[English] 日本語
![](img/lk-miru.gif)
- PDB-1nd9: Solution Structure of the N-terminal Subdomain of Translation Ini... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1nd9 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution Structure of the N-terminal Subdomain of Translation Initiation Factor IF2 | ||||||
![]() | Translation initiation factor IF-2 | ||||||
![]() | TRANSLATION / IF2 / initiation factor | ||||||
Function / homology | ![]() guanosine tetraphosphate binding / ribosomal small subunit binding / chaperone-mediated protein folding / translational initiation / translation initiation factor activity / response to cold / GTPase activity / GTP binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Laursen, B.S. / Mortensen, K.K. / Sperling-Petersen, H.U. / Hoffman, D.W. | ||||||
![]() | ![]() Title: A conserved structural motif at the N terminus of bacterial translation initiation factor IF2 Authors: Laursen, B.S. / Mortensen, K.K. / Sperling-Petersen, H.U. / Hoffman, D.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 153.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 125.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 338.5 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 429.4 KB | Display | |
Data in XML | ![]() | 19 KB | Display | |
Data in CIF | ![]() | 28 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 5405.960 Da / Num. of mol.: 1 / Fragment: N-terminal Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||
NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy |
-
Sample preparation
Details |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample conditions |
| ||||||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
-
Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 996 restraints, 918 are NOE-derived distance constraints, 63 dihedral angle restraints,15 distance restraints from hydrogen bonds. | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 10 |