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- PDB-1wfq: Solution structure of the first cold-shock domain of the human KI... -
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Basic information
Entry | Database: PDB / ID: 1wfq | ||||||
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Title | Solution structure of the first cold-shock domain of the human KIAA0885 protein (UNR protein) | ||||||
![]() | UNR protein | ||||||
![]() | RNA BINDING PROTEIN / Beta-barrel / translational regulation / RNA chaperone / RNA/DNA binding / QB fold / Greek-key topology / unr protein / structural genomics / 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. / Kigawa, T. / Koshiba, S. / Tomizawa, T. / Kobayashi, N. / Tochio, N. / Inoue, M. / 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 | ![]() | 508.2 KB | Display | ![]() |
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PDB format | ![]() | 428 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 341.8 KB | Display | ![]() |
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Full document | ![]() | 469.7 KB | Display | |
Data in XML | ![]() | 31.5 KB | Display | |
Data in CIF | ![]() | 49.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1x65C ![]() 2ytvC ![]() 2ytxC ![]() 2ytyC 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: 9469.500 Da / Num. of mol.: 1 / Fragment: First 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 U-15N, 13C; 20mM phosphate buffer Na; 100mM NaCl; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest target function | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |