BMRB Entry 51091
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51091
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H, 13C, and 15N Chemical Shift Assignments for Perna viridis foot protein 5b PubMed: 35879391
Deposition date: 2021-09-20 Original release date: 2022-07-28
Authors: Venturella, Francesca; Morando, Maria; Alfano, Caterina
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).
Assembly members:
entity_1, polymer, 83 residues, 9500 Da.
Natural source: Common Name: Asian green mussel Taxonomy ID: 73031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Perna viridis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET
Entity Sequences (FASTA):
entity_1: GVYYPNPCSPYPCRNGGTCK
KRGLYSYKCYCRKGYTGKNC
QYNACFPNPCLNGGTCGYVY
GYPYYKCSCPYGYYGKQCQL
KKY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 361 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 510 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | pvfp5b | 1 |
Entities:
Entity 1, pvfp5b 83 residues - 9500 Da.
Residue 1 is a residual no native residue after tag removal
| 1 | GLY | VAL | TYR | TYR | PRO | ASN | PRO | CYS | SER | PRO | ||||
| 2 | TYR | PRO | CYS | ARG | ASN | GLY | GLY | THR | CYS | LYS | ||||
| 3 | LYS | ARG | GLY | LEU | TYR | SER | TYR | LYS | CYS | TYR | ||||
| 4 | CYS | ARG | LYS | GLY | TYR | THR | GLY | LYS | ASN | CYS | ||||
| 5 | GLN | TYR | ASN | ALA | CYS | PHE | PRO | ASN | PRO | CYS | ||||
| 6 | LEU | ASN | GLY | GLY | THR | CYS | GLY | TYR | VAL | TYR | ||||
| 7 | GLY | TYR | PRO | TYR | TYR | LYS | CYS | SER | CYS | PRO | ||||
| 8 | TYR | GLY | TYR | TYR | GLY | LYS | GLN | CYS | GLN | LEU | ||||
| 9 | LYS | LYS | TYR |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_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 shifts
SPARKY: Backbone
or all simulated shifts