+Open data
-Basic information
Entry | Database: PDB / ID: 2mlj | ||||||
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Title | Structure of Lasso Peptide Caulonodin V | ||||||
Components | Caulonodin V | ||||||
Keywords | UNKNOWN FUNCTION / lariat protoknot | ||||||
Function / homology | Caulonodin V Function and homology information | ||||||
Biological species | Caulobacter sp. (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model15 | ||||||
Authors | Zimmermann, M. / Hegemann, J.D. / Xie, X. / Marahiel, M.A. | ||||||
Citation | Journal: CHEM SCI / Year: 2014 Title: Characterization of caulonodin lasso peptides revealed unprecedented N-terminal residues and a precursor motif essential for peptide maturation Authors: Zimmermann, M. / Hegemann, J.D. / Xie, X. / Marahiel, M.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mlj.cif.gz | 82.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mlj.ent.gz | 65.1 KB | Display | PDB format |
PDBx/mmJSON format | 2mlj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mlj_validation.pdf.gz | 383.9 KB | Display | wwPDB validaton report |
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Full document | 2mlj_full_validation.pdf.gz | 405.3 KB | Display | |
Data in XML | 2mlj_validation.xml.gz | 6.4 KB | Display | |
Data in CIF | 2mlj_validation.cif.gz | 9.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ml/2mlj ftp://data.pdbj.org/pub/pdb/validation_reports/ml/2mlj | 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: 2002.146 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Caulobacter sp. (bacteria) / Strain: K31 / Plasmid: pET41A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A0A0H2UKY1*PLUS |
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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: 10 mM cnd5, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 10 mM / Component: cnd5-1 |
Sample conditions | pH: 7 / Pressure: ambient / Temperature: 298 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: 15 |