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- PDB-1uaw: Solution structure of the N-terminal RNA-binding domain of mouse ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1uaw | ||||||
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Title | Solution structure of the N-terminal RNA-binding domain of mouse Musashi1 | ||||||
![]() | mouse-musashi-1 | ||||||
![]() | RNA BINDING PROTEIN / RNP-type structure | ||||||
Function / homology | ![]() poly(U) RNA binding / epithelial cell differentiation / response to hormone / central nervous system development / regulation of translation / single-stranded RNA binding / mRNA binding / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Miyanoiri, Y. / Kobayashi, H. / Watanabe, M. / Ikeda, T. / Nagata, T. / Okano, H. / Uesugi, S. / Katahira, M. | ||||||
![]() | ![]() Title: Origin of higher affinity to RNA of the N-terminal RNA-binding domain than that of the C-terminal one of a mouse neural protein, musashi1, as revealed by comparison of their structures, modes ...Title: Origin of higher affinity to RNA of the N-terminal RNA-binding domain than that of the C-terminal one of a mouse neural protein, musashi1, as revealed by comparison of their structures, modes of interaction, surface electrostatic potentials, and backbone dynamics Authors: Miyanoiri, Y. / Kobayashi, H. / Imai, T. / Watanabe, M. / Nagata, T. / Uesugi, S. / Okano, H. / Katahira, M. #1: ![]() Title: Structure, Backbone Dynamics and Interactions with RNA of the C-terminal RNA-binding Domain of a Mouse Neural RNA-binding Protein, Musashi1. Authors: Nagata, T. / Kanno, R. / Kurihara, Y. / Uesugi, S. / Imai, T. / Sakakibara, S. / Okano, H. / Katahira, M. #2: Journal: Gene / Year: 1997 Title: Structural properties and RNA-binding activities of two RNA recognition motifs of a mouse neural RNA-binding protein, mouse-Musashi-1. Authors: Kurihara, Y. / Nagata, T. / Imai, T. / Hiwatashi, A. / Horiuchi, M. / Sakakibara, S. / Katahira, M. / Okano, H. / Uesugi, S. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR DETERMINED |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 364.2 KB | Display | ![]() |
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PDB format | ![]() | 300.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344.2 KB | Display | ![]() |
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Full document | ![]() | 501.8 KB | Display | |
Data in XML | ![]() | 43.1 KB | Display | |
Data in CIF | ![]() | 61.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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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: 8776.088 Da / Num. of mol.: 1 / Fragment: N-terminal RNA-binding 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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NMR details | Text: The structure was determined using 2D homonuclear and 3D 15N-edited heteronuclear techniques. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 0.0mM / pH: 6.0 / Pressure: 1.0atm / Temperature: 298 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 103 / Conformers submitted total number: 15 |