+Open data
-Basic information
Entry | Database: PDB / ID: 7tio | ||||||
---|---|---|---|---|---|---|---|
Title | B Domain of Staphylococcal protein A: Native backbone | ||||||
Components | Immunoglobulin G binding protein A | ||||||
Keywords | DE NOVO PROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Staphylococcus aureus (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Santhouse, J.R. / Leung, J.M.G. / Chong, L.T. / Horne, W.S. | ||||||
Funding support | United States, 1items
| ||||||
Citation | Journal: Chem Sci / Year: 2022 Title: Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics. Authors: Santhouse, J.R. / Leung, J.M.G. / Chong, L.T. / Horne, W.S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 7tio.cif.gz | 198.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb7tio.ent.gz | 169 KB | Display | PDB format |
PDBx/mmJSON format | 7tio.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7tio_validation.pdf.gz | 348.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 7tio_full_validation.pdf.gz | 404.7 KB | Display | |
Data in XML | 7tio_validation.xml.gz | 11.1 KB | Display | |
Data in CIF | 7tio_validation.cif.gz | 17.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ti/7tio ftp://data.pdbj.org/pub/pdb/validation_reports/ti/7tio | HTTPS FTP |
-Related structure data
Related structure data | 7tipC 7tiqC 7tirC 7tisC C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
Other databases |
|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Antibody | Mass: 6618.271 Da / Num. of mol.: 1 / Fragment: B domain, residues 185-242 / Mutation: G29A / Source method: obtained synthetically / Source: (synth.) Staphylococcus aureus (bacteria) / References: UniProt: Q2UW47 |
---|---|
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Type: solution Contents: 2.5 mM B Domain of Staphylococcal protein A, 0.2 mM DSS, 90% H2O/10% D2O Label: sample_1 / Solvent system: 90% H2O/10% D2O | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||
Sample conditions | Ionic strength: 10 mM / Label: conditions_1 / pH: 5 pH* / Pressure: 1 atm / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
---|
-Processing
NMR software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 4 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |