[English] 日本語
![](img/lk-miru.gif)
- PDB-2dcr: Fully automated solution structure determination of the Fes SH2 domain -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2dcr | ||||||
---|---|---|---|---|---|---|---|
Title | Fully automated solution structure determination of the Fes SH2 domain | ||||||
![]() | Proto-oncogene tyrosine-protein kinase Fes/Fps | ||||||
![]() | TRANSFERASE / SH2 domain / Fes / feline sarcoma oncogene / fully automated structure determination / FLYA algorithm | ||||||
Function / homology | ![]() positive regulation of myeloid cell differentiation / regulation of mast cell degranulation / regulation of vesicle-mediated transport / cellular response to vitamin D / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / CRMPs in Sema3A signaling / microtubule bundle formation / positive regulation of monocyte differentiation / regulation of cell motility / centrosome cycle ...positive regulation of myeloid cell differentiation / regulation of mast cell degranulation / regulation of vesicle-mediated transport / cellular response to vitamin D / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / CRMPs in Sema3A signaling / microtubule bundle formation / positive regulation of monocyte differentiation / regulation of cell motility / centrosome cycle / myoblast proliferation / cardiac muscle cell proliferation / regulation of cell differentiation / Sema3A PAK dependent Axon repulsion / regulation of cell adhesion / positive regulation of microtubule polymerization / immunoglobulin receptor binding / phosphatidylinositol binding / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / Signaling by SCF-KIT / cytoplasmic side of plasma membrane / positive regulation of neuron projection development / peptidyl-tyrosine phosphorylation / chemotaxis / microtubule cytoskeleton / regulation of cell population proliferation / regulation of cell shape / cytoplasmic vesicle / microtubule binding / protein tyrosine kinase activity / protein autophosphorylation / cell adhesion / focal adhesion / Golgi apparatus / ATP binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / Fully automated NMR spectrum analysis, structure calculation without human intervention. Chemical shift assignments, conformational restraints have not been verified manually. | ||||||
![]() | Lopez-Mendez, B. / Guntert, P. | ||||||
![]() | ![]() Title: Automated protein structure determination from NMR spectra Authors: Lopez-Mendez, B. / Guntert, P. #1: ![]() Title: Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes Authors: Scott, A. / Pantoja-Uceda, D. / Koshiba, S. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Tanaka, A. / Sugano, S. / Yokoyama, S. / Guntert, P. #2: Journal: J.Biomol.Nmr / Year: 2004 Title: NMR assignment of the SH2 domain from the human feline sarcoma oncogene FES Authors: Scott, A. / Pantoja-Uceda, D. / Koshiba, S. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Tanaka, A. / Sugano, S. / Yokoyama, S. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 683.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 572.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 356.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 477.5 KB | Display | |
Data in XML | ![]() | 32.5 KB | Display | |
Data in CIF | ![]() | 57.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 12506.106 Da / Num. of mol.: 1 / Fragment: SH2 DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details | Contents: 1.2MM UNIFORMLY 13C AND 15N LABELED PROTEIN; 20MM TRIS-HCL BUFFER; 100MM NACL; 1MM DITHIOTHREITOL; 0.02% NAN3 |
---|---|
Sample conditions | pH: 7.0 / Pressure: AMBIENT / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
NMR software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: Fully automated NMR spectrum analysis, structure calculation without human intervention. Chemical shift assignments, conformational restraints have not been verified manually. Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |