BMRB Entry 50689

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50689

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Title:
Chemical shift assignments of the Campylobacter jejuni helical cell shape determining protein Pgp2 in its apo form
Deposition date:
2021-01-04
Original release date:
2021-07-27
Authors:
Lin, Chang Sheng-Huei; McIntosh, Lawrence; Murphy, Michael
Citation:

Citation: Lin, Chang Sheng-Huei; Chan, Anson; Vermeulen, Jenny; Brockerman, Jacob; Soni, Arvind; Tanner, Martin; Gaynor, Erin; Mclntosh, Lawrence; Simorre, Jean-Pierre; Murphy, Michael. "Peptidoglycan binding by a pocket on the accessory NTF2-domain of Pgp2 directs helical cell shape of Campylobacter jejuni"  J. Biol. Chem. 296, 100528-100528 (2021).
PubMed: 33711341

Assembly members:

Assembly members:
entity_1, polymer, 287 residues, 33604 Da.

Natural source:

Natural source:   Common Name: Campylobacter jejuni   Taxonomy ID: 197   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Campylobacter jejuni

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMQKDFWLSEIGDKNISL GYYDDNVAIVLTNKTDKILR VYSYEDGKIRKDFEQKEIIT GLMGDKKIEGDLKTPVGFYE LGRKFNPGDPYYGPFAFATT YPNLLDKVQGKTGGGIWIHG YPLDGSRLDEFKTRGCIALF NNNLEKFAQVVQDKKVFVMT EEKEKIRAKKDQIASLLADL FTWKLAWTNSDTNTYLSFYD EQEFKRFDKMKFEQFASMKK SIFSRKEDKKIKFSDINISP YPNLENETMYRISFYEDYYT KNYQFRGDKILYVKIDSKGK MKILAEQ

Data sets:
Data typeCount
13C chemical shifts755
15N chemical shifts242
1H chemical shifts242

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Apo-Pgp2 monomer1

Entities:

Entity 1, Apo-Pgp2 monomer 287 residues - 33604 Da.

Residues 1-4 represent a non-native affinity tag

1   GLYSERHISMETGLNLYSASPPHETRPLEU
2   SERGLUILEGLYASPLYSASNILESERLEU
3   GLYTYRTYRASPASPASNVALALAILEVAL
4   LEUTHRASNLYSTHRASPLYSILELEUARG
5   VALTYRSERTYRGLUASPGLYLYSILEARG
6   LYSASPPHEGLUGLNLYSGLUILEILETHR
7   GLYLEUMETGLYASPLYSLYSILEGLUGLY
8   ASPLEULYSTHRPROVALGLYPHETYRGLU
9   LEUGLYARGLYSPHEASNPROGLYASPPRO
10   TYRTYRGLYPROPHEALAPHEALATHRTHR
11   TYRPROASNLEULEUASPLYSVALGLNGLY
12   LYSTHRGLYGLYGLYILETRPILEHISGLY
13   TYRPROLEUASPGLYSERARGLEUASPGLU
14   PHELYSTHRARGGLYCYSILEALALEUPHE
15   ASNASNASNLEUGLULYSPHEALAGLNVAL
16   VALGLNASPLYSLYSVALPHEVALMETTHR
17   GLUGLULYSGLULYSILEARGALALYSLYS
18   ASPGLNILEALASERLEULEUALAASPLEU
19   PHETHRTRPLYSLEUALATRPTHRASNSER
20   ASPTHRASNTHRTYRLEUSERPHETYRASP
21   GLUGLNGLUPHELYSARGPHEASPLYSMET
22   LYSPHEGLUGLNPHEALASERMETLYSLYS
23   SERILEPHESERARGLYSGLUASPLYSLYS
24   ILELYSPHESERASPILEASNILESERPRO
25   TYRPROASNLEUGLUASNGLUTHRMETTYR
26   ARGILESERPHETYRGLUASPTYRTYRTHR
27   LYSASNTYRGLNPHEARGGLYASPLYSILE
28   LEUTYRVALLYSILEASPSERLYSGLYLYS
29   METLYSILELEUALAGLUGLN

Samples:

sample_1: Pgp2, [U-13C; U-15N; U-2H with amide-1H], 350 uM; TRIS 50 mM; sodium chloride 150 mM; DTT 1 mM; H2O 95%; D2O, [U-100% 2H], 5%

sample_conditions_1: pH: 7; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

TOPSPIN v3.0 - collection

NMRFAM-SPARKY v1.413 - chemical shift assignment, data analysis, peak picking

PINE - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

Related Database Links:

NCBI EAQ72310
PDB

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