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Yorodumi- PDB-2fho: NMR solution structure of the human spliceosomal protein complex ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 2fho | ||||||
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| Title | NMR solution structure of the human spliceosomal protein complex p14-SF3b155 | ||||||
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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 informationU11/U12 snRNP / B-WICH complex / U12-type spliceosomal complex / RNA splicing, via transesterification reactions / blastocyst formation / splicing factor binding / U2-type precatalytic spliceosome / U2-type spliceosomal complex / U2-type prespliceosome assembly / U2 snRNP ...U11/U12 snRNP / B-WICH complex / U12-type spliceosomal complex / RNA splicing, via transesterification reactions / blastocyst formation / splicing factor binding / U2-type precatalytic spliceosome / U2-type spliceosomal complex / U2-type prespliceosome assembly / U2 snRNP / U2-type prespliceosome / positive regulation of transcription by RNA polymerase III / spliceosomal complex assembly / mRNA Splicing - Minor Pathway / positive regulation of transcription by RNA polymerase I / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / spliceosomal complex / mRNA splicing, via spliceosome / B-WICH complex positively regulates rRNA expression / nuclear speck / chromatin remodeling / mRNA binding / nucleolus / positive regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | SOLUTION NMR / torsion angle dynamics, restrained ENERGY MINIMIZATION | ||||||
Authors | Kuwasako, K. / Dohmae, N. / Inoue, M. / Shirouzu, M. / Guntert, P. / Seraphin, B. / Muto, Y. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be PublishedTitle: NMR solution structure of the human spliceosomal protein complex p14-SF3b155 Authors: Kuwasako, K. / Dohmae, N. / Inoue, M. / Shirouzu, M. / Guntert, P. / Seraphin, B. / Muto, Y. / Yokoyama, S. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2fho.cif.gz | 896.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2fho.ent.gz | 764.1 KB | Display | PDB format |
| PDBx/mmJSON format | 2fho.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2fho_validation.pdf.gz | 366.1 KB | Display | wwPDB validaton report |
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| Full document | 2fho_full_validation.pdf.gz | 547.5 KB | Display | |
| Data in XML | 2fho_validation.xml.gz | 36.4 KB | Display | |
| Data in CIF | 2fho_validation.cif.gz | 65.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fh/2fho ftp://data.pdbj.org/pub/pdb/validation_reports/fh/2fho | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 5502.108 Da / Num. of mol.: 1 / Fragment: residues in database 379-424 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SF3b155 / Plasmid: PGEX6P-1-SF3B155(379-424)-HIS6-P14(8-93) / Production host: ![]() |
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| #2: Protein | Mass: 10148.584 Da / Num. of mol.: 1 / Fragment: RNA recognition motif Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: p14 / Plasmid: PGEX6P-1-SF3B155(379-424)-HIS6-P14(8-93) / Production host: ![]() |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||
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| NMR experiment |
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Sample preparation
| Details | Contents: 20mM Sodium Phosphate buffer (pH 6.5), 100mM NaCl, 1mM d-DTT; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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| Sample conditions | Ionic strength: 100 / pH: 6.5 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
| NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
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| Refinement | Method: torsion angle dynamics, restrained ENERGY MINIMIZATION 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 |
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