BMRB Entry 52238

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52238

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Title:
Backbone 1H, 13C, and 15N assignments of the C-terminal alpha helical domain from M. Bovis lactoferrin binding receptor B.
Deposition date:
2023-12-12
Original release date:
2024-08-05
Authors:
Ostan, Nicholas; Cole, Gregory; Reichheld, Sean; Sharpe, Simon; Moraes, Trevor
Citation:

Citation: Ostan, Nicholas; Cole, Gregory; Wang, Flora Zhiqi; Reichheld, Sean; Moore, Gaelen; Pan, Chuxi; Yu, Ronghua; Lai, Christine Chieh-Lin; Sharpe, Simon; Lee, Hyun; Schryvers, Anthony; Moraes, Trevor. "A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase-separated droplets"  PNAS Nexus 3, pgae139-pgae139 (2024).
PubMed: 38633880

Assembly members:

Assembly members:
entity_1, polymer, 281 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Moraxella bovis   Taxonomy ID: 476   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Moraxella bovis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET52-b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AEQNGKIAENAETTNKSGVI SKSTKPTKDQIEFAKQKLTE KVERLKKDLSDLIATYPNSK DKSALKKQITDKVLAGYVDV KEREYAEDDLKELLNALDVA EERANATEDILNILITGDKY KTDNEDNLKEFLVQSPLVQS TTNHTQEQLAIARDKLKAQL ETEKQDLEELLATFVIGNEI LGDEDGEEIDAKELDKLKAQ IIDKIKNAYTEDKRTEVEKQ AKLLIEQLKAEDEETTAKLV EFLAKGDKFDGENMANLTAY LPALVPRGSSAHHHHHHHHH H

Data sets:
Data typeCount
13C chemical shifts421
15N chemical shifts210
1H chemical shifts223

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CaHD1

Entities:

Entity 1, CaHD 281 residues - Formula weight is not available

1   ALAGLUGLNASNGLYLYSILEALAGLUASN
2   ALAGLUTHRTHRASNLYSSERGLYVALILE
3   SERLYSSERTHRLYSPROTHRLYSASPGLN
4   ILEGLUPHEALALYSGLNLYSLEUTHRGLU
5   LYSVALGLUARGLEULYSLYSASPLEUSER
6   ASPLEUILEALATHRTYRPROASNSERLYS
7   ASPLYSSERALALEULYSLYSGLNILETHR
8   ASPLYSVALLEUALAGLYTYRVALASPVAL
9   LYSGLUARGGLUTYRALAGLUASPASPLEU
10   LYSGLULEULEUASNALALEUASPVALALA
11   GLUGLUARGALAASNALATHRGLUASPILE
12   LEUASNILELEUILETHRGLYASPLYSTYR
13   LYSTHRASPASNGLUASPASNLEULYSGLU
14   PHELEUVALGLNSERPROLEUVALGLNSER
15   THRTHRASNHISTHRGLNGLUGLNLEUALA
16   ILEALAARGASPLYSLEULYSALAGLNLEU
17   GLUTHRGLULYSGLNASPLEUGLUGLULEU
18   LEUALATHRPHEVALILEGLYASNGLUILE
19   LEUGLYASPGLUASPGLYGLUGLUILEASP
20   ALALYSGLULEUASPLYSLEULYSALAGLN
21   ILEILEASPLYSILELYSASNALATYRTHR
22   GLUASPLYSARGTHRGLUVALGLULYSGLN
23   ALALYSLEULEUILEGLUGLNLEULYSALA
24   GLUASPGLUGLUTHRTHRALALYSLEUVAL
25   GLUPHELEUALALYSGLYASPLYSPHEASP
26   GLYGLUASNMETALAASNLEUTHRALATYR
27   LEUPROALALEUVALPROARGGLYSERSER
28   ALAHISHISHISHISHISHISHISHISHIS
29   HIS

Samples:

sample_1: CaHD, [U-13C; U-15N; U-2H], 1 mM; D2O, [U-100% 2H], 10%; Sodium Phosphate 50 mM; NaCl 50 mM; glutamate 50 mM; arginine 50 mM

sample_2: CaHD, [U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; Sodium Phosphate 50 mM; NaCl 50 mM; glutamate 50 mM; arginine 50 mM

sample_3: CaHD, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; Sodium Phosphate 50 mM; NaCl 50 mM; glutamate 50 mM; arginine 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCO TROSYsample_1isotropicsample_conditions_1
3D HNcoCAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D TROSY HNcaCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
hCcoNHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC TROSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
NOESY HSQCsample_1isotropicsample_conditions_1
hCccoNHsample_1isotropicsample_conditions_1
HBHAcoHNsample_1isotropicsample_conditions_1
HSQC HBHANHsample_1isotropicsample_conditions_1
NOESY HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
HNcoCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR v2 - chemical shift assignment

NMRPipe - processing

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE III 700 MHz
  • Bruker AVANCE III HD 800 MHz

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