+Open data
-Basic information
Entry | Database: PDB / ID: 2kbz | ||||||
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Title | NMR structure of protein gp15 of bacteriophage SPP1 | ||||||
Components | 15 protein (Bacteriophage SPP1 complete nucleotide sequence) | ||||||
Keywords | VIRAL PROTEIN / three alpha-helix bundle | ||||||
Function / homology | Function and homology information symbiont genome ejection through host cell envelope, long flexible tail mechanism / virion component Similarity search - Function | ||||||
Biological species | Bacillus phage SPP1 (virus) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Gallopin, M. / Gilquin, B. / Zinn-Justin, S. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2009 Title: Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating Authors: Lhuillier, S. / Gallopin, M. / Gilquin, B. / Brasiles, S. / Lancelot, N. / Letellier, G. / Gilles, M. / Dethan, G. / Orlova, E.V. / Couprie, J. / Tavares, P. / Zinn-Justin, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kbz.cif.gz | 626.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kbz.ent.gz | 540.7 KB | Display | PDB format |
PDBx/mmJSON format | 2kbz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kb/2kbz ftp://data.pdbj.org/pub/pdb/validation_reports/kb/2kbz | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11269.961 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus phage SPP1 (virus) / Production host: Escherichia coli (E. coli) / Strain (production host): DE3 / References: UniProt: Q38584 |
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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: 0.5 mM [U-100% 15N] gp15-1, 0.5 mM [U-100% 13C; U-100% 15N] gp15-2, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.3 / pH: 7.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 20 / Representative conformer: 1 |