+Open data
-Basic information
Entry | Database: PDB / ID: 1t2l | ||||||
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Title | Three Crystal Structures of Human Coactosin-like Protein | ||||||
Components | Coactosin-like protein | ||||||
Keywords | PROTEIN BINDING / beta-sheet | ||||||
Function / homology | Function and homology information site of polarized growth / regulation of actin filament polymerization / cortical actin cytoskeleton / defense response to fungus / actin filament / actin filament binding / actin binding / secretory granule lumen / ficolin-1-rich granule lumen / Neutrophil degranulation ...site of polarized growth / regulation of actin filament polymerization / cortical actin cytoskeleton / defense response to fungus / actin filament / actin filament binding / actin binding / secretory granule lumen / ficolin-1-rich granule lumen / Neutrophil degranulation / enzyme binding / extracellular exosome / extracellular region / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.8 Å | ||||||
Authors | Liu, L. / Wei, Z. / Chen, Z. / Wang, Y. / Gong, W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2004 Title: Crystal Structure of Human Coactosin-like Protein Authors: Liu, L. / Wei, Z. / Wang, Y. / Wan, M. / Cheng, Z. / Gong, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t2l.cif.gz | 58.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t2l.ent.gz | 46.5 KB | Display | PDB format |
PDBx/mmJSON format | 1t2l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1t2l_validation.pdf.gz | 433.2 KB | Display | wwPDB validaton report |
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Full document | 1t2l_full_validation.pdf.gz | 438.4 KB | Display | |
Data in XML | 1t2l_validation.xml.gz | 12.4 KB | Display | |
Data in CIF | 1t2l_validation.cif.gz | 15.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t2/1t2l ftp://data.pdbj.org/pub/pdb/validation_reports/t2/1t2l | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 15881.661 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Strain: B834(DE3) / Plasmid: pET22b(+) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q14019 #2: 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: 2.3 Å3/Da / Density % sol: 46.1 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 30% PEG400, 0.1M hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: BSRF / Beamline: 3W1A / Wavelength: 0.9813, 0.9816, 0.9 | ||||||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 12, 2004 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.8→50 Å / Num. obs: 6039 / Observed criterion σ(I): 3 / Biso Wilson estimate: 102.8 Å2 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.8→50 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 40.2211 Å2 / ksol: 0.349426 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→50 Å
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Refine LS restraints |
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