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- PDB-2liv: PERIPLASMIC BINDING PROTEIN STRUCTURE AND FUNCTION. REFINED X-RAY... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2liv | ||||||
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Title | PERIPLASMIC BINDING PROTEIN STRUCTURE AND FUNCTION. REFINED X-RAY STRUCTURES OF THE LEUCINE/ISOLEUCINE/VALINE-BINDING PROTEIN AND ITS COMPLEX WITH LEUCINE | ||||||
![]() | LEUCINE | ||||||
![]() | PERIPLASMIC BINDING PROTEIN | ||||||
Function / homology | ![]() branched-chain amino acid transport / isoleucine transport / valine transport / L-leucine transport / amino acid transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / outer membrane-bounded periplasmic space / periplasmic space / membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Sack, J.S. / Saper, M.A. / Quiocho, F.A. | ||||||
![]() | ![]() Title: Periplasmic binding protein structure and function. Refined X-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. Authors: Sack, J.S. / Saper, M.A. / Quiocho, F.A. #1: ![]() Title: Structure of the L-Leucine-Binding Protein Refined at 2.4 Angstroms Resolution and Comparison with the Leu(Slash)Ile(Slash)Val-Binding Protein Structure Authors: Sack, J.S. / Trakhanov, S.D. / Tsigannik, I.H. / Quiocho, F.A. #2: ![]() Title: Leucine, Isoleucine, Valine-Binding Protein from Escherichia Coli Authors: Saper, M.A. / Quiocho, F.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 77.8 KB | Display | ![]() |
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PDB format | ![]() | 58.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 370.8 KB | Display | ![]() |
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Full document | ![]() | 405.5 KB | Display | |
Data in XML | ![]() | 13.1 KB | Display | |
Data in CIF | ![]() | 18.9 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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Unit cell |
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Components
#1: Protein | Mass: 36784.344 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.69 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.6 / Method: other | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 12004 / Num. measured all: 41179 / Rmerge(I) obs: 0.021 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.4→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 10 Å / Num. reflection all: 11817 / Rfactor all: 0.179 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |