BMRB Entry 52394

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52394

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Title:
1H, 13C, and 15N Amide Backbone Chemical Shift Assignments for Lcl-CTD
Deposition date:
2024-04-13
Original release date:
2024-04-23
Authors:
Portlock, Theo; Garnett, James
Citation:

Citation: Rehman, Saima; Antonovic, Anna Katarina; McIntire, Ian; Zheng, Huaixin; Cleaver, Leanne; Baczynska, Maria; Adams, Carlton; Portlock, Theo; Richardson, Katherine; Shaw, Rosie; Oregioni, Alain; Mastroianni, Giulia; Whittaker, Sara B-M; Kelly, Geoff; Lorenz, Christian; Fornili, Arianna; Cianciotto, Nicholas; Garnett, James. "The Legionella collagen-like protein employs a distinct binding mechanism for the recognition of host glycosaminoglycans"  Nat. Commun. 15, 4912-4912 (2024).
PubMed: 38851738

Assembly members:

Assembly members:
entity_1, polymer, 401 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Legionella pneumoniae   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: Legionella pneumoniae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET46 Ek/LIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KSNPASQAYVDGKVSELKNE LTNKINSIPSGPQGPRGDKG EAGPKGDRGEAGPQGLPGPK GDRGEAGPQGLPGPKGDRGE AGPQGLPGPKGDRGEAGPQG LPGPKGDRGEAGPQGLPGPQ GLPGPKGDKGEAGPQGLPGP KGDKGEAGPQGLPGPKGDKG EAGAVGPQGMPGPKGDKGEA GPQGLPGPKGDRGEAGPQGL PGPKGDRGEAGPQGLPGPKG DKGETGAVGPQGMPGPKGEA GDDGQGVPAGGETGQVLAKS NDLDFNTMWVDPANSGIRRQ LGDKALGGTVIYVNALGTHG LVVANSDQVNSNTWWDAQDS ITNPAHFDNEGKLYSDWRLP TRFELNLIYMMRNELGNFLA GNYWSSIEKSSANSWVFNSK TGEIKDIAKSKTAAVRAVRA F

Data sets:
Data typeCount
13C chemical shifts253
15N chemical shifts92
1H chemical shifts92

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Lcl C-terminal domain1

Entities:

Entity 1, Lcl C-terminal domain 401 residues - Formula weight is not available

1   LYSSERASNPROALASERGLNALATYRVAL
2   ASPGLYLYSVALSERGLULEULYSASNGLU
3   LEUTHRASNLYSILEASNSERILEPROSER
4   GLYPROGLNGLYPROARGGLYASPLYSGLY
5   GLUALAGLYPROLYSGLYASPARGGLYGLU
6   ALAGLYPROGLNGLYLEUPROGLYPROLYS
7   GLYASPARGGLYGLUALAGLYPROGLNGLY
8   LEUPROGLYPROLYSGLYASPARGGLYGLU
9   ALAGLYPROGLNGLYLEUPROGLYPROLYS
10   GLYASPARGGLYGLUALAGLYPROGLNGLY
11   LEUPROGLYPROLYSGLYASPARGGLYGLU
12   ALAGLYPROGLNGLYLEUPROGLYPROGLN
13   GLYLEUPROGLYPROLYSGLYASPLYSGLY
14   GLUALAGLYPROGLNGLYLEUPROGLYPRO
15   LYSGLYASPLYSGLYGLUALAGLYPROGLN
16   GLYLEUPROGLYPROLYSGLYASPLYSGLY
17   GLUALAGLYALAVALGLYPROGLNGLYMET
18   PROGLYPROLYSGLYASPLYSGLYGLUALA
19   GLYPROGLNGLYLEUPROGLYPROLYSGLY
20   ASPARGGLYGLUALAGLYPROGLNGLYLEU
21   PROGLYPROLYSGLYASPARGGLYGLUALA
22   GLYPROGLNGLYLEUPROGLYPROLYSGLY
23   ASPLYSGLYGLUTHRGLYALAVALGLYPRO
24   GLNGLYMETPROGLYPROLYSGLYGLUALA
25   GLYASPASPGLYGLNGLYVALPROALAGLY
26   GLYGLUTHRGLYGLNVALLEUALALYSSER
27   ASNASPLEUASPPHEASNTHRMETTRPVAL
28   ASPPROALAASNSERGLYILEARGARGGLN
29   LEUGLYASPLYSALALEUGLYGLYTHRVAL
30   ILETYRVALASNALALEUGLYTHRHISGLY
31   LEUVALVALALAASNSERASPGLNVALASN
32   SERASNTHRTRPTRPASPALAGLNASPSER
33   ILETHRASNPROALAHISPHEASPASNGLU
34   GLYLYSLEUTYRSERASPTRPARGLEUPRO
35   THRARGPHEGLULEUASNLEUILETYRMET
36   METARGASNGLULEUGLYASNPHELEUALA
37   GLYASNTYRTRPSERSERILEGLULYSSER
38   SERALAASNSERTRPVALPHEASNSERLYS
39   THRGLYGLUILELYSASPILEALALYSSER
40   LYSTHRALAALAVALARGALAVALARGALA
41   PHE

Samples:

sample_1: Lcl C-terminal domain, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; HEPES 20 mM; NaCl 50 mM; EDTA 5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRView - chemical shift assignment

NMR spectrometers:

  • Bruker, Oxford Instruments Avance III HD 900 MHz MHz

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