BMRB Entry 27741

Name: Backbone Assignments of Bacillus subtilis Holo-Copper Binding Lipoprotein (bsCopL) with Cu(I).
Published: 2019-01-14

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PDB ID: 2ky9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27741
MolProbity Validation Chart

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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:

Backbone Assignments of Bacillus subtilis Holo-Copper Binding Lipoprotein (bsCopL) with Cu(I).

Deposition date:

2018-12-21

Original release date:

2019-01-14

Authors:

Daigham, Nourhan; Rosario-Cruz, Zuelay; Eletsky, Alexander; Szyperski, Thomas; Boyd, Jeffrey; Montelione, Gaetano

Citation:

Citation: Rosario-Cruz, Zuelay; Eletsky, Alexander; Daigham, Nourhan; Al-Tameemi, Hassan; Swapna, G; Kahn, Peter; Szyperski, Thomas; Montelione, Gaetano; Boyd, Jeffrey. "The" J. Biol. Chem. 294, 4027-4044 (2019).
PubMed: 30655293

Assembly members:

Assembly members:
bsCopL, polymer, 128 residues, Formula weight is not available

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: PET15

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	111
1H chemical shifts	111

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	bsCopL	1

Entities:

Entity 1, bsCopL 128 residues - Formula weight is not available

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

SER

HIS

MET

LYS

VAL

GLY

SER

GLN

VAL

ILE

2

ILE

ASN

THR

SER

HIS

MET

LYS

GLY

MET

LYS

3

GLY

ALA

GLU

ALA

THR

VAL

THR

GLY

ALA

TYR

4

ASP

THR

ALA

TYR

VAL

SER

TYR

THR

5

PRO

THR

ASN

GLY

GLN

ARG

VAL

ASP

HIS

6

HIS

LYS

TRP

VAL

ILE

GLN

GLU

ILE

LYS

7

ASP

ALA

GLY

ASP

LYS

THR

LEU

GLN

PRO

GLY

8

ASP

GLN

VAL

ILE

LEU

GLU

ALA

SER

HIS

MET

9

LYS

GLY

MET

LYS

GLY

ALA

THR

ALA

GLU

ILE

10

ASP

SER

ALA

GLU

LYS

THR

VAL

TYR

MET

11

VAL

ASP

TYR

THR

SER

THR

SER

GLY

GLU

12

LYS

VAL

LYS

ASN

HIS

LYS

TRP

VAL

THR

GLU

13

ASP

GLU

LEU

SER

ALA

LYS

LEU

GLU

Samples:

Holo-bsCopL: bsCopL, [U-100% 13C; U-100% 15N], 0.3 mM; TRIS pH 7.5 10 mM; sodium chloride 100 mM; D2O 5%; H2O 95%; Copper(I) Chloride 2.4 mM

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	Holo-bsCopL	isotropic	sample_conditions_1
3D HNCO	Holo-bsCopL	isotropic	sample_conditions_1
3D HNCA	Holo-bsCopL	isotropic	sample_conditions_1
3D HN(CO)CA	Holo-bsCopL	isotropic	sample_conditions_1
3D HNCACB	Holo-bsCopL	isotropic	sample_conditions_1
3D CBCA(CO)NH	Holo-bsCopL	isotropic	sample_conditions_1

Software:

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

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	16942 27493
PDB	2KY9
NESG	SR518