BMRB Entry 19007

Name: Solution structure of Bacillus subtilis MinC N-terminal domain
Published: 2014-03-03

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PDB ID: 2m4i
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19007
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of Bacillus subtilis MinC N-terminal domain

Deposition date:

2013-02-05

Original release date:

2014-03-03

Authors:

Castellen, Patricia; Sforca, Mauricio; Zeri, Ana; Gueiros-Filho, Frederico

Citation:

Citation: Castellen, Patricia; Sforca, Mauricio; Gueiros-Filho, Frederico; de Mattos Zeri, Ana Carolina. "Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis." Biomol. NMR Assignments ., .-. (2013).
PubMed: 24366721

Assembly members:

Assembly members:
N_MinC, polymer, 105 residues, 12028.750 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pAT6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N_MinC: GSHMKTKKQQYVTIKGTKNG LTLHLDDACSFDELLDGLQN MLSIEQYTDGKGQKISVHVK LGNRFLYKEQEEQLTELIAS KKDLFVHSIDSEVITKKEAQ QIREE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	396
15N chemical shifts	105
1H chemical shifts	570

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MinC N-terminal monomer	1

Entities:

Entity 1, MinC N-terminal monomer 105 residues - 12028.750 Da.

1

GLY

SER

HIS

MET

LYS

THR

LYS

GLN

2

TYR

VAL

THR

ILE

LYS

GLY

THR

LYS

ASN

GLY

3

LEU

THR

LEU

HIS

LEU

ASP

ALA

CYS

SER

4

PHE

ASP

GLU

LEU

ASP

GLY

LEU

GLN

ASN

5

MET

LEU

SER

ILE

GLU

GLN

TYR

THR

ASP

GLY

6

LYS

GLY

GLN

LYS

ILE

SER

VAL

HIS

VAL

LYS

7

LEU

GLY

ASN

ARG

PHE

LEU

TYR

LYS

GLU

GLN

8

GLU

GLN

LEU

THR

GLU

LEU

ILE

ALA

SER

9

LYS

ASP

LEU

PHE

VAL

HIS

SER

ILE

ASP

10

SER

GLU

VAL

ILE

THR

LYS

GLU

ALA

GLN

11

GLN

ILE

ARG

GLU

Samples:

sample_1: N_MinC, [U-99% 13C; U-99% 15N], 0.45 mM; sodium phosphate 50 mM; potassium chloride 50 mM; H2O 90%; D2O 10%

sample_2: protein, [U-100% 15N], 0.45 mM; sodium phosphate 50 mM; potassium chloride 50 mM; H2O 90%; D2O 10%

sample_3: protein, [U-99% 13C; U-99% 15N], 0.45 mM; sodium phosphate 50 mM; potassium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_3	isotropic	sample_conditions_1
T1 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
T2 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
NOE 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, refinement

VNMRJ, Varian - collection, processing

Smart_Notebook, (Smart Notebook) Slupsky et al., 2003. - processing

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2M4I
DBJ	BAI86288 BAM53235 BAM58877 GAK80357
EMBL	CAA78817 CAB14760 CCU59291 CEI58029 CEJ78451
GB	AAA22400 AAA22608 ADV93591 AEP87646 AEP91794
REF	NP_390678 WP_003222613 WP_003237567 WP_004398901 WP_014477549
SP	Q01463
AlphaFold	Q01463