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Open data
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Basic information
Entry | Database: PDB / ID: 2kih | ||||||
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Title | S31N mutant of M2 proton channel | ||||||
![]() | Matrix protein 2 | ||||||
![]() | TRANSPORT PROTEIN / S31N / M2 / proton channel / influenza / matrix protein 2 / Cell membrane / Disulfide bond / Hydrogen ion transport / Ion transport / Ionic channel / Membrane / Transmembrane / Transport / Virion | ||||||
Function / homology | ![]() : / suppression by virus of host autophagy / : / proton transmembrane transporter activity / protein complex oligomerization / monoatomic ion channel activity / membrane => GO:0016020 / host cell plasma membrane / virion membrane / identical protein binding / membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Pielak, R.M. | ||||||
![]() | ![]() Title: Mechanism of drug inhibition and drug resistance of influenza A M2 channel. Authors: Pielak, R.M. / Schnell, J.R. / Chou, J.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 507.2 KB | Display | ![]() |
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PDB format | ![]() | 426.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 376.4 KB | Display | ![]() |
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Full document | ![]() | 618.1 KB | Display | |
Data in XML | ![]() | 29.8 KB | Display | |
Data in CIF | ![]() | 42.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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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/peptide | Mass: 5035.910 Da / Num. of mol.: 4 / Mutation: S31N,C19S,C50S Source method: isolated from a genetically manipulated source 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 | Contents: 0.8 mM [U-100% 15N] potassium phosphate, sodium azide, glutamate, rimantadine, 0.8 mM [U-100% 13C; U-100% 15N] potassium phosphate, sodium azide, glutamate, rimantadine, 0.8 mM [U-100% 13C; ...Contents: 0.8 mM [U-100% 15N] potassium phosphate, sodium azide, glutamate, rimantadine, 0.8 mM [U-100% 13C; U-100% 15N] potassium phosphate, sodium azide, glutamate, rimantadine, 0.8 mM [U-100% 13C; U-100% 15N; U-90% D2O] potassium phosphate, sodium azide, glutamate, rimantadine, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.1 / pH: 7.5 / Pressure: ambient / Temperature: 303.1 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: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 10 |