BMRB Entry 34376

Name: The N-terminal domain of rhomboid protease YqgP
Published: 2020-01-06

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PDB ID: 6r0j
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34376
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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:

The N-terminal domain of rhomboid protease YqgP

Deposition date:

2019-03-13

Original release date:

2020-01-06

Authors:

Began, J.; Strisovsky, K.; Veverka, V.

Citation:

Citation: Began, Jakub; Cordier, Baptiste; Brezinova, Jana; Delisle, Jordan; Hexnerova, Rozalie; Srb, Pavel; Rampirova, Petra; Kozisek, Milan; Baudet, Mathieu; Coute, Yohann; Galinier, Anne; Veverka, Vaclav; Doan, Thierry; Strisovsky, Kvido. "Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease" Embo J. 39, e102935-e102935 (2020).
PubMed: 31930742

Assembly members:

Assembly members:
entity_1, polymer, 185 residues, 21836.576 Da.

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MFLLEYTYWKIAAHLVNSGY GVIQAGESDEIWLEAPDKSS HDLVRLYKHDLDFRQEMVRD IEEQAERVERVRHQLGRRRM KLLNVFFSTEAPVDDWEEIA KKTFEKGTVSVEPAIVRGTM LRDDLQAVFPSFRTEDCSEE HASFENAQMARERFLSLVLK QEEQRKTEAAVFQNGKLERE NLYFQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	773
15N chemical shifts	192
1H chemical shifts	1279

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 185 residues - 21836.576 Da.

1

MET

PHE

LEU

GLU

TYR

THR

TYR

TRP

LYS

2

ILE

ALA

HIS

LEU

VAL

ASN

SER

GLY

TYR

3

GLY

VAL

ILE

GLN

ALA

GLY

GLU

SER

ASP

GLU

4

ILE

TRP

LEU

GLU

ALA

PRO

ASP

LYS

SER

5

HIS

ASP

LEU

VAL

ARG

LEU

TYR

LYS

HIS

ASP

6

LEU

ASP

PHE

ARG

GLN

GLU

MET

VAL

ARG

ASP

7

ILE

GLU

GLN

ALA

GLU

ARG

VAL

GLU

ARG

8

VAL

ARG

HIS

GLN

LEU

GLY

ARG

MET

9

LYS

LEU

ASN

VAL

PHE

SER

THR

GLU

10

ALA

PRO

VAL

ASP

TRP

GLU

ILE

ALA

11

LYS

THR

PHE

GLU

LYS

GLY

THR

VAL

SER

12

VAL

GLU

PRO

ALA

ILE

VAL

ARG

GLY

THR

MET

13

LEU

ARG

ASP

LEU

GLN

ALA

VAL

PHE

PRO

14

SER

PHE

ARG

THR

GLU

ASP

CYS

SER

GLU

15

HIS

ALA

SER

PHE

GLU

ASN

ALA

GLN

MET

ALA

16

ARG

GLU

ARG

PHE

LEU

SER

LEU

VAL

LEU

LYS

17

GLN

GLU

GLN

ARG

LYS

THR

GLU

ALA

18

VAL

PHE

GLN

ASN

GLY

LYS

LEU

GLU

ARG

GLU

19

ASN

LEU

TYR

PHE

GLN

Samples:

sample_1: YqgP, [U-13C; U-15N], 1 mM; sodium chloride 150 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 175 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment

YASARA, YASARA - refinement

NMR spectrometers:

Bruker AVANCE III 850 MHz

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