BMRB Entry 28005

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for phosphomimetic mutant of cytoplasmic domain of MapZ protein
Published: 2020-04-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28005

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for phosphomimetic mutant of cytoplasmic domain of MapZ protein

Deposition date:

2019-08-22

Original release date:

2020-04-03

Authors:

Hosek, Tomas; Bougault, Catherine; Simorre, Jean-Pierre

Citation:

Citation: Hosek, Tomas; Bougault, Catherine; Lavergne, Jean-Pierre; Martinez, Denis; Ayala, Isabel; Fenel, Daphna; Restelli, Marine; Morlot, Cecile; Habenstein, Birgit; Grangeasse, Christophe; Simorre, Jean-Pierre. "Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae" Sci. Rep. 10, 4051-4051 (2020).
PubMed: 32132631

Assembly members:

Assembly members:
MapZcyto-2TE, polymer, 168 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptococcus pneumoniae Taxonomy ID: 1313 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pneumoniae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MapZcyto-2TE: MSKKRRNRHKKEAQEPQFDF DEAKELTVGQAIRKNEEVEA GVLPEDSILDKYVKQHRDEI EADKFAERQYKKEEFVEEQS LDDLIQEMREAVEKSEASSE EVPSSEDILLPLPLDDEEQG LDPLLLDDENPTEMTEEVEE EQNLSRLDQEDSEKKSKKGL QGENLYFQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	318
15N chemical shifts	150
1H chemical shifts	150

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cytoplasmic domain	1

Entities:

Entity 1, cytoplasmic domain 168 residues - Formula weight is not available

Residues 159-168 represent the rest of a non-native tag used for purification. This is the phosphomimetic mutant (T67E,T78E) of cytoplasmic domain of a transmembrane protein

1

MET

SER

LYS

ARG

ASN

ARG

HIS

LYS

2

LYS

GLU

ALA

GLN

GLU

PRO

GLN

PHE

ASP

PHE

3

ASP

GLU

ALA

LYS

GLU

LEU

THR

VAL

GLY

GLN

4

ALA

ILE

ARG

LYS

ASN

GLU

VAL

GLU

ALA

5

GLY

VAL

LEU

PRO

GLU

ASP

SER

ILE

LEU

ASP

6

LYS

TYR

VAL

LYS

GLN

HIS

ARG

ASP

GLU

ILE

7

GLU

ALA

ASP

LYS

PHE

ALA

GLU

ARG

GLN

TYR

8

LYS

GLU

PHE

VAL

GLU

GLN

SER

9

LEU

ASP

LEU

ILE

GLN

GLU

MET

ARG

GLU

10

ALA

VAL

GLU

LYS

SER

GLU

ALA

SER

GLU

11

GLU

VAL

PRO

SER

GLU

ASP

ILE

LEU

12

PRO

LEU

PRO

LEU

ASP

GLU

GLN

GLY

13

LEU

ASP

PRO

LEU

ASP

GLU

ASN

14

PRO

THR

GLU

MET

THR

GLU

VAL

GLU

15

GLU

GLN

ASN

LEU

SER

ARG

LEU

ASP

GLN

GLU

16

ASP

SER

GLU

LYS

SER

LYS

GLY

LEU

17

GLN

GLY

GLU

ASN

LEU

TYR

PHE

GLN

Samples:

sample_1: MapZcyto-2TE, [U-99% 13C; U-99% 15N], 0.2 mM; HEPES 30 mM; potassium chloride 200 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 700 MHz

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