BMRB Entry 52156

Name: LTA-binding domain of SlpA, the S-layer protein from Lactobacillus amylovorus
Published: 2024-09-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52156

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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:

LTA-binding domain of SlpA, the S-layer protein from Lactobacillus amylovorus

Deposition date:

2023-09-29

Original release date:

2024-09-10

Authors:

Gubensak, Nina

Citation:

Citation: Gubensak, Nina; Sagmeister, Theo; Buhlheller, Christoph; Grinninger, Christoph; Eder, Markus; Dordic, Andela; Millan, Claudia; Medina, Ana; Sanchez Murcia, Pedro; Berni, Francesca; Hynonen, Ulla; Vejzovic, Djenana; Damisch, Elisabeth; Kulminskaya, Natalia; Petrowitsch, Lukas; Oberer, Monika; Palva, Airi; Malanovic, Nermina; Codee, Jeroen; Keller, Walter; Uson, Isabel; Pavkov-Keller, Tea. "The molecular architecture of Lactobacillus S-layer: Assembly and attachment to teichoic acids" Proc. Natl. Acad. Sci. U. S. A. 121, e2401686121-e2401686121 (2024).
PubMed: 38838019

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Lactobacillus amylovorus Taxonomy ID: 1604 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactobacillus amylovorus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MVSVANAAQTPAAQETTKNV TIMHISTIYDKTGKATNEPA LRAYDTVSVVSDPVTINNAK FYKLAGKDQYIKVGNVDGTS RTLKHNSYVYKSSGKRANKK TLKKGSSVTTYGKSFMIAGH QMYRIGKNQYVKKANFLE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	339
15N chemical shifts	111
1H chemical shifts	111

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SlpA_amy_III	1

Entities:

Entity 1, SlpA_amy_III 138 residues - Formula weight is not available

1

MET

VAL

SER

VAL

ALA

ASN

ALA

GLN

THR

2

PRO

ALA

GLN

GLU

THR

LYS

ASN

VAL

3

THR

ILE

MET

HIS

ILE

SER

THR

ILE

TYR

ASP

4

LYS

THR

GLY

LYS

ALA

THR

ASN

GLU

PRO

ALA

5

LEU

ARG

ALA

TYR

ASP

THR

VAL

SER

VAL

6

SER

ASP

PRO

VAL

THR

ILE

ASN

ALA

LYS

7

PHE

TYR

LYS

LEU

ALA

GLY

LYS

ASP

GLN

TYR

8

ILE

LYS

VAL

GLY

ASN

VAL

ASP

GLY

THR

SER

9

ARG

THR

LEU

LYS

HIS

ASN

SER

TYR

VAL

TYR

10

LYS

SER

GLY

LYS

ARG

ALA

ASN

LYS

11

THR

LEU

LYS

GLY

SER

VAL

THR

12

TYR

GLY

LYS

SER

PHE

MET

ILE

ALA

GLY

HIS

13

GLN

MET

TYR

ARG

ILE

GLY

LYS

ASN

GLN

TYR

14

VAL

LYS

ALA

ASN

PHE

LEU

GLU

Samples:

sample_1: ADA 20 mM; sodium chloride 50 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 273 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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