BMRB Entry 50122

Name: Backbone 1H, 13C and 15N Chemical Shift Assignments for Full length Exon-1 Huntington protein
Published: 2020-06-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50122

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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:

Backbone 1H, 13C and 15N Chemical Shift Assignments for Full length Exon-1 Huntington protein

Deposition date:

2019-12-11

Original release date:

2020-06-09

Authors:

Ceccon, Alberto; Tugarinov, Vitali; Ghirlando, Rodolfo; Clore, G. Marius

Citation:

Citation: Ceccon, Alberto; Tugarinov, Vitali; Ghirlando, Rodolfo; Clore, G. Marius. "Abrogation of pre-nucleation, transient oligomerization of the Huntingtin exon-1 protein by human profilin-I" Proc. Natl. Acad. Sci. U.S.A. 117, 5844-5852 (2020).
PubMed: 32127471

Assembly members:

Assembly members:
entity_1, polymer, 73 residues, Formula weight is not available

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: E.coli Vector: pET-21d(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ATLEKLMKAFESLKSFQQQQ QQQPPPPPPPPPPPQLPQPP PQAQPLLPQPQPPPPPPPPP PGPAVAEEPLHRP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	94
15N chemical shifts	41
1H chemical shifts	41

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Huntingtin	1

Entities:

Entity 1, Huntingtin 73 residues - Formula weight is not available

1

ALA

THR

LEU

GLU

LYS

LEU

MET

LYS

ALA

PHE

2

GLU

SER

LEU

LYS

SER

PHE

GLN

3

GLN

PRO

4

PRO

GLN

LEU

PRO

GLN

PRO

5

PRO

GLN

ALA

GLN

PRO

LEU

PRO

GLN

PRO

6

GLN

PRO

7

PRO

GLY

PRO

ALA

VAL

ALA

GLU

PRO

LEU

8

HIS

ARG

PRO

Samples:

sample_1: Full length exon1, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 0.02 mM; sodium chloride 0.05 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.079 M; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis, CCPN - chemical shift assignment

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

NMR spectrometers:

Bruker Avance III 600 MHz

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