BMRB Entry 5967

Title:
Solution structure of the mature HIV-1 protease monomer
Deposition date:
2003-10-13
Original release date:
2004-05-15
Authors:
Ishima, R.; Torchia, D.; Lynch, S.; Gronenborn, A.; Louis, J.
Citation:

Citation: Ishima, R.; Torchia, D.; Lynch, S.; Gronenborn, A.; Louis, J.. "Solution structure of the mature HIV-1 protease monomer: Insight into the tertiary fold and stability of a precursor "  J. Biol. Chem. 278, 43311-43319 (2003).
PubMed: 12933791

Assembly members:

Assembly members:
HIV-1 protease (E.C.3.4.23.16), 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: chemical synthesis

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts89
13C chemical shifts175
15N chemical shifts89

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-1 protease1

Entities:

Entity 1, HIV-1 protease 95 residues - Formula weight is not available

1   PROGLNILETHRLEUTRPLYSARGPROLEU
2   VALTHRILELYSILEGLYGLYGLNLEULYS
3   GLUALALEULEUASPTHRGLYALAASPASP
4   THRVALILEGLUGLUMETSERLEUPROGLY
5   ARGTRPLYSPROLYSMETILEGLYGLYILE
6   GLYGLYPHEILELYSVALARGGLNTYRASP
7   GLNILEILEILEGLUILEALAGLYHISLYS
8   ALAILEGLYTHRVALLEUVALGLYPROTHR
9   PROVALASNILEILEGLYARGASNLEULEU
10   THRGLNILEGLYALA

Samples:

sample_1: HIV-1 protease (E.C.3.4.23.16), [U-13C; U-15N], 0.5 mM; phosphate buffer 20 mM; D2O 5%; H2O 95%

sample_cond_1: pH: 5.8 na; temperature: 293 K; ionic strength: 20 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available

Software:

XWINNMR v2.6 - collection

NMRPipe - data analysis

X-PLOR v1.0.6 - structure solution, refinement

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

BMRB 16416
PDB

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