+Open data
-Basic information
Entry | Database: PDB / ID: 2lwb | ||||||
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Title | Structural model of BAD-1 repeat loop by NMR | ||||||
Components | Adhesin WI-1 | ||||||
Keywords | CELL ADHESION | ||||||
Function / homology | Adhesin WI-1 Function and homology information | ||||||
Biological species | Ajellomyces dermatitidis (fungus) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Authors | Brandhorst, T. / Klein, B. / Tonelli, M. | ||||||
Citation | Journal: To be Published Title: Structure and function of a fungal adhesin that mimics thrombospondin-1 by binding heparin sulfate glycosaminoglycan and suppressing T cell activation via interaction with CD47 Authors: Brandhorst, T. / Klein, B. / Tonelli, M. / Roy, R. / Wuethrich, M. / McCaslin, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lwb.cif.gz | 124.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lwb.ent.gz | 93.7 KB | Display | PDB format |
PDBx/mmJSON format | 2lwb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lwb_validation.pdf.gz | 450.2 KB | Display | wwPDB validaton report |
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Full document | 2lwb_full_validation.pdf.gz | 531.8 KB | Display | |
Data in XML | 2lwb_validation.xml.gz | 9.8 KB | Display | |
Data in CIF | 2lwb_validation.cif.gz | 14.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lw/2lwb ftp://data.pdbj.org/pub/pdb/validation_reports/lw/2lwb | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2690.917 Da / Num. of mol.: 1 / Fragment: BAD-1 REPEAT LOOP Source method: isolated from a genetically manipulated source Source: (gene. exp.) Ajellomyces dermatitidis (fungus) / Strain: ER-3 / ATCC MYA-2586 / Gene: BDCG_07013 / Plasmid: pQETR4 / Production host: Escherichia coli (E. coli) / References: UniProt: C5GR14 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.1 mM [U-100% 13C; U-100% 15N] TR4, 10 mM potassium phosphate, 0.1 % sodium azide, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | pH: 8.0 / Pressure: ambient / Temperature: 25 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 18 |