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- PDB-6y96: solution structure of cold-shock domain 9 of drosophila Upstream ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6y96 | ||||||
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Title | solution structure of cold-shock domain 9 of drosophila Upstream of N-Ras (Unr) | ||||||
![]() | Upstream of N-ras, isoform A | ||||||
![]() | RNA BINDING PROTEIN / CSD / RBP | ||||||
Function / homology | ![]() dosage compensation complex assembly / protein-RNA adaptor activity / RISC complex binding / lncRNA binding / negative regulation of translational initiation / mRNA regulatory element binding translation repressor activity / mRNA 3'-UTR binding / RNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Sweetapple, L.J. / Hollmann, N.M. / Simon, B. / Hennig, J. | ||||||
![]() | ![]() Title: Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras. Authors: Hollmann, N.M. / Jagtap, P.K.A. / Masiewicz, P. / Guitart, T. / Simon, B. / Provaznik, J. / Stein, F. / Haberkant, P. / Sweetapple, L.J. / Villacorta, L. / Mooijman, D. / Benes, V. / ...Authors: Hollmann, N.M. / Jagtap, P.K.A. / Masiewicz, P. / Guitart, T. / Simon, B. / Provaznik, J. / Stein, F. / Haberkant, P. / Sweetapple, L.J. / Villacorta, L. / Mooijman, D. / Benes, V. / Savitski, M.M. / Gebauer, F. / Hennig, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 618 KB | Display | ![]() |
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PDB format | ![]() | 529 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 461.8 KB | Display | ![]() |
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Full document | ![]() | 701.4 KB | Display | |
Data in XML | ![]() | 51.6 KB | Display | |
Data in CIF | ![]() | 63.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6y4hC ![]() 6y6eC ![]() 6y6mC 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: 10246.532 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: the first two residues (GA) are leftovers from the cleavage/cloning sequence Source: (gene. exp.) ![]() ![]() Gene: Unr, BcDNA:LD13080, CR32028, Dmel\CG7015, dUNR, MRE30, UNR, unr, CG7015, Dmel_CG7015 Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 50 mM / Label: conditions_1 / pH: 6.8 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |