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Open data
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Basic information
| Entry | Database: PDB / ID: 2m37 | ||||||
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| Title | Structure of lasso peptide astexin-1 | ||||||
Components | ASTEXIN-1 | ||||||
Keywords | UNKNOWN FUNCTION / ASTEXIN-1 / LASSO PEPTIDE / LARIAT PROTOKNOT | ||||||
| Function / homology | defense response to bacterium / Astexin-1 Function and homology information | ||||||
| Biological species | Asticcacaulis excentricus (bacteria) | ||||||
| Method | SOLUTION NMR / simulated annealing | ||||||
| Model details | lowest energy, model1 | ||||||
Authors | Zimmermann, M. / Hegemann, J.D. / Xie, X. / Marahiel, M.A. | ||||||
Citation | Journal: Chem.Biol. / Year: 2013Title: The astexin-1 lasso peptides: biosynthesis, stability, and structural studies. Authors: Zimmermann, M. / Hegemann, J.D. / Xie, X. / Marahiel, M.A. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2m37.cif.gz | 119.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2m37.ent.gz | 88.6 KB | Display | PDB format |
| PDBx/mmJSON format | 2m37.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2m37_validation.pdf.gz | 381.5 KB | Display | wwPDB validaton report |
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| Full document | 2m37_full_validation.pdf.gz | 407.7 KB | Display | |
| Data in XML | 2m37_validation.xml.gz | 7.1 KB | Display | |
| Data in CIF | 2m37_validation.cif.gz | 11.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m3/2m37 ftp://data.pdbj.org/pub/pdb/validation_reports/m3/2m37 | HTTPS FTP |
-Related structure data
| Similar structure data | |
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| Other databases |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 2113.219 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Asticcacaulis excentricus (bacteria) / Strain: ATCC 15261 / DSM 4724 / VKM B-1370 / CB 48 / Gene: ATXA / Strain (production host): CB48 / References: UniProt: E8RMD3 |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||
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| NMR experiment |
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Sample preparation
| Details | Contents: 5.7 mM ASTEXIN-1, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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| Sample | Conc.: 5.7 mM / Component: ASTEXIN-1(19)-1 |
| Sample conditions | Pressure: ambient atm / Temperature: 283 K |
-NMR measurement
| NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
| NMR software |
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| Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
| NMR representative | Selection criteria: lowest energy | ||||||||||||
| NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |
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Asticcacaulis excentricus (bacteria)
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