BMRB Entry 19263
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19263
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Title: NMR assignment and structure of a peptide derived from the membrane proximal external region of HIV-1 gp41 in DPC
Deposition date: 2013-05-23 Original release date: 2014-01-21
Authors: Serrano, Soraya; Huarte, Nerea; Nieva, Jose; Jimenez, M. Angeles
Citation: Serrano, Soraya; Araujo, Aitziber; Apellaniz, Beatriz; de la Arada, Igor; Huarte, Nerea; Arrondo, Jose; Jimenez, M. Angeles; Nieva, Jose. "Structure and immunogenicity of a peptide vaccine based on the membrane proximal external region of HIV-1 gp41" Not known ., .-..
Assembly members:
MPERp, polymer, 28 residues, 3656.148 Da.
Natural source: Common Name: HIV Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus Human Immunodeficiency Virus 1
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
MPERp: NEQELLELDKWASLWNWFNI
TNWLWYIK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 7 |
1H chemical shifts | 229 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MPERp-1 | 1 |
Entities:
Entity 1, MPERp-1 28 residues - 3656.148 Da.
The sequence corresponds to residues 656-683 of HIV-1 Env protein (BH10 isolate)
1 | ASN | GLU | GLN | GLU | LEU | LEU | GLU | LEU | ASP | LYS | ||||
2 | TRP | ALA | SER | LEU | TRP | ASN | TRP | PHE | ASN | ILE | ||||
3 | THR | ASN | TRP | LEU | TRP | TYR | ILE | LYS |
Samples:
sample_1: MPERp 0.5 mM; H2O 90%; D2O, [U-100% 2H], 10%; DPC, [U-99% 2H], 20 mM; HEPES 2 mM; DSS 0.1 mM
sample_conditions_1: ionic strength: 2 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker Avance 600 MHz