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Yorodumi- PDB-1lgr: INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE S... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lgr | ||||||
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Title | INTERACTIONS OF NUCLEOTIDES WITH FULLY UNADENYLYLATED GLUTAMINE SYNTHETASE FROM SALMONELLA TYPHIMURIUM | ||||||
Components | GLUTAMINE SYNTHETASE | ||||||
Keywords | LIGASE(AMIDE SYNTHETASE) | ||||||
Function / homology | Function and homology information nitrogen utilization / glutamine synthetase / glutamine biosynthetic process / glutamine synthetase activity / protein homooligomerization / manganese ion binding / ATP binding / membrane / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Salmonella typhimurium (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.79 Å | ||||||
Authors | Liaw, S.-H. / Eisenberg, D. | ||||||
Citation | Journal: Biochemistry / Year: 1994 Title: Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium. Authors: Liaw, S.H. / Jun, G. / Eisenberg, D. #1: Journal: J.Biol.Chem. / Year: 1989 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: Journal: Nature / Year: 1986 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lgr.cif.gz | 910.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lgr.ent.gz | 763.7 KB | Display | PDB format |
PDBx/mmJSON format | 1lgr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lg/1lgr ftp://data.pdbj.org/pub/pdb/validation_reports/lg/1lgr | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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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:
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-Components
#1: Protein | Mass: 51744.418 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella typhimurium (bacteria) References: UniProt: P06201, UniProt: P0A1P6*PLUS, glutamine synthetase #2: Chemical | ChemComp-MN / #3: Chemical | ChemComp-AMP / |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.54 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 22 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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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 |
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Refinement | Resolution: 2.79→8 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.79→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 99220 / Rfactor all: 0.233 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3 |