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BMRB: 5628

1PBU

1H, 15N and 13C resonance assignments of the highly conserved 19kDa C-terminal domain from human Elongation Factor 1Bgamma

Authors

Vanwetswinkel, S., Kriek, J., Andersen, G.R., Dijk, J., Canters, G.W., Siegal, G.

Assembly

C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1

Entity

1. C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1 (polymer, Thiol state: all free), 162 monomers, 19045.11 Da Detail

AKDPFAHLPK STFALDEFKR KYSNEDTLSV ALPYFWEHFD KDGWSLWYSE YRFPEELTQT FMSCNLITGM FQRLDKLRKN AFASVILFGT NNSSSISGVW VFRGQELAFP LSPDWQVDYE SYTWRKLDPG SEETQTLVRE YFSWEGAFQH VGKAFNQGKI FK

Formula weight

19045.11 Da

Source organism

Homo sapiens

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 100.0 %, Completeness: 88.6 %, Completeness (bb): 85.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	88.6 % (1773 of 2001)	97.5 % (1013 of 1039)	75.3 % (593 of 787)	95.4 % (167 of 175)
Backbone	85.0 % (814 of 958)	98.5 % (321 of 326)	72.1 % (344 of 477)	96.1 % (149 of 155)
Sidechain	93.0 % (1112 of 1196)	97.1 % (692 of 713)	86.8 % (402 of 463)	90.0 % (18 of 20)
Aromatic	79.5 % (248 of 312)	92.9 % (145 of 156)	64.4 % (96 of 149)	100.0 % (7 of 7)
Methyl	98.5 % (134 of 136)	98.5 % (67 of 68)	98.5 % (67 of 68)

1. C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1

AKDPFAHLPK STFALDEFKR KYSNEDTLSV ALPYFWEHFD KDGWSLWYSE YRFPEELTQT FMSCNLITGM FQRLDKLRKN AFASVILFGT NNSSSISGVW VFRGQELAFP LSPDWQVDYE SYTWRKLDPG SEETQTLVRE YFSWEGAFQH VGKAFNQGKI FK

Show sample condition

Sample #1

Temperature 298 (±0.5) K, pH 7.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1	[U-15N]	1.0 mM
2	Tris		20 mM
3	potassium chloride		75 mM
4	DTT		1 mM
5	sodium azide		0.02 %

Sample #2

Temperature 298 (±0.5) K, pH 7.5 (±0.2)

#	Name	Isotope labeling	Concentration
6	C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1	[U-15N; U-13C]	1.0 mM
7	Tris		20 mM
8	potassium chloride		75 mM
9	DTT		1 mM
10	sodium azide		0.02 %

Sample #3

Temperature 298 (±0.5) K, pH 7.5 (±0.2)

#	Name	Isotope labeling	Concentration
11	C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1	[U-10% 13C]	1.0 mM
12	Tris		20 mM
13	potassium chloride		75 mM
14	DTT		1 mM
15	sodium azide		0.02 %

Chem. Shift Complete2

Sequence coverage: 28.4 %, Completeness: 53.2 %, Completeness (bb): 54.0 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	53.2 % (2130 of 4002)	57.5 % (1195 of 2078)	46.2 % (727 of 1574)	59.4 % (208 of 350)
Backbone	54.0 % (1035 of 1916)	60.9 % (397 of 652)	47.0 % (448 of 954)	61.3 % (190 of 310)
Sidechain	53.6 % (1282 of 2392)	56.0 % (798 of 1426)	50.3 % (466 of 926)	45.0 % (18 of 40)
Aromatic	41.0 % (256 of 624)	47.8 % (149 of 312)	33.6 % (100 of 298)	50.0 % (7 of 14)
Methyl	56.3 % (153 of 272)	55.9 % (76 of 136)	56.6 % (77 of 136)

1. C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1

AKDPFAHLPK STFALDEFKR KYSNEDTLSV ALPYFWEHFD KDGWSLWYSE YRFPEELTQT FMSCNLITGM FQRLDKLRKN AFASVILFGT NNSSSISGVW VFRGQELAFP LSPDWQVDYE SYTWRKLDPG SEETQTLVRE YFSWEGAFQH VGKAFNQGKI FK

Show sample condition

Sample #1

Temperature 298 (±0.5) K, pH 7.5 (±0.2)

#	Name	Isotope labeling	Concentration
1	C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1	[U-15N]	1.0 mM
2	Tris		20 mM
3	potassium chloride		75 mM
4	DTT		1 mM
5	sodium azide		0.02 %

Sample #2

Temperature 298 (±0.5) K, pH 7.5 (±0.2)

#	Name	Isotope labeling	Concentration
6	C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1	[U-15N; U-13C]	1.0 mM
7	Tris		20 mM
8	potassium chloride		75 mM
9	DTT		1 mM
10	sodium azide		0.02 %

Sample #3

Temperature 298 (±0.5) K, pH 7.5 (±0.2)

#	Name	Isotope labeling	Concentration
11	C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1	[U-10% 13C]	1.0 mM
12	Tris		20 mM
13	potassium chloride		75 mM
14	DTT		1 mM
15	sodium azide		0.02 %

Release date

2003-04-29

Citation

Letter to the Editor: 1H, 15N and 13C resonance assignments of the highly conserved 19kDa C-terminal domain from human Elongation Factor 1Bgamma
Vanwetswinkel, S., Kriek, J., Andersen, G.R., Dijk, J., Siegal, G.
J. Biomol. NMR (2003), 26, 189-190, PubMed , DOI:

Related entities 1. C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1, : 1 : 4 : 50 entities Detail

Interaction partners 1. C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1, : 191 interactors Detail

More details for 191 interactors identified by 49 citations

Chemical shift validation 4 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr5628_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: bmr5628_3.str

#	Content subtype	Saveframe	Status	# of rows	Sequence coverage (%)
1	Assigned chemical shifts	shift_set_1	Warning	1873	100.0 (chain: 1, length: 162)
2	Assigned chemical shifts	shift_set_2	Warning	19	4.9 (chain: 1, length: 162)
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: 162, Sequence coverage: 100.0%
- Total number of assignments
  - ¹³C chemical shifts: 560
  - ¹H chemical shifts: 1146
  - ¹⁵N chemical shifts: 167
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Peptide bond of PRO
- Tautomeric state of HIS
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1
Saveframe: shift_set_2
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 162, Sequence coverage: 4.9%
- Total number of assignments
  - ¹H chemical shifts: 10
  - ¹⁵N chemical shifts: 8
  - ¹³C chemical shifts: 1
- Completeness of assignments
- 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 (%)
¹³C chemical shifts	787	560	71.2
¹H chemical shifts	1039	1008	97.0
¹⁵N chemical shifts	182	167	91.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	324	162	50.0
¹H chemical shifts	326	320	98.2
¹⁵N chemical shifts	155	148	95.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	463	398	86.0
¹H chemical shifts	713	688	96.5
¹⁵N chemical shifts	27	19	70.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	70	69	98.6
¹H chemical shifts	70	69	98.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	149	93	62.4
¹H chemical shifts	156	145	92.9
¹⁵N chemical shifts	7	7	100.0

Keywords eukaryotic protein synthesis, elongation factor 1, tryptic fragment, aromatic content

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Found 1 Document (7.186 seconds)

BMRB: 5628

Sample #1

Sample #2

Sample #3

Sample #1

Sample #2

Sample #3

Related entities 1. C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1, : 1 : 4 : 50 entities Detail

Interaction partners 1. C-terminal domain [276-437] of the human EF1Bgamma subunit from elongation factor 1, : 191 interactors Detail

Chemical shift validation 4 contents Detail