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Yorodumi- PDB-1tdp: NMR solution structure of the carnobacteriocin B2 immunity protein -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tdp | ||||||
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Title | NMR solution structure of the carnobacteriocin B2 immunity protein | ||||||
Components | carnobacteriocin B2 immunity protein | ||||||
Keywords | ANTIMICROBIAL PROTEIN / four-helix bundle | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Carnobacterium maltaromaticum (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Sprules, T. / Kawulka, K.E. / Vederas, J.C. | ||||||
Citation | Journal: Biochemistry / Year: 2004 Title: NMR Solution Structure of ImB2, a Protein Conferring Immunity to Antimicrobial Activity of the Type IIa Bacteriocin, Carnobacteriocin B2 Authors: Sprules, T. / Kawulka, K.E. / Vederas, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tdp.cif.gz | 530.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tdp.ent.gz | 441.6 KB | Display | PDB format |
PDBx/mmJSON format | 1tdp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/td/1tdp ftp://data.pdbj.org/pub/pdb/validation_reports/td/1tdp | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12680.632 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Carnobacterium maltaromaticum (bacteria) Gene: cbiB2 / Plasmid: pMALc / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P38582 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 20 mM sodium phosphate; 25 mM NaCl / pH: 6.6 / Pressure: ambient / Temperature: 288 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Structures are based on 2118 NOE-derived distance restraints, 84 hydrogen bonds and 130 dihedral angle restraints. | ||||||||||||||||||||||||
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: 15 |