BMRB Entry 6142

Title:
1H 13C and 15N resonance assignments for peptide deformylase-actinonin complex
Deposition date:
2004-03-05
Original release date:
2008-07-01
Authors:
LARUE, Valery; BOULAROT, Adrien; ARTAUD, Isabelle; MEINNEL, Thierry; DARDEL, Frederic
Citation:

Citation: Boularot, Adrien; Giglione, Carmela; Petit, Sylvain; Duroc, Yann; de Sousa, Rodolphe; Larue, Valery; Cresteil, Thierry; Dardel, Frederic; Artaud, Isabelle; Meinnel, Thierry. "Discovery and Refinement of a New Structural Class of Potent Peptide Deformylase Inhibitors"  J. Med. Chem. 50, 10-20 (2007).
PubMed: 17201406

Assembly members:

Assembly members:
Peptide Deformylase-actinonin complex, polymer, 147 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PTRC99A

Data sets:
Data typeCount
1H chemical shifts903
13C chemical shifts421
15N chemical shifts135

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Deformylase complex1

Entities:

Entity 1, Deformylase complex 147 residues - Formula weight is not available

1   ALAVALLEUGLNVALLEUHISILEPROASP
2   GLUARGLEUARGLYSVALALALYSPROVAL
3   GLUGLUVALASNALAGLUILEGLNARGILE
4   VALASPASPMETPHEGLUTHRMETTYRALA
5   GLUGLUGLYILEGLYLEUALAALATHRGLN
6   VALASPILEHISGLNARGILEILEVALILE
7   ASPVALSERGLUASNARGASPGLUARGLEU
8   VALLEUILEASNPROGLULEULEUGLULYS
9   SERGLYGLUTHRGLYILEGLUGLUGLYCYS
10   LEUSERILEPROGLUGLNARGALALEUVAL
11   PROARGALAGLULYSVALLYSILEARGALA
12   LEUASPARGASPGLYLYSPROPHEGLULEU
13   GLUALAASPGLYLEULEUALAILECYSILE
14   GLNHISGLUMETASPHISLEUVALGLYLYS
15   LEUPHEMETASPTYRLEUSER

Samples:

sample_1: Peptide Deformylase-actinonin complex, [U-13C; U-15N], 0.001 M; Actinonin 0.001 M

Ex-cond_1: pH: 7; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
HSQCsample_1not availableEx-cond_1
HNCAsample_1not availableEx-cond_1
HNCACBsample_1not availableEx-cond_1
CBCACONHsample_1not availableEx-cond_1
TOCSYHSQCsample_1not availableEx-cond_1
HCCH-TOCSYsample_1not availableEx-cond_1
NOESYHSQCsample_1not availableEx-cond_1

Software:

No software information available

NMR spectrometers:

  • BRUKER ADVANCE 600 MHz

Related Database Links:

BMRB 4089 5404
PDB
DBJ BAB37575 BAE78005 BAG79085 BAH66202 BAI27558
EMBL CAA11508 CAA45206 CAA54367 CAA54826 CAD09179
GB AAA58084 AAC76312 AAF76758 AAG58408 AAL22269
PIR AB1010
REF NP_289848 NP_312179 NP_417745 NP_458493 NP_462310
SP A1AGH8 A8A591 A8AQI1 A9MN80 A9N8B1
AlphaFold A1AGH8 A8A591 A8AQI1 A9MN80 A9N8B1

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