BMRB Entry 28034

Name: Backbone resonance assignments for the HSP27 (HSPB1) alpha-crystallin domain monomer
Published: 2020-02-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28034

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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 resonance assignments for the HSP27 (HSPB1) alpha-crystallin domain monomer

Deposition date:

2019-10-29

Original release date:

2020-02-26

Authors:

Alderson, Reid; Bax, Ad; Baldwin, Andrew

Citation:

Citation: Alderson, T. Reid; Ying, Jinfa; Bax, Ad; Benesch, Justin; Baldwin, Andrew. "Conditional disorder in small heat-shock proteins" J. Mol. Biol. 432, 3033-3049 (2020).
PubMed: 32081587

Assembly members:

Assembly members:
HSP27 (HSPB1), polymer, 88 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: pET-29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HSP27 (HSPB1): GVSEIRHTADRWRVSLDVNH FAPDELTVKTKDGVVEITGK HEERQDEHGYISRSFTRKYT LPPGVDPTQVSSSLSPEGTL TVEAPMPK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	167
15N chemical shifts	80
1H chemical shifts	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HSP27 (HSPB1)	1

Entities:

Entity 1, HSP27 (HSPB1) 88 residues - Formula weight is not available

This construct contains the C137S mutation to prevent disulfide bond formation."

1

GLY

VAL

SER

GLU

ILE

ARG

HIS

THR

ALA

ASP

2

ARG

TRP

ARG

VAL

SER

LEU

ASP

VAL

ASN

HIS

3

PHE

ALA

PRO

ASP

GLU

LEU

THR

VAL

LYS

THR

4

LYS

ASP

GLY

VAL

GLU

ILE

THR

GLY

LYS

5

HIS

GLU

ARG

GLN

ASP

GLU

HIS

GLY

TYR

6

ILE

SER

ARG

SER

PHE

THR

ARG

LYS

TYR

THR

7

LEU

PRO

GLY

VAL

ASP

PRO

THR

GLN

VAL

8

SER

LEU

SER

PRO

GLU

GLY

THR

LEU

9

THR

VAL

GLU

ALA

PRO

MET

PRO

LYS

Samples:

sample_1: HSP27 (HSPB1), [U-13C; U-15N; U-2H], 0.1 mM; sodium phosphate 30 mM; EDTA 2 mM

sample_conditions_1: pH: 4.1; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

SPARKY vNMRFAM-SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

Bruker Avance 600 MHz

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