BMRB Entry 25527

Name: Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5
Published: 2015-06-01

Click here to enlarge.

PDB ID: 2n0k
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25527
MolProbity Validation Chart

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:

Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5

Deposition date:

2015-06-01

Original release date:

2015-06-01

Authors:

Rajagopal, Ponni; Klevit, Rachel; Shi, Lei; Baker, David

Citation:

Citation: Rajagopal, Ponni; Tse, Eric; Borst, Andrew; Delbecq, Scott; Shi, Lei; Dove, Katja; Baker, David; Southworth, Daniel; Klevit, Rachel. "A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis" eLife ., .-. (2015).
PubMed: 25962097

Assembly members:

Assembly members:
HSPB5-ACD, polymer, 89 residues, 10200.596 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: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HSPB5-ACD: GLSEMRLEKDRFSVNLDVKH FSPEELKVKVLGDVIEVHGK HEERQDEHGFISREFHRKYR IPADVDPLTITSSLSSDGVL TVDGPRKQV

Data sets:

assigned_chemical_shifts
- HSPB5_ACD_chemical_shifts

Data type	Count
13C chemical shifts	359
15N chemical shifts	95
1H chemical shifts	622

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HSPB5-ACD_1	1
2	HSPB5-ACD_2	1

Entities:

Entity 1, HSPB5-ACD_1 89 residues - 10200.596 Da.

This is the alpha-crystallin domain from human HSPB5.

1

GLY

LEU

SER

GLU

MET

ARG

LEU

GLU

LYS

ASP

2

ARG

PHE

SER

VAL

ASN

LEU

ASP

VAL

LYS

HIS

3

PHE

SER

PRO

GLU

LEU

LYS

VAL

LYS

VAL

4

LEU

GLY

ASP

VAL

ILE

GLU

VAL

HIS

GLY

LYS

5

HIS

GLU

ARG

GLN

ASP

GLU

HIS

GLY

PHE

6

ILE

SER

ARG

GLU

PHE

HIS

ARG

LYS

TYR

ARG

7

ILE

PRO

ALA

ASP

VAL

ASP

PRO

LEU

THR

ILE

8

THR

SER

LEU

SER

ASP

GLY

VAL

LEU

9

THR

VAL

ASP

GLY

PRO

ARG

LYS

GLN

VAL

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	HSPB5-ACD_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	HSPB5-ACD_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	HSPB5-ACD_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	HSPB5-ACD_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	HSPB5-ACD_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	HSPB5-ACD_4	isotropic	sample_conditions_1
3D HNCACB	HSPB5-ACD_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	HSPB5-ACD_2	isotropic	sample_conditions_1
3D HNCO	HSPB5-ACD_2	isotropic	sample_conditions_1
3D HNCA	HSPB5-ACD_2	isotropic	sample_conditions_1
3D HN(CO)CA	HSPB5-ACD_2	isotropic	sample_conditions_1
3D HN(COCA)CB	HSPB5-ACD_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	HSPB5-ACD_4	isotropic	sample_conditions_1
3D H(CCO)NH	HSPB5-ACD_5	isotropic	sample_conditions_1
3D C(CO)NH	HSPB5-ACD_5	isotropic	sample_conditions_1

BMRB	16391 26640
PDB	2KLR 2N0K 2Y1Y 2YGD 3L1G 4M5S 4M5T
DBJ	BAD51947 BAE27257 BAE40798 BAE87237 BAG36739
EMBL	CAA64669 CAH91560 CAJ18549 CAL37427 CAL37905
GB	AAA37472 AAA52104 AAA60267 AAA67045 AAB23453
REF	NP_001075876 NP_001125917 NP_001166547 NP_001247830 NP_001271991
SP	P02511 P23927 P41316 Q5R9K0 Q60HG8
AlphaFold	P02511 P23927 P41316 Q5R9K0 Q60HG8

BMRB Entry 25527

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: