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Yorodumi- PDB-2dh9: Solution structure of the C-terminal RNA binding domain in Hetero... -
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-Basic information
Entry | Database: PDB / ID: 2dh9 | ||||||
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Title | Solution structure of the C-terminal RNA binding domain in Heterogeneous nuclear ribonucleoprotein M | ||||||
Components | Heterogeneous nuclear ribonucleoprotein M | ||||||
Keywords | RNA BINDING PROTEIN / RRM domain / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information alternative mRNA splicing, via spliceosome / paraspeckles / FGFR2 alternative splicing / Processing of Capped Intron-Containing Pre-mRNA / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / nuclear matrix / collagen-containing extracellular matrix ...alternative mRNA splicing, via spliceosome / paraspeckles / FGFR2 alternative splicing / Processing of Capped Intron-Containing Pre-mRNA / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / nuclear matrix / collagen-containing extracellular matrix / protein domain specific binding / mRNA binding / synapse / nucleolus / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics,restrained molecular dynamics | ||||||
Authors | Ochi, T. / Tsuda, K. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the C-terminal RNA binding domain in Heterogeneous nuclear ribonucleoprotein M Authors: Ochi, T. / Tsuda, K. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2dh9.cif.gz | 524.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2dh9.ent.gz | 440.5 KB | Display | PDB format |
PDBx/mmJSON format | 2dh9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2dh9_validation.pdf.gz | 339.9 KB | Display | wwPDB validaton report |
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Full document | 2dh9_full_validation.pdf.gz | 473.3 KB | Display | |
Data in XML | 2dh9_validation.xml.gz | 31.7 KB | Display | |
Data in CIF | 2dh9_validation.cif.gz | 49.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dh/2dh9 ftp://data.pdbj.org/pub/pdb/validation_reports/dh/2dh9 | HTTPS FTP |
-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: 9779.211 Da / Num. of mol.: 1 / Fragment: RNA recognition motif Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: HNRPM / Plasmid: P050711-05 / Production host: Cell free synthesis / References: UniProt: P52272 |
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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: 100mM / pH: 7 / 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,restrained molecular 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 |