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Yorodumi- PDB-2eap: Solution structure of the N-terminal SAM-domain of human lymphocy... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2eap | ||||||
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Title | Solution structure of the N-terminal SAM-domain of human lymphocyte cytosolic protein 2 | ||||||
Components | Lymphocyte cytosolic protein 2 | ||||||
Keywords | SIGNALING PROTEIN / CELL-FREE PROTEIN SYNTHESIS / PROTEIN REGULATION / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information TCR signalosome / mast cell activation / plasma membrane raft / Generation of second messenger molecules / positive regulation of protein kinase activity / GPVI-mediated activation cascade / cell surface receptor protein tyrosine kinase signaling pathway / FCERI mediated Ca+2 mobilization / FCERI mediated MAPK activation / cell-cell junction ...TCR signalosome / mast cell activation / plasma membrane raft / Generation of second messenger molecules / positive regulation of protein kinase activity / GPVI-mediated activation cascade / cell surface receptor protein tyrosine kinase signaling pathway / FCERI mediated Ca+2 mobilization / FCERI mediated MAPK activation / cell-cell junction / DAP12 signaling / T cell receptor signaling pathway / intracellular signal transduction / immune response / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Goroncy, A.K. / Sato, M. / Tochio, N. / Koshiba, S. / Watanabe, S. / Harada, T. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the N-terminal SAM-domain of human lymphocyte cytosolic protein 2 Authors: Goroncy, A.K. / Sato, M. / Tochio, N. / Koshiba, S. / Watanabe, S. / Harada, T. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2eap.cif.gz | 571.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2eap.ent.gz | 477.6 KB | Display | PDB format |
PDBx/mmJSON format | 2eap.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2eap_validation.pdf.gz | 345 KB | Display | wwPDB validaton report |
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Full document | 2eap_full_validation.pdf.gz | 474.6 KB | Display | |
Data in XML | 2eap_validation.xml.gz | 26.4 KB | Display | |
Data in CIF | 2eap_validation.cif.gz | 42.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ea/2eap ftp://data.pdbj.org/pub/pdb/validation_reports/ea/2eap | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10367.814 Da / Num. of mol.: 1 / Fragment: N-terminal SAM domain, residues 8-90 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: CELL-FREE PROTEIN SYNTHESIS / Gene: LCP2 / Plasmid: P060327-18 / References: UniProt: Q13094 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.16mM SAM DOMAIN; 20mM d-TRIS-HCL; 100mM NaCl; 1mM d-DTT; 0.02 % NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: AMBIENT / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |