- PDB-1wcn: NMR structure of the carboxyterminal domains of Escherichia coli NusA -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1wcn
Title
NMR structure of the carboxyterminal domains of Escherichia coli NusA
Components
TRANSCRIPTION ELONGATION PROTEIN NUSA
Keywords
RNA BINDING PROTEIN / RNA-BINDING PROTEIN / ESCHERICHIA COLI NUSA / TRANSCRIPTION REGULATION / REGULATION OF RNA BINDING / TRANSCRIPTION ANTITERMINATION AND TERMINATION / C-TERMINAL REPEAT UNITS / RNA-BINDING
TRANSCRIPTIONELONGATIONPROTEINNUSA / N UTILIZATION SUBSTANCE PROTEIN A / L FACTOR NUSA
Mass: 7469.270 Da / Num. of mol.: 1 / Fragment: ACIDIC REPEAT 2, RESIDUES 426-495 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PTKK19 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P03003, UniProt: P0AFF6*PLUS
Compound details
FUNCTION: PARTICIPATES IN BOTH THE TERMINATION AND ANTITERMINATION OF TRANSCRIPTION. NUSA BINDS ...FUNCTION: PARTICIPATES IN BOTH THE TERMINATION AND ANTITERMINATION OF TRANSCRIPTION. NUSA BINDS DIRECTLY TO THE CORE ENZYME OF THE DNA-DEPENDENT RNA POLYMERASE. NUSA ALSO INTERACTS WITH LAMBDA N PROTEIN, RNA, RHO FACTOR, AND PERHAPS NUSB. BINDS RNA.
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Type: SEE PUBLICATION
NMR details
Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N LABELED GP-NUSA(339-495)
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Sample preparation
Details
Contents: 90% WATER / 10% D2O
Sample conditions
Ionic strength: 50 mM / pH: 6.8 / Pressure: 1.0 atm / Temperature: 298.0 K
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NMR measurement
NMR spectrometer
Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz
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Processing
NMR software
Name
Version
Developer
Classification
Xplor-NIH
1.2.1
SCHWIETERS, KUSZEWSKI, TJ
refinement
NMRView
structuresolution
Refinement
Method: MANUAL / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JOURNAL CITATION ABOVE
NMR ensemble
Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 90 / Conformers submitted total number: 19
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