+Open data
-Basic information
Entry | Database: PDB / ID: 6fia | ||||||
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Title | Structure of the human LINE-1 ORF1p coiled coil domain | ||||||
Components | LINE-1 retrotransposable element ORF1 protein | ||||||
Keywords | RNA BINDING PROTEIN / coiled coil / genome evolution / nucleic acid chaperone / retrotransposition / RNP | ||||||
Function / homology | Function and homology information retrotransposition / cytoplasmic ribonucleoprotein granule / cytoplasmic stress granule / single-stranded DNA binding / single-stranded RNA binding / ribonucleoprotein complex / nucleotide binding / nucleolus / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.65 Å | ||||||
Authors | Khazina, E. / Weichenrieder, O. | ||||||
Citation | Journal: Elife / Year: 2018 Title: Human LINE-1 retrotransposition requires a metastable coiled coil and a positively charged N-terminus in L1ORF1p. Authors: Khazina, E. / Weichenrieder, O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6fia.cif.gz | 257.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6fia.ent.gz | 212.2 KB | Display | PDB format |
PDBx/mmJSON format | 6fia.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fi/6fia ftp://data.pdbj.org/pub/pdb/validation_reports/fi/6fia | HTTPS FTP |
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-Related structure data
Related structure data | 2ykpS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 12597.237 Da / Num. of mol.: 6 / Mutation: M121A, M125I, M128I Source method: isolated from a genetically manipulated source Details: The first four amino acids GPHM remain from the purification tag. Engineered mutations, M121A, M125I, M128I. Source: (gene. exp.) Homo sapiens (human) / Gene: L1RE1, LRE1 / Plasmid: pnEA / Details (production host): pH / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta2 / References: UniProt: Q9UN81 #2: Chemical | ChemComp-CL / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.41 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 0.1M HEPES, 0.15M AMMONIUM SULFATE, 12% PEG 2000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Dec 14, 2013 / Details: dynamically bendable mirrors |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.65→125.31 Å / Num. obs: 23830 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 5.4 % / Biso Wilson estimate: 71.15 Å2 / Rsym value: 0.073 / Net I/σ(I): 14.9 |
Reflection shell | Resolution: 2.65→2.72 Å / Redundancy: 5.5 % / Mean I/σ(I) obs: 2.2 / Num. unique obs: 1688 / Rsym value: 0.813 / % possible all: 98.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2ykp Resolution: 2.65→125.31 Å / Cor.coef. Fo:Fc: 0.9372 / Cor.coef. Fo:Fc free: 0.9248 / SU R Cruickshank DPI: 0.599 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.662 / SU Rfree Blow DPI: 0.286 / SU Rfree Cruickshank DPI: 0.285
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Displacement parameters | Biso mean: 87.23 Å2
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Refine analyze | Luzzati coordinate error obs: 0.374 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 2.65→125.31 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.65→2.77 Å / Total num. of bins used: 12
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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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