+Open data
-Basic information
Entry | Database: PDB / ID: 8ox2 | ||||||
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Title | BRICHOS trimer | ||||||
Components | Pulmonary surfactant-associated protein C | ||||||
Keywords | CHAPERONE / PROTEIN | ||||||
Function / homology | Function and homology information respiratory gaseous exchange by respiratory system / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Ghosh, D. / Torres, F. / Guentert, P. / Riek, R. | ||||||
Funding support | Switzerland, 1items
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Citation | Journal: To Be Published Title: The inhibitory action of the chaperone BRICHOS against the alpha-Synuclein secondary nucleation pathway at near-atomic resolution Authors: Ghosh, D. / Torres, F. / Guentert, P. / Riek, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8ox2.cif.gz | 1.9 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8ox2.ent.gz | 1.6 MB | Display | PDB format |
PDBx/mmJSON format | 8ox2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8ox2_validation.pdf.gz | 573 KB | Display | wwPDB validaton report |
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Full document | 8ox2_full_validation.pdf.gz | 2 MB | Display | |
Data in XML | 8ox2_validation.xml.gz | 235.4 KB | Display | |
Data in CIF | 8ox2_validation.cif.gz | 280.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ox/8ox2 ftp://data.pdbj.org/pub/pdb/validation_reports/ox/8ox2 | HTTPS FTP |
-Related structure data
Related structure data | 8oviC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12007.753 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SFTPC / Production host: Escherichia coli (E. coli) / References: UniProt: E5RI64 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Sample state: isotropic / Type: NOESY |
-Sample preparation
Details | Type: solution Contents: 1 mM [U-13C; U-15N] BRICHOS monomer, 25 mM potassium phosphate, 25 mM NaCl, 0.01 % sodium azide, 90% H2O/10% D2O Label: 1 / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 50 mM / Label: 1 / pH: 6.8 Not defined / Pressure: AMBIENT Pa / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software | Name: CYANA / Version: 3.98.15 / Developer: P. Guentert / Classification: structure calculation |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 200 / Conformers submitted total number: 20 |