BMRB Entry 18470

Name: Cu(I) form gt CsoR
Published: 2019-08-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18470

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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:

Cu(I) form gt CsoR

Deposition date:

2012-05-17

Original release date:

2019-08-30

Authors:

Coyne, Harold; Giedroc, David; Kester, Benjamin

Citation:

Citation: Coyne, Harold; Giedroc, David. "Backbone resonance assignments of the homotetrameric (48 kD) copper sensor CsoR from Geobacillus thermodenitrificans in the apo- and Cu(I)-bound states: insights into copper-mediated allostery" Biomol. NMR Assign. 7, 279-283 (2013).
PubMed: 23001947

Assembly members:

Assembly members:
gt_CsoR, polymer, 105 residues, Formula weight is not available
entity_CU1, non-polymer, 63.546 Da.

Natural source:

Natural source: Common Name: Geobacillus thermodenitrifcans Taxonomy ID: 33940 Superkingdom: Bacteria Kingdom: not available Genus/species: Geobacillus thermodenitrifcans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gt_CsoR: MAHPSQEEHVLHGTMIPRTK EEIENIMKRLKRIEGQVRGV QKMVEDNRYCIDILVQISAI QAALRQVGMQLLERHANHCV AKAIREGSGEQSLRELMDVI KQFAK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	297
15N chemical shifts	98
1H chemical shifts	98

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cu(I) gt CsoR, 1	1
2	Cu(I) gt CsoR, 2	1
3	Cu(I) gt CsoR, 3	1
4	Cu(I) gt CsoR, 4	1
5	Cu(I), 1	2
6	Cu(I), 2	2
7	Cu(I), 3	2
8	Cu(I), 4	2

Entities:

Entity 1, Cu(I) gt CsoR, 1 105 residues - Formula weight is not available

1

MET

ALA

HIS

PRO

SER

GLN

GLU

HIS

VAL

2

LEU

HIS

GLY

THR

MET

ILE

PRO

ARG

THR

LYS

3

GLU

ILE

GLU

ASN

ILE

MET

LYS

ARG

LEU

4

LYS

ARG

ILE

GLU

GLY

GLN

VAL

ARG

GLY

VAL

5

GLN

LYS

MET

VAL

GLU

ASP

ASN

ARG

TYR

CYS

6

ILE

ASP

ILE

LEU

VAL

GLN

ILE

SER

ALA

ILE

7

GLN

ALA

LEU

ARG

GLN

VAL

GLY

MET

GLN

8

LEU

GLU

ARG

HIS

ALA

ASN

HIS

CYS

VAL

9

ALA

LYS

ALA

ILE

ARG

GLU

GLY

SER

GLY

GLU

10

GLN

SER

LEU

ARG

GLU

LEU

MET

ASP

VAL

ILE

11

LYS

GLN

PHE

ALA

LYS

Entity 2, Cu(I), 1 - Cu - 63.546 Da.

1

CU1

Samples:

sample_1: Cu(I) gt CsoR, [U-100% 13C; U-100% 15N; U-70% 2H], 0.4 – 0.8 mM; Cu(I) ion0.4 – 0.8 mM; NaCl 115 mM; TCEP 5 mM; EDTA 3 mM; ARG 20 mM; GLU 20 mM

sample_conditions_1: ionic strength: 0.115 M; pH: 6.0; pressure: 1 atm; temperature: 322 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 800 MHz

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