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Open data
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Basic information
Entry | Database: PDB / ID: 1fxz | ||||||
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Title | CRYSTAL STRUCTURE OF SOYBEAN PROGLYCININ A1AB1B HOMOTRIMER | ||||||
![]() | GLYCININ G1 | ||||||
![]() | PLANT PROTEIN / Proglycinin / Glycinin / Legumin / Seed Storage Protein | ||||||
Function / homology | ![]() protein storage vacuole / nutrient reservoir activity / endoplasmic reticulum Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Adachi, M. / Takenaka, Y. / Gidamis, A.B. / Mikami, B. / Utsumi, S. | ||||||
![]() | ![]() Title: Crystal structure of soybean proglycinin A1aB1b homotrimer. Authors: Adachi, M. / Takenaka, Y. / Gidamis, A.B. / Mikami, B. / Utsumi, S. #1: ![]() Title: Crystallization and preliminary X-ray Crystallographic analysis of the soybean proglycinin expressed in Escherichia coli. Authors: Utsumi, S. / Gidamis, A.B. / Mikami, B. / Kito, M. #2: ![]() Title: Signal sequence of preproglycinin affects production of the expressed protein in Escherichia coli. Authors: Utsumi, S. / Kim, C.S. / Sato, T. / Kito, M. #3: ![]() Title: An alternate cDNA encoding glycinin A1aBx subunit Authors: Utsumi, S. / Kohno, T. / Mori, T. / Kito, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 225.3 KB | Display | ![]() |
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PDB format | ![]() | 180.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 387.4 KB | Display | ![]() |
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Full document | ![]() | 422.1 KB | Display | |
Data in XML | ![]() | 25.3 KB | Display | |
Data in CIF | ![]() | 38.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Details | The biological assembly is a trimer corresponding to that in asymmetric unit. |
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Components
#1: Protein | Mass: 53682.500 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Has protein modification | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.04 Å3/Da / Density % sol: 59.59 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 302 K / Method: dialysis / pH: 7.6 / Details: pH 7.6, Dialysis, temperature 302.0K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 281 K / pH: 5.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 68 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS HI-STAR / Detector: AREA DETECTOR / Date: Jan 17, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.8 Å / Num. obs: 142631 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Redundancy: 3.1 % |
Reflection | *PLUS Lowest resolution: 9999 Å / Num. obs: 46010 / Num. measured all: 142631 / Rmerge(I) obs: 0.089 |
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Processing
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Refinement | Resolution: 2.8→8 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Software | *PLUS Name: ![]() | |||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 8 Å / σ(F): 2 / Rfactor obs: 0.199 / Rfactor Rfree: 0.25 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.92 Å / Rfactor Rfree: 0.341 / Rfactor obs: 0.271 |