BMRB Entry 26853

Name: Identification and structural characterization of LytU
Published: 2017-08-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26853

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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:

Identification and structural characterization of LytU

Deposition date:

2016-07-14

Original release date:

2017-08-23

Authors:

Tossavainen, Helena; Raulinaitis, Vytas; Permi, Perttu

Citation:

Citation: Raulinaitis, Vytas; Tossavainen, Helena; Aitio, Olli; Juuti, Jarmo; Hiramatsu, Keiichi; Kontinen, Vesa; Permi, Perttu. "Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family" Sci. Rep. 7, 6020-6020 (2017).
PubMed: 28729697

Assembly members:

Assembly members:
LytU, polymer, 145 residues, Formula weight is not available

Natural source:

Natural source: Common Name: firmicutes 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: pGEX-2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LytU: GSKWEDFFRGSRITETFGKY QHSPFDGKHYGIDFALPKGT PIKAPTNGKVTRIFNNELGG KVLQIAEDNGEYHQWYLHLD KYNVKVGDRVKAGDIIAYSG NTGIQTTGAHLHFQRMKGGV GNAYAEDPKPFIDQLPDGER SLYDL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	467
15N chemical shifts	136
1H chemical shifts	933

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LytU	1

Entities:

Entity 1, LytU 145 residues - Formula weight is not available

1

GLY

SER

LYS

TRP

GLU

ASP

PHE

ARG

GLY

2

SER

ARG

ILE

THR

GLU

THR

PHE

GLY

LYS

TYR

3

GLN

HIS

SER

PRO

PHE

ASP

GLY

LYS

HIS

TYR

4

GLY

ILE

ASP

PHE

ALA

LEU

PRO

LYS

GLY

THR

5

PRO

ILE

LYS

ALA

PRO

THR

ASN

GLY

LYS

VAL

6

THR

ARG

ILE

PHE

ASN

GLU

LEU

GLY

7

LYS

VAL

LEU

GLN

ILE

ALA

GLU

ASP

ASN

GLY

8

GLU

TYR

HIS

GLN

TRP

TYR

LEU

HIS

LEU

ASP

9

LYS

TYR

ASN

VAL

LYS

VAL

GLY

ASP

ARG

VAL

10

LYS

ALA

GLY

ASP

ILE

ALA

TYR

SER

GLY

11

ASN

THR

GLY

ILE

GLN

THR

GLY

ALA

HIS

12

LEU

HIS

PHE

GLN

ARG

MET

LYS

GLY

VAL

13

GLY

ASN

ALA

TYR

ALA

GLU

ASP

PRO

LYS

PRO

14

PHE

ILE

ASP

GLN

LEU

PRO

ASP

GLY

GLU

ARG

15

SER

LEU

TYR

ASP

LEU

Samples:

sample_1: LytU, [U-13C; U-15N], 0.5 mM; Bis-Tris 20 mM; H2O 93%; D2O 7%

sample_conditions_1: 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
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 800 MHz

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