BMRB Entry 52395

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52395

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Title:
Complete 1H, 13C, and 15N Chemical Shift Assignments for Lcl collagen-like repeat (CLR) peptide
Deposition date:
2024-04-13
Original release date:
2024-04-23
Authors:
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, 21 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XEAGPQGLPGPKGDRGEAGP X

Data sets:
Data typeCount
13C chemical shifts52
15N chemical shifts17
1H chemical shifts115

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lcl-CLR1

Entities:

Entity 1, Lcl-CLR 21 residues - Formula weight is not available

1   ACEGLUALAGLYPROGLNGLYLEUPROGLY
2   PROLYSGLYASPARGGLYGLUALAGLYPRO
3   NH2

Samples:

sample_1: Lcl-CLR 3 mM; HEPES 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-13C TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H ROESYsample_1isotropicsample_conditions_1

Software:

ANALYSIS - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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