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Open data
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Basic information
Entry | Database: PDB / ID: 1hh9 | ||||||
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Title | ANTI-P24 (HIV-1) FAB FRAGMENT CB41 COMPLEXED WITH A PEPTIDE | ||||||
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![]() | IMMUNE SYSTEM/PEPTIDE / COMPLEX (ANTIBODY-PEPTIDE) / POLYSPECIFICITY / CROSSREACTIVITY / FAB-FRAGMENT / HIV-1 / IMMUNE SYSTEM-PEPTIDE complex | ||||||
Function / homology | ![]() immunoglobulin complex, circulating / immunoglobulin receptor binding / B cell differentiation / complement activation, classical pathway / antigen binding / antibacterial humoral response / blood microparticle / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() synthetic construct (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hahn, M. / Wessner, H. / Schneider-Mergener, J. / Hohne, W. | ||||||
![]() | ![]() Title: Evolutionary Transition Pathways for Changing Peptide Ligand Specificity and Structure Authors: Hoffmuller, U. / Knaute, T. / Hahn, M. / Hohne, W. / Schneider-Mergener, J. / Kramer, A. #1: ![]() Title: Crystallographic Analysis of Anti-P24 (HIV-1) Monoclonal Antibody Cross-Reactivity and Polyspecificity Authors: Keitel, T. / Kramer, A. / Wessner, H. / Scholz, C. / Schneider-Mergener, J. / Hohne, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 97.6 KB | Display | ![]() |
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PDB format | ![]() | 74.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 442.6 KB | Display | ![]() |
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Full document | ![]() | 456.4 KB | Display | |
Data in XML | ![]() | 19.3 KB | Display | |
Data in CIF | ![]() | 25.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1hh6C ![]() 1bogS S: Starting model for refinement C: citing same article ( |
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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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Components
#1: Antibody | Mass: 23928.721 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Antibody | Mass: 22669.508 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: Protein/peptide | Mass: 1185.285 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: EPITOPE-RELATED PEPTIDE / Source: (synth.) synthetic construct (others) |
#4: Water | ChemComp-HOH / |
Compound details | NH2: THE SYNTHETIC PEPTIDE HAS ITS C-TERMINAL END BLOCKED WITH AN AMIDE GROUP. |
Sequence details | THE SEQUENCE IS RELATED TO THE ENTRY 1BOG. THE TWO RESIDUES IN THIS ENTRY VALB168, VALB171 ARE ...THE SEQUENCE IS RELATED TO THE ENTRY 1BOG. THE TWO RESIDUES IN THIS ENTRY VALB168, VALB171 ARE LEU168 AND LEU171 RESPECTIVE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.7 Å3/Da / Density % sol: 71 % | ||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: HANGING DROP SET UP AT ROOM TEMPERATURE PROTEIN CONCENTRATION: 10 MG/ML RESERVOIR: 1.8 M AMMONIUM SULFATE, 0.1 M MOPS-BUFFER, PH 7.5. | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / pH: 7.5 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→16 Å / Num. obs: 24567 / % possible obs: 95.6 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 14 |
Reflection shell | Resolution: 2.7→2.8 Å / Rmerge(I) obs: 0.451 / Mean I/σ(I) obs: 2.7 / % possible all: 98.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1BOG Resolution: 2.7→16 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.7→16 Å
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Refine LS restraints |
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Xplor file |
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