BMRB Entry 26613

Name: Periplasmic chaperone Skp from E. coli in 8 m Urea
Published: 2020-08-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26613

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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:

Periplasmic chaperone Skp from E. coli in 8 m Urea

Deposition date:

2015-07-15

Original release date:

2020-08-30

Authors:

Burmann, Bjoern; Hiller, Sebastian

Citation:

Citation: Mas, Guillaume; Burmann, Bjorn; Sharpe, Timothy; Claudi, Beatrice; Bumann, Dirk; Hiller, Sebastian. "Regulation of chaperone function by coupled folding and oligomerization" Sci. Adv. 6, eabc5822-eabc5822 (2020).
PubMed: 33087350

Assembly members:

Assembly members:
Skp, polymer, 162 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):
Skp: MGSSHHHHHHSSGLVPRGSH MADKIAIVNMGSLFQQVAQK TGVSNTLENEFKGRASELQR METDLQAKMKKLQSMKAGSD RTKLEKDVMAQRQTFAQKAQ AFEQDRARRSNEERGKLVTR IQTAVKSVANSQDIDLVVDA NAVAYNSSDVKDITADVLKQ VK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	417
15N chemical shifts	141
1H chemical shifts	141

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Skp	1

Entities:

Entity 1, Skp 162 residues - Formula weight is not available

His-tag including thrombin-cleavage site (residues -20 - 0) followed by mature Skp (residues 1 - 141)

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ALA

ASP

LYS

ILE

ALA

ILE

VAL

ASN

MET

4

GLY

SER

LEU

PHE

GLN

VAL

ALA

GLN

LYS

5

THR

GLY

VAL

SER

ASN

THR

LEU

GLU

ASN

GLU

6

PHE

LYS

GLY

ARG

ALA

SER

GLU

LEU

GLN

ARG

7

MET

GLU

THR

ASP

LEU

GLN

ALA

LYS

MET

LYS

8

LYS

LEU

GLN

SER

MET

LYS

ALA

GLY

SER

ASP

9

ARG

THR

LYS

LEU

GLU

LYS

ASP

VAL

MET

ALA

10

GLN

ARG

GLN

THR

PHE

ALA

GLN

LYS

ALA

GLN

11

ALA

PHE

GLU

GLN

ASP

ARG

ALA

ARG

SER

12

ASN

GLU

ARG

GLY

LYS

LEU

VAL

THR

ARG

13

ILE

GLN

THR

ALA

VAL

LYS

SER

VAL

ALA

ASN

14

SER

GLN

ASP

ILE

ASP

LEU

VAL

ASP

ALA

15

ASN

ALA

VAL

ALA

TYR

ASN

SER

ASP

VAL

16

LYS

ASP

ILE

THR

ALA

ASP

VAL

LEU

LYS

GLN

17

VAL

LYS

Samples:

sample_1: Skp, [U-13C; U-15N; U-2H], 0.6 mM; D2O 10%; DSS 50 uM; MES 25 mM; NaCl 150 mM; urea 8 M; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 288.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
5D APSY HNCOCACB	sample_1	isotropic	sample_conditions_1
4D APSY HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin, Guntert, Herrmann and Wuthrich, Keller and Wuthrich - chemical shift assignment, collection, processing

NMR spectrometers:

Bruker Ascend 700 MHz

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