BMRB Entry 51091

Title:
1H, 13C, and 15N Chemical Shift Assignments for Perna viridis foot protein 5b
Deposition date:
2021-09-20
Original release date:
2022-07-28
Authors:
Venturella, Francesca; Morando, Maria; Alfano, Caterina
Citation:

Citation: Morando, Maria Agnese; Venturella, Francesca; Sollazzo, Martina; Monaca, Elisa; Sabbatella, Raffaele; Vetri, Valeria; Passantino, Rosa; Pastore, Annalisa; Alfano, Caterina. "Solution structure of recombinant Pvfp-5b reveals insights into mussel adhesion"  Commun. Biol. 5, 739-739 (2022).
PubMed: 35879391

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, 9500 Da.

Natural source:

Natural source:   Common Name: Asian green mussel   Taxonomy ID: 73031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Perna viridis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts361
15N chemical shifts73
1H chemical shifts510

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pvfp5b1

Entities:

Entity 1, pvfp5b 83 residues - 9500 Da.

Residue 1 is a residual no native residue after tag removal

1   GLYVALTYRTYRPROASNPROCYSSERPRO
2   TYRPROCYSARGASNGLYGLYTHRCYSLYS
3   LYSARGGLYLEUTYRSERTYRLYSCYSTYR
4   CYSARGLYSGLYTYRTHRGLYLYSASNCYS
5   GLNTYRASNALACYSPHEPROASNPROCYS
6   LEUASNGLYGLYTHRCYSGLYTYRVALTYR
7   GLYTYRPROTYRTYRLYSCYSSERCYSPRO
8   TYRGLYTYRTYRGLYLYSGLNCYSGLNLEU
9   LYSLYSTYR

Samples:

sample_1: Pvfp5b, [U-98% 13C; U-98% 15N], 0.65 mM

sample_conditions_1: ionic strength: 0 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

ANALYSIS v2.4.2 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz
  • 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