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- PDB-1qr9: INHIBITION OF HIV-1 INFECTIVITY BY THE GP41 CORE: ROLE OF A CONSE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qr9 | ||||||
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Title | INHIBITION OF HIV-1 INFECTIVITY BY THE GP41 CORE: ROLE OF A CONSERVED HYDROPHOBIC CAVITY IN MEMBRANE FUSION | ||||||
![]() | GP41 ENVELOPE PROTEIN | ||||||
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Function / homology | ![]() host cell plasma membrane / virion membrane / structural molecule activity / ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ji, H. / Shu, W. / Burling, F.T. / Jiang, S.B. / Lu, M. | ||||||
![]() | ![]() Title: Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusion. Authors: Ji, H. / Shu, W. / Burling, F.T. / Jiang, S. / Lu, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 24.9 KB | Display | ![]() |
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PDB format | ![]() | 16.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 7837.673 Da / Num. of mol.: 1 / Fragment: SUBDOMAIN N34(L6)C28 / Mutation: L568A / Source method: isolated from a natural source / Source: (natural) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.82 Å3/Da / Density % sol: 32.55 % | |||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: SODIUM ACETATE, AMMONIUM SULFATE, GLYCEROL, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||
Crystal grow | *PLUS | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 20, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.6→15 Å / Num. all: 7043 / Num. obs: 7043 / % possible obs: 96.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 21 Å2 / Rmerge(I) obs: 0.034 / Net I/σ(I): 33.4 |
Reflection shell | Resolution: 1.6→1.66 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.138 / % possible all: 69.1 |
Reflection | *PLUS Lowest resolution: 30 Å / Num. measured all: 29806 / Rmerge(I) obs: 0.036 |
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Processing
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Refinement | Resolution: 1.6→15 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER
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Displacement parameters | Biso mean: 21.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→15 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 21.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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