BMRB Entry 31187

Name: Solution NMR structure of the RiPP proteusin DprE2 from Desulfotomaculum sp.
Published: 2026-01-18

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PDB ID: 9cjx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31187
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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:

Solution NMR structure of the RiPP proteusin DprE2 from Desulfotomaculum sp.

Deposition date:

2024-07-08

Original release date:

2026-01-18

Authors:

McShan, A.; Agarwal, V.; Vidya, F.

Citation:

Citation: McShan, A.; Agarwal, V.; Vidya, F.. "Solution NMR structure of the RiPP proteusin DprE2" .

Assembly members:

Assembly members:
entity_1, polymer, 107 residues, 11447.863 Da.

Natural source:

Natural source: Common Name: Desulfotomaculum sp. Taxonomy ID: 41211 Superkingdom: Bacteria Kingdom: not available Genus/species: Desulfotomaculum sp.

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MMNNWTEEEVQKVVAEIGKK AAADPAFRKLCLANPTGAVK EVSGKDLPQGLKVRFVENEG AHMTFVLPDPAGSGELGEED LNRVAGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	184
15N chemical shifts	63
1H chemical shifts	63

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 107 residues - 11447.863 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ASN

TRP

THR

GLU

VAL

4

GLN

LYS

VAL

ALA

GLU

ILE

GLY

LYS

5

ALA

ASP

PRO

ALA

PHE

ARG

LYS

LEU

6

CYS

LEU

ALA

ASN

PRO

THR

GLY

ALA

VAL

LYS

7

GLU

VAL

SER

GLY

LYS

ASP

LEU

PRO

GLN

GLY

8

LEU

LYS

VAL

ARG

PHE

VAL

GLU

ASN

GLU

GLY

9

ALA

HIS

MET

THR

PHE

VAL

LEU

PRO

ASP

PRO

10

ALA

GLY

SER

GLY

GLU

LEU

GLY

GLU

ASP

11

LEU

ASN

ARG

VAL

ALA

GLY

Samples:

sample_1: DprE2, [U-13C; U-15N], 192 uM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

Sparky, Goddard - chemical shift assignment

CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE III HD 800 MHz

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