+Open data
-Basic information
Entry | Database: PDB / ID: 1waa | ||||||
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Title | IG27 protein domain | ||||||
Components | (TITIN) x 3 | ||||||
Keywords | METAL BINDING PROTEIN / CALMODULIN-BINDING / CYTOSKELETON / IMMUNOGLOBULIN DOMAIN / MUSCLE PROTEIN / PHOSPHORYLATION / SERINE/THREONINE- PROTEIN KINASE / STRUCTURAL PROTEIN. | ||||||
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 / condensed nuclear chromosome / striated muscle contraction / muscle contraction / cardiac muscle contraction / protein kinase A signaling / positive regulation of protein secretion / response to calcium ion / Z disc / actin filament binding / Platelet degranulation / protein tyrosine kinase activity / protease binding / 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 / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Vega, M.C. / Valencia, L. / Zou, P. / Wilmanns, M. | ||||||
Citation | Journal: Plos Comput.Biol. / Year: 2009 Title: Mechanical Network in Titin Immunoglobulin from Force Distribution Analysis. Authors: Stacklies, W. / Vega, M.C. / Wilmanns, M. / Grater, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1waa.cif.gz | 134.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1waa.ent.gz | 105.2 KB | Display | PDB format |
PDBx/mmJSON format | 1waa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1waa_validation.pdf.gz | 402.5 KB | Display | wwPDB validaton report |
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Full document | 1waa_full_validation.pdf.gz | 418.5 KB | Display | |
Data in XML | 1waa_validation.xml.gz | 13.5 KB | Display | |
Data in CIF | 1waa_validation.cif.gz | 23.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wa/1waa ftp://data.pdbj.org/pub/pdb/validation_reports/wa/1waa | HTTPS FTP |
-Related structure data
Related structure data | 1titS 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: 10124.597 Da / Num. of mol.: 4 / Fragment: IG DOMAIN, RESIDUES 12801-12889 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: MUSCLE / Organ: HEART / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: Q8WZ42, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor #2: Protein | | Mass: 10138.623 Da / Num. of mol.: 1 / Fragment: IG DOMAIN, RESIDUES 12801-12889 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: MUSCLE / Organ: HEART / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: Q8WZ42, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor #3: Protein | | Mass: 10138.622 Da / Num. of mol.: 1 / Fragment: IG DOMAIN, RESIDUES 12801-12889 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: MUSCLE / Organ: HEART / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: Q8WZ42, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor #4: Chemical | ChemComp-ZN / #5: Water | ChemComp-HOH / | Compound details | FUNCTION: THIS MUSCLE PROTEIN MAY BE INVOLVED IN MUSCLE ASSEMBLY AND MAINTAINING THE STRUCTURAL ...FUNCTION: THIS MUSCLE PROTEIN MAY BE INVOLVED IN MUSCLE ASSEMBLY AND MAINTAININ | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.9 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.84 |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.84 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. obs: 53298 / % possible obs: 89.2 % / Observed criterion σ(I): 0 / Redundancy: 5.5 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 11.3 |
Reflection shell | Resolution: 1.8→2 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 5.4 / % possible all: 92.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1TIT Resolution: 1.8→15 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.904 / SU B: 13.244 / SU ML: 0.16 / Cross valid method: THROUGHOUT / ESU R: 0.159 / ESU R Free: 0.162 / 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: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.07 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→15 Å
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Refine LS restraints |
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