BMRB Entry 52146

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

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52146

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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 lysostaphin 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, 136 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Staphylococcus simulans Taxonomy ID: 1286 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus simulans

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGHEHSAQWLNNYKKGYGYG PYPLGINGGMHYGVDFFMNI GTPVKAISSGKIVEAGWSNY GGGNQIGLIENDGVHRQWYM HLSKYNVKVGDYVKAGQIIG WSGSTGASTAPHLHFQRMVN SFSNSTAQDPMPFLKS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	289
15N chemical shifts	113
1H chemical shifts	113

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LssCD	1

Entities:

Entity 1, LssCD 136 residues - Formula weight is not available

1

MET

GLY

HIS

GLU

HIS

SER

ALA

GLN

TRP

LEU

2

ASN

TYR

LYS

GLY

TYR

GLY

TYR

GLY

3

PRO

TYR

PRO

LEU

GLY

ILE

ASN

GLY

MET

4

HIS

TYR

GLY

VAL

ASP

PHE

MET

ASN

ILE

5

GLY

THR

PRO

VAL

LYS

ALA

ILE

SER

GLY

6

LYS

ILE

VAL

GLU

ALA

GLY

TRP

SER

ASN

TYR

7

GLY

ASN

GLN

ILE

GLY

LEU

ILE

GLU

8

ASN

ASP

GLY

VAL

HIS

ARG

GLN

TRP

TYR

MET

9

HIS

LEU

SER

LYS

TYR

ASN

VAL

LYS

VAL

GLY

10

ASP

TYR

VAL

LYS

ALA

GLY

GLN

ILE

GLY

11

TRP

SER

GLY

SER

THR

GLY

ALA

SER

THR

ALA

12

PRO

HIS

LEU

HIS

PHE

GLN

ARG

MET

VAL

ASN

13

SER

PHE

SER

ASN

SER

THR

ALA

GLN

ASP

PRO

14

MET

PRO

PHE

LEU

LYS

SER

Samples:

sample_1: LssCD, [U-100% 13C; U-100% 15N], 970 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