BMRB Entry 28002

Name: FDX1
Published: 2019-08-22

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR28002

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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:

FDX1

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:
FDX1, polymer, 124 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):
FDX1: SSSEDKITVHFINRDGETLT TKGKVGDSLLDVVVENNLDI DGFGACEGTLACSTCHLIFE DHIYEKLDAITDEENDMLDL AYGLTDRSRLGCQICLTKSM DNMTVRVPETVADARQSIDV GKTS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	204
15N chemical shifts	103
1H chemical shifts	103

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FDX1	1
2	2Fe-2S CLUSTER	2

Entities:

Entity 1, FDX1 124 residues - Formula weight is not available

1

SER

GLU

ASP

LYS

ILE

THR

VAL

HIS

2

PHE

ILE

ASN

ARG

ASP

GLY

GLU

THR

LEU

THR

3

THR

LYS

GLY

LYS

VAL

GLY

ASP

SER

LEU

4

ASP

VAL

GLU

ASN

LEU

ASP

ILE

5

ASP

GLY

PHE

GLY

ALA

CYS

GLU

GLY

THR

LEU

6

ALA

CYS

SER

THR

CYS

HIS

LEU

ILE

PHE

GLU

7

ASP

HIS

ILE

TYR

GLU

LYS

LEU

ASP

ALA

ILE

8

THR

ASP

GLU

ASN

ASP

MET

LEU

ASP

LEU

9

ALA

TYR

GLY

LEU

THR

ASP

ARG

SER

ARG

LEU

10

GLY

CYS

GLN

ILE

CYS

LEU

THR

LYS

SER

MET

11

ASP

ASN

MET

THR

VAL

ARG

VAL

PRO

GLU

THR

12

VAL

ALA

ASP

ALA

ARG

GLN

SER

ILE

ASP

VAL

13

GLY

LYS

THR

SER

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

1

FES

Samples:

sample_1: FDX1, [U-100% 13C; U-100% 15N], 0.8 mM; sodium chloride 150 mM; TCEP 3 mM; HEPES 30 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 25 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

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