BMRB Entry 15605

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15605

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
HIV-1 gp41 Membrane Proximal Ectodomain Region peptide in DPC micelle
Deposition date:
2007-12-26
Original release date:
2008-01-18
Authors:
Sun, Z.; Oh, K.; Kim, M.; Reinherz, E.; Wagner, G.
Citation:

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).
PubMed: 18191596

Assembly members:

Assembly members:
mper, polymer, 22 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mper: ELDKWASLWNWFNITNWLWY IK

Data sets:
Data typeCount
13C chemical shifts118
15N chemical shifts28
1H chemical shifts142

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Envelope glycoprotein1

Entities:

Entity 1, Envelope glycoprotein 22 residues - Formula weight is not available

1   GLULEUASPLYSTRPALASERLEUTRPASN
2   TRPPHEASNILETHRASNTRPLEUTRPTYR
3   ILELYS

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:

NameSampleSample stateSample conditions
triple resonance backbone experimentssample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
2D NOESYsample_3isotropicsample_conditions_1
HNHAsample_2isotropicsample_conditions_1
HNHBsample_2isotropicsample_conditions_1
3D_15N-separated N(H)-NH NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_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
AlphaFold P03375 P03377 P04578 P04582 P04624

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks