+Open data
-Basic information
Entry | Database: PDB / ID: 2kxa | ||||||
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Title | The hemagglutinin fusion peptide (H1 subtype) at pH 7.4 | ||||||
Components | Haemagglutinin HA2 CHAIN PEPTIDE | ||||||
Keywords | VIRAL PROTEIN / IMMUNE SYSTEM / fusion peptide / influenza | ||||||
Function / homology | Function and homology information viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / membrane => GO:0016020 / host cell surface receptor binding / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane Similarity search - Function | ||||||
Biological species | Influenza A virus | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Lorieau, J.L. / Louis, J.M. / Bax, A. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2010 Title: The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface. Authors: Lorieau, J.L. / Louis, J.M. / Bax, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kxa.cif.gz | 63.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kxa.ent.gz | 42 KB | Display | PDB format |
PDBx/mmJSON format | 2kxa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kx/2kxa ftp://data.pdbj.org/pub/pdb/validation_reports/kx/2kxa | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3151.596 Da / Num. of mol.: 1 Fragment: RESIDUES 1 TO 23 OF HA2 SUBUNIT (UNP Residues 345-367) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Influenza A virus / Strain: A/swine/Scotland/410440/94(H1N2) / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9YTC2 |
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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: 20mM Tris / pH: 7.4 / Pressure: ambient / Temperature: 305 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 449 / NOE intraresidue total count: 109 / NOE long range total count: 66 / NOE medium range total count: 144 / NOE sequential total count: 130 / Protein chi angle constraints total count: 4 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 18 / Protein psi angle constraints total count: 18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Average torsion angle constraint violation: 0 ° Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 60 / Conformers submitted total number: 10 / Maximum lower distance constraint violation: 1 Å / Maximum torsion angle constraint violation: 0 ° / Maximum upper distance constraint violation: 1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.031 Å |