[English] 日本語
Yorodumi- PDB-8t0g: Backbone Dialkylation in Peptide Hairpins: Natural Backbone Prototype -
+Open data
-Basic information
Entry | Database: PDB / ID: 8t0g | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Backbone Dialkylation in Peptide Hairpins: Natural Backbone Prototype | |||||||||
Components | Immunoglobulin G-binding protein G | |||||||||
Keywords | DE NOVO PROTEIN / hairpin / peptidomimetic / backbone modification | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Streptococcus sp. group G (bacteria) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Authors | Heath, S.L. / Horne, W.S. / Lengyel, G.A. | |||||||||
Funding support | United States, 2items
| |||||||||
Citation | Journal: Org.Biomol.Chem. / Year: 2023 Title: Effects of chirality and side chain length in C alpha , alpha-dialkylated residues on beta-hairpin peptide folded structure and stability. Authors: Heath, S.L. / Horne, W.S. / Lengyel, G.A. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 8t0g.cif.gz | 50.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb8t0g.ent.gz | 32.4 KB | Display | PDB format |
PDBx/mmJSON format | 8t0g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8t0g_validation.pdf.gz | 408.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 8t0g_full_validation.pdf.gz | 440.6 KB | Display | |
Data in XML | 8t0g_validation.xml.gz | 8.5 KB | Display | |
Data in CIF | 8t0g_validation.cif.gz | 10.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t0/8t0g ftp://data.pdbj.org/pub/pdb/validation_reports/t0/8t0g | HTTPS FTP |
-Related structure data
Related structure data | 8t0hC 8t0iC 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: 1826.960 Da / Num. of mol.: 1 / Mutation: T13A / Source method: obtained synthetically / Source: (synth.) Streptococcus sp. group G (bacteria) / References: UniProt: P06654 |
---|---|
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Type: solution Contents: 2 mM GB1 C-terminal Hairpin Mutant: Ala13 variant, 50 mM sodium phosphate, 0.2 mM DSS, 90% H2O/10% D2O Label: sample_1 / Solvent system: 90% H2O/10% D2O | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||
Sample conditions | Ionic strength: 250 mM / Label: conditions_1 / pH: 6.3 pH* / Pressure: 1 atm / Temperature: 298 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 |