BMRB Entry 53293

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53293

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Title:
HtrA FL
Deposition date:
2025-07-30
Original release date:
2026-01-23
Authors:
Lee, Eunjeong
Citation:

Citation: Lee, Eunjeong; Redzic, Jasmina; Gordon, Blaine; Saviola, Anthony; Tran, Norman; Maroney, Sean; Ashby, Nathanael; Shaw, Steven; Fulte, Sam; McCarty, Arianna; Holyoak, Todd; Meyer, Nancy; Hansen, Kirk; Clark, Sarah; Eisenmesser, Elan. "Streptococcus pneumoniae HtrA is a dynamic and monomeric virulence factor capable of forming larger oligomeric complexes"  Protein Sci. 35, e70411-e70411 (2026).
PubMed: 41457497

Assembly members:

Assembly members:
entity_1, polymer, 334 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: pet21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: STTQAVNKVKDAVVSVITYS ANRQNSVFGNDDTDTDSQRI SSEGSGVIYKKNDKEAYIVT NNHVINGASKVDIRLSDGTK VPGEIVGADTFSDIAVVKIS SEKVTTVAEFGDSSKLTVGE TAIAIGSPLGSEYANTVTQG IVSSLNRNVSLKSEDGQAIS TKAIQTDTAINPGNSGGPLI NIQGQVIGITSSKIATNGGT SVEGLGFAIPANDAINIIEQ LEKNGKVTRPALGIQMVNLS NVSTSDIRRLNIPSNVTSGV IVRSVQSNMPANGHLEKYDV ITKVDDKEIASSTDLQSALY NHSIGDTIKITYYRNGKEET TSIKLNKSSGDLES

Data sets:
Data typeCount
13C chemical shifts46
15N chemical shifts289
1H chemical shifts289

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HtrA FL1

Entities:

Entity 1, HtrA FL 334 residues - Formula weight is not available

1   SERTHRTHRGLNALAVALASNLYSVALLYS
2   ASPALAVALVALSERVALILETHRTYRSER
3   ALAASNARGGLNASNSERVALPHEGLYASN
4   ASPASPTHRASPTHRASPSERGLNARGILE
5   SERSERGLUGLYSERGLYVALILETYRLYS
6   LYSASNASPLYSGLUALATYRILEVALTHR
7   ASNASNHISVALILEASNGLYALASERLYS
8   VALASPILEARGLEUSERASPGLYTHRLYS
9   VALPROGLYGLUILEVALGLYALAASPTHR
10   PHESERASPILEALAVALVALLYSILESER
11   SERGLULYSVALTHRTHRVALALAGLUPHE
12   GLYASPSERSERLYSLEUTHRVALGLYGLU
13   THRALAILEALAILEGLYSERPROLEUGLY
14   SERGLUTYRALAASNTHRVALTHRGLNGLY
15   ILEVALSERSERLEUASNARGASNVALSER
16   LEULYSSERGLUASPGLYGLNALAILESER
17   THRLYSALAILEGLNTHRASPTHRALAILE
18   ASNPROGLYASNSERGLYGLYPROLEUILE
19   ASNILEGLNGLYGLNVALILEGLYILETHR
20   SERSERLYSILEALATHRASNGLYGLYTHR
21   SERVALGLUGLYLEUGLYPHEALAILEPRO
22   ALAASNASPALAILEASNILEILEGLUGLN
23   LEUGLULYSASNGLYLYSVALTHRARGPRO
24   ALALEUGLYILEGLNMETVALASNLEUSER
25   ASNVALSERTHRSERASPILEARGARGLEU
26   ASNILEPROSERASNVALTHRSERGLYVAL
27   ILEVALARGSERVALGLNSERASNMETPRO
28   ALAASNGLYHISLEUGLULYSTYRASPVAL
29   ILETHRLYSVALASPASPLYSGLUILEALA
30   SERSERTHRASPLEUGLNSERALALEUTYR
31   ASNHISSERILEGLYASPTHRILELYSILE
32   THRTYRTYRARGASNGLYLYSGLUGLUTHR
33   THRSERILELYSLEUASNLYSSERSERGLY
34   ASPLEUGLUSER

Samples:

sample_1: HtrA FL mM; D2O, [U-2H], 10%; sodium chloride 50 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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