BMRB Entry 11566

Name: L105P-RPEL1 motif of MKL1
Published: 2017-03-08

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11566

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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:

L105P-RPEL1 motif of MKL1

Deposition date:

2014-04-18

Original release date:

2017-03-08

Authors:

Mizuguchi, Mineyuki; Fuju, Takahiro; Obita, Takayuki

Citation:

Citation: Mizuguchi, Mineyuki; Fuju, Takahiro; Obita, Takayuki; Ishikawa, Mitsuru; Tsuda, Masaaki; Tabuchi, Akiko. "Transient alpha-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1" Sci. Rep. 4, 5224-5224 (2014).
PubMed: 24909411

Assembly members:

Assembly members:
L105P-MKL1, polymer, 36 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pOP3C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
L105P-MKL1: GPHMLSERKNVLQLKLQQRR TREEPVSQGIMPPLKS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	61
15N chemical shifts	28
1H chemical shifts	28

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	L105P-RPEL1	1

Entities:

Entity 1, L105P-RPEL1 36 residues - Formula weight is not available

This is the L105P-RPEL motif of rat MKL1 protein.

1

GLY

PRO

HIS

MET

LEU

SER

GLU

ARG

LYS

ASN

2

VAL

LEU

GLN

LEU

LYS

LEU

GLN

ARG

3

THR

ARG

GLU

PRO

VAL

SER

GLN

GLY

ILE

4

MET

PRO

LEU

LYS

SER

Samples:

sample_1: L105P-MKL1, [U-100% 13C; U-100% 15N], 0.12 – 0.50 mM; sodium phosphate 10 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 7%; sodium azide 1 mM; DSS 20 uM; H2O 93%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRView v8.0.3, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz