BMRB Entry 27161

Name: Httex1 25Q
Published: 2018-05-22

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27161

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:

Httex1 25Q

Deposition date:

2017-06-23

Original release date:

2018-05-22

Authors:

Newcombe, Estella; Sethi, Ashish; Hatters, Danny; Gooley, Paul

Citation:

Citation: Newcombe, Estella; Ruff, Kiersten; Sethi, Ashish; Ormsby, Angelique; Ramdzan, Yasmin; Fox, Archa; Purcell, Anthony; Gooley, Paul; Pappu, Rohit; Hatters, Danny. "Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length" J. Mol. Biol. 430, 1442-1458 (2018).
PubMed: 29627459

Assembly members:

Assembly members:
Httex1_25Q, polymer, 97 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: Escherichia coli Vector: pet28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Httex1_25Q: GHMATLEKLMKAFESLKSFQ QQQQQQQQQQQQQQQQQQQQ QQQQPPPPPPPPPPPQLPQP PPQAQPLLPQPQPPPPPPPP PPGPAVAEEPLHRPKKW

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	142
15N chemical shifts	44
1H chemical shifts	44

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Htt monomer	1

Entities:

Entity 1, Htt monomer 97 residues - Formula weight is not available

1

GLY

HIS

MET

ALA

THR

LEU

GLU

LYS

LEU

MET

2

LYS

ALA

PHE

GLU

SER

LEU

LYS

SER

PHE

GLN

3

GLN

4

GLN

5

GLN

PRO

6

PRO

GLN

LEU

PRO

GLN

PRO

7

PRO

GLN

ALA

GLN

PRO

LEU

PRO

GLN

8

PRO

GLN

PRO

9

PRO

GLY

PRO

ALA

VAL

ALA

GLU

PRO

10

LEU

HIS

ARG

PRO

LYS

TRP

Samples:

SampleHttex1_25Q: Httex1_25Q, [U-100% 13C; U-100% 15N], 100 uM

sample_conditionsHttex1_25Qx1_: ionic strength: 150 mM; pH: 4; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	SampleHttex1_25Q	isotropic	sample_conditionsHttex1_25Qx1_
3D HNCO	SampleHttex1_25Q	isotropic	sample_conditionsHttex1_25Qx1_
3D HNCACB	SampleHttex1_25Q	isotropic	sample_conditionsHttex1_25Qx1_
3D HNCACO	SampleHttex1_25Q	isotropic	sample_conditionsHttex1_25Qx1_
3D CBCA(CO)NH	SampleHttex1_25Q	isotropic	sample_conditionsHttex1_25Qx1_

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

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

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

NMR spectrometers:

Bruker Avance 700 MHz

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