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Open data
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Basic information
Entry | Database: PDB / ID: 1afv | ||||||
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Title | HIV-1 CAPSID PROTEIN (P24) COMPLEX WITH FAB25.3 | ||||||
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![]() | Viral protein/Immune system / COMPLEX (VIRAL CAPSID-IMMUNOGLOBULIN) / HIV / CAPSID PROTEIN / P24 / Viral protein-Immune system COMPLEX | ||||||
Function / homology | ![]() immunoglobulin complex, circulating / immunoglobulin receptor binding / complement activation, classical pathway / antigen binding / HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration ...immunoglobulin complex, circulating / immunoglobulin receptor binding / complement activation, classical pathway / antigen binding / HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / viral penetration into host nucleus / RNA stem-loop binding / RNA-directed DNA polymerase activity / host cell / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / symbiont-mediated suppression of host gene expression / antibacterial humoral response / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / blood microparticle / symbiont entry into host cell / lipid binding / host cell nucleus / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis / DNA binding / zinc ion binding / extracellular exosome / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Momany, C. / Kovari, L.C. / Prongay, A.J. / Keller, W. / Gitti, R.K. / Lee, B.M. / Gorbalenya, A.E. / Tong, L. / Mcclure, J. / Ehrlich, L.S. ...Momany, C. / Kovari, L.C. / Prongay, A.J. / Keller, W. / Gitti, R.K. / Lee, B.M. / Gorbalenya, A.E. / Tong, L. / Mcclure, J. / Ehrlich, L.S. / Summers, M.F. / Carter, C. / Rossmann, M.G. | ||||||
![]() | ![]() Title: Crystal structure of dimeric HIV-1 capsid protein. Authors: Momany, C. / Kovari, L.C. / Prongay, A.J. / Keller, W. / Gitti, R.K. / Lee, B.M. / Gorbalenya, A.E. / Tong, L. / McClure, J. / Ehrlich, L.S. / Summers, M.F. / Carter, C. / Rossmann, M.G. #1: ![]() Title: The Use of Antibody Fragments for Crystallization and Structure Determinations Authors: Kovari, L.C. / Momany, C. / Rossmann, M.G. #2: ![]() Title: Preparation and Crystallization of a Human Immunodeficiency Virus P24-Fab Complex Authors: Prongay, A.J. / Smith, T.J. / Rossmann, M.G. / Ehrlich, L.S. / Carter, C.A. / Mcclure, J. #3: ![]() Title: Expression in Escherichia Coli and Purification of Human Immunodeficiency Virus Type 1 Capsid Protein (P24) Authors: Ehrlich, L.S. / Krausslich, H.G. / Wimmer, E. / Carter, C.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 205.1 KB | Display | ![]() |
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PDB format | ![]() | 160.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 454.1 KB | Display | ![]() |
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Full document | ![]() | 494.5 KB | Display | |
Data in XML | ![]() | 28.8 KB | Display | |
Data in CIF | ![]() | 43.2 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 16716.189 Da / Num. of mol.: 2 / Fragment: AMINO-TERMINAL DOMAIN RESIDUES 1 - 151 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Antibody | Mass: 23741.270 Da / Num. of mol.: 2 Fragment: LIGHT CHAIN RESIDUES 1 - 217, HEAVY CHAIN RESIDUES 1 - 220 Source method: isolated from a natural source / Source: (natural) ![]() ![]() #3: Antibody | Mass: 23701.412 Da / Num. of mol.: 2 Fragment: LIGHT CHAIN RESIDUES 1 - 217, HEAVY CHAIN RESIDUES 1 - 220 Source method: isolated from a natural source / Source: (natural) ![]() ![]() #4: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 Details: 16% PEG 3350, 50 MM BISTRIS-HCL, PH 7.0, 0.1% BETA-OCTYLGLUCOSIDE, 1 MM NAN3 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop / PH range low: 7.5 / PH range high: 6 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: PRINCETON 2K / Detector: CCD / Date: Dec 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.909 Å / Relative weight: 1 |
Reflection | Resolution: 3→100 Å / Num. obs: 29703 / % possible obs: 87.1 % / Observed criterion σ(I): 2 / Redundancy: 3.5 % / Rmerge(I) obs: 0.064 |
Reflection shell | Resolution: 3→3.11 Å / Rmerge(I) obs: 0.37 / % possible all: 50.4 |
Reflection shell | *PLUS % possible obs: 50.4 % |
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Processing
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Refinement | Method to determine structure: ![]() ![]() Starting model: FAB Resolution: 3.7→12 Å / Cross valid method: THROUGHOUT / σ(F): 2 Details: THE CARBOXY-TERMINAL RESIDUES 152 - 231 OF THE HIV-1 CAPSID PROTEIN ARE DISORDERED AND NOT VISIBLE IN THE ELECTRON DENSITY MAPS.
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Displacement parameters | Biso mean: 36.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.7→12 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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