+Open data
-Basic information
Entry | Database: PDB / ID: 1s79 | ||||||
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Title | Solution structure of the central RRM of human La protein | ||||||
Components | Lupus La protein | ||||||
Keywords | RNA BINDING PROTEIN / TRANSLATION / RRM / alpha/beta | ||||||
Function / homology | Function and homology information nuclear histone mRNA catabolic process / histone mRNA metabolic process / tRNA 3'-end processing / protein localization to cytoplasmic stress granule / RNA Polymerase III Transcription Termination / IRES-dependent viral translational initiation / tRNA export from nucleus / tRNA modification / RNA Polymerase III Abortive And Retractive Initiation / tRNA 5'-leader removal ...nuclear histone mRNA catabolic process / histone mRNA metabolic process / tRNA 3'-end processing / protein localization to cytoplasmic stress granule / RNA Polymerase III Transcription Termination / IRES-dependent viral translational initiation / tRNA export from nucleus / tRNA modification / RNA Polymerase III Abortive And Retractive Initiation / tRNA 5'-leader removal / sequence-specific mRNA binding / poly(U) RNA binding / tRNA processing / positive regulation of translation / cytoplasmic stress granule / chromosome, telomeric region / tRNA binding / ribonucleoprotein complex / mRNA binding / RNA binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Alfano, C. / Sanfelice, D. / Babon, J. / Kelly, G. / Jacks, A. / Curry, S. / Conte, M.R. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2004 Title: Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein. Authors: Alfano, C. / Sanfelice, D. / Babon, J. / Kelly, G. / Jacks, A. / Curry, S. / Conte, M.R. #1: Journal: J.Biomol.NMR / Year: 2003 Title: Resonance assignment and secondary structure of an N-terminal fragment of the human La protein Authors: Alfano, C. / Babon, J. / Kelly, G. / Curry, S. / Conte, M.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1s79.cif.gz | 679.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1s79.ent.gz | 568.2 KB | Display | PDB format |
PDBx/mmJSON format | 1s79.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1s79_validation.pdf.gz | 352 KB | Display | wwPDB validaton report |
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Full document | 1s79_full_validation.pdf.gz | 553.4 KB | Display | |
Data in XML | 1s79_validation.xml.gz | 63.2 KB | Display | |
Data in CIF | 1s79_validation.cif.gz | 79.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s7/1s79 ftp://data.pdbj.org/pub/pdb/validation_reports/s7/1s79 | HTTPS FTP |
-Related structure data
Related structure data | 1s7aC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12193.004 Da / Num. of mol.: 1 / Fragment: Central RRM Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SSB / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)PlysS / References: UniProt: P05455 |
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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: 0.4 mM RRM U-15N,13C; 20mM phosphate buffer, 100mM KCl, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 100 mM KCl / pH: 6 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |