BMRB Entry 27681

Name: Chemical shift assignments for HSPB1 containing residues 1-176
Published: 2019-10-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27681

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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:

Chemical shift assignments for HSPB1 containing residues 1-176

Deposition date:

2018-11-05

Original release date:

2019-10-10

Authors:

Clouser, Amanda; Klevit, Rachel

Citation:

Citation: Clouser, Amanda; Baughman, Hannah Er; Basanta, Benjamin; Guttman, Miklos; Nath, Abhinav; Klevit, Rachel. "Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of 'quasi-ordered' states" Elife 8, e50259-e50259 (2019).
PubMed: 31573509

Assembly members:

Assembly members:
HSPB1, polymer, 176 residues, 19853 Da.

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: pET151d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HSPB1: MTERRVPFSLLRGPDWDPFR DWYPHSRLFDQAFGLPRLPE EWSQWLGGSSWPGYVRPLPP AAIESPAVAAPAYSRALDRQ LDSGVSEIRHTADRWRVSLD VNHFAPDELTVKTKDGVVEI TGKHEERQDEHGYISRCFTR KYTLPPGVDPTQVSSSLSPE GTLTVEAPMPKLATQS

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	294
15N chemical shifts	100
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HSPB1, Subunit 1	1
2	HSPB1, Subunit 2	1

Entities:

Entity 1, HSPB1, Subunit 1 176 residues - 19853 Da.

Phosphomimetic form of HSPB1 (Ser15Asp, Ser78Asp, Ser82Asp) truncated after residue 176

1

MET

THR

GLU

ARG

VAL

PRO

PHE

SER

LEU

2

LEU

ARG

GLY

PRO

ASP

TRP

ASP

PRO

PHE

ARG

3

ASP

TRP

TYR

PRO

HIS

SER

ARG

LEU

PHE

ASP

4

GLN

ALA

PHE

GLY

LEU

PRO

ARG

LEU

PRO

GLU

5

GLU

TRP

SER

GLN

TRP

LEU

GLY

SER

6

TRP

PRO

GLY

TYR

VAL

ARG

PRO

LEU

PRO

7

ALA

ILE

GLU

SER

PRO

ALA

VAL

ALA

8

PRO

ALA

TYR

SER

ARG

ALA

LEU

ASP

ARG

GLN

9

LEU

ASP

SER

GLY

VAL

SER

GLU

ILE

ARG

HIS

10

THR

ALA

ASP

ARG

TRP

ARG

VAL

SER

LEU

ASP

11

VAL

ASN

HIS

PHE

ALA

PRO

ASP

GLU

LEU

THR

12

VAL

LYS

THR

LYS

ASP

GLY

VAL

GLU

ILE

13

THR

GLY

LYS

HIS

GLU

ARG

GLN

ASP

GLU

14

HIS

GLY

TYR

ILE

SER

ARG

CYS

PHE

THR

ARG

15

LYS

TYR

THR

LEU

PRO

GLY

VAL

ASP

PRO

16

THR

GLN

VAL

SER

LEU

SER

PRO

GLU

17

GLY

THR

LEU

THR

VAL

GLU

ALA

PRO

MET

PRO

18

LYS

LEU

ALA

THR

GLN

SER

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCOCANNH	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCB	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 27681

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: