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Open data
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Basic information
| Entry | Database: PDB / ID: 2ltf | ||||||
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| Title | The solution structure of Phage P2 gpX | ||||||
Components | Tail protein X | ||||||
Keywords | VIRAL PROTEIN / LysM / phage tail | ||||||
| Function / homology | Phage Tail Protein X-like / Phage Tail Protein X / virus tail, baseplate / Baseplate protein X Function and homology information | ||||||
| Biological species | Enterobacteria phage P2 (virus) | ||||||
| Method | SOLUTION NMR / distance geometry | ||||||
| Model details | lowest energy, model 1 | ||||||
Authors | Maxwell, K.L. / Bona, D. / Chang, T.L. / Edwards, A.M. / Davidson, A.R. | ||||||
Citation | Journal: To be PublishedTitle: Structural characterization of the phage P2 baseplate Authors: Maxwell, K.L. / Hassanabad, M.F. / Chang, T. / Pirani, N. / Paul, V.D. / Bona, D. / Edwards, A.M. / Davidson, A.R. | ||||||
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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 | 2ltf.cif.gz | 473.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2ltf.ent.gz | 402 KB | Display | PDB format |
| PDBx/mmJSON format | 2ltf.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2ltf_validation.pdf.gz | 457.4 KB | Display | wwPDB validaton report |
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| Full document | 2ltf_full_validation.pdf.gz | 569.1 KB | Display | |
| Data in XML | 2ltf_validation.xml.gz | 26.6 KB | Display | |
| Data in CIF | 2ltf_validation.cif.gz | 39.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lt/2ltf ftp://data.pdbj.org/pub/pdb/validation_reports/lt/2ltf | 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 | Mass: 7591.540 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage P2 (virus) / Gene: X / Production host: ![]() |
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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 |
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| Sample conditions | Ionic strength: 200 / pH: 6.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
| NMR spectrometer |
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Processing
| NMR software | Name: CYANA / Developer: Guntert P. / Classification: refinement |
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| Refinement | Method: distance geometry / Software ordinal: 1 |
| NMR constraints | NOE constraints total: 1144 / NOE long range total count: 307 / NOE medium range total count: 264 / NOE sequential total count: 573 |
| 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: 20 |
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Enterobacteria phage P2 (virus)
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