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- PDB-1tnn: Tertiary structure of an immunoglobulin-like domain from the gian... -
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Basic information
Entry | Database: PDB / ID: 1tnn | ||||||
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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 | ||||||
![]() | TITIN MODULE M5 | ||||||
![]() | MUSCLE PROTEIN | ||||||
Function / homology | ![]() 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 / regulation of catalytic 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 / regulation of catalytic activity / cardiac muscle hypertrophy / mitotic chromosome condensation / Striated Muscle Contraction / actinin binding / M band / I band / cardiac muscle cell development / regulation of protein kinase activity / structural constituent of muscle / sarcomere organization / skeletal muscle thin filament assembly / striated muscle thin filament / striated muscle contraction / cardiac muscle contraction / protein kinase A signaling / condensed nuclear chromosome / muscle contraction / positive regulation of protein secretion / Z disc / response to calcium ion / : / actin filament binding / Platelet degranulation / protein tyrosine kinase activity / protease binding / non-specific serine/threonine protein kinase / calmodulin binding / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / extracellular exosome / extracellular region / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Pfuhl, M. / Pastore, A. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 446.3 KB | Display | ![]() |
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PDB format | ![]() | 368.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 355.3 KB | Display | ![]() |
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Full document | ![]() | 527 KB | Display | |
Data in XML | ![]() | 43.7 KB | Display | |
Data in CIF | ![]() | 63.1 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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Atom site foot note | 1: CIS PROLINE - PRO 27 MODEL 1 / 2: CIS PROLINE - PRO 27 MODEL 2 / 3: CIS PROLINE - PRO 27 MODEL 3 / 4: CIS PROLINE - PRO 27 MODEL 4 / 5: CIS PROLINE - PRO 27 MODEL 5 / 6: CIS PROLINE - PRO 27 MODEL 6 / 7: CIS PROLINE - PRO 27 MODEL 7 / 8: CIS PROLINE - PRO 27 MODEL 8 / 9: CIS PROLINE - PRO 27 MODEL 9 / 10: CIS PROLINE - PRO 27 MODEL 10 / 11: CIS PROLINE - PRO 27 MODEL 11 / 12: CIS PROLINE - PRO 27 MODEL 12 / 13: CIS PROLINE - PRO 27 MODEL 13 / 14: CIS PROLINE - PRO 27 MODEL 14 / 15: CIS PROLINE - PRO 27 MODEL 15 / 16: CIS PROLINE - PRO 27 MODEL 16 | |||||||||
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.) ![]() ![]() ![]() |
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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
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NMR software |
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NMR ensemble | Conformers submitted total number: 16 |