BMRB Entry 5062

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignment for Unfolded HIV-1 protease tethered dimer
Deposition date:
2001-06-19
Original release date:
2002-01-23
Authors:
Bhavesh, Neel; Panchal, Sanjay; Mittal, Rohit; Hosur, Ramkrishna
Citation:

Citation: Bhavesh, Neel; Panchal, Sanjay; Mittal, Rohit; Hosur, Ramkrishna. "NMR Identification of local Structural Preferences in HIV-I Protease Tethered Heterodimer in 6 M Guanidine Hydrochloride"  FEBS Lett. 509, 218-224 (2001).
PubMed: 11741592

Assembly members:

Assembly members:
HIV-1 protease, polymer, 203 residues, 21971 Da.

Natural source:

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus Lentivirus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11a

Data sets:
Data typeCount
13C chemical shifts569
15N chemical shifts191
1H chemical shifts190

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-1 protease1

Entities:

Entity 1, HIV-1 protease 203 residues - 21971 Da.

1   PROGLNVALTHRLEUTRPGLNARGPROLEU
2   VALTHRILELYSILEGLYGLYGLNLEULYS
3   GLUALALEULEUASPTHRGLYALAASPASP
4   THRVALLEUGLUGLUMETSERLEUPROGLY
5   ARGTRPLYSPROLYSMETILEGLYGLYILE
6   GLYGLYPHEILELYSVALARGGLNTYRASP
7   GLNILELEUILEGLUILECYSALAHISLYS
8   ALAILEGLYTHRVALLEUVALGLYPROTHR
9   PROVALASNILEILEGLYARGASNLEULEU
10   THRGLNILEGLYMETTHRLEUASNPHEGLY
11   GLYSERSERGLYPROGLNVALTHRLEUTRP
12   GLNARGPROLEUVALTHRILELYSILEGLY
13   GLYGLNLEULYSGLUALALEULEUASPTHR
14   GLYALAASPASPTHRVALLEUGLUGLUMET
15   SERLEUPROGLYARGTRPLYSPROLYSMET
16   ILEGLYGLYILEGLYGLYPHEILELYSVAL
17   ARGGLNTYRASPGLNILELEUILEGLUILE
18   CYSALAHISLYSALAILEGLYTHRVALLEU
19   VALGLYPROTHRPROVALASNILEILEGLY
20   ARGASNLEULEUTHRGLNILEGLYALATHR
21   LEUASNPHE

Samples:

sample_1: HIV-1 protease, [U-95% 13C; U-90% 15N], 1.2 mM; guanidine hydrochloride 6 M

cond_1: pH: 5.2; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
Two new pulse sequences HNN, HN(C)N were used to get HN, NH assignmentssample_1not availablecond_1
in this poorly amide proton dispersed spectra in unfolded condition.sample_1not availablecond_1

Software:

FELIX v97 -

NMR spectrometers:

  • Varian UNITYplus 600 MHz

Related Database Links:

BMRB 4356
PDB

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