BMRB Entry 30855

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30855
MolProbity Validation Chart

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Title:
Structure of the HIV-1 gp41 transmembrane domain and cytoplasmic tail
Deposition date:
2021-02-10
Original release date:
2021-04-23
Authors:
Piai, A.; Fu, Q.; Sharp, A.; Bighi, B.; Brown, A.; Chou, J.
Citation:

Citation: Piai, A.; Fu, Q.; Sharp, A.; Bighi, B.; Brown, A.; Chou, J.. "NMR Model of the Entire Membrane-Interacting Region of the HIV-1 Fusion Protein and Its Perturbation of Membrane Morphology"  J. Am. Chem. Soc. 143, 6609-6615 (2021).
PubMed: 33882664

Assembly members:

Assembly members:
entity_1, polymer, 180 residues, 20846.182 Da.

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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NWLWYIRIFIIIVGSLIGLR IVFAVLSLVNRVRQGYSPLS FQTHLPTPRGPDRPEGIEEE GGERDRDRSIRLVNGSLALI WDDLRSLSLFSYHRLRDLLL IVTRIVELLGRRGWEALKYW WNLLQYWSQELKNSAVSLLN ATAIAVGEGTDRVIEVVQGA SRAIRHIPRRIRQGLERILL

Data sets:
Data typeCount
13C chemical shifts301
15N chemical shifts147
1H chemical shifts147

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_21
3unit_31

Entities:

Entity 1, unit_1 180 residues - 20846.182 Da.

1   ASNTRPLEUTRPTYRILEARGILEPHEILE
2   ILEILEVALGLYSERLEUILEGLYLEUARG
3   ILEVALPHEALAVALLEUSERLEUVALASN
4   ARGVALARGGLNGLYTYRSERPROLEUSER
5   PHEGLNTHRHISLEUPROTHRPROARGGLY
6   PROASPARGPROGLUGLYILEGLUGLUGLU
7   GLYGLYGLUARGASPARGASPARGSERILE
8   ARGLEUVALASNGLYSERLEUALALEUILE
9   TRPASPASPLEUARGSERLEUSERLEUPHE
10   SERTYRHISARGLEUARGASPLEULEULEU
11   ILEVALTHRARGILEVALGLULEULEUGLY
12   ARGARGGLYTRPGLUALALEULYSTYRTRP
13   TRPASNLEULEUGLNTYRTRPSERGLNGLU
14   LEULYSASNSERALAVALSERLEULEUASN
15   ALATHRALAILEALAVALGLYGLUGLYTHR
16   ASPARGVALILEGLUVALVALGLNGLYALA
17   SERARGALAILEARGHISILEPROARGARG
18   ILEARGGLNGLYLEUGLUARGILELEULEU

Samples:

sample_1: HIV1 gp41 TMD-CT, [U-100% 13C; U-100% 15N; U-85% 2H], 1.2 mM; DMPC 40 mM; DHPC 80 mM; MES 40 mM; sodium azide 1%

sample_2: HIV1 gp41 TMD-CT, [ILV-100% 13C; U-100% 15N; U-85% 2H], 1 mM; DMPC 40 mM; DHPC 80 mM; MES 40 mM; sodium azide 1%

sample_conditions_1: ionic strength: 0 M; pH: 6.7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY HSQCsample_1isotropicsample_conditions_1
3D TROSY HNCOsample_1isotropicsample_conditions_1
3D TROSY HNCAsample_1isotropicsample_conditions_1
2D 1H-15N TROSY HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 15N-edited NOESY-TROSY-HSQCsample_2isotropicsample_conditions_1
3D 13C-edited NOESYsample_2isotropicsample_conditions_1
3D 15N-edited TROSY-NOESY-TROSY-HSQCsample_2isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

CARA, Keller and Wuthrich - peak picking

XEASY, Bartels et al. - peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE III 900 MHz

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