BMRB Entry 30682

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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/BMR30682
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Title:
Structure of acrorhagin I from the sea anemone Actinia equina
Deposition date:
2019-11-06
Original release date:
2020-11-13
Authors:
Krishnarjuna, B.; Sunanda, P.; Norton, R.
Citation:

Citation: Krishnarjuna, Bankala; Sunanda, Punnepalli; Villegas-Moreno, Jessica; Csoti, Agota; A V Morales, Rodrigo; Wai, Dorothy; Panyi, Gyorgy; Prentis, Peter; Norton, Raymond. "A disulfide-stabilised helical hairpin fold in acrorhagin I: An emerging structural motif in peptide toxins"  J. Struct. Biol. 213, 107692-107692 (2021).
PubMed: 33387653

Assembly members:

Assembly members:
entity_1, polymer, 50 residues, 5672.312 Da.

Natural source:

Natural source:   Common Name: Beadlet anemone   Taxonomy ID: 6106   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Actinia equina

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SSTPDGTWVKCRHDCFTKYK SCQMSDSCHDEQSCHQCHVK HTDCVNTGCP

Data sets:
Data typeCount
13C chemical shifts188
15N chemical shifts52
1H chemical shifts296

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 50 residues - 5672.312 Da.

1   SERSERTHRPROASPGLYTHRTRPVALLYS
2   CYSARGHISASPCYSPHETHRLYSTYRLYS
3   SERCYSGLNMETSERASPSERCYSHISASP
4   GLUGLNSERCYSHISGLNCYSHISVALLYS
5   HISTHRASPCYSVALASNTHRGLYCYSPRO

Samples:

sample_1: acrorhagin I, [U-13C; U-15N], 0.5 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

CcpNmr Analysis, CCPN - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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