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- PDB-7r3m: Structure in solution of the TANGO1 cargo-binding domain (21-131) -
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Open data
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Basic information
Entry | Database: PDB / ID: 7r3m | ||||||
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Title | Structure in solution of the TANGO1 cargo-binding domain (21-131) | ||||||
![]() | Transport and Golgi organization protein 1 homolog | ||||||
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Function / homology | ![]() vesicle cargo loading / negative regulation of lymphocyte migration / protein localization to endoplasmic reticulum exit site / cellular response to oxidised low-density lipoprotein particle stimulus / COPII-coated vesicle cargo loading / Cargo concentration in the ER / negative regulation of leukocyte cell-cell adhesion / negative regulation of cell adhesion / endoplasmic reticulum organization / cell migration involved in sprouting angiogenesis ...vesicle cargo loading / negative regulation of lymphocyte migration / protein localization to endoplasmic reticulum exit site / cellular response to oxidised low-density lipoprotein particle stimulus / COPII-coated vesicle cargo loading / Cargo concentration in the ER / negative regulation of leukocyte cell-cell adhesion / negative regulation of cell adhesion / endoplasmic reticulum organization / cell migration involved in sprouting angiogenesis / cargo receptor activity / positive regulation of leukocyte migration / lipoprotein transport / ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Arnolds, O. / Stoll, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Characterization of a fold in TANGO1 evolved from SH3 domains for the export of bulky cargos. Authors: Arnolds, O. / Stoll, 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 | ![]() | 674.9 KB | Display | ![]() |
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PDB format | ![]() | 566.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 12890.382 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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 1 mM [U-100% 13C; U-100% 15N] TANGO1(21-131), 90% H2O/10% D2O Label: TANGO1(21-131) / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: TANGO1(21-131) / Isotopic labeling: [U-100% 13C; U-100% 15N] |
Sample conditions | Details: 25 mM HEPES, 150 mM NaCl, 1% CHAPS (w/v), 10% D2O (v/v), 0.02% (w/v) NaN3, DSS. Ionic strength: 195 mM / Label: TANGO1(21-131) / pH: 7.4 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 2 | |||||||||||||||
NMR representative | Selection criteria: medoid | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 6000 / Conformers submitted total number: 20 |