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Found 1 Document (0.571 seconds)

BMRB: 15233

1LY7

1H, 15N backbone chemical shift assignment of the G130V mutant of the C terminal domain of human frataxin

Authors

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

Assembly

hfraG130V

Entity

1. hfraG130V (polymer, Thiol state: not present), 123 monomers, 13662.02 Da Detail

GAMDETTYER LAEETLDSLA EFFEDLADKP YTFEDYDVSF GSVVLTVKLG GDLGTYVINK QTPNKQIWLS SPSSGPKRYD WTGKNWVYSH DGVSLHELLA AELTKALKTK LDLSSLAYSG KDA

Formula weight

13662.02 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 87.0 %, Completeness: 27.2 %, Completeness (bb): 59.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	27.2 % (231 of 849)	16.8 % (121 of 722)	86.6 % (110 of 127)
Backbone	59.5 % (220 of 370)	45.0 % (113 of 251)	89.9 % (107 of 119)
Sidechain	2.5 % (12 of 479)	1.9 % (9 of 471)	37.5 % (3 of 8)
Aromatic	8.2 % (6 of 73)	4.3 % (3 of 70)	100.0 % (3 of 3)
Methyl	1.4 % (1 of 69)	1.4 % (1 of 69)

1. hfraG130V

GAMDETTYER LAEETLDSLA EFFEDLADKP YTFEDYDVSF GSVVLTVKLG GDLGTYVINK QTPNKQIWLS SPSSGPKRYD WTGKNWVYSH DGVSLHELLA AELTKALKTK LDLSSLAYSG KDA

Show sample condition

Sample

Temperature 298 K, pH 7

#	Name	Isotope labeling	Concentration
1	hfraG130V	[U-98% 15N]	0.5 mM
2	NaP		20 mM
3	NaCl		50 mM
4	DTT		2 mM

Release date

2007-05-17

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

Entries sharing articles BMRB: 3 entries Detail

  BMRB: 15234 released on 2008-05-17
    Title 1H, 15N backbone chemical shift assignment of D122Y mutant of the C terminal domain of human frataxin
  BMRB: 15235 released on 2007-05-17
    Title 1H, 15N backbone chemical shift assignment of the W155R mutant of the C terminal domain of human frataxin
  BMRB: 15236 released on 2007-05-17
    Title 1H, 15N backbone chemical shift assignemnt of the G26K,D27S,D31A triple mutant of the protein CyaY

Related entities 1. hfraG130V, : 1 : 117 entities Detail

Interaction partners 1. hfraG130V, : 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	bmr15233_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: bmr15233_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	218		86.2 (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: 86.2%
- Total number of assignments
  - ¹H chemical shifts: 109
  - ¹⁵N chemical shifts: 109
- 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	722	109	15.1
¹⁵N chemical shifts	129	109	84.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	251	106	42.2
¹⁵N chemical shifts	119	106	89.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	471	3	0.6
¹⁵N chemical shifts	10	3	30.0

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Found 1 Document (0.571 seconds)

BMRB: 15233

Sample

Entries sharing articles BMRB: 3 entries Detail

Related entities 1. hfraG130V, : 1 : 117 entities Detail

Interaction partners 1. hfraG130V, : 4 interactors Detail

Experiments performed 2 experiments Detail

Instrument

Sample

Instrument

Sample

Chemical shift validation 3 contents Detail