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Yorodumi- PDB-2diw: Solution structure of the RPR domain of Putative RNA-binding prot... -
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-Basic information
Entry | Database: PDB / ID: 2diw | ||||||
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Title | Solution structure of the RPR domain of Putative RNA-binding protein 16 | ||||||
Components | Putative RNA-binding protein 16 | ||||||
Keywords | RNA BINDING PROTEIN / structure genomics / RPR domain / Putative RNA-binding protein 16 / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled / RNA polymerase II C-terminal domain phosphoserine binding / RNA polymerase core enzyme binding / mRNA cleavage factor complex / positive regulation of DNA-templated transcription, elongation / termination of RNA polymerase II transcription / : / RNA polymerase II complex binding / nuclear matrix / mRNA binding ...negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled / RNA polymerase II C-terminal domain phosphoserine binding / RNA polymerase core enzyme binding / mRNA cleavage factor complex / positive regulation of DNA-templated transcription, elongation / termination of RNA polymerase II transcription / : / RNA polymerase II complex binding / nuclear matrix / mRNA binding / RNA binding / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Dang, W. / Muto, Y. / Inoue, M. / Kigawa, T. / Shirouzu, M. / Terada, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the RPR domain of Putative RNA-binding protein 16 Authors: Dang, W. / Muto, Y. / Inoue, M. / Kigawa, T. / Shirouzu, M. / Terada, T. / Yokoyama, S. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2diw.cif.gz | 930.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2diw.ent.gz | 781.1 KB | Display | PDB format |
PDBx/mmJSON format | 2diw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/di/2diw ftp://data.pdbj.org/pub/pdb/validation_reports/di/2diw | 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: 17076.582 Da / Num. of mol.: 1 / Fragment: RPR domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell free protein synthesis / Gene: RBM16; KIAA1116 / Plasmid: P050719-03 / Production host: Cell free synthesis / References: GenBank: 40789049, UniProt: Q9UPN6*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: 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / 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: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function,structures with the lowest energy,structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |