BMRB Entry 15235

Name: 1H, 15N backbone chemical shift assignment of the W155R mutant of the C terminal domain of human frataxin
Published: 2007-05-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15235

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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, 15N backbone chemical shift assignment of the W155R mutant of the C terminal domain of human frataxin

Deposition date:

2007-05-04

Original release date:

2007-05-18

Authors:

Pastore, Chiara; Pastore, Annalisa; Correia, Ana; Gomes, Claudio

Citation:

Citation: Correia, Ana; Pastore, Chiara; Adinolfi, Salvatore; Pastore, Annalisa; Gomes, Claudio. "Dynamics, stability and iron-binding activity of frataxin clinical mutants." FEBS J. 275, 3680-3690 (2008).
PubMed: 18537827

Assembly members:

Assembly members:
hfraW155R, polymer, 123 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hfraW155R: GAMDETTYERLAEETLDSLA EFFEDLADKPYTFEDYDVSF GSGVLTVKLGGDLGTYVINK QTPNKQIRLSSPSSGPKRYD WTGKNWVYSHDGVSLHELLA AELTKALKTKLDLSSLAYSG KDA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	106
1H chemical shifts	106

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hfraW155R	1

Entities:

Entity 1, hfraW155R 123 residues - Formula weight is not available

1

GLY

ALA

MET

ASP

GLU

THR

TYR

GLU

ARG

2

LEU

ALA

GLU

THR

LEU

ASP

SER

LEU

ALA

3

GLU

PHE

GLU

ASP

LEU

ALA

ASP

LYS

PRO

4

TYR

THR

PHE

GLU

ASP

TYR

ASP

VAL

SER

PHE

5

GLY

SER

GLY

VAL

LEU

THR

VAL

LYS

LEU

GLY

6

GLY

ASP

LEU

GLY

THR

TYR

VAL

ILE

ASN

LYS

7

GLN

THR

PRO

ASN

LYS

GLN

ILE

ARG

LEU

SER

8

SER

PRO

SER

GLY

PRO

LYS

ARG

TYR

ASP

9

TRP

THR

GLY

LYS

ASN

TRP

VAL

TYR

SER

HIS

10

ASP

GLY

VAL

SER

LEU

HIS

GLU

LEU

ALA

11

ALA

GLU

LEU

THR

LYS

ALA

LEU

LYS

THR

LYS

12

LEU

ASP

LEU

SER

LEU

ALA

TYR

SER

GLY

13

LYS

ASP

ALA

Samples:

sample_1: hfraW155R, [U-98% 15N], 0.48 mM; NaP 20 mM; NaCl 50 mM; DTT 2 mM

sample_conditions_1: pH: 7; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	15233 15234 15736 15906 16581 4342
PDB	1EKG 1LY7 3S4M 3S5D 3S5E 3S5F
GB	AAH23633 AAH48097 ADQ32463 AIC54401 AIC62492
REF	NP_000135 XP_001137864 XP_003824802 XP_004048150 XP_010344443
SP	Q16595
AlphaFold	Q16595