+Open data
-Basic information
Entry | Database: PDB / ID: 2pii | ||||||
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Title | PII, GLNB PRODUCT | ||||||
Components | PII | ||||||
Keywords | SIGNAL TRANSDUCTION PROTEIN | ||||||
Function / homology | Function and homology information regulation of fatty acid biosynthetic process / regulation of nitrogen utilization / small molecule binding / enzyme activator activity / enzyme regulator activity / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Carr, P.D. / Cheah, E. / Suffolk, P.M. / Ollis, D.L. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1996 Title: X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A. Authors: Carr, P.D. / Cheah, E. / Suffolk, P.M. / Vasudevan, S.G. / Dixon, N.E. / Ollis, D.L. #1: Journal: FEBS Lett. / Year: 1994 Title: Escherichia Coli Pii Protein: Purification, Crystallization and Oligomeric Structure Authors: Vasudevan, S.G. / Gedye, C. / Dixon, N.E. / Cheah, E. / Carr, P.D. / Suffolk, P.M. / Jeffrey, P.D. / Ollis, D.L. #2: Journal: Structure / Year: 1994 Title: Structure of the Escherichia Coli Signal Transducing Protein Pii Authors: Cheah, E. / Carr, P.D. / Suffolk, P.M. / Vasudevan, S.G. / Dixon, N.E. / Ollis, D.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2pii.cif.gz | 40.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2pii.ent.gz | 28.5 KB | Display | PDB format |
PDBx/mmJSON format | 2pii.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pi/2pii ftp://data.pdbj.org/pub/pdb/validation_reports/pi/2pii | 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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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 12443.442 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: DERIVED FROM K12 / Gene: GLNB / Variant: AN1459 / Plasmid: PCG646 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A9Z1 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 / Method: vapor diffusion, hanging drop / Details: Vasudevan, S.G., (1994) FEBS Lett., 337, 255. | ||||||||||||||||||||
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 | Num. obs: 11079 / Observed criterion σ(I): 1 |
Reflection | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 10 Å / Num. measured all: 45387 / Rmerge(I) obs: 0.071 |
-Processing
Software |
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Refinement | Resolution: 1.9→10 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.132 / Rfactor Rwork: 0.132 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |