BMRB Entry 34966

Name: A conserved beta-sandwich fold is required for secretion of lipoproteins by a novel Type I secretion system
Published: 2025-12-03

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PDB ID: 9hho
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34966
MolProbity Validation Chart

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NMR-STAR v3 text file.
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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:

A conserved beta-sandwich fold is required for secretion of lipoproteins by a novel Type I secretion system

Deposition date:

2024-11-22

Original release date:

2025-12-03

Authors:

Hodges, F.; Icke, C.; Knowles, T.; Rooke, J.; Cole, J.; Cunningham, A.; Torres, V.; Henderson, I.

Citation:

Citation: Hodges, F.; Icke, C.; Knowles, T.; Rooke, J.; Cole, J.; Cunningham, A.; Torres, V.; Henderson, I.. "A conserved beta-sandwich fold is required for secretion of lipoproteins by a novel Type I secretion system" .

Assembly members:

Assembly members:
entity_1, polymer, 109 residues, 11764.057 Da.

Natural source:

Natural source: Common Name: Escherichia coli ETEC H10407 Taxonomy ID: 316401 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGGNSERPPSVAAGECVTFN SKLGEIGGYSWKYSNDACNE TVAKGYAIGVAMHRTVNYEG GYSIQSSGIVKPGSDFIMKG GKTYKGHKKVSAGGDTPYWY KLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	312
15N chemical shifts	104
1H chemical shifts	636

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_1 109 residues - 11764.057 Da.

1

GLY

ASN

SER

GLU

ARG

PRO

SER

2

VAL

ALA

GLY

GLU

CYS

VAL

THR

PHE

ASN

3

SER

LYS

LEU

GLY

GLU

ILE

GLY

TYR

SER

4

TRP

LYS

TYR

SER

ASN

ASP

ALA

CYS

ASN

GLU

5

THR

VAL

ALA

LYS

GLY

TYR

ALA

ILE

GLY

VAL

6

ALA

MET

HIS

ARG

THR

VAL

ASN

TYR

GLU

GLY

7

GLY

TYR

SER

ILE

GLN

SER

GLY

ILE

VAL

8

LYS

PRO

GLY

SER

ASP

PHE

ILE

MET

LYS

GLY

9

GLY

LYS

THR

TYR

LYS

GLY

HIS

LYS

VAL

10

SER

ALA

GLY

ASP

THR

PRO

TYR

TRP

TYR

11

LYS

LEU

GLU

HIS

Samples:

sample_1: CexE, [U-100% 13C; U-100% 15N], 1.83 mM; sodium phosphate 20 mM; sodium chloride 150 mM; L-glutamine 50 mM; L-arginine 50 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 bar; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

Sparky, Goddard - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ARIA, Linge, O'Donoghue and Nilges - refinement

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 900 MHz

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