BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19007

Title: Solution structure of Bacillus subtilis MinC N-terminal domain   PubMed: 24366721

Deposition date: 2013-02-05 Original release date: 2014-03-03

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

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts396
15N chemical shifts105
1H chemical shifts570

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MinC N-terminal monomer1

Entities:

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

1   GLYSERHISMETLYSTHRLYSLYSGLNGLN
2   TYRVALTHRILELYSGLYTHRLYSASNGLY
3   LEUTHRLEUHISLEUASPASPALACYSSER
4   PHEASPGLULEULEUASPGLYLEUGLNASN
5   METLEUSERILEGLUGLNTYRTHRASPGLY
6   LYSGLYGLNLYSILESERVALHISVALLYS
7   LEUGLYASNARGPHELEUTYRLYSGLUGLN
8   GLUGLUGLNLEUTHRGLULEUILEALASER
9   LYSLYSASPLEUPHEVALHISSERILEASP
10   SERGLUVALILETHRLYSLYSGLUALAGLN
11   GLNILEARGGLUGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_conditions_1
T1 1H-15N HSQCsample_2isotropicsample_conditions_1
T2 1H-15N HSQCsample_2isotropicsample_conditions_1
NOE 1H-15N HSQCsample_2isotropicsample_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

Related Database Links:

PDB
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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts