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- PDB-3u1c: Anti-parallel dimer of N-terminal 98-aa fragment of smooth muscle... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3u1c | ||||||
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Title | Anti-parallel dimer of N-terminal 98-aa fragment of smooth muscle tropomyosin alpha | ||||||
![]() | Tropomyosin alpha-1 chain | ||||||
![]() | CONTRACTILE PROTEIN / Anti-parallel coiled coil | ||||||
Function / homology | ![]() Smooth Muscle Contraction / Striated Muscle Contraction / cardiac muscle contraction / cytoskeletal protein binding / actin filament / actin filament organization / actin filament binding / actin cytoskeleton / protein heterodimerization activity / protein homodimerization activity ...Smooth Muscle Contraction / Striated Muscle Contraction / cardiac muscle contraction / cytoskeletal protein binding / actin filament / actin filament organization / actin filament binding / actin cytoskeleton / protein heterodimerization activity / protein homodimerization activity / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Jampani, N. / Dominguez, R. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 96.7 KB | Display | ![]() |
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PDB format | ![]() | 76.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.9 KB | Display | ![]() |
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Full document | ![]() | 443.6 KB | Display | |
Data in XML | ![]() | 12 KB | Display | |
Data in CIF | ![]() | 16.4 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 11595.910 Da / Num. of mol.: 2 / Fragment: unp residues 1-98 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 51.26 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4 Details: 0.1 M Sodium acetate, pH 4.0, 40 mM Calcium chloride, 32-35 % 2-METHYL-2,4-PENTANEDIOL, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.75→25 Å / Num. all: 24608 / Num. obs: 23590 / % possible obs: 95.9 % / Redundancy: 17.76 % / Rmerge(I) obs: 0.0757 / Net I/σ(I): 24.9 | ||||||||||||||||||
Reflection shell | Resolution: 1.75→1.85 Å / Redundancy: 12.69 % / Rmerge(I) obs: 0.4364 / Mean I/σ(I) obs: 4.59 / Num. unique all: 3675 / % possible all: 94.8 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.72 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 54.254 Å2 / ksol: 0.378 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.8→25 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION
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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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