BMRB Entry 51723

Name: 1H, 13C, 15N chemical shift assignments for soluble domain of Rieske iron-sulfur protein from Chlorobaculum tepidum
Published: 2023-05-24

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PDB ID: 8hn2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51723
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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, 13C, 15N chemical shift assignments for soluble domain of Rieske iron-sulfur protein from Chlorobaculum tepidum

Deposition date:

2022-12-07

Original release date:

2023-05-24

Authors:

Kishimoto, Hiraku; Mutoh, Risa; Miyanoiri, Yohei; Tanaka, Hideaki; Kurisu, Genji; Oh-oka, Hirozo

Citation:

Citation: Kishimoto, Hiraku; Azai, Chihiro; Yamamoto, Tomoya; Mutoh, Risa; Nakaniwa, Tetsuko; Tanaka, Hideaki; Miyanoiri, Yohei; Kurisu, Genji; Oh-oka, Hirozo. "Soluble domains of cytochrome c-556 and Rieske iron-sulfur protein from Chlorobaculum tepidu m: Crystal structures and interaction analysis" Curr. Res. Struct. Biol. 5, 100101-100101 (2023).
PubMed: 37180033

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 12798 Da.
entity_FES, non-polymer, 175.820 Da.

Natural source:

Natural source: Common Name: green sulfur bacteria Taxonomy ID: 1097 Superkingdom: Bacteria Kingdom: not available Genus/species: Chlorobaculum tepidum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AKKIKIVNELAVGPASDVPN GTGKIYQFNDDKVIVVNHGG SLTAVSAICTHLGCLVHWDE AADMIACPCHGAKYRQDGKI ISGPQPLPLKQYKVKIEDGK IVVSIAKLAAALEHHHHHH

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	1338
15N chemical shifts	609
1H chemical shifts	609

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rieske protein	1
2	[2Fe-2S]	2

Entities:

Entity 1, Rieske protein 119 residues - 12798 Da.

Residues 182-194 is Histidine tag. This is the soluble domain (Residues 76-181) of a transmembrane protein.

1

ALA

LYS

ILE

LYS

ILE

VAL

ASN

GLU

LEU

2

ALA

VAL

GLY

PRO

ALA

SER

ASP

VAL

PRO

ASN

3

GLY

THR

GLY

LYS

ILE

TYR

GLN

PHE

ASN

ASP

4

ASP

LYS

VAL

ILE

VAL

ASN

HIS

GLY

5

SER

LEU

THR

ALA

VAL

SER

ALA

ILE

CYS

THR

6

HIS

LEU

GLY

CYS

LEU

VAL

HIS

TRP

ASP

GLU

7

ALA

ASP

MET

ILE

ALA

CYS

PRO

CYS

HIS

8

GLY

ALA

LYS

TYR

ARG

GLN

ASP

GLY

LYS

ILE

9

ILE

SER

GLY

PRO

GLN

PRO

LEU

PRO

LEU

LYS

10

GLN

TYR

LYS

VAL

LYS

ILE

GLU

ASP

GLY

LYS

11

ILE

VAL

SER

ILE

ALA

LYS

LEU

ALA

12

ALA

LEU

GLU

HIS

Entity 2, [2Fe-2S] - Fe2 S2 - 175.820 Da.

1

FES

Samples:

sample_1: Rieske iron-sulfur protein, [U-13C; U-15N], 1.36 mM; TRIS 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

SPARKY - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz

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