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Open data
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Basic information
Entry | Database: PDB / ID: 7qjf | ||||||
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Title | Llp mutant C1G, lytic conversion lipoprotein of phage T5 | ||||||
![]() | Lytic conversion lipoprotein | ||||||
![]() | VIRAL PROTEIN / Phage protein / Periplasmic protein / Soluble of acylated WT protein STRUCTURE FROM UNIO / UNIO VERSION 2.9.5 | ||||||
Function / homology | negative regulation of receptor-mediated virion attachment to host cell / : / superinfection exclusion / host cell plasma membrane / Lytic conversion lipoprotein![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Degroux, S. / Mestdach, E. / Vives, C. / Le Roy, A. / Salmon, L. / Herrman, T. / Breyton, C. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Llp mutant C1G, lytic conversion lipoprotein of phage T5 Authors: Degroux, S. / Mestdach, E. / Vives, C. / Le Roy, A. / Salmon, L. / Herrman, T. / Breyton, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 372.7 KB | Display | ![]() |
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PDB format | ![]() | 312.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 399.6 KB | Display | ![]() |
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Full document | ![]() | 520.7 KB | Display | |
Data in XML | ![]() | 22 KB | Display | |
Data in CIF | ![]() | 37.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 7052.991 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Mutated version of the lytic conversion lipoprotein produced from a MBP-Llp fusion protein with TEV cleavage site. The mature protein results in the same protein sequence as the WT protein, ...Details: Mutated version of the lytic conversion lipoprotein produced from a MBP-Llp fusion protein with TEV cleavage site. The mature protein results in the same protein sequence as the WT protein, with a Glycine in amino acide +1 in place of the acylated cysteine. Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 25 mM no Tris, 75 mM no NaCl, 1.024 mM 13C 15N Sol-Llp, 90% H2O/10% D2O Details: Sol-Llp protein is soluble and the buffer is 25 mM Tris pH6.5, 75 mM NaCL. Label: 15N_C13_Sol-Llp / Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 75 mM / Label: 15N_C13_Sol-Llp / pH: 6.5 / Pressure: 1 atm / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 4 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 80 / Conformers submitted total number: 20 |