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Open data
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Basic information
Entry | Database: PDB / ID: 1s79 | ||||||
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Title | Solution structure of the central RRM of human La protein | ||||||
![]() | Lupus La protein | ||||||
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Function / homology | ![]() nuclear histone mRNA catabolic process / histone mRNA metabolic process / tRNA 3'-end processing / IRES-dependent viral translational initiation / RNA Polymerase III Transcription Termination / protein localization to cytoplasmic stress granule / 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 / IRES-dependent viral translational initiation / RNA Polymerase III Transcription Termination / protein localization to cytoplasmic stress granule / 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 / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Alfano, C. / Sanfelice, D. / Babon, J. / Kelly, G. / Jacks, A. / Curry, S. / Conte, M.R. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 675.2 KB | Display | ![]() |
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PDB format | ![]() | 585.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 352 KB | Display | ![]() |
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Full document | ![]() | 553.4 KB | Display | |
Data in XML | ![]() | 63.2 KB | Display | |
Data in CIF | ![]() | 79.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1s7aC C: citing same article ( |
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Similar structure data | |
Other databases |
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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 | Mass: 12193.004 Da / Num. of mol.: 1 / Fragment: Central RRM Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||
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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
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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 |