BMRB Entry 52145

Name: NMR assignment of LytM catalytic domain
Published: 2023-09-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52145

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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:

NMR assignment of LytM catalytic domain

Deposition date:

2023-09-25

Original release date:

2023-09-29

Authors:

Razew, Alicja; Laguri, Cedric; Vallet, Alicia; Bougault, Catherine; Kaus-Drobek, Magdalena; Sabala, Izabela; Simorre, Jean-Pierre

Citation:

Citation: Razew, Alicja; Laguri, Cedric; Vallet, Alicia; Bougault, Catherine; Kaus-Drobek, Magdalena; Sabala, Izabela; Simorre, Jean-Pierre. "Staphylococcus aureus sacculus mediates activities of M23 hydrolases" Nat. Commun. 14, 6706-6706 (2023).
PubMed: 37872144

Assembly members:

Assembly members:
entity_1, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HAKDASWLTSRKQLQPYGQY HGGGAHYGVDYAMPENSPVY SLTDGTVVQAGWSNYGGGNQ VTIKEANSNNYQWYMHNNRL TVSAGDKVKAGDQIAYSGST GNSTAPHVHFQRMSGGIGNQ YAVDPTSYLQSR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	282
15N chemical shifts	102
1H chemical shifts	102

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LytMCD	1

Entities:

Entity 1, LytMCD 132 residues - Formula weight is not available

1

HIS

ALA

LYS

ASP

ALA

SER

TRP

LEU

THR

SER

2

ARG

LYS

GLN

LEU

GLN

PRO

TYR

GLY

GLN

TYR

3

HIS

GLY

ALA

HIS

TYR

GLY

VAL

ASP

4

TYR

ALA

MET

PRO

GLU

ASN

SER

PRO

VAL

TYR

5

SER

LEU

THR

ASP

GLY

THR

VAL

GLN

ALA

6

GLY

TRP

SER

ASN

TYR

GLY

ASN

GLN

7

VAL

THR

ILE

LYS

GLU

ALA

ASN

SER

ASN

8

TYR

GLN

TRP

TYR

MET

HIS

ASN

ARG

LEU

9

THR

VAL

SER

ALA

GLY

ASP

LYS

VAL

LYS

ALA

10

GLY

ASP

GLN

ILE

ALA

TYR

SER

GLY

SER

THR

11

GLY

ASN

SER

THR

ALA

PRO

HIS

VAL

HIS

PHE

12

GLN

ARG

MET

SER

GLY

ILE

GLY

ASN

GLN

13

TYR

ALA

VAL

ASP

PRO

THR

SER

TYR

LEU

GLN

14

SER

ARG

Samples:

sample_1: LytMCD, [U-100% 13C; U-100% 15N], 670 uM; Tris-HCl buffer 20 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D CBCACONH	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:

CcpNMR v3.0.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 850 MHz

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