BMRB Entry 28003

Name: FDX2
Published: 2019-08-22

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR28003

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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:

FDX2

Deposition date:

2019-08-18

Original release date:

2019-08-22

Authors:

Cai, Kai; Markley, John

Citation:

Citation: Cai, Kai; Tonelli, Marco; Frederick, Ronnie; Markley, John. "Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis" Biochemistry 56, 487-499 (2017).
PubMed: 28001042

Assembly members:

Assembly members:
FDX2, polymer, 131 residues, Formula weight is not available
FE2/S2 (INORGANIC) CLUSTER, non-polymer, 175.820 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FDX2: AGEEDAGGPERPGDVVNVVF VDRSGQRIPVSGRVGDNVLH LAQRHGVDLEGACEASLACS TCHVYVSEDHLDLLPPPEER EDDMLDMAPLLQENSRLGCQ IVLTPELEGAEFTLPKITRN FYVDGHVPKPH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	221
15N chemical shifts	108
1H chemical shifts	108

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FDX2	1
2	2Fe-2S CLUSTER	2

Entities:

Entity 1, FDX2 131 residues - Formula weight is not available

1

ALA

GLY

GLU

ASP

ALA

GLY

PRO

GLU

2

ARG

PRO

GLY

ASP

VAL

ASN

VAL

PHE

3

VAL

ASP

ARG

SER

GLY

GLN

ARG

ILE

PRO

VAL

4

SER

GLY

ARG

VAL

GLY

ASP

ASN

VAL

LEU

HIS

5

LEU

ALA

GLN

ARG

HIS

GLY

VAL

ASP

LEU

GLU

6

GLY

ALA

CYS

GLU

ALA

SER

LEU

ALA

CYS

SER

7

THR

CYS

HIS

VAL

TYR

VAL

SER

GLU

ASP

HIS

8

LEU

ASP

LEU

PRO

GLU

ARG

9

GLU

ASP

MET

LEU

ASP

MET

ALA

PRO

LEU

10

LEU

GLN

GLU

ASN

SER

ARG

LEU

GLY

CYS

GLN

11

ILE

VAL

LEU

THR

PRO

GLU

LEU

GLU

GLY

ALA

12

GLU

PHE

THR

LEU

PRO

LYS

ILE

THR

ARG

ASN

13

PHE

TYR

VAL

ASP

GLY

HIS

VAL

PRO

LYS

PRO

14

HIS

Entity 2, 2Fe-2S CLUSTER - Fe2 S2 - 175.820 Da.

1

FES

Samples:

sample_1: FDX2, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM; Fe-S cluster 0.8 ± 0.1 mM; sodium chloride 150 mM; HEPES 30 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.15 M; 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift calculation

NMR spectrometers:

Bruker Avance 750 MHz

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