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Open data
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Basic information
Entry | Database: PDB / ID: 2jvv | ||||||
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Title | Solution Structure of E. coli NusG carboxyterminal domain | ||||||
![]() | Transcription antitermination protein nusG | ||||||
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Function / homology | ![]() transcription elongation-coupled chromatin remodeling / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription termination / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Schweimer, K. / Scheckenhofer, U. / Roesch, P. | ||||||
![]() | ![]() Title: Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. Authors: Mooney, R.A. / Schweimer, K. / Rosch, P. / Gottesman, M. / Landick, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 381.1 KB | Display | ![]() |
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PDB format | ![]() | 305.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 20560.523 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
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NMR experiment |
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NMR details | Text: The protein shows aggregation via the aminoterminal domain, and the resulting line broading of the signals of the aminoterminal domain did not allow a structure determination of the ...Text: The protein shows aggregation via the aminoterminal domain, and the resulting line broading of the signals of the aminoterminal domain did not allow a structure determination of the aminoterminal domain using the full length protein. Becuase of flexible linked domains the carboxyterminal domain showed sufficient signals to determine the structure of this domain using the full length protein. Only the carboxyterminal domain (res. 124-181) gave interpretable NMR data for assignment and structure determination. |
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Sample preparation
Details | Contents: 0.45 mM [U-95% 13C; U-95% 15N] NusG, 10 mM potassium phosphate, 50 mM sodium chloride, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | pH: 6.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: ![]() | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 120 / Conformers submitted total number: 20 |