+Open data
-Basic information
Entry | Database: PDB / ID: 2ee2 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structures of the fn3 domain of human contactin 1 | ||||||
Components | Contactin-1 | ||||||
Keywords | SIGNALING PROTEIN / Neural cell surface protein F3 / Glycoprotein gp135 / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information L1CAM interactions / cell-cell adhesion mediator activity / Neurofascin interactions / central nervous system myelin formation / positive regulation of sodium ion transport / side of membrane / Notch signaling pathway / NOTCH2 Activation and Transmission of Signal to the Nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / cerebellum development ...L1CAM interactions / cell-cell adhesion mediator activity / Neurofascin interactions / central nervous system myelin formation / positive regulation of sodium ion transport / side of membrane / Notch signaling pathway / NOTCH2 Activation and Transmission of Signal to the Nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / cerebellum development / locomotory behavior / axon guidance / brain development / cell-cell adhesion / positive regulation of neuron projection development / presynaptic membrane / gene expression / postsynaptic membrane / carbohydrate binding / cell adhesion / axon / positive regulation of gene expression / extracellular exosome / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Sato, M. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structures of the fn3 domain of human contactin 1 Authors: Sato, M. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2ee2.cif.gz | 673 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2ee2.ent.gz | 566.2 KB | Display | PDB format |
PDBx/mmJSON format | 2ee2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ee/2ee2 ftp://data.pdbj.org/pub/pdb/validation_reports/ee/2ee2 | HTTPS FTP |
---|
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 12640.807 Da / Num. of mol.: 1 / Fragment: Fibronectin type III domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: CNTN1 / Plasmid: P050711-22 / References: UniProt: Q12860 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1mM fn3 domain U-15N, 13C; 20mM d-Tris HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
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: 900 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |