+Open data
-Basic information
Entry | Database: PDB / ID: 2rq1 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the 4.1R FERM alpha lobe domain | ||||||
Components | Protein 4.1 | ||||||
Keywords | MEMBRANE PROTEIN / PROTEIN / Actin-binding / Alternative splicing / Cytoplasm / Cytoskeleton / Elliptocytosis / Glycoprotein / Hereditary hemolytic anemia / Nucleus / Phosphoprotein / Polymorphism / Pyropoikilocytosis | ||||||
Function / homology | Function and homology information 1-phosphatidylinositol binding / regulation of intestinal absorption / spectrin-associated cytoskeleton / actomyosin structure organization / Neurexins and neuroligins / cortical actin cytoskeleton organization / spectrin binding / cortical cytoskeleton / intercellular bridge / regulation of calcium ion transport ...1-phosphatidylinositol binding / regulation of intestinal absorption / spectrin-associated cytoskeleton / actomyosin structure organization / Neurexins and neuroligins / cortical actin cytoskeleton organization / spectrin binding / cortical cytoskeleton / intercellular bridge / regulation of calcium ion transport / positive regulation of protein localization to cell cortex / phosphoprotein binding / structural constituent of cytoskeleton / cytoplasmic side of plasma membrane / mitotic spindle / cell junction / actin binding / cell cortex / positive regulation of protein binding / actin cytoskeleton organization / basolateral plasma membrane / protein-containing complex assembly / nuclear body / cytoskeleton / calmodulin binding / cell cycle / cell division / protein-containing complex / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Kusunoki, H. / Kohno, T. | ||||||
Citation | Journal: Proteins / Year: 2009 Title: Solution structure and glycophorin C binding studies of the protein 4.1R FERM alpha-lobe domain Authors: Kusunoki, H. / Kohno, T. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2rq1.cif.gz | 665.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2rq1.ent.gz | 577.4 KB | Display | PDB format |
PDBx/mmJSON format | 2rq1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rq/2rq1 ftp://data.pdbj.org/pub/pdb/validation_reports/rq/2rq1 | HTTPS FTP |
---|
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 12420.041 Da / Num. of mol.: 1 / Fragment: 4.1R_FERM_alpha-lobe_domain, UNP residues 292-396 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EPB41, E41P / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / References: UniProt: P11171 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 0.12-0.8mM 4.1R FERM alpha-lobe domain-1, 0.12-0.8mM [U-98% 15N] 4.1R FERM alpha-lobe domain-2, 0.12-0.8mM [U-98% 13C; U-98% 15N] 4.1R FERM alpha-lobe domain-3, 90% H2O/10% D2O or 100% D2O Solvent system: 90% H2O/10% D2O or 100% D2O | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||||
Sample conditions | Ionic strength: 45 / pH: 6.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 / Representative conformer: 1 |