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Yorodumi- PDB-2lm7: NMR structure of the C-terminal domain of VP7 in membrane mimicki... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lm7 | ||||||
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Title | NMR structure of the C-terminal domain of VP7 in membrane mimicking micelles | ||||||
Components | Outer capsid glycoprotein VP7 | ||||||
Keywords | VIRAL PROTEIN / alpha helix / amphipathic / perforating peptide | ||||||
Function / homology | Function and homology information host cell endoplasmic reticulum lumen / T=13 icosahedral viral capsid / viral outer capsid / viral process / metal ion binding Similarity search - Function | ||||||
Biological species | Rotavirus A | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Elaid, S. / Libersou, S. / Ouldali, M. / Morellet, N. / Lepault, J. / Bouaziz, S. | ||||||
Citation | Journal: To be Published Title: NMR structure of the C-terminal domain of VP7 in membrane mimicking micelles Authors: Elaid, S. / Libersou, S. / Ouldali, M. / Rhayyat, R. / Henry, C. / Morellet, N. / Lepault, J. / Bouaziz, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lm7.cif.gz | 167.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lm7.ent.gz | 137.9 KB | Display | PDB format |
PDBx/mmJSON format | 2lm7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lm7_validation.pdf.gz | 368.8 KB | Display | wwPDB validaton report |
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Full document | 2lm7_full_validation.pdf.gz | 391.5 KB | Display | |
Data in XML | 2lm7_validation.xml.gz | 10.3 KB | Display | |
Data in CIF | 2lm7_validation.cif.gz | 15.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lm/2lm7 ftp://data.pdbj.org/pub/pdb/validation_reports/lm/2lm7 | HTTPS FTP |
-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 | Mass: 7341.409 Da / Num. of mol.: 1 / Fragment: UNP residues 266-326 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rotavirus A / Strain: isolate Human/Belgium/4106/2000 G3-P11[14] / References: UniProt: Q3ZK60 |
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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: 1 mM VP7-61-1, 100 mM [U-100% 2H] DPC-2, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 3 / Pressure: ambient / Temperature: 323 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||
NMR constraints | NOE constraints total: 1210 / NOE intraresidue total count: 879 / NOE long range total count: 0 / NOE medium range total count: 119 / NOE sequential total count: 212 | ||||||||||||
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: 8 |