BMRB Entry 51091

Name: 1H, 13C, and 15N Chemical Shift Assignments for Perna viridis foot protein 5b
Published: 2022-07-28

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PDB ID: 7qab
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

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
entity_1: GVYYPNPCSPYPCRNGGTCK KRGLYSYKCYCRKGYTGKNC QYNACFPNPCLNGGTCGYVY GYPYYKCSCPYGYYGKQCQL KKY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	361
15N chemical shifts	73
1H chemical shifts	510

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

PRO

ASN

PRO

CYS

SER

PRO

2

TYR

PRO

CYS

ARG

ASN

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

THR

CYS

GLY

TYR

VAL

TYR

7

GLY

TYR

PRO

TYR

LYS

CYS

SER

CYS

PRO

8

TYR

GLY

TYR

GLY

LYS

GLN

CYS

GLN

LEU

9

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 peaks
SPARKY: Backbone or all simulated peaks