BMRB Entry 15894

Name: Mechanism of metal delivery to the CuA center in terminal oxidases from bacteria: a redox m nage- -trois
Published: 2008-11-14

Click here to enlarge.

PDB ID: 2k6w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15894
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: Mechanism of metal delivery to the CuA center in terminal oxidases from bacteria: a redox m nage- -trois PubMed: 18758441

Deposition date: 2008-07-28 Original release date: 2008-11-14

Authors: Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Wang, Shenlin

Citation: Abriata, Luciano; Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Gkazonis, Petros; Spyroulias, Georgios; Vila, Alejandro; Wang, Shenlin. "Mechanism of Cu(A) assembly." Nat. Chem. Biol. 4, 599-601 (2008).

Assembly members:
CuA center, polymer, 120 residues, 13222.670 Da.

Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus

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

Entity Sequences (FASTA):
CuA center: GSFTEGWVRFSPGPNAAAYL TLENPGDLPLRLVGARTPVA ERVELHETFMREVEGKKVMG MRPVPFLEVPPKGRVELKPG GYHFMLLGLKRPLKAGEEVE LDLLFAGGKVLKVVLPVEAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	482
15N chemical shifts	104
1H chemical shifts	850

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

1	GLY	SER	PHE	THR	GLU	GLY	TRP	VAL	ARG	PHE
2	SER	PRO	GLY	PRO	ASN	ALA	ALA	ALA	TYR	LEU
3	THR	LEU	GLU	ASN	PRO	GLY	ASP	LEU	PRO	LEU
4	ARG	LEU	VAL	GLY	ALA	ARG	THR	PRO	VAL	ALA
5	GLU	ARG	VAL	GLU	LEU	HIS	GLU	THR	PHE	MET
6	ARG	GLU	VAL	GLU	GLY	LYS	LYS	VAL	MET	GLY
7	MET	ARG	PRO	VAL	PRO	PHE	LEU	GLU	VAL	PRO
8	PRO	LYS	GLY	ARG	VAL	GLU	LEU	LYS	PRO	GLY
9	GLY	TYR	HIS	PHE	MET	LEU	LEU	GLY	LEU	LYS
10	ARG	PRO	LEU	LYS	ALA	GLY	GLU	GLU	VAL	GLU
11	LEU	ASP	LEU	LEU	PHE	ALA	GLY	GLY	LYS	VAL
12	LEU	LYS	VAL	VAL	LEU	PRO	VAL	GLU	ALA	ARG

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
15N R1	sample_1	isotropic	sample_conditions_1
15N R2	sample_1	isotropic	sample_conditions_1
1H-15N NOE	sample_1	isotropic	sample_conditions_1

BMRB	15895 15896 15897
PDB	2K6W 2K6Y 2K6Z 2K70
DBJ	BAD71766
GB	AAS81922 AEG34334 AFH39883
REF	WP_011173952 WP_011229034 WP_014510965 WP_014630387 YP_145209

Biological Magnetic Resonance Data Bank

BMRB Entry 15894

Title: Mechanism of metal delivery to the CuA center in terminal oxidases from bacteria: a redox m nage- -trois PubMed: 18758441

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	GLY	SER	PHE	THR	GLU	GLY	TRP	VAL	ARG	PHE
2	SER	PRO	GLY	PRO	ASN	ALA	ALA	ALA	TYR	LEU
3	THR	LEU	GLU	ASN	PRO	GLY	ASP	LEU	PRO	LEU
4	ARG	LEU	VAL	GLY	ALA	ARG	THR	PRO	VAL	ALA
5	GLU	ARG	VAL	GLU	LEU	HIS	GLU	THR	PHE	MET
6	ARG	GLU	VAL	GLU	GLY	LYS	LYS	VAL	MET	GLY
7	MET	ARG	PRO	VAL	PRO	PHE	LEU	GLU	VAL	PRO
8	PRO	LYS	GLY	ARG	VAL	GLU	LEU	LYS	PRO	GLY
9	GLY	TYR	HIS	PHE	MET	LEU	LEU	GLY	LEU	LYS
10	ARG	PRO	LEU	LYS	ALA	GLY	GLU	GLU	VAL	GLU
11	LEU	ASP	LEU	LEU	PHE	ALA	GLY	GLY	LYS	VAL
12	LEU	LYS	VAL	VAL	LEU	PRO	VAL	GLU	ALA	ARG

1	GLY	SER	PHE	THR	GLU	GLY	TRP	VAL	ARG	PHE
2	SER	PRO	GLY	PRO	ASN	ALA	ALA	ALA	TYR	LEU
3	THR	LEU	GLU	ASN	PRO	GLY	ASP	LEU	PRO	LEU
4	ARG	LEU	VAL	GLY	ALA	ARG	THR	PRO	VAL	ALA
5	GLU	ARG	VAL	GLU	LEU	HIS	GLU	THR	PHE	MET
6	ARG	GLU	VAL	GLU	GLY	LYS	LYS	VAL	MET	GLY
7	MET	ARG	PRO	VAL	PRO	PHE	LEU	GLU	VAL	PRO
8	PRO	LYS	GLY	ARG	VAL	GLU	LEU	LYS	PRO	GLY
9	GLY	TYR	HIS	PHE	MET	LEU	LEU	GLY	LEU	LYS
10	ARG	PRO	LEU	LYS	ALA	GLY	GLU	GLU	VAL	GLU
11	LEU	ASP	LEU	LEU	PHE	ALA	GLY	GLY	LYS	VAL
12	LEU	LYS	VAL	VAL	LEU	PRO	VAL	GLU	ALA	ARG

1	GLY	SER	PHE	THR	GLU	GLY	TRP	VAL	ARG	PHE
2	SER	PRO	GLY	PRO	ASN	ALA	ALA	ALA	TYR	LEU
3	THR	LEU	GLU	ASN	PRO	GLY	ASP	LEU	PRO	LEU
4	ARG	LEU	VAL	GLY	ALA	ARG	THR	PRO	VAL	ALA
5	GLU	ARG	VAL	GLU	LEU	HIS	GLU	THR	PHE	MET
6	ARG	GLU	VAL	GLU	GLY	LYS	LYS	VAL	MET	GLY
7	MET	ARG	PRO	VAL	PRO	PHE	LEU	GLU	VAL	PRO
8	PRO	LYS	GLY	ARG	VAL	GLU	LEU	LYS	PRO	GLY
9	GLY	TYR	HIS	PHE	MET	LEU	LEU	GLY	LEU	LYS
10	ARG	PRO	LEU	LYS	ALA	GLY	GLU	GLU	VAL	GLU
11	LEU	ASP	LEU	LEU	PHE	ALA	GLY	GLY	LYS	VAL
12	LEU	LYS	VAL	VAL	LEU	PRO	VAL	GLU	ALA	ARG