BMRB Entry 17146

Name: 1H, 13C, and 15N backbone, side-chain, and heme chemical shift assignments for the reduced form of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum
Published: 2010-10-04

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17146

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N backbone, side-chain, and heme chemical shift assignments for the reduced form of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum

Deposition date:

2010-08-24

Original release date:

2010-10-04

Authors:

Cort, John; Swenson, Michael; Magnuson, Timothy

Citation:

Citation: Cort, John; Swenson, Michael; Magnuson, Timothy. "(1)H, (13)C, and (15)N backbone, side-chain, and heme chemical shift assignments for oxidized and reduced forms of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum." Biomol. NMR Assignments 5, 89-92 (2011).
PubMed: 21197590

Assembly members:

Assembly members:
ApcA, polymer, 102 residues, Formula weight is not available
HEM, non-polymer, 616.487 Da.

Natural source:

Natural source: Common Name: a-proteobacteria Taxonomy ID: 524 Superkingdom: Bacteria Kingdom: not available Genus/species: Acidiphilium cryptum

Experimental source:

Experimental source: Production method: purified from the natural source Host organism: Acidiphilium cryptum

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ApcA: ANVAHGKALFQAQCAACHSV SPGQNGIGPSLAGVYGAKAA ATPGFQFSPALKKSGIVWNA STLDKFLANPQADVPGTKMP YMGMANATDRADVVAYLQTL GK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	431
15N chemical shifts	107
1H chemical shifts	670

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ApcA	1
2	heme	2

Entities:

Entity 1, ApcA 102 residues - Formula weight is not available

An N-terminal 21 amino acid signal sequence is not present and presumably was cleaved by the host organism.

1

ALA

ASN

VAL

ALA

HIS

GLY

LYS

ALA

LEU

PHE

2

GLN

ALA

GLN

CYS

ALA

CYS

HIS

SER

VAL

3

SER

PRO

GLY

GLN

ASN

GLY

ILE

GLY

PRO

SER

4

LEU

ALA

GLY

VAL

TYR

GLY

ALA

LYS

ALA

5

ALA

THR

PRO

GLY

PHE

GLN

PHE

SER

PRO

ALA

6

LEU

LYS

SER

GLY

ILE

VAL

TRP

ASN

ALA

7

SER

THR

LEU

ASP

LYS

PHE

LEU

ALA

ASN

PRO

8

GLN

ALA

ASP

VAL

PRO

GLY

THR

LYS

MET

PRO

9

TYR

MET

GLY

MET

ALA

ASN

ALA

THR

ASP

ARG

10

ALA

ASP

VAL

ALA

TYR

LEU

GLN

THR

LEU

11

GLY

LYS

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

1

HEM

Samples:

sample_1: ApcA, [U-100% 13C; U-100% 15N], 0.5 mM; sodium acetate 25 mM; sodium chloride 100 mM; DTT 5 mM

sample_2: ApcA 0.5 mM; sodium acetate 25 mM; sodium chloride 100 mM; DTT 5 mM

sample_3: ApcA, [U-100% 13C; U-100% 15N], 0.5 mM; sodium acetate 25 mM; sodium chloride 100 mM; DTT 5 mM

sample_4: ApcA, 7%-biosynthetically directed 13C, 50%-U-15N, 0.5 mM; sodium acetate 25 mM; sodium chloride 100 mM; DTT 5 mM

sample_conditions_1: ionic strength: 125 mM; pH: 5.0; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_4	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
4D 1H-13C HMQC-NOESY-HMQC	sample_3	isotropic	sample_conditions_1
2D HBCBCGCDHD-ARO	sample_3	isotropic	sample_conditions_1
2D HBCBCGCDCEHE-ARO	sample_3	isotropic	sample_conditions_1
3D CBCA(COCA)HA	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1

Software:

FELIX, Accelrys Software Inc. - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz
Varian UnityPlus 500 MHz

NCBI	YP_001235217.1
UNP	A5G0B6
BMRB	17144
DBJ	BAJ81692 GAN75771
GB	ABQ31298 EGO93894 KDM67854
REF	WP_007424422
AlphaFold	A5G0B6