Download MendeleyLipopolysaccharide bound structure of antimicrobial peptide cecropin P1 by NMR spectroscopy
Baek, M., Kamiya, M., Kushibiki, T., Nakazumi, T., Tomisawa, S., Abe, C., Kumaki, Y., Kikukawa, T., Demura, M., Kawano, K., Aizawa, T.To be published.
2N92
Solution structure of cecropin P1 with LPS
- PDB DOI: https://doi.org/10.2210/pdb2N92/pdb
- BMRB: 25877
- Classification: ANTIMICROBIAL PROTEIN
- Organism(s): Ascaris suum
- Expression System: Escherichia coli
- Mutation(s): No
- Membrane Protein: Yes OPM
- Deposited: 2015-11-04 Released: 2016-11-09
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: target function
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 |
| Cecropin-P1 | 31 | Ascaris suum | Mutation(s): 0 Gene Names: ASCEC-1 Membrane Entity: Yes |  | |
UniProt | |||||
Find proteins for P14661 (Ascaris suum) Explore P14661 Go to UniProtKB: P14661 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P14661 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: target function
Entry History
Deposition Data
- Released Date: 2016-11-09 Deposition Author(s): Baek, M., Kamiya, M., Kushibiki, T., Nakazumi, T., Tomisawa, S., Abe, C., Kumaki, Y., Kikukawa, T., Demura, M., Kawano, K., Aizawa, T.
Revision History (Full details and data files)
- Version 1.0: 2016-11-09
Type: Initial release
