+Open data
-Basic information
Entry | Database: PDB / ID: 3ui2 | ||||||
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Title | Crystal structure of the cpSRP54 tail bound to cpSRP43 | ||||||
Components |
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Keywords | TRANSPORT PROTEIN / ankyrin repeat / chromodomain / aromatic cage / signal recognition particle / protein targeting / membrane protein chaperone / chloroplast | ||||||
Function / homology | Function and homology information protein import into chloroplast thylakoid membrane / protein heterotrimerization / response to high light intensity / signal recognition particle, endoplasmic reticulum targeting / endoplasmic reticulum signal peptide binding / signal-recognition-particle GTPase / 7S RNA binding / chloroplast envelope / SRP-dependent cotranslational protein targeting to membrane, translocation / chloroplast stroma ...protein import into chloroplast thylakoid membrane / protein heterotrimerization / response to high light intensity / signal recognition particle, endoplasmic reticulum targeting / endoplasmic reticulum signal peptide binding / signal-recognition-particle GTPase / 7S RNA binding / chloroplast envelope / SRP-dependent cotranslational protein targeting to membrane, translocation / chloroplast stroma / chloroplast thylakoid membrane / chloroplast / disordered domain specific binding / protein-macromolecule adaptor activity / protein domain specific binding / GTPase activity / GTP binding / ATP hydrolysis activity / protein-containing complex / identical protein binding / metal ion binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.178 Å | ||||||
Authors | Holdermann, I. / Wild, K. / Sinning, I. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2012 Title: Chromodomains read the arginine code of post-translational targeting. Authors: Holdermann, I. / Meyer, N.H. / Round, A. / Wild, K. / Sattler, M. / Sinning, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ui2.cif.gz | 109.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ui2.ent.gz | 86.4 KB | Display | PDB format |
PDBx/mmJSON format | 3ui2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3ui2_validation.pdf.gz | 422 KB | Display | wwPDB validaton report |
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Full document | 3ui2_full_validation.pdf.gz | 429.7 KB | Display | |
Data in XML | 3ui2_validation.xml.gz | 11.7 KB | Display | |
Data in CIF | 3ui2_validation.cif.gz | 14.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ui/3ui2 ftp://data.pdbj.org/pub/pdb/validation_reports/ui/3ui2 | HTTPS FTP |
-Related structure data
Related structure data | 3deoS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | the biological unit corresponds to the asymmetric unit |
-Components
#1: Protein | Mass: 26838.002 Da / Num. of mol.: 1 / Fragment: UNP residues 84-327 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At2g47450, CAO, CPSRP43, T30B22.25 / Plasmid: pET24 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta2(DE3)pLysS / References: UniProt: O22265 |
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#2: Protein/peptide | Mass: 1499.806 Da / Num. of mol.: 1 / Fragment: RRKR motif, UNP residues 528-540 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At5g03940, CPSRP54, F8F6_150, FFC / Plasmid: pETtrx / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta2(DE3)pLysS / References: UniProt: P37107 |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.74 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.1 M BisTris, 25% (w/v) PEG 3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 21, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 3.178→57.831 Å / Num. all: 5401 / Num. obs: 5382 / % possible obs: 99.7 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.068 / Net I/σ(I): 14.1 |
Reflection shell | Resolution: 3.178→3.35 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.434 / Mean I/σ(I) obs: 2.2 / Num. unique all: 753 / % possible all: 98.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3DEO Resolution: 3.178→57.831 Å / SU ML: 0.42 / σ(F): 1.37 / Phase error: 32.9 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 57.469 Å2 / ksol: 0.309 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3.178→57.831 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Num. reflection Rfree: 123
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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