BMRB Entry 51949

Name: Assignments of mature MepS peptidoglycan hydrolase (residues 1-162)
Published: 2024-05-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51949

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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:

Assignments of mature MepS peptidoglycan hydrolase (residues 1-162)

Deposition date:

2023-05-03

Original release date:

2024-05-28

Authors:

Wang, Shen; Tzeng, Shiou-Ru

Citation:

Citation: Wang, Shen; Huang, Chun-Hsiang; Lin, Te-Sheng; Yeh, Yi-Qi; Fan, Yun-Sheng; Wang, Si-Wei; Tseng, Hsi-Ching; Huang, Shing-Jong; Chang, Yu-Yang; Jeng, U-Ser; Chang, Chung-I; Tzeng, Shiou-Ru. "Structural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI" Nat. Commun. 15, 5461-5461 (2024).
PubMed: 38937433

Assembly members:

Assembly members:
entity_1, polymer, 168 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSANNTAKNMHPETRAVGSE TSSLQASQDEFENLVRNVDV KSRIMDQYADWKGVRYRLGG STKKGIDCSGFVQRTFREQF GLELPRSTYEQQEMGKSVSR SNLRTGDLVLFRAGSTGRHV GIYIGNNQFVHASTSSGVII SSMNEPYWKKRYNEARRVLS RSHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	342
15N chemical shifts	142
1H chemical shifts	142

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MepS	1

Entities:

Entity 1, MepS 168 residues - Formula weight is not available

1

MET

SER

ALA

ASN

THR

ALA

LYS

ASN

MET

2

HIS

PRO

GLU

THR

ARG

ALA

VAL

GLY

SER

GLU

3

THR

SER

LEU

GLN

ALA

SER

GLN

ASP

GLU

4

PHE

GLU

ASN

LEU

VAL

ARG

ASN

VAL

ASP

VAL

5

LYS

SER

ARG

ILE

MET

ASP

GLN

TYR

ALA

ASP

6

TRP

LYS

GLY

VAL

ARG

TYR

ARG

LEU

GLY

7

SER

THR

LYS

GLY

ILE

ASP

CYS

SER

GLY

8

PHE

VAL

GLN

ARG

THR

PHE

ARG

GLU

GLN

PHE

9

GLY

LEU

GLU

LEU

PRO

ARG

SER

THR

TYR

GLU

10

GLN

GLU

MET

GLY

LYS

SER

VAL

SER

ARG

11

SER

ASN

LEU

ARG

THR

GLY

ASP

LEU

VAL

LEU

12

PHE

ARG

ALA

GLY

SER

THR

GLY

ARG

HIS

VAL

13

GLY

ILE

TYR

ILE

GLY

ASN

GLN

PHE

VAL

14

HIS

ALA

SER

THR

SER

GLY

VAL

ILE

15

SER

MET

ASN

GLU

PRO

TYR

TRP

LYS

16

ARG

TYR

ASN

GLU

ALA

ARG

VAL

LEU

SER

17

ARG

SER

HIS

Samples:

sample_1: MepS peptidoglycan hydrolase, [U-13C; U-15N], 618 uM

sample_conditions_1: ionic strength: 0.2 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 CBCANH	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

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