[English] 日本語
![](img/lk-miru.gif)
- PDB-1lgr: INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE S... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1lgr | ||||||
---|---|---|---|---|---|---|---|
Title | INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM | ||||||
![]() | GLUTAMINE SYNTHETASE![]() | ||||||
![]() | LIGASE(AMIDE SYNTHETASE) | ||||||
Function / homology | ![]() nitrogen utilization / ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Liaw, S.-H. / Eisenberg, D. | ||||||
![]() | ![]() Title: Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium. Authors: Liaw, S.H. / Jun, G. / Eisenberg, D. #1: ![]() Title: Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution Authors: Yamashita, M.M. / Almassy, R.J. / Janson, C.A. / Cascio, D. / Eisenberg, D. #2: ![]() Title: Novel Subunit-Subunit Interactions in the Structure of Glutamine Synthetase Authors: Almassy, R.J. / Janson, C.A. / Hamlin, R. / Xuong, N.-H. / Eisenberg, D. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 910.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 763.7 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 |
| ||||||||||||||||||||||||||||||||||||||||||||||||
Unit cell |
| ||||||||||||||||||||||||||||||||||||||||||||||||
Atom site foot note | 1: CIS PROLINE - PRO 184 2: SER 350 - PRO 351 OMEGA = 218.02 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-
Components
#1: Protein | ![]() Mass: 51744.418 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P06201, UniProt: P0A1P6*PLUS, ![]() #2: Chemical | ChemComp-MN / #3: Chemical | ChemComp-AMP / ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.54 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow![]() | *PLUS Temperature: 22 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.8 Å / Num. obs: 99219 / Num. measured all: 146242 / Rmerge(I) obs: 0.066 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.79→8 Å / σ(F): 0 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.79→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 99220 / Rfactor all![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3 |