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Open data
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Basic information
Entry | Database: PDB / ID: 1abe | |||||||||
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Title | NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN | |||||||||
![]() | L-ARABINOSE-BINDING PROTEIN | |||||||||
![]() | BINDING PROTEIN | |||||||||
Function / homology | ![]() L-arabinose transmembrane transport / ABC-type monosaccharide transporter activity / monosaccharide binding / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / outer membrane-bounded periplasmic space / carbohydrate binding / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Vyas, N.K. / Quiocho, F.A. | |||||||||
![]() | ![]() Title: Novel stereospecificity of the L-arabinose-binding protein Authors: Quiocho, F.A. / Vyas, N.K. #1: ![]() Title: Substrate Specificity and Affinity of a Protein Modulated by Bound Water Molecules Authors: Quiocho, F.A. / Wilson, D.K. / Vyas, N.K. #2: ![]() Title: Crystallographic Data of an L-Arabinose-Binding Protein from Escherichia Coli Authors: Quiocho, F.A. / Phillips Jr., G.N. / Parsons, R.G. / Hogg, R.W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.4 KB | Display | ![]() |
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PDB format | ![]() | 55.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 401 KB | Display | ![]() |
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Full document | ![]() | 409.6 KB | Display | |
Data in XML | ![]() | 8.6 KB | Display | |
Data in CIF | ![]() | 13.8 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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Components
#1: Protein | Mass: 33250.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Sugar | ChemComp-ARA / |
#3: Sugar | ChemComp-ARB / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.21 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: microdialysisDetails: referred to 'Quiocho, F.A.', (1974) J.Mol.Biol., 86, 491-493 | ||||||||||||||||||||
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 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.7→8 Å /
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Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 8 Å / Num. reflection obs: 26634 / σ(I): 3 / Rfactor obs: 0.137 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |