BMRB Entry 52546

Name: NMR chemical shifts for a 37-residue peptide corresponding to exon-5 of murine ameloblastin (AB2) free in solution at pH 6.3.
Published: 2024-08-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52546

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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:

NMR chemical shifts for a 37-residue peptide corresponding to exon-5 of murine ameloblastin (AB2) free in solution at pH 6.3.

Deposition date:

2024-07-10

Original release date:

2024-08-12

Authors:

Buchko, Garry

Citation:

Citation: Buchko, Garry; Kegulian, Natalie; Moradian-Oldak, Janet. "Ameloblastin binding to biomimetic models of cell membranes - A continuum of intrinsic disorder" Arch. Oral Biol. 169, 106124-106124 (2024).
PubMed: 39514919

Assembly members:

Assembly members:
entity_1, polymer, 41 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSYSRLGFGKALNSLWLH GLLPPHNSFPWIGPREHETQ Q

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	136
15N chemical shifts	34
1H chemical shifts	105

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AB37*	1

Entities:

Entity 1, AB37* 41 residues - Formula weight is not available

1

GLY

PRO

GLY

SER

TYR

SER

ARG

LEU

GLY

PHE

2

GLY

LYS

ALA

LEU

ASN

SER

LEU

TRP

LEU

HIS

3

GLY

LEU

PRO

HIS

ASN

SER

PHE

PRO

4

TRP

ILE

GLY

PRO

ARG

GLU

HIS

GLU

THR

GLN

5

GLN

Samples:

sample_1: AB37*, [U-98% 13C; U-98% 15N], 0.5 ± 0.1 mM; sodium phosphate 25 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 125 mM; pH: 6.3; pressure: 1 atm; temperature: 293 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic3	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY - data analysis, processing

NMR spectrometers:

Varian INOVA 600 MHz

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