+Open data
-Basic information
Entry | Database: PDB / ID: 1g1c | ||||||
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Title | I1 DOMAIN FROM TITIN | ||||||
Components | IMMUNOGLOBULIN-LIKE DOMAIN I1 FROM TITIN | ||||||
Keywords | STRUCTURAL PROTEIN / immunoglobulin domain / Beta-sandwhich / I-set | ||||||
Function / homology | Function and homology information sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / cardiac muscle tissue morphogenesis / cardiac muscle hypertrophy / mitotic chromosome condensation ...sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / cardiac muscle tissue morphogenesis / cardiac muscle hypertrophy / mitotic chromosome condensation / Striated Muscle Contraction / actinin binding / M band / I band / protein kinase regulator activity / cardiac muscle cell development / structural constituent of muscle / sarcomere organization / skeletal muscle thin filament assembly / striated muscle thin filament / striated muscle contraction / muscle contraction / cardiac muscle contraction / protein kinase A signaling / condensed nuclear chromosome / positive regulation of protein secretion / Z disc / response to calcium ion / actin filament binding / Platelet degranulation / protease binding / protein tyrosine kinase activity / calmodulin binding / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / protein homodimerization activity / extracellular exosome / extracellular region / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.1 Å | ||||||
Authors | Mayans, O. / Wuerges, J. / Gautel, M. / Wilmanns, M. | ||||||
Citation | Journal: Structure / Year: 2001 Title: Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin. Authors: Mayans, O. / Wuerges, J. / Canela, S. / Gautel, M. / Wilmanns, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g1c.cif.gz | 50.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g1c.ent.gz | 40.2 KB | Display | PDB format |
PDBx/mmJSON format | 1g1c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g1/1g1c ftp://data.pdbj.org/pub/pdb/validation_reports/g1/1g1c | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 11239.681 Da / Num. of mol.: 2 / Fragment: MOST N-TERMINAL IG DOMAIN, RESIDUES 2027-2125 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: HEART / Plasmid: PET8C / Production host: Escherichia coli (E. coli) / References: UniProt: Q10466, UniProt: Q8WZ42*PLUS #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: 2.66 Å3/Da / Density % sol: 53.82 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 3.25 M NaCl, 0.1 M Tris-HCL pH 8.0, 1mM EDTA, 1mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 294K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.906 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.906 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 14589 / % possible obs: 99.6 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.068 / Net I/σ(I): 10.9 |
Reflection shell | Resolution: 2.1→2.15 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.274 / Num. unique all: 966 / % possible all: 99.9 |
Reflection shell | *PLUS % possible obs: 99.9 % / Num. unique obs: 966 / Mean I/σ(I) obs: 2.7 |
-Processing
Software |
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Refinement | Resolution: 2.1→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 5.9 % / Rfactor obs: 0.202 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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