BMRB Entry 27993

Name: MYB29 residues 118-178 chemical shifts
Published: 2019-10-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27993

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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:

MYB29 residues 118-178 chemical shifts

Deposition date:

2019-08-02

Original release date:

2019-10-29

Authors:

Millard, Peter; Marabini, Riccardo; Kragelund, Birthe

Citation:

Citation: Millard, Peter; Bugge, Katrine; Marabini, Riccardo; Boomsma, Wouter; Burow, Meike; Kragelund, Birthe. "IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions - insights from transcription factors" Protein Sci. 29, 169-183 (2020).
PubMed: 31642121

Assembly members:

Assembly members:
MYB29_residues_118-178, polymer, 61 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MYB29_residues_118-178: GSGIDPVTHKPLAYDSNPDE QSQSGSISPKSLPPSSSKNV PEITSSDETPKYDASLSSKK R

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	151
15N chemical shifts	45
1H chemical shifts	45

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MYB29 residues 118-178	1

Entities:

Entity 1, MYB29 residues 118-178 61 residues - Formula weight is not available

1

GLY

SER

GLY

ILE

ASP

PRO

VAL

THR

HIS

LYS

2

PRO

LEU

ALA

TYR

ASP

SER

ASN

PRO

ASP

GLU

3

GLN

SER

GLN

SER

GLY

SER

ILE

SER

PRO

LYS

4

SER

LEU

PRO

SER

LYS

ASN

VAL

5

PRO

GLU

ILE

THR

SER

ASP

GLU

THR

PRO

6

LYS

TYR

ASP

ALA

SER

LEU

SER

LYS

7

ARG

Samples:

sample_1: DSS 1 mM; TCEP 100 uM; sodium azide 0.03 % v/v; sodium phosphate 50 mM; MYB29 residues 118-178, [U-13C; U-15N], 225 uM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 273 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(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNmr, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance III 800 MHz

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