BMRB Entry 50391

Title:
DedD
Deposition date:
2020-07-16
Original release date:
2020-11-18
Authors:
Simorre, Jean-pierre; Kenward, Calem; Laguri, Cedric; Caveney, Nathanael; Strynadka, Natalie
Citation:

Citation: Pazos, Manuel; Peters, Katharina; Boes, Adrien; Safaei, Yalda; Kenward, Calem; Caveney, Nathanael; Laguri, Cedric; Breukink, Eefjan; Strynadka, Natalie; Simorre, Jean-Pierre; Terrak, Mohammed; Vollmer, Waldemar. "SPOR Proteins Are Required for Functionality of Class A Penicillin-Binding Proteins in Escherichia coli"  mBio 11, e02796-e02796 (2020).
PubMed: 33144379

Assembly members:

Assembly members:
entity_1, polymer, 193 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts150
1H chemical shifts839

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DedD1

Entities:

Entity 1, DedD 193 residues - Formula weight is not available

1   ASPGLYGLNLYSLYSHISTYRGLNASPGLU
2   PHEALAALAILEPROLEUVALPROLYSALA
3   GLYASPARGASPGLUPROASPMETMETPRO
4   ALAALATHRGLNALALEUPROTHRGLNPRO
5   PROGLUGLYALAALAGLUGLUVALARGALA
6   GLYASPALAALAALAPROSERLEUASPPRO
7   ALATHRILEALAALAASNASNTHRGLUPHE
8   GLUPROGLUPROALAPROVALALAPROPRO
9   LYSPROLYSPROVALGLUPROLEULYSPRO
10   LYSVALGLUALAPROPROALAPROLYSPRO
11   GLUPROLYSPROVALVALGLUGLULYSALA
12   ALAPROTHRGLYLYSALATYRVALVALGLN
13   LEUGLYALALEULYSASNALAASPLYSVAL
14   ASNGLUILEVALGLYLYSLEUARGGLYALA
15   GLYTYRARGVALTYRTHRSERPROSERTHR
16   PROVALGLNGLYLYSILETHRARGILELEU
17   VALGLYPROASPALASERLYSGLULYSLEU
18   LYSGLYSERLEUGLYGLULEULYSGLNLEU
19   SERGLYLEUSERGLYVALVALMETGLYTYR
20   THRPROASN

Samples:

sample_1: DedD, [U-99% 13C; U-99% 15N], 1.08 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CcpNMR v2.2 - chemical shift assignment

TOPSPIN - processing

NMR spectrometers:

  • Bruker AVANCE III 950 MHz

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