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BMRB: 15234

1LY7

1H, 15N backbone chemical shift assignment of D122Y mutant of the C terminal domain of human frataxin

Authors

Pastore, C., Pastore, A., Correia, A.R., Gomes, C.M.

Assembly

D122Y mutant of the C terminal domain of human frataxin

Entity

1. D122Y mutant of the C terminal domain of human frataxin (polymer, Thiol state: not present), 123 monomers, 13668.03 Da Detail

GAMDETTYER LAEETLDSLA EFFEDLADKP YTFEYYDVSF GSGVLTVKLG GDLGTYVINK QTPNKQIWLS SPSSGPKRYD WTGKNWVYSH DGVSLHELLA AELTKALKTK LDLSSLAYSG KDA

Formula weight

13668.03 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 85.4 %, Completeness: 27.8 %, Completeness (bb): 57.4 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	27.8 % (237 of 851)	18.0 % (130 of 724)	84.3 % (107 of 127)
Backbone	57.4 % (213 of 371)	43.3 % (109 of 252)	87.4 % (104 of 119)
Sidechain	5.0 % (24 of 480)	4.4 % (21 of 472)	37.5 % (3 of 8)
Aromatic	7.8 % (6 of 77)	4.1 % (3 of 74)	100.0 % (3 of 3)
Methyl	7.5 % (5 of 67)	7.5 % (5 of 67)

1. hfraD122Y

GAMDETTYER LAEETLDSLA EFFEDLADKP YTFEYYDVSF GSGVLTVKLG GDLGTYVINK QTPNKQIWLS SPSSGPKRYD WTGKNWVYSH DGVSLHELLA AELTKALKTK LDLSSLAYSG KDA

Show sample condition

Sample

Temperature 298 K, pH 7.0

#	Name	Isotope labeling	Concentration
1	hfraD122Y	[U-98% 15N]	0.5 mM
2	NaP		20 mM
3	NaCl		50 mM
4	DTT		2 mM

Release date

2008-05-17

Citation

Dynamics, stability and iron-binding activity of frataxin clinical mutants
Correia, A.R., Pastore, C., Adinolfi, S., Pastore, A., Gomes, C.M.
FEBS J. (2008), 275, 3680-3690, PubMed 18537827 , DOI 10.1111/j.1742-4658.2008.06512.x , Abstract

Related entities 1. D122Y mutant of the C terminal domain of human frataxin, : 1 : 114 entities Detail

Interaction partners 1. D122Y mutant of the C terminal domain of human frataxin, : 4 interactors Detail

More details for 4 interactors identified by 2 citations

Experiments performed 2 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr15234_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	OK

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr15234_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	212		83.7 (chain: 1, length: 123)
1	Chemical shift references	chemical_shift_reference_1	OK	2		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 123, Sequence coverage: 83.7%
- Total number of assignments
  - ¹H chemical shifts: 106
  - ¹⁵N chemical shifts: 106
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	724	106	14.6
¹⁵N chemical shifts	129	106	82.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	252	103	40.9
¹⁵N chemical shifts	119	103	86.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	472	3	0.6
¹⁵N chemical shifts	10	3	30.0

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Found 1 Document (0.437 seconds)

BMRB: 15234

Sample

Related entities 1. D122Y mutant of the C terminal domain of human frataxin, : 1 : 114 entities Detail

Interaction partners 1. D122Y mutant of the C terminal domain of human frataxin, : 4 interactors Detail

Experiments performed 2 experiments Detail

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Sample

Instrument

Sample

Chemical shift validation 3 contents Detail