BMRB Entry 16685

Name: NMR resonance assignment of the major extracytoplasmic domain of MreC from Bacillus subtilis
Published: 2010-07-27

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16685

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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 resonance assignment of the major extracytoplasmic domain of MreC from Bacillus subtilis

Deposition date:

2010-01-20

Original release date:

2010-07-27

Authors:

Kyburz, Annika; Raulinaitis, Vytautas; Koskela, Outi; Kontinen, Vesa; Permi, Perttu; Kilpelainen, Ilkka; Seppala-Lehto, Raili

Citation:

Citation: Kyburz, Annika; Raulinaitis, Vytautas; Koskela, Outi; Kontinen, Vesa; Permi, Perttu; Kilpelainen, Ilkka; Seppala, Raili. "1H, 13C and 15N resonance assignments of the major extracytoplasmic domain of the cell shape-determining protein MreC from Bacillus subtilis." Biomol. NMR Assignments 4, 235-238 (2010).
PubMed: 20623345

Assembly members:

Assembly members:
MreC, polymer, 178 residues, 19225.8340 Da.

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Eubacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-2T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MreC: GSGHVKSIKDYKPILATVIA RSPDNWAKQVTINKGTQQNV AKDMAVTNEKGALIGKIKSS GLNNFTSAVQLLSDTDRNNR VATKISGKKGSKGYGLIEGY DKEKKRLKMTIIERKDKQDV KKGDLIETSGTGGVFPEGLT IGEVTDIESDSYGLTKVAYV KPAADLTDLNNVIVVNRD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	566
15N chemical shifts	170
1H chemical shifts	1165

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MreC	1

Entities:

Entity 1, MreC 178 residues - 19225.8340 Da.

1

GLY

SER

GLY

HIS

VAL

LYS

SER

ILE

LYS

ASP

2

TYR

LYS

PRO

ILE

LEU

ALA

THR

VAL

ILE

ALA

3

ARG

SER

PRO

ASP

ASN

TRP

ALA

LYS

GLN

VAL

4

THR

ILE

ASN

LYS

GLY

THR

GLN

ASN

VAL

5

ALA

LYS

ASP

MET

ALA

VAL

THR

ASN

GLU

LYS

6

GLY

ALA

LEU

ILE

GLY

LYS

ILE

LYS

SER

7

GLY

LEU

ASN

PHE

THR

SER

ALA

VAL

GLN

8

LEU

SER

ASP

THR

ASP

ARG

ASN

ARG

9

VAL

ALA

THR

LYS

ILE

SER

GLY

LYS

GLY

10

SER

LYS

GLY

TYR

GLY

LEU

ILE

GLU

GLY

TYR

11

ASP

LYS

GLU

LYS

ARG

LEU

LYS

MET

THR

12

ILE

GLU

ARG

LYS

ASP

LYS

GLN

ASP

VAL

13

LYS

GLY

ASP

LEU

ILE

GLU

THR

SER

GLY

14

THR

GLY

VAL

PHE

PRO

GLU

GLY

LEU

THR

15

ILE

GLY

GLU

VAL

THR

ASP

ILE

GLU

SER

ASP

16

SER

TYR

GLY

LEU

THR

LYS

VAL

ALA

TYR

VAL

17

LYS

PRO

ALA

ASP

LEU

THR

ASP

LEU

ASN

18

ASN

VAL

ILE

VAL

ASN

ARG

ASP

Samples:

sample_1: MreC 104-279, [U-100% 13C; U-100% 15N], 0.54 mM; potassium phosphate 20 mM; sodium azide 2 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CC)(CO)NH	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
2D 1H-13C-CT-HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY_aromatics	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection, processing

SPARKY v3.113, Goddard - chemical shift assignments, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz

DBJ	BAI86290 BAM53237 BAM58879 GAK80355
EMBL	CAB14762 CCU59293 CEI58031 CEJ78453 CJR47029
GB	AAA22398 AAA22606 ADM38751 ADV93593 AEP87648
PRF	2207195A
REF	NP_390680 WP_003222609 WP_003237571 WP_009967915 WP_010335163
SP	P84480 Q01466
AlphaFold	P84480 Q01466