[English] 日本語
![](img/lk-miru.gif)
- PDB-1b64: SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMA... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1b64 | ||||||
---|---|---|---|---|---|---|---|
Title | SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES | ||||||
![]() | ELONGATION FACTOR 1-BETA | ||||||
![]() | ![]() ![]() | ||||||
Function / homology | ![]() Eukaryotic Translation Elongation / eukaryotic translation elongation factor 1 complex / translational elongation / ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Perez, J.M.J. / Siegal, G. / Kriek, J. / Hard, K. / Dijk, J. / Canters, G.W. / Moller, W. | ||||||
![]() | ![]() Title: The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli. Authors: Perez, J.M. / Siegal, G. / Kriek, J. / Hard, K. / Dijk, J. / Canters, G.W. / Moller, W. #1: ![]() Title: 1H, 15N and 13C Chemical Shift Assignment of the Guanine Nucleotide Exchange Domain of Human Elongation Factor-One Beta Authors: Perez, J.M. / Kriek, J. / Dijk, J. / Moller, W. / Siegal, G. / Hard, K. / Kalverda, A.P. / Canters, G.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 552.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 461.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 10148.631 Da / Num. of mol.: 1 / Fragment: GUANINE EXCHANGE FACTOR DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|---|
NMR experiment | Type![]() |
NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY OF 13C, 15N-LABELED EF-1BETA. |
-
Sample preparation
Details | Contents: 95% H2O AND 5% D2O |
---|---|
Sample conditions | Ionic strength: 100 mM / pH: 6.9 / Pressure: 1 atm / Temperature: 303 K |
Crystal grow![]() | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX600 / Manufacturer: Bruker / Model![]() |
---|
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR software |
| ||||||||||||
Refinement | Method: ![]() Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 50 / Conformers submitted total number: 20 |