BMRB Entry 50799

Name: Backbone chemical shift assignment of the alpha-crystallin domain of the Small heat shock protein, IbpB from E. coli
Published: 2021-05-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50799

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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 chemical shift assignment of the alpha-crystallin domain of the Small heat shock protein, IbpB from E. coli

Deposition date:

2021-03-04

Original release date:

2021-05-27

Authors:

Pirog, Artur; Cantini, Francesca; Nierzwicki, Lukasz; Obuchowski, Igor; Tomiczek, Bartlomiej; Czub, Jacek; Liberek, Krzysztof

Citation:

Citation: Pirog, Artur; Cantini, Francesca; Nierzwicki, Lukasz; Obuchowski, Igor; Tomiczek, Bartlomiej; Czub, Jacek; Liberek, Krzysztof. "Two bacterial small heat shock proteins, IbpA and IbpB, form a functional heterodimer" J. Mol. Biol. 433, 167054-167054 (2021).
PubMed: 34022209

Assembly members:

Assembly members:
entity_1, polymer, 97 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHSQSFPPYNIEKSDDNHY RITLALAGFRQEDLEIQLEG TRLSVKGTPEQPKEEKKWLH QGLMNQPFSLSFTLAENMEV SGATFVNGLLHIDLIRN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	132
15N chemical shifts	58
1H chemical shifts	58

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IbpB	1

Entities:

Entity 1, IbpB 97 residues - Formula weight is not available

The first three aminoacids GSH belong to the tag

1

GLY

SER

HIS

SER

GLN

SER

PHE

PRO

TYR

2

ASN

ILE

GLU

LYS

SER

ASP

ASN

HIS

TYR

3

ARG

ILE

THR

LEU

ALA

LEU

ALA

GLY

PHE

ARG

4

GLN

GLU

ASP

LEU

GLU

ILE

GLN

LEU

GLU

GLY

5

THR

ARG

LEU

SER

VAL

LYS

GLY

THR

PRO

GLU

6

GLN

PRO

LYS

GLU

LYS

TRP

LEU

HIS

7

GLN

GLY

LEU

MET

ASN

GLN

PRO

PHE

SER

LEU

8

SER

PHE

THR

LEU

ALA

GLU

ASN

MET

GLU

VAL

9

SER

GLY

ALA

THR

PHE

VAL

ASN

GLY

LEU

10

HIS

ILE

ASP

LEU

ILE

ARG

ASN

Samples:

sample_1: 15N alpha-crystallin domain of IbpB, [U-100% 15N], 700 uM; phosphate buffer 20 mM; KCl 35 mM

sample_2: 15N-13C alpha-crystallin domain of IbpB, [U-100% 13C; U-100% 15N], 700 uM; phosphate buffer 20 mM; KCl 35 mM

sample_conditions_1: ionic strength: 0.105 M; pH: 7.2; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_2	isotropic	sample_conditions_1
3D CBCANH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.01 - collection, processing

TALOS+ - data analysis

CARA v1.8 - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 MHz

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