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Yorodumi- PDB-2k7a: Ensemble Structures of the binary complex between the SH3 and SH2... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2k7a | ||||||
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Title | Ensemble Structures of the binary complex between the SH3 and SH2 domain of interleukin-2 tyrosine kinase. | ||||||
Components |
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Keywords | TRANSFERASE / SH3 / SH2 / novel / cis / ATP-binding / Cell membrane / Kinase / Membrane / Metal-binding / Nucleotide-binding / Phosphoprotein / SH2 domain / SH3 domain / Tyrosine-protein kinase / Zinc / Zinc-finger | ||||||
Function / homology | Function and homology information Generation of second messenger molecules / FCERI mediated Ca+2 mobilization / NK T cell differentiation / gamma-delta T cell activation / positive regulation of cytokine production / non-specific protein-tyrosine kinase / B cell receptor signaling pathway / non-membrane spanning protein tyrosine kinase activity / cell-cell junction / T cell receptor signaling pathway ...Generation of second messenger molecules / FCERI mediated Ca+2 mobilization / NK T cell differentiation / gamma-delta T cell activation / positive regulation of cytokine production / non-specific protein-tyrosine kinase / B cell receptor signaling pathway / non-membrane spanning protein tyrosine kinase activity / cell-cell junction / T cell receptor signaling pathway / adaptive immune response / intracellular signal transduction / protein phosphorylation / ATP binding / nucleus / metal ion binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Andreotti, A.H. / Severin, A.J. / Fulton, D.B. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2009 Title: Proline isomerization preorganizes the Itk SH2 domain for binding to the Itk SH3 domain. Authors: Severin, A. / Joseph, R.E. / Boyken, S. / Fulton, D.B. / Andreotti, A.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k7a.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2k7a.ent.gz | 908.6 KB | Display | PDB format |
PDBx/mmJSON format | 2k7a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2k7a_validation.pdf.gz | 354.1 KB | Display | wwPDB validaton report |
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Full document | 2k7a_full_validation.pdf.gz | 657.2 KB | Display | |
Data in XML | 2k7a_validation.xml.gz | 89.7 KB | Display | |
Data in CIF | 2k7a_validation.cif.gz | 117 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k7/2k7a ftp://data.pdbj.org/pub/pdb/validation_reports/k7/2k7a | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7355.936 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Itk, Emt, Tlk, Tsk / Production host: Escherichia coli (E. coli) References: UniProt: Q03526, non-specific protein-tyrosine kinase |
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#2: Protein | Mass: 12678.335 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Itk, Emt, Tlk, Tsk / Production host: Escherichia coli (E. coli) References: UniProt: Q03526, non-specific protein-tyrosine kinase |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 75 / pH: 7.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avii / Manufacturer: Bruker / Model: Avii / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 / Details: refine.py script from xplor-nih 2.19 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 60 / Conformers submitted total number: 20 / Representative conformer: 1 |