BMRB Entry 17994

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignment for inactive HIV-1 protease Bmut5
Deposition date:
2011-10-11
Original release date:
2012-06-05
Authors:
Huang, Xi; Fanucci, Gail
Citation:

Citation: Huang, Xi; Fanucci, Gail. "Backbone 1H, 13C, and 15N Chemical Shift Assignment for HIV-1 protease Variants"  Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
HIV-1_PR_Homodimer_Bmut5, polymer, 99 residues, 21115.04 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: chemical synthesis   Host organism: Escherichia coli

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts177
15N chemical shifts88
1H chemical shifts88

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-1 Protease Bmut5, chain 11
2HIV-1 Protease Bmut5, chain 21

Entities:

Entity 1, HIV-1 Protease Bmut5, chain 1 99 residues - 21115.04 Da.

1   PROGLNILETHRLEUTRPLYSARGPROLEU
2   VALTHRILELYSVALGLYGLYGLNLEULYS
3   GLUALALEULEUASNTHRGLYALAASPASP
4   THRVALILEGLUASPMETASNLEUPROGLY
5   LYSTRPLYSPROLYSMETILEGLYGLYILE
6   GLYGLYPHEILELYSVALLYSGLNTYRASP
7   GLNILEILEILEGLUILEALAGLYHISLYS
8   ALAILEGLYTHRVALLEUVALGLYPROTHR
9   PROVALASNILEILEGLYARGASNLEULEU
10   THRGLNILEGLYALATHRLEUASNPHE

Samples:

sample_1: HIV-1 PR Homodimer Bmut5, [U-100% 13C; U-100% 15N], 0.1 mM

sample_conditions_1: ionic strength: 2 mM; pH: 5.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - peak picking, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19072

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