Download MendeleyModular recognition of antigens provides a mechanism that improves vaccine-elicited antibody-class frequencies
Xu, K., Liu, K., Wang, Y., Kwong, P.D.To be published.
6PDR
Vaccine-elicited murine FP-targeting antibody vFP25.18 in complex with HIV fusion peptide (residue 512-519)
- PDB DOI: https://doi.org/10.2210/pdb6PDR/pdb
- Classification: IMMUNE SYSTEM
- Organism(s): Mus musculus, Human immunodeficiency virus 1
- Expression System: Homo sapiens
- Mutation(s): No
- Deposited: 2019-06-19 Released: 2020-06-24
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.200
- R-Value Work: 0.175
- R-Value Observed: 0.176
wwPDB Validation 3D Report Full Report
This is version 1.0 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| antibody vFP25.18 light chain | A [auth L] | 219 | Mus musculus | Mutation(s): 0 |  |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| antibody vFP25.18 heavy chain | B [auth H] | 218 | Mus musculus | Mutation(s): 0 |  |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by: Sequence | 3D Structure
Entity ID: 3 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| HIV fusion peptide residue 512-519 | C [auth A] | 8 | Human immunodeficiency virus 1 | Mutation(s): 0 |  |
UniProt | |||||
Find proteins for P04578 (Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)) Explore P04578 Go to UniProtKB: P04578 | |||||
Entity Groups | |||||
| UniProt Group | P04578 | ||||
Sequence AnnotationsExpand | |||||
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Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.200
- R-Value Work: 0.175
- R-Value Observed: 0.176
- Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 128.124 | α = 90 |
| b = 51.189 | β = 114.47 |
| c = 75.258 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data scaling |
| PHENIX | refinement |
| PDB_EXTRACT | data extraction |
| HKL-2000 | data reduction |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2020-06-24 Deposition Author(s): Xu, K., Liu, K., Wang, Y., Kwong, P.D.
Revision History (Full details and data files)
- Version 1.0: 2020-06-24
Type: Initial release
