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- PDB-2lqu: Structure of decorbin-binding protein A from Borrelia burgdorferi -
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Open data
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Basic information
Entry | Database: PDB / ID: 2lqu | ||||||
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Title | Structure of decorbin-binding protein A from Borrelia burgdorferi | ||||||
![]() | Decorin-binding protein A | ||||||
![]() | CELL ADHESION / GAG-binding protein / helical bundle protein / Lyme disease / bacterial adhesin | ||||||
Function / homology | Decorin-binding protein / Decorin-binding protein / Decorin-binding superfamily / Decorin binding protein / A middle domain of Talin 1 / Up-down Bundle / Mainly Alpha / membrane / Decorin-binding protein A![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | fewest violations, model 1 | ||||||
![]() | Wang, X. | ||||||
![]() | ![]() Title: Solution structure of decorin-binding protein A from Borrelia burgdorferi. Authors: Wang, X. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 512 KB | Display | ![]() |
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PDB format | ![]() | 427.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 536 KB | Display | ![]() |
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Full document | ![]() | 891.8 KB | Display | |
Data in XML | ![]() | 71.4 KB | Display | |
Data in CIF | ![]() | 78 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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NMR ensembles |
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Components
#1: Protein | Mass: 18555.178 Da / Num. of mol.: 1 / Fragment: UNP residues 26-191 / Mutation: C25A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: B31 / Gene: BB_A24, dbpA / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 0.05 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Agilent Inova 800 / Manufacturer: Agilent / Model: Inova 800 / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 / Details: XPLOR-NIH refinement with RDCs | ||||||||||||
NMR constraints | NOE constraints total: 1288 / NOE intraresidue total count: 198 / NOE long range total count: 452 / NOE medium range total count: 396 / NOE sequential total count: 242 / Protein phi angle constraints total count: 105 / Protein psi angle constraints total count: 105 | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Average torsion angle constraint violation: 0.3 ° Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 10 / Maximum torsion angle constraint violation: 10 ° / Maximum upper distance constraint violation: 0.49 Å | ||||||||||||
NMR ensemble rms | Distance rms dev: 0.05 Å |