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 27493

Title: 1H, and 15N Chemical Shift Titration Study of Copper Binding Lipoprotein (bsCopL)   PubMed: 30655293

Deposition date: 2018-05-23 Original release date: 2018-07-06

Authors: Daigham, Nourhan; Rosario-Cruz, Zuelay; Eletsky, Alexander; Swapna, G.V.T.; Szyperski, Thomas; Boyd, Jeffrey; Montelione, Gaetano

Citation: Rosario-Cruz, Zuelay; Eletsky, Alexander; Daigham, Nourhan; Al-Tameemi, Hassan; Swapna, G; Kahn, Peter; Szyperski, Thomas; Montelione, Gaetano; Boyd, Jeffrey. "The copBL operon protects Staphylococcus aureus from copper toxicity: CopL is an extracellular membrane-associated copper-binding protein"  J. Biol. Chem. 294, 4027-4044 (2019).

Assembly members:
bsCopL, polymer, 126 residues, 13745.39 Da.
COPPER (II) ION, non-polymer, 63.546 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   Vector: PET15

Entity Sequences (FASTA):
bsCopL: SHMKVGSQVIINTSHMKGMK GAEATVTGAYDTTAYVVSYT PTNGGQRVDHHKWVIQEEIK DAGDKTLQPGDQVILEASHM KGMKGATAEIDSAEKTTVYM VDYTSTTSGEKVKNHKWVTE DELSAK

Data sets:
Data typeCount
15N chemical shifts130
1H chemical shifts130

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1bsCopL1
2copper ion2

Entities:

Entity 1, bsCopL 126 residues - 13745.39 Da.

Residues SHM result from cleavage of the N-terminal His-tag by a TEV protease. Residues K4 of the above sequence corresponds to residues K83 of the protein.

1   SERHISMETLYSVALGLYSERGLNVALILE
2   ILEASNTHRSERHISMETLYSGLYMETLYS
3   GLYALAGLUALATHRVALTHRGLYALATYR
4   ASPTHRTHRALATYRVALVALSERTYRTHR
5   PROTHRASNGLYGLYGLNARGVALASPHIS
6   HISLYSTRPVALILEGLNGLUGLUILELYS
7   ASPALAGLYASPLYSTHRLEUGLNPROGLY
8   ASPGLNVALILELEUGLUALASERHISMET
9   LYSGLYMETLYSGLYALATHRALAGLUILE
10   ASPSERALAGLULYSTHRTHRVALTYRMET
11   VALASPTYRTHRSERTHRTHRSERGLYGLU
12   LYSVALLYSASNHISLYSTRPVALTHRGLU
13   ASPGLULEUSERALALYS

Entity 2, copper ion - Cu - 63.546 Da.

1   CU

Samples:

Apo-bsCopL: bsCopL, [U-100% 15N], 0.4 mM; TRIS pH 7.5 10 mM; sodium chloride 100 mM; D2O 5%; H2O 95%

1X_Cu2+_holo-bsCopL: bsCopL, [U-100% 15N], 0.4 mM; Copper Sulfate 0.4 mM; TRIS pH 7.5 10 mM; sodium chloride 100 mM; D2O 5%; H2O 95 mM

2X_Cu2+_holo-bsCopL: bsCopL, [U-100% 15N], 0.4 mM; Copper Sulfate 0.8 mM; TRIS pH 7.5 10 mM; sodium chloride 100 mM; D2O 5%; H2O 95%

3X_Cu2+_holo-bsCopL: bsCopL, [U-100% 15N], 0.4 mM; Copper Sulfate 1.2 mM; TRIS pH 7.5 10 mM; sodium chloride 100 mM; D2O 5 mM; H2O 95 mM

4X_Cu2+_holo-bsCopL: bsCopL, [U-100% 15N], 0.4 mM; Copper Sulfate 1.6 mM; TRIS pH 7.5 10 mM; sodium chloride 100 mM; D2O 5%; H2O 95%

6X_Cu2+_holo-bsCopL: bsCopL, [U-100% 15N], 0.4 mM; Copper Sulfate 2.4 mM; TRIS pH 7.5 10 mM; sodium chloride 100 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCApo-bsCopLisotropicsample_conditions_1
2D 1H-15N HSQC1X_Cu2+_holo-bsCopLisotropicsample_conditions_1
2D 1H-15N HSQC2X_Cu2+_holo-bsCopLisotropicsample_conditions_1
2D 1H-15N HSQC3X_Cu2+_holo-bsCopLisotropicsample_conditions_1
2D 1H-15N HSQC4X_Cu2+_holo-bsCopLisotropicsample_conditions_1
2D 1H-15N HSQC6X_Cu2+_holo-bsCopLisotropicsample_conditions_1

Software:

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

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

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16942
PDB
NESG SR518

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