / Tejero, R. / Montelione, G.T. | |||||||||
![]() | ![]() Title: Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site. Authors: Feng, W. / Tejero, R. / Zimmerman, D.E. / Inouye, M. / Montelione, G.T. #1: ![]() Title: Solution NMR Structure of the Major Cold Shock Protein (CspA) from Escherichia Coli: Identification of a Binding Epitope for DNA Authors: Newkirk, K. / Feng, W. / Jiang, W. / Tejero, R. / Emerson, S.D. / Inouye, M. / Montelione, G.T. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 318.3 KB | Display | ![]() |
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PDB format | ![]() | 263 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 344 KB | Display | ![]() |
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Full document | ![]() | 470.1 KB | Display | |
Data in XML | ![]() | 23.9 KB | Display | |
Data in CIF | ![]() | 35.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 7280.057 Da / Num. of mol.: 1 / Fragment: FULL LENGTH PROTEIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURES WERE DETERMINED USING DOUBLE- AND TRIPLE-RESONANCE NMR SPECTROSCOPY METHODS ON UNENRICHED, 15N-ENRICHED, AND 13C,15N-ENRICHED CSPA FROM E.COLI - |
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Sample preparation
Sample conditions | Ionic strength: 50 MILLIMOLAR SODIUM PHOSPHATE / pH: 6.0 / Pressure: 1 atm / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITY 500 / Manufacturer: Varian / Model: UNITY 500 / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: CONSTRAINT-VIOLATION MINIMIZATION IN DIHEDRAL ANGLE SPACE Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION | |||||||||
NMR ensemble | Conformer selection criteria: LOWEST VALUE OF TARGET FUNCTION Conformers calculated total number: 500 / Conformers submitted total number: 16 |