+Open data
-Basic information
Entry | Database: PDB / ID: 1s7p | ||||||
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Title | Solution structure of thermolysin digested microcin J25 | ||||||
Components | (microcin J25) x 2 | ||||||
Keywords | ANTIBIOTIC / thermolysin digested microcin J25 / t-Mccj25 / thermolysin digest / two-chain peptide / steric link / ANTIMICROBIAL PROTEIN | ||||||
Function / homology | killing of cells of another organism / defense response to bacterium / extracellular region / Microcin J25 Function and homology information | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / Structures were calculated using torsion angle dynamics in CNS, refined in explicit solvent. | ||||||
Authors | Rosengren, K.J. / Blond, A. / Afonso, C. / Tabet, J.C. / Rebuffat, S. / Craik, D.J. | ||||||
Citation | Journal: Biochemistry / Year: 2004 Title: Structure of thermolysin cleaved microcin J25: extreme stability of a two-chain antimicrobial peptide devoid of covalent links Authors: Rosengren, K.J. / Blond, A. / Afonso, C. / Tabet, J.C. / Rebuffat, S. / Craik, D.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1s7p.cif.gz | 106.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1s7p.ent.gz | 82.9 KB | Display | PDB format |
PDBx/mmJSON format | 1s7p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s7/1s7p ftp://data.pdbj.org/pub/pdb/validation_reports/s7/1s7p | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 1110.261 Da / Num. of mol.: 1 / Fragment: Residues 48-58 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Description: DIGESTED WITH THERMOLYSIN; / Gene: mcj25A / Plasmid: pTUC202 / Production host: Escherichia coli (E. coli) / Strain (production host): MC4100 / References: UniProt: Q9X2V7 |
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#2: Protein/peptide | Mass: 1034.102 Da / Num. of mol.: 1 / Fragment: Residues 38-47 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Description: digested with thermolysin / Gene: mcj25A / Plasmid: pTUC202 / Production host: Escherichia coli (E. coli) / Strain (production host): MC4100 / References: UniProt: Q9X2V7 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 6mM t-MccJ25 / Solvent system: 100% CD3OH |
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Sample conditions | Ionic strength: 0 / Pressure: ambient / Temperature: 295 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: Structures were calculated using torsion angle dynamics in CNS, refined in explicit solvent. Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |