[English] 日本語
![](img/lk-miru.gif)
- PDB-2ver: Structural model for the complex between the Dr adhesins and carc... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2ver | ||||||
---|---|---|---|---|---|---|---|
Title | Structural model for the complex between the Dr adhesins and carcinoembryonic antigen (CEA) | ||||||
![]() |
| ||||||
![]() | CELL ADHESION / MEMBRANE / FIMBRIUM / GPI-ANCHOR / LIPOPROTEIN / IMMUNOGLOBULIN DOMAIN / CELL PROJECTION | ||||||
Function / homology | ![]() GPI anchor binding / homotypic cell-cell adhesion / Post-translational modification: synthesis of GPI-anchored proteins / negative regulation of myotube differentiation / regulation of immune system process / pilus / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / homophilic cell adhesion via plasma membrane adhesion molecules / negative regulation of anoikis / side of membrane ...GPI anchor binding / homotypic cell-cell adhesion / Post-translational modification: synthesis of GPI-anchored proteins / negative regulation of myotube differentiation / regulation of immune system process / pilus / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / homophilic cell adhesion via plasma membrane adhesion molecules / negative regulation of anoikis / side of membrane / protein tyrosine kinase binding / Cell surface interactions at the vascular wall / basolateral plasma membrane / apical plasma membrane / apoptotic process / negative regulation of apoptotic process / cell surface / signal transduction / protein homodimerization activity / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / HADDOCK | ||||||
Model type details | MINIMIZED AVERAGE | ||||||
![]() | Korotkova, N. / Yang, Y. / Le Trong, I. / Cota, E. / Demeler, B. / Marchant, J. / Thomas, W.E. / Stenkamp, R.E. / Moseley, S.L. / Matthews, S. | ||||||
![]() | ![]() Title: Binding of Dr Adhesins of Escherichia Coli to Carcinoembryonic Antigen Triggers Receptor Dissociation. Authors: Korotkova, N. / Yang, Y. / Le Trong, I. / Cota, E. / Demeler, B. / Marchant, J. / Thomas, W.E. / Stenkamp, R.E. / Moseley, S.L. / Matthews, S. | ||||||
History |
| ||||||
Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 95.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 78.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 497.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 499.7 KB | Display | |
Data in XML | ![]() | 7 KB | Display | |
Data in CIF | ![]() | 9.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 15456.051 Da / Num. of mol.: 1 / Fragment: RESIDUES 38-160 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|---|
#2: Protein | Mass: 12314.913 Da / Num. of mol.: 1 / Fragment: N DOMAIN, RESIDUES 35-144 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|---|
NMR experiment | Type: ![]() |
NMR details | Text: STRUCTURE WAS DETERMINED USING NMR RESTRAINT DRIVEN DOCKING (CHEMICAL SHIFTA AND PARAMAGNETIC RELAXATION ENHANCEMENTS (PRES) |
-
Sample preparation
Details | Contents: 10% H20/90% D20 |
---|---|
Sample conditions | Ionic strength: 2- mM / pH: 7.0 / Pressure: 1.0 atm / Temperature: 303.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker OTHER / Manufacturer: Bruker / Model: OTHER / Field strength: 500 MHz |
---|
-
Processing
NMR software |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: HADDOCK / Software ordinal: 1 / Details: WATER SHELL | |||||||||
NMR ensemble | Conformer selection criteria: REPRESENTATIVE STRUCTURE / Conformers calculated total number: 200 / Conformers submitted total number: 1 |