+Open data
-Basic information
Entry | Database: PDB / ID: 1qm9 | ||||||
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Title | NMR, REPRESENTATIVE STRUCTURE | ||||||
Components | POLYPYRIMIDINE TRACT-BINDING PROTEIN | ||||||
Keywords | RIBONUCLEOPROTEIN / POLYPYRIMIDINE TRACT BINDING PROTEIN / RNP / RNA / SPICING / TRANSLATION | ||||||
Function / homology | Function and homology information negative regulation of muscle cell differentiation / poly-pyrimidine tract binding / IRES-dependent viral translational initiation / positive regulation of calcineurin-NFAT signaling cascade / negative regulation of RNA splicing / pre-mRNA binding / FGFR2 alternative splicing / regulation of alternative mRNA splicing, via spliceosome / regulation of cell differentiation / regulation of RNA splicing ...negative regulation of muscle cell differentiation / poly-pyrimidine tract binding / IRES-dependent viral translational initiation / positive regulation of calcineurin-NFAT signaling cascade / negative regulation of RNA splicing / pre-mRNA binding / FGFR2 alternative splicing / regulation of alternative mRNA splicing, via spliceosome / regulation of cell differentiation / regulation of RNA splicing / negative regulation of mRNA splicing, via spliceosome / Processing of Capped Intron-Containing Pre-mRNA / negative regulation of neuron differentiation / positive regulation of protein dephosphorylation / neurogenesis / mRNA Splicing - Major Pathway / RNA splicing / mRNA processing / mRNA binding / nucleolus / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model type details | MINIMIZED AVERAGE | ||||||
Authors | Conte, M.R. / Grune, T. / Curry, S. / Matthews, S. | ||||||
Citation | Journal: Embo J. / Year: 2000 Title: Structure of Tandem RNA Recognition Motifs from Polypyrimidine Tract Binding Protein Reveals Novel Features of the Rrm Fold Authors: Conte, M.R. / Grune, T. / Kelly, G. / Ladas, A. / Matthews, S. / Curry, S. #1: Journal: J.Biomol.NMR / Year: 1999 Title: Resonance Assignment and Topology of a 22kDa C-Terminal Fragment of the Polypyriine Tract Binding Protein Containing Two RNA Binding Domain Authors: Conte, M.R. / Grune, T. / Curry, S. / Matthews, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qm9.cif.gz | 73 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qm9.ent.gz | 55.5 KB | Display | PDB format |
PDBx/mmJSON format | 1qm9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qm/1qm9 ftp://data.pdbj.org/pub/pdb/validation_reports/qm/1qm9 | 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: 22117.322 Da / Num. of mol.: 1 / Fragment: RNA BINDING FRAGMENT Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Cellular location: NUCLEUS/CYTOPLASM / Plasmid: PET-15B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P26599 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: HSQC-NOESY-HSQC |
NMR details | Text: MEAN STRUCTURE. REPRESENTATIVE STRUCTURE. THIS STRUCTURE WAS DETERMINED BY MULTINUCLEAR NMR EXPERIMENTS THE ORIENTATION OF THE TWO RNP DOMAINS (RESIDUES 1-98 AND 120-198 RESPECTIVELY) IS NOT ...Text: MEAN STRUCTURE. REPRESENTATIVE STRUCTURE. THIS STRUCTURE WAS DETERMINED BY MULTINUCLEAR NMR EXPERIMENTS THE ORIENTATION OF THE TWO RNP DOMAINS (RESIDUES 1-98 AND 120-198 RESPECTIVELY) IS NOT DEFINED WITH RESPECT TO EACH OTHER. THIS ENTRY IS REPRESENTATIVE STRUCTURE FROM THE LOWEST ENERGY FAMILY. |
-Sample preparation
Sample conditions | pH: 5.00 / Temperature: 302.00 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 1 |