BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51661

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51661

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Title: 1H, 13C, and 15N resonance assignments of SarA monomer from Staphylococcus aureus in complex with DNA   PubMed: 37405582

Deposition date: 2022-10-12 Original release date: 2023-12-19

Authors: Fu, Dihong; Xia, Bin

Citation: Fu, Dihong; Duan, Bo; Dong, Xianzhi; Xia, Bin. "1H, 13C, and 15N resonance assignments of SarA monomer from Staphylococcus aureus in complex with DNA"  Biomol. NMR Assignments 17, 193-197 (2023).

Assembly members:
entity_1, polymer, 114 residues, Formula weight is not available
entity_2, polymer, 18 residues, Formula weight is not available
entity_3, polymer, 18 residues, Formula weight is not available

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-21a

Entity Sequences (FASTA):
entity_1: MDKLKSLIKKEFSISFEEFA VLTYISENKEKEYYLKDIIN HLNYKQPQVVKAVKILSQED YFDKKRNEHDQRTVLILVNA QQRKKIESLLSRVNKRITEA NNEIELLEHHHHHH
entity_2: CGCGAATATATATTCGCG
entity_3: CGCGAATATATATTCGCG

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts116
1H chemical shifts1104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SarADN191
2Seq4, chain A2
3Seq4, chain B3

Entities:

Entity 1, SarADN19 114 residues - Formula weight is not available

The first Met residue is artificially added at the N-terminus of the recombinant protein, L125-H132is artificially added at the C-terminus of the recombinant protein. D2-L124 is the remainder based on Uniprot Q2G2U9.

1   METASPLYSLEULYSSERLEUILELYSLYS
2   GLUPHESERILESERPHEGLUGLUPHEALA
3   VALLEUTHRTYRILESERGLUASNLYSGLU
4   LYSGLUTYRTYRLEULYSASPILEILEASN
5   HISLEUASNTYRLYSGLNPROGLNVALVAL
6   LYSALAVALLYSILELEUSERGLNGLUASP
7   TYRPHEASPLYSLYSARGASNGLUHISASP
8   GLNARGTHRVALLEUILELEUVALASNALA
9   GLNGLNARGLYSLYSILEGLUSERLEULEU
10   SERARGVALASNLYSARGILETHRGLUALA
11   ASNASNGLUILEGLULEULEUGLUHISHIS
12   HISHISHISHIS

Entity 2, Seq4, chain A 18 residues - Formula weight is not available

1   DCDGDCDGDADADTDADTDA
2   DTDADTDTDCDGDCDG

Entity 3, Seq4, chain B 18 residues - Formula weight is not available

1   DCDGDCDGDADADTDADTDA
2   DTDADTDTDCDGDCDG

Samples:

sample_1: SarADN19, [U-100% 13C; U-100% 15N], 0.25 mM; Seq4 2.5 mM; Seq4 2.5 mM; sodium phosphate 10 mM; sodium chloride 10 mM; NaN3 0.03%; Protease inhibitor cocktail 2%; DSS 0.01%

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D F1, F2-15N/13C-filtered 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRView - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz MHz
  • Bruker Avance 600 MHz MHz
  • Bruker Avance 950 MHz MHz

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