BMRB Entry 34982

Name: The solution NMR structure of OB domain of ComEC from Moorella glycerini
Published: 2025-10-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34982

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

The solution NMR structure of OB domain of ComEC from Moorella glycerini

Deposition date:

2025-02-15

Original release date:

2025-10-02

Authors:

Stedman, M.; Gossert, A.; Hospenthal, M.

Citation:

Citation: Stedman, M.; Deselaers, S.; Braus, S.; Wang, D.; Balaguer, M.; Gossert, A.; Hospenthal, M.. "Molecular interplay between ComEC domains leads to efficient DNA translocation during natural transformation" .

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 14283.295 Da.

Natural source:

Natural source: Common Name: Moorella glycerini Taxonomy ID: 55779 Superkingdom: Bacteria Kingdom: not available Genus/species: Moorella glycerini

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HQSRLTGDRETFLDLTGVVI EEPRVYPNRVVYTLAAREIR QGDYHKRVREKVQVVLYRSA KGGEPVLYRYGDVLRVHGQL AAPPAARNPGELDYRAYLAR QYIYNRMLIDNPRAIVKLGT EPGH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	196
15N chemical shifts	53
1H chemical shifts	411

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 124 residues - 14283.295 Da.

1

HIS

GLN

SER

ARG

LEU

THR

GLY

ASP

ARG

GLU

2

THR

PHE

LEU

ASP

LEU

THR

GLY

VAL

ILE

3

GLU

PRO

ARG

VAL

TYR

PRO

ASN

ARG

VAL

4

VAL

TYR

THR

LEU

ALA

ARG

GLU

ILE

ARG

5

GLN

GLY

ASP

TYR

HIS

LYS

ARG

VAL

ARG

GLU

6

LYS

VAL

GLN

VAL

LEU

TYR

ARG

SER

ALA

7

LYS

GLY

GLU

PRO

VAL

LEU

TYR

ARG

TYR

8

GLY

ASP

VAL

LEU

ARG

VAL

HIS

GLY

GLN

LEU

9

ALA

PRO

ALA

ARG

ASN

PRO

GLY

10

GLU

LEU

ASP

TYR

ARG

ALA

TYR

LEU

ALA

ARG

11

GLN

TYR

ILE

TYR

ASN

ARG

MET

LEU

ILE

ASP

12

ASN

PRO

ARG

ALA

ILE

VAL

LYS

LEU

GLY

THR

13

GLU

PRO

GLY

HIS

Samples:

sample_1: OB Domain, [U-13C; U-15N], 0.8 ± 0.4 mM; HEPES 50 mM; sodium chloride 50 mM; D2O, [U-2H], 10%; H2O 90%

sample_2: OB Domain, [U-13C; U-15N], 0.4 ± 0.2 mM; sodium chloride 50 mM; D2O, [U-2H], 10%; H2O 90%; TRIS, [U-2H], 50 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 bar; 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 HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D NOESY combined	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CcpNmr Analysis, CCPN - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker AVANCE NEO 700 MHz
Bruker AVANCE III HD 900 MHz
Bruker AVANCE III HD 600 MHz

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