BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19512

Title: HIV-1 gp41 clade B double alanine mutant Membrane Proximal External Region peptide in DPC micelle   PubMed: 24075869

Deposition date: 2013-09-20 Original release date: 2013-10-08

Authors: Sun, Zhenyu; Wagner, Gerhard; Reinherz, Ellis; Kim, Mikyung; Song, Likai; Choi, Jaewon; Cheng, Yuxing; Chowdhury, Barnali; Bellot, Gaetan; Shih, William

Citation: Sun, Zhen-Yu; Cheng, Yuxing; Kim, Mikyung; Song, Likai; Choi, Jaewon; Kudahl, Ulrich; Brusic, Vladimir; Chowdhury, Barnali; Yu, Lu; Seaman, Michael; Bellot, Gaetan; Shih, William; Wagner, Gerhard; Reinherz, Ellis. "Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41."  J. Mol. Biol. 426, 1095-1108 (2014).

Assembly members:
MPER-HxB2-AA, polymer, 27 residues, 3455.994 Da.

Natural source:   Common Name: Human immunodeficiency virus type 1   Taxonomy ID: 11706   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus Human immunodeficiency virus type 1

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

Entity Sequences (FASTA):
MPER-HxB2-AA: EQELLELDKWASLWAWFAIT NWLWYIK

Data sets:
Data typeCount
13C chemical shifts142
15N chemical shifts32
1H chemical shifts223

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MPER-HxB2-AA1

Entities:

Entity 1, MPER-HxB2-AA 27 residues - 3455.994 Da.

double alanine mutation hiv-1 clade B HxB2 MPER peptide. Residues 657-661 are from gp41 CHR.

1   GLUGLNGLULEULEUGLULEUASPLYSTRP
2   ALASERLEUTRPALATRPPHEALAILETHR
3   ASNTRPLEUTRPTYRILELYS

Samples:

sample_1: MPER-HxB2-AA, [U-100% 13C; U-100% 15N], 1 mM; DPC, [U-100% 2H], 100 mM; H2O 90%; D2O 10%

sample_2: MPER-HxB2-AA, [U-100% 15N], 1 mM; DPC, [U-100% 2H], 100 mM; H2O 90%; D2O 10%

sample_3: MPER-HxB2-AA 1 mM; DPC, [U-100% 2H], 100 mM; D2O 100%

sample_4: MPER-HxB2-AA, [U-100% 13C; U-100% 15N], 1 mM; DPC, [U-100% 2H], 100 mM; DNA nanotube 20 mg/mL; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D backbonesample_1isotropicsample_conditions_1
3D C(CO)NH,H(CCO)NH,HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
2D 1H-1H NOESY,TOCSYsample_3isotropicsample_conditions_1
Q-J RDCsample_4anisotropicsample_conditions_1

Software:

NMRPipe v9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CARA v1.8.4, Rochus Keller - chemical shift assignment, data analysis, peak picking

TALOS v+, (TALOS+) Shen, Cornilescu, Delaglio and Bax - data analysis

CYANA v3.0c, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.28, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

GB AF033819
PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts