BMRB Entry 30503

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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/BMR30503
MolProbity Validation Chart

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Title:
MPER-TM Domain of HIV-1 envelope glycoprotein (Env)
Deposition date:
2018-07-31
Original release date:
2018-08-31
Authors:
Fu, Q.; Shaik, M.; Cai, Y.; Ghantous, F.; Piai, A.; Peng, H.; Rits-Volloch, S.; Liu, Z.; Harrison, S.; Seaman, M.; Chen, B.; Chou, J.
Citation:

Citation: Fu, Q.; Shaik, M.; Cai, Y.; Ghantous, F.; Piai, A.; Peng, H.; Rits-Volloch, S.; Liu, Z.; Harrison, S.; Seaman, M.; Chen, B.; Chou, J.. "Structure of the membrane proximal external region of HIV-1 envelope glycoprotein"  Proc. Natl. Acad. Sci. U.S.A. 115, E8892-E8899 (2018).
PubMed: 30185554

Assembly members:

Assembly members:
entity_1, polymer, 51 residues, 6179.373 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   Vector: pMM - LR6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LLELDKWASLWNWFDITNWL WYIRIFIIIVGSLIGLRIVF AVLSLVNRVRQ

Data sets:
Data typeCount
13C chemical shifts88
15N chemical shifts49
1H chemical shifts49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21
3entity_1, 31

Entities:

Entity 1, entity_1, 1 51 residues - 6179.373 Da.

1   LEULEUGLULEUASPLYSTRPALASERLEU
2   TRPASNTRPPHEASPILETHRASNTRPLEU
3   TRPTYRILEARGILEPHEILEILEILEVAL
4   GLYSERLEUILEGLYLEUARGILEVALPHE
5   ALAVALLEUSERLEUVALASNARGVALARG
6   GLN

Samples:

sample_1: DMPC 50 mM; DHPC 100 mM; Envelope glycoprotein gp160, 15N, 2H,

sample_2: DMPC 50 mM; DHPC 100 mM; Envelope glycoprotein gp160, [U-13C; U-15N; U-2H],

sample_3: DMPC, [U-99% 2H], 50 mM; DHPC, [U-99% 2H], 100 mM; Envelope glycoprotein gp160, [U-100% 13C; U-100% 15N],

sample_4: DMPC, [U-99% 2H], 50 mM; DHPC, [U-99% 2H], 100 mM; Envelope glycoprotein gp160, 15N, 2H mixed with 13C(15%),

sample_5: DMPC, [U-99% 2H], 50 mM; DHPC, [U-99% 2H], 100 mM; Envelope glycoprotein gp160, 15N, 2H mixed with 13C,

sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N Trosy HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-15N NOESY tr-HSQCsample_3isotropicsample_conditions_1
3D Jch Modulated 1H-15N NOESYsample_5isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
3D 1H-15N NOESY tr-HSQCsample_4isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

X-PLOR NIH v2.48, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceII 800 MHz
  • Bruker AvanceIII 900 MHz
  • Bruker AvanceII 600 MHz

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