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Yorodumi- PDB-1ri9: Structure of a helically extended SH3 domain of the T cell adapte... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ri9 | ||||||
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Title | Structure of a helically extended SH3 domain of the T cell adapter protein ADAP | ||||||
Components | FYN-binding protein | ||||||
Keywords | SIGNALING PROTEIN / SH3-LIKE / HELICALLY EXTENDED | ||||||
Function / homology | Function and homology information anchoring junction / Signal regulatory protein family interactions / Generation of second messenger molecules / protein localization to plasma membrane / integrin-mediated signaling pathway / actin cytoskeleton / T cell receptor signaling pathway / immune response / signaling receptor binding / lipid binding ...anchoring junction / Signal regulatory protein family interactions / Generation of second messenger molecules / protein localization to plasma membrane / integrin-mediated signaling pathway / actin cytoskeleton / T cell receptor signaling pathway / immune response / signaling receptor binding / lipid binding / protein-containing complex binding / protein-containing complex / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Heuer, K. / Kofler, M. / Langdon, G. / Thiemke, K. / Freund, C. | ||||||
Citation | Journal: STRUCTURE / Year: 2004 Title: Structure of a Helically Extended SH3 Domain of the T Cell Adapter Protein ADAP. Authors: Heuer, K. / Kofler, M. / Langdon, G. / Thiemke, K. / Freund, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ri9.cif.gz | 497.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ri9.ent.gz | 413 KB | Display | PDB format |
PDBx/mmJSON format | 1ri9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ri9_validation.pdf.gz | 478.6 KB | Display | wwPDB validaton report |
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Full document | 1ri9_full_validation.pdf.gz | 842.4 KB | Display | |
Data in XML | 1ri9_validation.xml.gz | 83.5 KB | Display | |
Data in CIF | 1ri9_validation.cif.gz | 103.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ri/1ri9 ftp://data.pdbj.org/pub/pdb/validation_reports/ri/1ri9 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11901.391 Da / Num. of mol.: 1 / Fragment: RESIDUES 683-771 OF ADAP PROTEIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FYB, SLAP130 / Plasmid: pTFT74 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: O15117 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear and 3D heteronuclear techniques. |
-Sample preparation
Details | Contents: 1.8mM ADAP-hSH3 domain "[U-95% 13C; U-90% 15N]" / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0.05 / pH: 6.3 / Pressure: ambient / Temperature: 300 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: the structures are based on a total of 1136 restraints, 718 are NOE-derived distance constraints, 388 dihedral angle restraints,30 distance restraints from hydrogen bonds. | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations,lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: The submitted conformer models are the 20 structures with the lowest energy. Conformers calculated total number: 51 / Conformers submitted total number: 20 |