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- PDB-1e8s: Alu domain of the mammalian SRP (potential Alu retroposition inte... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1e8s | ||||||
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Title | Alu domain of the mammalian SRP (potential Alu retroposition intermediate) | ||||||
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![]() | ALU RIBONUCLEOPROTEIN PARTICLE / ALU RNP ASSEMBLY AND DIMERISATION / TRANSLATIONAL CONTROL / ALU RETROPOSITION | ||||||
Function / homology | ![]() signal recognition particle receptor complex / signal recognition particle, endoplasmic reticulum targeting / signal recognition particle binding / cotranslational protein targeting to membrane / endoplasmic reticulum signal peptide binding / negative regulation of translational elongation / protein targeting to ER / SRP-dependent cotranslational protein targeting to membrane / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane ...signal recognition particle receptor complex / signal recognition particle, endoplasmic reticulum targeting / signal recognition particle binding / cotranslational protein targeting to membrane / endoplasmic reticulum signal peptide binding / negative regulation of translational elongation / protein targeting to ER / SRP-dependent cotranslational protein targeting to membrane / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane / secretory granule lumen / ficolin-1-rich granule lumen / Neutrophil degranulation / RNA binding / extracellular region / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
Model type details | CA ATOMS ONLY, CHAIN A, B ; P ATOMS ONLY, CHAIN C | ||||||
![]() | Weichenrieder, O. / Wild, K. / Strub, K. / Cusack, S. | ||||||
![]() | ![]() Title: Structure and Assembly of the Alu Domain of the Mammalian Signal Recognition Particle Authors: Weichenrieder, O. / Wild, K. / Strub, K. / Cusack, 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 | ![]() | 22.6 KB | Display | ![]() |
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PDB format | ![]() | 9.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 348 KB | Display | ![]() |
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Full document | ![]() | 348 KB | Display | |
Data in XML | ![]() | 928 B | Display | |
Data in CIF | ![]() | 3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 9996.567 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Protein | Mass: 12114.235 Da / Num. of mol.: 1 / Fragment: TRUNCATED AFTER K107 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
#3: RNA chain | Mass: 28490.900 Da / Num. of mol.: 1 / Fragment: ALU RNA / Mutation: YES / Source method: obtained synthetically Details: THE RNA WAS PRODUCED BY IN VITRO TRANSCRIPTION WITH T7 RNA POLYMERASE USING RIBOZYME TECHNOLOGY. Source: (synth.) ![]() | ||
#4: Chemical | Compound details | SIGNAL-RECOGNITION-PARTICLE ASSEMBLY HAS A CRUCIAL ROLE IN TARGETING SECRETORY PROTEINS TO THE ...SIGNAL-RECOGNITIO | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.06 Å3/Da / Density % sol: 66 % / Description: EUROPIUM L(III) EDGE | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 Details: 50MM HEPES, 10MM MGCL2, 150MM NACL, 0.8 MM EU(NO3)3, 390MM (NH4)2SO4, 23% PEG400, pH 7.00 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 67 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 12 ℃ / Method: vapor diffusion, hanging drop / pH: 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 15, 1999 | |||||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 4→50 Å / Num. obs: 5053 / % possible obs: 90.3 % / Redundancy: 2.9 % / Biso Wilson estimate: 211.4 Å2 / Rsym value: 0.059 / Net I/σ(I): 5.9 | |||||||||||||||
Reflection shell | Resolution: 4→4.1 Å / Redundancy: 1.9 % / Mean I/σ(I) obs: 1.5 / Rsym value: 0.541 / % possible all: 59.6 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 15 Å2 / ksol: 0.25 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 50 Å2
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Refinement step | Cycle: LAST / Resolution: 4→37.46 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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