BMRB Entry 51151

Name: OmpR
Published: 2024-08-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51151

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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:

OmpR

Deposition date:

2021-10-22

Original release date:

2024-08-09

Authors:

Kim, Ju-Sim; Born, Alexandra; Till, James; Liu, Lin; Kant, Sashi; Henen, Morkos; Vogeli, Beat; Vasquez-Torres, Andres

Citation:

Citation: Kim, Ju-Sim; Born, Alexandra; Till, James; Liu, Lin; Kant, Sashi; Henen, Morkos; Vogeli, Beat; Vasquez-Torres, Andres. "Promiscuity of response regulators for thioredoxin steers bacterial virulence" Nat. Commun. 13, 6210-6210 (2022).
PubMed: 36266276

Assembly members:

Assembly members:
entity_1, polymer, 247 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Salmonella enterica Taxonomy ID: 28901 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella enterica

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQENYKILVVDDDMRLRALL ERYLTEQGFQVRSVANAEQM DRLLTRESFHLMVLDLMLPG EDGLSICRRLRSQSNPMPII MVTAKGEEVDRIVGLEIGAD DYIPKPFNPRELLARIRAVL RRQANELPGAPSQEEAVIAF GKFKLNLGTREMFREDEPMP LTSGEFAVLKALVSHPREPL SRDKLMNLARGREYSAMERS IDVQISRLRRMVEEDPAHPR YIQTVWGLGYVFVPDGSKAL EHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	345
15N chemical shifts	150
1H chemical shifts	150

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OmpR	1

Entities:

Entity 1, OmpR 247 residues - Formula weight is not available

1

MET

GLN

GLU

ASN

TYR

LYS

ILE

LEU

VAL

2

ASP

MET

ARG

LEU

ARG

ALA

LEU

3

GLU

ARG

TYR

LEU

THR

GLU

GLN

GLY

PHE

GLN

4

VAL

ARG

SER

VAL

ALA

ASN

ALA

GLU

GLN

MET

5

ASP

ARG

LEU

THR

ARG

GLU

SER

PHE

HIS

6

LEU

MET

VAL

LEU

ASP

LEU

MET

LEU

PRO

GLY

7

GLU

ASP

GLY

LEU

SER

ILE

CYS

ARG

LEU

8

ARG

SER

GLN

SER

ASN

PRO

MET

PRO

ILE

9

MET

VAL

THR

ALA

LYS

GLY

GLU

VAL

ASP

10

ARG

ILE

VAL

GLY

LEU

GLU

ILE

GLY

ALA

ASP

11

ASP

TYR

ILE

PRO

LYS

PRO

PHE

ASN

PRO

ARG

12

GLU

LEU

ALA

ARG

ILE

ARG

ALA

VAL

LEU

13

ARG

GLN

ALA

ASN

GLU

LEU

PRO

GLY

ALA

14

PRO

SER

GLN

GLU

ALA

VAL

ILE

ALA

PHE

15

GLY

LYS

PHE

LYS

LEU

ASN

LEU

GLY

THR

ARG

16

GLU

MET

PHE

ARG

GLU

ASP

GLU

PRO

MET

PRO

17

LEU

THR

SER

GLY

GLU

PHE

ALA

VAL

LEU

LYS

18

ALA

LEU

VAL

SER

HIS

PRO

ARG

GLU

PRO

LEU

19

SER

ARG

ASP

LYS

LEU

MET

ASN

LEU

ALA

ARG

20

GLY

ARG

GLU

TYR

SER

ALA

MET

GLU

ARG

SER

21

ILE

ASP

VAL

GLN

ILE

SER

ARG

LEU

ARG

22

MET

VAL

GLU

ASP

PRO

ALA

HIS

PRO

ARG

23

TYR

ILE

GLN

THR

VAL

TRP

GLY

LEU

GLY

TYR

24

VAL

PHE

VAL

PRO

ASP

GLY

SER

LYS

ALA

LEU

25

GLU

HIS

Samples:

sample_1: OmpR, [U-100% 13C; U-100% 15N; U-80% 2H], 300 uM; TRIS 50 mM; sodium chloride 50 mM; D2O, [U-2H], 3%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

NMRDraw - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Varian INOVA 900 MHz
Bruker Avance 600 MHz

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