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Yorodumi- PDB-1tnm: TERTIARY STRUCTURE OF AN IMMUNOGLOBULIN-LIKE DOMAIN FROM THE GIAN... -
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-Basic information
Entry | Database: PDB / ID: 1tnm | ||||||
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Title | TERTIARY STRUCTURE OF AN IMMUNOGLOBULIN-LIKE DOMAIN FROM THE GIANT MUSCLE PROTEIN TITIN: A NEW MEMBER OF THE I SET | ||||||
Components | TITIN MODULE M5 | ||||||
Keywords | MUSCLE 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 / protein kinase regulator activity / cardiac muscle hypertrophy ...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 / protein kinase regulator activity / cardiac muscle hypertrophy / mitotic chromosome condensation / actinin binding / Striated Muscle Contraction / M band / I band / cardiac muscle cell development / structural constituent of muscle / sarcomere organization / skeletal muscle thin filament assembly / striated muscle thin filament / cardiac muscle contraction / striated muscle contraction / 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 | SOLUTION NMR | ||||||
Authors | Pfuhl, M. / Pastore, A. | ||||||
Citation | Journal: Structure / Year: 1995 Title: Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: a new member of the I set. Authors: Pfuhl, M. / Pastore, A. #1: Journal: To be Published Title: Secondary Structure Determination by NMR Spectroscopy of an Immunoglobulin-Like Domain from the Giant Muscle Protein Titin Authors: Pfuhl, M. / Gautel, M. / Politou, A. / Joseph, C. / Pastore, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tnm.cif.gz | 43 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tnm.ent.gz | 30.8 KB | Display | PDB format |
PDBx/mmJSON format | 1tnm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tnm_validation.pdf.gz | 335.2 KB | Display | wwPDB validaton report |
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Full document | 1tnm_full_validation.pdf.gz | 344.1 KB | Display | |
Data in XML | 1tnm_validation.xml.gz | 4.5 KB | Display | |
Data in CIF | 1tnm_validation.cif.gz | 5.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tn/1tnm ftp://data.pdbj.org/pub/pdb/validation_reports/tn/1tnm | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Atom site foot note | 1: CIS PROLINE - PRO 27 | |||||||||
NMR ensembles |
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-Components
#1: Protein | Mass: 11295.468 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: BL21 / Gene: TTN / Organ: CARDIAC MUSCLE / Plasmid: PET8C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 PLYS / References: UniProt: Q8WZ42 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software |
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NMR ensemble | Conformers submitted total number: 1 |