BMRB Entry 50473

Name: Backbone Resonance Assignments of OmpR DNA-binding domain.
Published: 2020-12-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50473

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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 Resonance Assignments of OmpR DNA-binding domain.

Deposition date:

2020-09-21

Original release date:

2020-12-29

Authors:

Sadotra, Sushant; Lou, Yuan-Chao; Chen, Chinpan

Citation:

Citation: Sadotra, Sushant; Lou, Yuan-Chao; Tang, Hao-Cheng; Chiu, Yi-Chih; Hsu, Chun-Hua; Chen, Chinpan. "Structural basis for promoter DNA recognition by the response regulator OmpR" J. Struct. Biol. 213, 107638-107638 (2020).
PubMed: 33152421

Assembly members:

Assembly members:
entity_1, polymer, 103 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: pET-29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: VIAFGKFKLNLGTREMFRED EPMPLTSGEFAVLKALVSHP REPLSRDKLMNLARGREYSA MERSIDVQISRLRRMVEEDP AHPRYIQTVWGLGYVFVPDG SKA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	262
15N chemical shifts	92
1H chemical shifts	92

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OmpRc	1

Entities:

Entity 1, OmpRc 103 residues - Formula weight is not available

1

VAL

ILE

ALA

PHE

GLY

LYS

PHE

LYS

LEU

ASN

2

LEU

GLY

THR

ARG

GLU

MET

PHE

ARG

GLU

ASP

3

GLU

PRO

MET

PRO

LEU

THR

SER

GLY

GLU

PHE

4

ALA

VAL

LEU

LYS

ALA

LEU

VAL

SER

HIS

PRO

5

ARG

GLU

PRO

LEU

SER

ARG

ASP

LYS

LEU

MET

6

ASN

LEU

ALA

ARG

GLY

ARG

GLU

TYR

SER

ALA

7

MET

GLU

ARG

SER

ILE

ASP

VAL

GLN

ILE

SER

8

ARG

LEU

ARG

MET

VAL

GLU

ASP

PRO

9

ALA

HIS

PRO

ARG

TYR

ILE

GLN

THR

VAL

TRP

10

GLY

LEU

GLY

TYR

VAL

PHE

VAL

PRO

ASP

GLY

11

SER

LYS

ALA

Samples:

sample_1: OmpRc, [U-100% 15N], 1.1 mM

sample_conditions_1: pH: 6; temperature: 298 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
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMR spectrometers:

Bruker Avance 800 MHz

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