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- PDB-2dci: NMR structure of influenza HA fusion peptide mutant W14A in DPC in pH5 -
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Open data
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Basic information
Entry | Database: PDB / ID: 2dci | ||||||
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Title | NMR structure of influenza HA fusion peptide mutant W14A in DPC in pH5 | ||||||
![]() | Hemagglutinin | ||||||
![]() | VIRAL PROTEIN / HA / fusion peptide | ||||||
Function / homology | ![]() clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / 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 / membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
![]() | Tamm, L.K. / Lai, A.L. | ||||||
![]() | ![]() Title: Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity Authors: Lai, A.L. / Park, H. / White, J.M. / Tamm, L.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 152.2 KB | Display | ![]() |
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PDB format | ![]() | 106.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 341 KB | Display | ![]() |
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Full document | ![]() | 433 KB | Display | |
Data in XML | ![]() | 9.3 KB | Display | |
Data in CIF | ![]() | 16.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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: 1939.152 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: Derived from the influenza (X11) hemagglutinin HA2, residue 1-20 except the 14th residue W was replaced with A. References: UniProt: P11134 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
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Sample preparation
Details | Contents: 2mM peptide, 400mM d38-DPC, 5mM dtt, 20 mMd4-acetic acid, pH 5; 95% H2O, 5% D2O Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 0 / pH: 5 / Pressure: 1 atm / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software | Name: OPAL Developer: Luginbuhl, P., Guntert, P., Billeter, M. & Wuthrich K. Classification: refinement |
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Refinement | Method: distance geometry / Software ordinal: 1 |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 33 |