BMRB Entry 16735

Title:
NMR resonance assignment of the apo C-terminal polypeptide of the Anthrax Lethal Factor catalytic domain
Deposition date:
2010-02-18
Original release date:
2010-05-18
Authors:
Dalkas, Georgios; Chasapis, Christos; Gkazonis, Petros; Bentrop, Detlef; Spyroulias, Georgios
Citation:

Citation: Gkazonis, Petros; Dalkas, Georgios; Chasapis, Christos; Vlamis-Gardikas, Alexios; Bentrop, Detlef; Spyroulias, Georgios. "Purification and biophysical characterization of the core protease domain of anthrax lethal factor."  Biochem. Biophys. Res. Commun. 396, 643-647 (2010).
PubMed: 20438702

Assembly members:

Assembly members:
Anthrax_LF_C-terminal, polymer, 106 residues, 12122.4 Da.

Natural source:

Natural source:   Common Name: Bacillus Anthracis   Taxonomy ID: 1392   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus Anthracis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-4T1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts88
1H chemical shifts88

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Anthrax Lethal Factor C-terminal1

Entities:

Entity 1, Anthrax Lethal Factor C-terminal 106 residues - 12122.4 Da.

1   GLYSERLYSGLYVALGLULEUARGASNASP
2   SERGLUGLYPHEILEHISGLUPHEGLYHIS
3   ALAVALASPASPTYRALAGLYTYRLEULEU
4   ASPLYSASNGLNSERASPLEUVALTHRASN
5   SERLYSLYSPHEILEASPILEPHELYSGLU
6   GLUGLYSERASNLEUTHRSERTYRGLYARG
7   THRASNGLUALAGLUPHEPHEALAGLUALA
8   PHEARGLEUMETHISSERTHRASPHISALA
9   GLUARGLEULYSVALGLNLYSASNALAPRO
10   LYSTHRPHEGLNPHEILEASNASPGLNILE
11   LYSPHEILEILEASNSER

Samples:

sample_1: Anthrax Lethal Factor, [U-98% 13C; U-98% 15N], 0.6 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAR79124 GAF01219 GAO62612 GAO68443
EMBL CAC93932 CAC93933
GB AAA22569 AAA79216 AAD32411 AAM26117 AAT28913
REF NP_052803 WP_001022096 WP_001022097 WP_001022099 WP_001022100
SP P15917
AlphaFold P15917

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