BMRB Entry 51829

Name: Backbone assignment of Human SERF1a short form
Published: 2024-09-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51829

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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 assignment of Human SERF1a short form

Deposition date:

2023-02-14

Original release date:

2024-09-28

Authors:

Huang, Yi-Ping; Chen, Chun-Yu; Chen, Yun-Ru; Chang, Chi-Fon

Citation:

Citation: Lin, Tien Chang; Shih, Orion; Tsai, Tien Ying; Yeh, Yi Qi; Liao, Kuei Fen; Mansel, Bradley; Shiu, Ying Jen; Chang, Chi Fon; Su, An Chung; Chen, Yun Ru; Jeng, U Ser. "Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation" IUCrJ 11, 849-858 (2024).
PubMed: 39120045

Assembly members:

Assembly members:
entity_1, polymer, 62 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: pET14b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MARGNQRELARQKNMKKTQE ISKGKRKEDSLTASQRKQRD SEIMQEKQKAANEKKSMQTR EK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	169
15N chemical shifts	54
1H chemical shifts	54

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SERF1a	1

Entities:

Entity 1, SERF1a 62 residues - Formula weight is not available

1

MET

ALA

ARG

GLY

ASN

GLN

ARG

GLU

LEU

ALA

2

ARG

GLN

LYS

ASN

MET

LYS

THR

GLN

GLU

3

ILE

SER

LYS

GLY

LYS

ARG

LYS

GLU

ASP

SER

4

LEU

THR

ALA

SER

GLN

ARG

LYS

GLN

ARG

ASP

5

SER

GLU

ILE

MET

GLN

GLU

LYS

GLN

LYS

ALA

6

ALA

ASN

GLU

LYS

SER

MET

GLN

THR

ARG

7

GLU

LYS

Samples:

sample_1: SERF1a short form, [U-99% 13C; U-99% 15N], 0.1 mM; TRIS, [U-99% 2H], 50 mM; sodium chloride 20 mM; sodium azide 3 mM

sample_2: TRIS, [U-99% 2H], 50 mM; sodium chloride 20 mM; sodium azide 3 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1 - collection

SPARKY v3.114 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 850 MHz
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