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- PDB-2yty: Solution structure of the fourth cold-shock domain of the human K... -
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Basic information
Entry | Database: PDB / ID: 2yty | ||||||
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Title | Solution structure of the fourth cold-shock domain of the human KIAA0885 protein (UNR protein) | ||||||
![]() | Cold shock domain-containing protein E1 | ||||||
![]() | RNA BINDING PROTEIN / CELL-FREE PROTEIN SYNTHESIS / BETA-BARREL / TRANSLATIONAL REGULATION / RNA CHAPERONE / RNA/DNA BINDING / QB FOLD / GREEK-KEY TOPOLOGY / UNR PROTEIN / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | ![]() CRD-mediated mRNA stability complex / nuclear-transcribed mRNA catabolic process, no-go decay / mCRD-mediated mRNA stability complex / RISC complex binding / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / IRES-dependent viral translational initiation / positive regulation of cytoplasmic translation / regulation of translational initiation / stress granule assembly ...CRD-mediated mRNA stability complex / nuclear-transcribed mRNA catabolic process, no-go decay / mCRD-mediated mRNA stability complex / RISC complex binding / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / IRES-dependent viral translational initiation / positive regulation of cytoplasmic translation / regulation of translational initiation / stress granule assembly / P-body / cytoplasmic stress granule / RNA stem-loop binding / male gonad development / Golgi apparatus / RNA binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Goroncy, A.K. / Tomizawa, T. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: The NMR solution structures of the five constituent cold-shock domains (CSD) of the human UNR (upstream of N-ras) protein. Authors: Goroncy, A.K. / Koshiba, S. / Tochio, N. / Tomizawa, T. / Inoue, M. / Watanabe, S. / Harada, T. / Tanaka, A. / Ohara, O. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 502.5 KB | Display | ![]() |
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PDB format | ![]() | 428.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 346 KB | Display | ![]() |
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Full document | ![]() | 459.1 KB | Display | |
Data in XML | ![]() | 24.8 KB | Display | |
Data in CIF | ![]() | 39.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1wfqC ![]() 1x65C ![]() 2ytvC ![]() 2ytxC 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: 9422.335 Da / Num. of mol.: 1 / Fragment: FOURTH COLD-SHOCK DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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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: 1.09mM COLD-SHOCK DOMAIN, 20mM PHOSPHATE BUFFER NA, 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: 120 mM / pH: 6.0 / Pressure: AMBIENT / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |