+Open data
-Basic information
Entry | Database: PDB / ID: 3u59 | ||||||
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Title | N-terminal 98-aa fragment of smooth muscle tropomyosin beta | ||||||
Components | Tropomyosin beta chain | ||||||
Keywords | CONTRACTILE PROTEIN / Muscle contraction / Actin | ||||||
Function / homology | Function and homology information muscle contraction / actin filament / actin filament organization / actin filament binding / actin cytoskeleton / protein heterodimerization activity / protein homodimerization activity / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.5 Å | ||||||
Authors | Jampani, N. / Dominguez, R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2012 Title: Structural analysis of smooth muscle tropomyosin alpha and beta isoforms. Authors: Rao, J.N. / Rivera-Santiago, R. / Li, X.E. / Lehman, W. / Dominguez, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3u59.cif.gz | 89.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3u59.ent.gz | 71.5 KB | Display | PDB format |
PDBx/mmJSON format | 3u59.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3u59_validation.pdf.gz | 461.9 KB | Display | wwPDB validaton report |
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Full document | 3u59_full_validation.pdf.gz | 484.8 KB | Display | |
Data in XML | 3u59_validation.xml.gz | 19.7 KB | Display | |
Data in CIF | 3u59_validation.cif.gz | 27 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/u5/3u59 ftp://data.pdbj.org/pub/pdb/validation_reports/u5/3u59 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 11571.923 Da / Num. of mol.: 4 / Fragment: unp residues 1-98 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Gene: TPM2 / Plasmid: PRSF-Duet-1 / Production host: Escherichia coli (E. coli) / References: UniProt: P19352 #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: 2.43 Å3/Da / Density % sol: 49.32 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 0.1 M HEPES, 5 mM CaCl2, 28-31 % 2- methyl-2,4-pentanediol, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 7.4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 0.9789 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 25, 2011 |
Radiation | Monochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9789 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→29 Å / Num. all: 20821 / Num. obs: 20734 / % possible obs: 99.6 % / Redundancy: 7.2 % / Rmerge(I) obs: 0.0706 / Net I/σ(I): 15.82 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 7.63 % / Rmerge(I) obs: 0.5048 / Mean I/σ(I) obs: 2.98 / Num. unique all: 2445 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.5→29 Å / Cor.coef. Fo:Fc: 0.894 / Cor.coef. Fo:Fc free: 0.876 / SU B: 13.696 / SU ML: 0.303 / Cross valid method: THROUGHOUT / ESU R Free: 4.699 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 61.004 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→29 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.565 Å / Total num. of bins used: 20
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