+Open data
-Basic information
Entry | Database: PDB / ID: 2jx2 | ||||||
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Title | Solution conformation of RNA-bound NELF-E RRM | ||||||
Components | Negative elongation factor E | ||||||
Keywords | TRANSCRIPTION / nelfe-rrm / Coiled coil / Nucleus / Phosphorylation / Repressor / RNA-binding / Transcription regulation / Ubl conjugation | ||||||
Function / homology | Function and homology information NELF complex / positive regulation of protein modification process / Abortive elongation of HIV-1 transcript in the absence of Tat / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / negative regulation of transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation ...NELF complex / positive regulation of protein modification process / Abortive elongation of HIV-1 transcript in the absence of Tat / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / negative regulation of transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / localization / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / positive regulation of ERK1 and ERK2 cascade / nuclear body / mRNA binding / chromatin binding / chromatin / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Jampani, N. / Schweimer, K. / Wenzel, S. / Woehrl, B.M. / Roesch, P. | ||||||
Citation | Journal: Biochemistry / Year: 2008 Title: NELF-E RRM Undergoes Major Structural Changes in Flexible Protein Regions on Target RNA Binding Authors: Rao, J.N. / Schweimer, K. / Wenzel, S. / Wohrl, B.M. / Rosch, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jx2.cif.gz | 516.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jx2.ent.gz | 436.8 KB | Display | PDB format |
PDBx/mmJSON format | 2jx2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jx/2jx2 ftp://data.pdbj.org/pub/pdb/validation_reports/jx/2jx2 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13384.088 Da / Num. of mol.: 1 / Fragment: RRM domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RDBP, NELFE, RD / Production host: Escherichia coli (E. coli) / References: UniProt: P18615 |
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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: 0.4 mM [U-98% 13C; U-98% 15N] rna bound nelfe-rrm, 0.8 mM TAR(49-57), 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | pH: 6.9 / Pressure: ambient / Temperature: 298 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 / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 160 / Conformers submitted total number: 20 |