BMRB Entry 36730

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36730
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution NMR structure of the rosin A1 lanthipeptide
Deposition date:
2025-02-20
Original release date:
2026-03-26
Authors:
Yao, H.; Xie, X.; Wang, H.
Citation:

Citation: Xie, Xiang-Qian; Guo, Wen; Xia, Yin-Zheng; Liao, Li-Juan; Sun, Meng-Xin; Wang, Jing-Xue; Gao, Jiang-Tao; Yao, Hong-Wei; Wang, Huan. "A Unique Class of Cyclases with a Kinase Fold Catalyzes Enethiol-Mediated Macrocyclization of Aminovinyl-Cysteine Motifs in Lanthipeptides."  ACS Cent. Sci. 11, 1178-1188 (2025).
PubMed: 40726796

Assembly members:

Assembly members:
rosin A1, polymer, 25 residues, 2353.759 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 58117   Superkingdom: not available   Kingdom: Bacillati   Genus/species: Microbispora rosea

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Streptomyces lividans TK24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rosin A1: XXPXLXXAVCAXAVXVXVAX WYYGX

Data sets:
Data typeCount
13C chemical shifts102
15N chemical shifts22
1H chemical shifts145

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 25 residues - 2353.759 Da.

1   2KTDBUPRODBULEUDALDBUALAVALCYS
2   ALADALALAVALDALVALDBUVALALADBB
3   TRPTYRTYRGLYTEE

Samples:

sample_1: rosinA1 1 mM; CD3OH 100%

sample_conditions_1: ionic strength: 0 Not defined; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HMBCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - chemical shift assignment

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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