BMRB Entry 6967

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6967

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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:

1H and 15N assignment of cytochrome c552 from Thermus thermophilus in the oxidized state

Deposition date:

2006-02-02

Original release date:

2006-04-27

Authors:

Muresanu, Lucia; Pristovsek, Primoz; Loehr, Frank; Maneg, Oliver; Mukrasch, Marco; Rueterjans, Heinz; Ludwig, Bernd; Luecke, Christian

Citation:

Citation: Muresanu, Lucia; Pristovsek, Primoz; Loehr, Frank; Maneg, Oliver; Mukrasch, Marco; Rueterjans, Heinz; Ludwig, Bernd; Luecke, Christian. "The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach" J. Biol. Chem. 281, 14503-14513 (2006).
PubMed: 16554303

Assembly members:

Assembly members:
cytochrome c552, polymer, 133 residues, Formula weight is not available
HEM, non-polymer, 616.487 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Vector: pET-22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cytochrome c552: MAQADGAKIYAQCAGCHQQN GQGIPGAFPPLAGHVAEILA KEGGREYLILVLLYGLQGQI EVKGMKYNGVMSSFAQLKDE EIAAVLNHIATAWGDAKKVK GFKPFTAEEVKKLRAKKLTP QQVLTERKKLGLK

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
15N chemical shifts	144
1H chemical shifts	969

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cyt c552	1
2	heme c	2

Entities:

Entity 1, cyt c552 133 residues - Formula weight is not available

The first 2 residues (Met1 and Ala2) are recombinant artifacts.

1

MET

ALA

GLN

ALA

ASP

GLY

ALA

LYS

ILE

TYR

2

ALA

GLN

CYS

ALA

GLY

CYS

HIS

GLN

ASN

3

GLY

GLN

GLY

ILE

PRO

GLY

ALA

PHE

PRO

4

LEU

ALA

GLY

HIS

VAL

ALA

GLU

ILE

LEU

ALA

5

LYS

GLU

GLY

ARG

GLU

TYR

LEU

ILE

LEU

6

VAL

LEU

TYR

GLY

LEU

GLN

GLY

GLN

ILE

7

GLU

VAL

LYS

GLY

MET

LYS

TYR

ASN

GLY

VAL

8

MET

SER

PHE

ALA

GLN

LEU

LYS

ASP

GLU

9

GLU

ILE

ALA

VAL

LEU

ASN

HIS

ILE

ALA

10

THR

ALA

TRP

GLY

ASP

ALA

LYS

VAL

LYS

11

GLY

PHE

LYS

PRO

PHE

THR

ALA

GLU

VAL

12

LYS

LEU

ARG

ALA

LYS

LEU

THR

PRO

13

GLN

VAL

LEU

THR

GLU

ARG

LYS

LEU

14

GLY

LEU

LYS

Entity 2, heme c - C34 H32 Fe N4 O4 - 616.487 Da.

1

HEM

Samples:

sample_1: cytochrome c552 2 mM; potassium phosphate 20 mM; potassium hexacyanoferrate (III) 5 mM

sample_2: cytochrome c552, [U-98% 15N], 2 mM; potassium phosphate 20 mM; potassium hexacyanoferrate (III) 5 mM

conditions_1: pH: 6.0; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-1H_TOCSY	not available	not available	conditions_1
1H-1H_NOESY	not available	not available	conditions_1
15N-1H_TROSY	not available	not available	conditions_1
15N-1H_TOCSY-TROSY	not available	not available	conditions_1
15N-1H_NOESY-TROSY	not available	not available	conditions_1

Software:

xwinnmr v3.5, Bruker - data collection and processing

AURELIA v2.5.9, Bruker - data analysis

NMR spectrometers:

Bruker DMX 600 MHz

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