BMRB Entry 15605
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15605
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Title: HIV-1 gp41 Membrane Proximal Ectodomain Region peptide in DPC micelle PubMed: 18191596
Deposition date: 2007-12-26 Original release date: 2008-01-18
Authors: Sun, Z.; Oh, K.; Kim, M.; Reinherz, E.; Wagner, G.
Citation: Sun, Zhen-Yu; Oh, Kyoung; Kim, Mikyung; Yu, Jessica; Brusic, Vladimir; Song, Likai; Qiao, Zhisong; Wang, Jia-huai; Wagner, Gerhard; Reinherz, Ellis. "HIV-1 Broadly Neutralizing Antibody Extracts Its Epitope from a Kinked gp41 Ectodomain Region on the Viral Membrane" Immunity 28, 52-63 (2008).
Assembly members:
mper, polymer, 22 residues, Formula weight is not available
Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
mper: ELDKWASLWNWFNITNWLWY
IK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 118 |
15N chemical shifts | 28 |
1H chemical shifts | 142 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Envelope glycoprotein | 1 |
Entities:
Entity 1, Envelope glycoprotein 22 residues - Formula weight is not available
1 | GLU | LEU | ASP | LYS | TRP | ALA | SER | LEU | TRP | ASN | ||||
2 | TRP | PHE | ASN | ILE | THR | ASN | TRP | LEU | TRP | TYR | ||||
3 | ILE | LYS |
Samples:
sample_1: mper, [U-100% 13C; U-100% 15N], 1 mM; DPC-d38 100 mM
sample_2: mper, [U-100% 15N], 1 mM; DPC-d38 100 mM
sample_3: mper 1 mM; DPC-d38 100 mM
sample_conditions_1: ionic strength: 0 mM; pH: 6.6; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
triple resonance backbone experiments | sample_1 | isotropic | sample_conditions_1 |
3D_13C-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
3D_15N-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
2D NOESY | sample_3 | isotropic | sample_conditions_1 |
HNHA | sample_2 | isotropic | sample_conditions_1 |
HNHB | sample_2 | isotropic | sample_conditions_1 |
3D_15N-separated N(H)-NH NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
PROSA v6.0, Guntert - processing
CARA v1.8.2, Keller - data analysis
CYANA v2.1, Guntert - structure solution
X-PLOR vxplor-nih-2.9.7, Brunger, Schwieters - structure solution
TALOS v2003.027.13.05, Cornilescu - data analysis
NMR spectrometers:
- Bruker AVANCE 750 MHz
- Bruker AVANCE 600 MHz
- Bruker AVANCE 500 MHz
- Varian INOVA 600 MHz
Related Database Links:
BMRB | 18237 19215 19262 19263 |
PDB | |
DBJ | BAA12995 BAA13003 BAD66665 BAF34648 BAH97413 |
EMBL | CAA25903 CAA77628 CAD10137 CAD20942 |
GB | AAA44073 AAA44205 AAA44221 AAA44661 AAA44679 |
PIR | VCLJSC |
PRF | 1102247A |
REF | NP_057856 NP_579895 |
SP | P03375 P03377 P04578 P04582 P04624 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts