[English] 日本語
Yorodumi- PDB-2fho: NMR solution structure of the human spliceosomal protein complex ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fho | ||||||
---|---|---|---|---|---|---|---|
Title | NMR solution structure of the human spliceosomal protein complex p14-SF3b155 | ||||||
Components |
| ||||||
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 U11/U12 snRNP / B-WICH complex / splicing factor binding / U12-type spliceosomal complex / RNA splicing, via transesterification reactions / blastocyst formation / U2-type spliceosomal complex / U2-type precatalytic spliceosome / : / U2-type prespliceosome assembly ...U11/U12 snRNP / B-WICH complex / splicing factor binding / U12-type spliceosomal complex / RNA splicing, via transesterification reactions / blastocyst formation / U2-type spliceosomal complex / U2-type precatalytic spliceosome / : / U2-type prespliceosome assembly / U2 snRNP / positive regulation of transcription by RNA polymerase III / U2-type prespliceosome / precatalytic spliceosome / spliceosomal complex assembly / positive regulation of transcription by RNA polymerase I / mRNA Splicing - Minor Pathway / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / spliceosomal complex / B-WICH complex positively regulates rRNA expression / mRNA splicing, via spliceosome / 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 Published Title: 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. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2fho.cif.gz | 892.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2fho.ent.gz | 783 KB | Display | PDB format |
PDBx/mmJSON format | 2fho.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
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 |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-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: Escherichia coli (E. coli) / References: UniProt: O75533 |
---|---|
#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: Escherichia coli (E. coli) / References: UniProt: Q9Y3B4 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-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 |
---|---|
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 |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |