+Open data
-Basic information
Entry | Database: PDB / ID: 1wf2 | ||||||
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Title | Solution structure of RRM domain in HNRPC protein | ||||||
Components | Heterogeneous nuclear ribonucleoproteins C1/C2 | ||||||
Keywords | RNA BINDING PROTEIN / structural genomics / RRM domain / HNRPC protein / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information N6-methyladenosine-containing RNA reader activity / telomerase holoenzyme complex / SUMOylation of RNA binding proteins / telomerase RNA binding / poly(U) RNA binding / RHOBTB1 GTPase cycle / 3'-UTR-mediated mRNA stabilization / Processing of Capped Intron-Containing Pre-mRNA / negative regulation of telomere maintenance via telomerase / nucleosomal DNA binding ...N6-methyladenosine-containing RNA reader activity / telomerase holoenzyme complex / SUMOylation of RNA binding proteins / telomerase RNA binding / poly(U) RNA binding / RHOBTB1 GTPase cycle / 3'-UTR-mediated mRNA stabilization / Processing of Capped Intron-Containing Pre-mRNA / negative regulation of telomere maintenance via telomerase / nucleosomal DNA binding / RHOBTB2 GTPase cycle / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / mRNA 3'-UTR binding / spliceosomal complex / mRNA splicing, via spliceosome / osteoblast differentiation / actin cytoskeleton / chromatin remodeling / chromatin / protein-containing complex / RNA binding / extracellular exosome / extracellular region / nucleoplasm / membrane / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | He, F. / 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 RRM domain in HNRPC protein Authors: He, F. / Muto, Y. / Inoue, M. / Kigawa, T. / Shirouzu, M. / Terada, T. / Yokoyama, S. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wf2.cif.gz | 560.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wf2.ent.gz | 469.8 KB | Display | PDB format |
PDBx/mmJSON format | 1wf2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wf/1wf2 ftp://data.pdbj.org/pub/pdb/validation_reports/wf/1wf2 | 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: 10287.608 Da / Num. of mol.: 1 / Fragment: RRM domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell free protein synthesis / Gene: adKA0528 / Plasmid: P040301-06 / References: UniProt: P07910 |
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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: 0.8mM U-15,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 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
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-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: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |