BMRB Entry 27415

Name: Chemical shift assignments for TRAP, a MMP20 proteolysis product of murine amelogenin.
Published: 2018-04-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27415

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Chemical shift assignments for TRAP, a MMP20 proteolysis product of murine amelogenin.

Deposition date:

2018-03-05

Original release date:

2018-04-11

Authors:

Buchko, Garry

Citation:

Citation: Buchko, Garry; Jayasinha Arachchige, Rajith; Tao, Jinhui; Tarasevich, Barbara; Shaw, Wendy. "Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amelogenin peptide using a nuclear magnetic resonance spectroscopy based method" Arch. Oral Biol. 93, 187-194 (2018).
PubMed: 29960917

Assembly members:

Assembly members:
TRAP, polymer, 49 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: pJexpress414

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TRAP: GPGSMPLPPHPGSPGYINLS YEVLTPLKWYQSMIRQPYPS YGYEPMGGW

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	162
15N chemical shifts	42
1H chemical shifts	150

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TRAP	1

Entities:

Entity 1, TRAP 49 residues - Formula weight is not available

1

GLY

PRO

GLY

SER

MET

PRO

LEU

PRO

HIS

2

PRO

GLY

SER

PRO

GLY

TYR

ILE

ASN

LEU

SER

3

TYR

GLU

VAL

LEU

THR

PRO

LEU

LYS

TRP

TYR

4

GLN

SER

MET

ILE

ARG

GLN

PRO

TYR

PRO

SER

5

TYR

GLY

TYR

GLU

PRO

MET

GLY

TRP

Samples:

sample_1: TRAP, [U-99% 13C; U-99% 15N], 0.5 mM; acetic acid 2%

sample_conditions_1: ionic strength: 0 M; pH: 2.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

Felix v2007, Accelrys Software Inc. - processing

SPARKY v1.4, Goddard - data analysis

NMR spectrometers:

Bruker Avance 750 MHz
Agilent VXRS 600 MHz
Agilent VXRS 750 MHz

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