BMRB Entry 25992

Name: Backbone and Side Chain Chemical Shift Assignments for the myosin IIA fragment 1893-1937 (MPT)
Published: 2016-08-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25992

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:

Backbone and Side Chain Chemical Shift Assignments for the myosin IIA fragment 1893-1937 (MPT)

Deposition date:

2016-03-11

Original release date:

2016-08-19

Authors:

Bodor, Andrea; Palfy, Gyula; Kiss, Bence; Nyitray, Laszlo

Citation:

Citation: Palfy, Gyula; Kiss, Bence; Nyitray, Laszlo; Bodor, Andrea. "Multilevel Changes in Protein Dynamics upon Complex Formation of the Calcium-Loaded S100A4 with a Nonmuscle Myosin IIA Tail Fragment" Chembiochem. 17, 1829-1838 (2016).
PubMed: 27418229

Assembly members:

Assembly members:
MPT, polymer, 45 residues, 5346.1 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MPT: YRKLQRELEDATETADAMNR EVSSLKNKLRRGDLPFVVPR RMARK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	136
15N chemical shifts	41
1H chemical shifts	251

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MPT	1

Entities:

Entity 1, MPT 45 residues - 5346.1 Da.

1

TYR

ARG

LYS

LEU

GLN

ARG

GLU

LEU

GLU

ASP

2

ALA

THR

GLU

THR

ALA

ASP

ALA

MET

ASN

ARG

3

GLU

VAL

SER

LEU

LYS

ASN

LYS

LEU

ARG

4

ARG

GLY

ASP

LEU

PRO

PHE

VAL

PRO

ARG

5

ARG

MET

ALA

ARG

LYS

Samples:

sample_1: MPT, [U-100% 15N], 0.7 mM; CaCl2 1 mM; MES 20 mM; NaCl 20 mM; TCEP 10 mM; NaN3 10 mM; D2O, [U-100% 2H], 10%

sample_2: MPT, [U-100% 13C; U-100% 15N], 0.80 mM; CaCl2 1 mM; MES 20 mM; NaCl 20 mM; TCEP 10 mM; NaN3 10 mM; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.2; pressure: 1 atm; temperature: 283 K

sample_conditions_2: ionic strength: 0.1 M; pH: 5.4; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0.3, Bruker Biospin - collection, processing

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 700 MHz

UNP	P35579
AlphaFold	Q86T83