BMRB Entry 26987

Title:
HIV1 protease folded and cold-denatured
Deposition date:
2017-01-03
Original release date:
2021-07-22
Authors:
Roesner, Heike; Kragelund, Birthe; Prestel, Andreas; Caldarini, Martina; Tiana, Guido; Broglia, Ricardo; Vanoni, Maria; Aliverti, Alessandro
Citation:

Citation: Roesner, Heike; Caldarini, Martina; Prestel, Andreas; Broglia, Ricardo; Vanoni, Maria; Aliverti, Alessandro; Tiana, Guido; Kragelund, Birthe. "Cold denaturation of the HIV-1 protease monomer"  Biochemistry 56, 1029-1032 (2017).
PubMed: 28168877

Assembly members:

Assembly members:
HIV1_protease_monomer, polymer, 95 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: pET11a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts259
15N chemical shifts158
1H chemical shifts158

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV1 protease monomer, folded1
2HIV1 protease monomer, unfolded1

Entities:

Entity 1, HIV1 protease monomer, folded 95 residues - Formula weight is not available

1   PROGLNILETHRLEUTRPLYSARGPROLEU
2   VALTHRILEARGILEGLYGLYGLNLEULYS
3   GLUALALEULEUASNTHRGLYALAASPASP
4   THRVALLEUGLUGLUMETASNLEUPROGLY
5   LYSTRPLYSPROLYSMETILEGLYGLYILE
6   GLYGLYPHEILELYSVALARGGLNTYRASP
7   GLNILEPROVALGLUILEALAGLYHISLYS
8   ALAILEGLYTHRVALLEUVALGLYPROTHR
9   PROVALASNILEILEGLYARGASNLEULEU
10   THRGLNILEGLYALA

Samples:

sample_1: HIV1 protease monomer, [U-13C; U-15N], 200 uM; sodium phosphate 20 mM; DSS 125 uM

sample_2: HIV1 protease monomer, [U-13C; U-15N], 200 uM; sodium phosphate 20 mM; DSS 125 uM

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 273 K

sample_conditions_2: pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2

Software:

NMRDraw, CCPN - chemical shift assignment

NMR spectrometers:

  • Agilent Avance 800 MHz
  • Varian INOVA 750 MHz

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