BMRBj - BMREntryMaster

Found 1 Document (1.796 seconds)

BMRB: 6116

3E1Y

Backbone 1H, 13C and 15N resonance assignment of the N-terminal domain of human eRF1

Authors

Oda, Y.

Assembly

N-terminal domain of human eRF1

Entity

1. N-terminal domain of human eRF1 (polymer, Thiol state: all free), 142 monomers, 15677.01 Da Detail

MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADEFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI NTSLYLCDNK FHTEALTALL SD

Formula weight

15677.01 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.3 %, Completeness: 38.7 %, Completeness (bb): 69.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	38.7 % (645 of 1665)	23.4 % (203 of 868)	47.1 % (306 of 649)	91.9 % (136 of 148)
Backbone	69.0 % (578 of 838)	53.5 % (152 of 284)	69.5 % (291 of 419)	100.0 % (135 of 135)
Sidechain	21.0 % (202 of 962)	8.9 % (52 of 584)	40.8 % (149 of 365)	7.7 % (1 of 13)
Aromatic	0.0 % (0 of 80)	0.0 % (0 of 40)	0.0 % (0 of 39)	0.0 % (0 of 1)
Methyl	17.0 % (31 of 182)	15.4 % (14 of 91)	18.7 % (17 of 91)

1. N-terminal domain of human eRF1

MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADEFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI NTSLYLCDNK FHTEALTALL SD

Show sample condition

Sample

Temperature 298 (±1) K, pH 6.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
1	N-terminal domain of human eRF1	[U-95% 13C; U-95% 15N]		0.5 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: -0.09 ppm, Outliers: 3 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: -0.09 ppm, Outliers: 3 Detail

Release date

2004-09-30

Citation

Backbone (1)H, (13)C and (15)N resonance assignment of the N-terminal domain of human eRF1
Oda, Y., Muramatsu, T., Yumoto, F., Ito, M., Tanokura, M.
J. Biomol. NMR (2004), 30, 109-110, PubMed 15452443 , DOI 10.1023/B:JNMR.0000042944.14441.d6 , Abstract

Related entities 1. N-terminal domain of human eRF1, : 1 : 14 : 2 : 7 : 86 entities Detail

Interaction partners 1. N-terminal domain of human eRF1, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr6116_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	Warning

Disulfide bonds

None

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

None

Non-standard residues

None

Content subtype: bmr6116_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	543		98.6 (chain: 1, length: 142)
1	Chemical shift references	chemical_shift_reference	OK	3		No information

Assigned chemical shifts

Saveframe: shift_set_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 142, Sequence coverage: 98.6%
- Total number of assignments
  - ¹H chemical shifts: 135
  - ¹⁵N chemical shifts: 135
  - ¹³C chemical shifts: 273
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

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Found 1 Document (1.796 seconds)

BMRB: 6116

Sample

Chemical shift reference

Chemical shift reference

Related entities 1. N-terminal domain of human eRF1, : 1 : 14 : 2 : 7 : 86 entities Detail

Interaction partners 1. N-terminal domain of human eRF1, : 1 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample

Chemical shift validation 3 contents Detail

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	868	135	15.6
¹⁵N chemical shifts	154	135	87.7
¹³C chemical shifts	649	273	42.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	284	135	47.5
¹⁵N chemical shifts	135	135	100.0
¹³C chemical shifts	284	140	49.3