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BMRB: 30569

6NX4

Structure of the C-terminal Helical Repeat Domain of Eukaryotic Elongation Factor 2 Kinase (eEF-2K)

Authors

Piserchio, A., Will, N., Giles, D.H., Hajredini, F., Dalby, K.N., Ghose, R.

Assembly

Eukaryotic elongation factor 2 kinase (E.C.2.7.11.20)

Entity

1. Eukaryotic elongation factor 2 kinase (E.C.2.7.11.20) (polymer, Thiol state: all free), 167 monomers, 18874.86 Da Detail

SHMGELEAIV GLGLMYSQLP HHILADVSLK ETEENKTKGF DYLLKAAEAG DRQSMILVAR AFDSGQNLSP DRCQDWLEAL HWYNTALEMT DCDEGGEYDG MQDEPRYMML AREAEMLFTG GYGLEKDPQR SGDLYTQAAE AAMEAMKGRL ANQYYQKAEE AWAQMEE

Formula weight

18874.86 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts, spectral_peak_list

Chem. Shift Complete

Sequence coverage: 99.4 %, Completeness: 97.2 %, Completeness (bb): 98.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	97.2 % (1845 of 1898)	96.7 % (954 of 987)	97.5 % (713 of 731)	98.9 % (178 of 180)
Backbone	98.6 % (980 of 994)	98.0 % (337 of 344)	99.0 % (482 of 487)	98.8 % (161 of 163)
Sidechain	96.2 % (1017 of 1057)	96.0 % (617 of 643)	96.5 % (383 of 397)	100.0 % (17 of 17)
Aromatic	89.6 % (138 of 154)	89.6 % (69 of 77)	89.2 % (66 of 74)	100.0 % (3 of 3)
Methyl	98.6 % (146 of 148)	98.6 % (73 of 74)	98.6 % (73 of 74)

1. entity 1

SHMGELEAIV GLGLMYSQLP HHILADVSLK ETEENKTKGF DYLLKAAEAG DRQSMILVAR AFDSGQNLSP DRCQDWLEAL HWYNTALEMT DCDEGGEYDG MQDEPRYMML AREAEMLFTG GYGLEKDPQR SGDLYTQAAE AAMEAMKGRL ANQYYQKAEE AWAQMEE

Show sample condition

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 200 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 20 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	200 (±20.0) uM
2	sodium phosphate	natural abundance	20 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	4 (±0.4) mM
5	EDTA	natural abundance	0.2 (±0.02) mM
6	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

Sample #2

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 400 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 20 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

Sample #3

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 340 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 14 mg/mL Pf1 phage, 14 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
13	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	340 (±35.0) uM
14	sodium phosphate	natural abundance	14 (±2.0) mM
15	sodium chloride	natural abundance	100 (±5.0) mM
16	DTT	natural abundance	4 (±0.4) mM
17	EDTA	natural abundance	0.2 (±0.02) mM
18	AEBSF protease inhibitor	natural abundance	2 (±0.2) mM
19	Pf1 phage	natural abundance	14 (±2.0) mg/mL

Sample #4

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 360 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 20 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
20	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	360 (±36.0) uM
21	sodium phosphate	natural abundance	20 (±1.0) mM
22	sodium chloride	natural abundance	100 (±5.0) mM
23	DTT	natural abundance	4 (±0.4) mM
24	EDTA	natural abundance	0.2 (±0.02) mM
25	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

LACS Plot; CA

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

Referencing offset: -0.2 ppm, Outliers: 1 Detail

LACS Plot; CB

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

Referencing offset: -0.2 ppm, Outliers: 1 Detail

LACS Plot; HA

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

Referencing offset: 0.05 ppm, Outliers: 1 Detail

LACS Plot; CO

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

Referencing offset: -0.05 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 6NX4, Strand ID: A Detail

Release date

2019-05-20

Citation

Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and its Role in Substrate Recognition
Piserchio, A., Will, N., Giles, D.H., Hajredini, F., Dalby, K.N., Ghose, R.
J. Mol. Biol. (2019), 431, 2700-2717, PubMed 31108082 , DOI 10.1016/j.jmb.2019.05.019 , Abstract

Related entities 1. Eukaryotic elongation factor 2 kinase (E.C.2.7.11.20), : 1 : 2 : 8 entities Detail

Interaction partners 1. Eukaryotic elongation factor 2 kinase (E.C.2.7.11.20), : 7 interactors Detail

More details for 7 interactors identified by 5 citations

Experiments performed 17 experiments Detail

1 3D 1H-15N NOESY

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 200 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 20 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
1	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	200 (±20.0) uM
2	sodium phosphate	natural abundance	20 (±1.0) mM
3	sodium chloride	natural abundance	100 (±5.0) mM
4	DTT	natural abundance	4 (±0.4) mM
5	EDTA	natural abundance	0.2 (±0.02) mM
6	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

2 4D HC-HSQC-NOESY-HN-HSQC

Instrument

Bruker Avance - 900 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 360 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 20 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
20	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	360 (±36.0) uM
21	sodium phosphate	natural abundance	20 (±1.0) mM
22	sodium chloride	natural abundance	100 (±5.0) mM
23	DTT	natural abundance	4 (±0.4) mM
24	EDTA	natural abundance	0.2 (±0.02) mM
25	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

3 3D 3D NNH (15N-HSQC-NOESY-15N-HSQC

Instrument

Bruker AVANCE III - 800 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 400 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 20 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

4 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
20	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	360 (±36.0) uM
21	sodium phosphate	natural abundance	20 (±1.0) mM
22	sodium chloride	natural abundance	100 (±5.0) mM
23	DTT	natural abundance	4 (±0.4) mM
24	EDTA	natural abundance	0.2 (±0.02) mM
25	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

5 3D H-13C NOESY aromatic

Instrument

Bruker Avance - 800 MHz

Sample

#	Name	Isotope labeling	Concentration
20	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	360 (±36.0) uM
21	sodium phosphate	natural abundance	20 (±1.0) mM
22	sodium chloride	natural abundance	100 (±5.0) mM
23	DTT	natural abundance	4 (±0.4) mM
24	EDTA	natural abundance	0.2 (±0.02) mM
25	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

6 3D HNCO

Instrument

Bruker AVANCE III - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

7 3D HNCA

Instrument

Bruker AVANCE III - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

8 3D HN(CO)CA

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

9 3D HNCACB

Instrument

Bruker AVANCE III - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

10 3D CBCA(CO)NH

Instrument

Bruker AVANCE III - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

11 3D HN(CA)CO

Instrument

Bruker AVANCE III - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

12 3D Hcc(co)NH

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

13 3D hCc(co)NH

Instrument

Bruker AVANCE III - 600 MHz

Sample

State anisotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 400 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 20 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

14 3D HCCH-TOCSY

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

15 3D HCCH-TOCSY

Instrument

Bruker AVANCE III - 600 MHz

Sample

#	Name	Isotope labeling	Concentration
7	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	400 (±40.0) uM
8	sodium phosphate	natural abundance	20 (±1.0) mM
9	sodium chloride	natural abundance	100 (±5.0) mM
10	DTT	natural abundance	4 (±0.4) mM
11	EDTA	natural abundance	0.2 (±0.02) mM
12	AEBSF protease inhibitor	natural abundance	2 (±0.02) mM

16 2D 15N HSQC-IPAP

Instrument

Bruker AVANCE III - 700 MHz

Sample

State anisotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298.15 K, pH 6.5 (±0.1), Details 340 uM [U-99% 13C; U-99% 15N] eEF2K (562-725), 14 mg/mL Pf1 phage, 14 mM sodium phosphate, 100 mM sodium chloride, 4 mM DTT, 0.2 mM EDTA, 2 mM AEBSF protease inhibitor, 95% H2O/5% D2O

#	Name	Isotope labeling	Concentration
13	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	340 (±35.0) uM
14	sodium phosphate	natural abundance	14 (±2.0) mM
15	sodium chloride	natural abundance	100 (±5.0) mM
16	DTT	natural abundance	4 (±0.4) mM
17	EDTA	natural abundance	0.2 (±0.02) mM
18	AEBSF protease inhibitor	natural abundance	2 (±0.2) mM
19	Pf1 phage	natural abundance	14 (±2.0) mg/mL

17 3D IPAP-J-HNCO

Instrument

Bruker AVANCE III - 700 MHz

Sample

#	Name	Isotope labeling	Concentration
13	eEF2K (562-725)	[U-99% 13C; U-99% 15N]	340 (±35.0) uM
14	sodium phosphate	natural abundance	14 (±2.0) mM
15	sodium chloride	natural abundance	100 (±5.0) mM
16	DTT	natural abundance	4 (±0.4) mM
17	EDTA	natural abundance	0.2 (±0.02) mM
18	AEBSF protease inhibitor	natural abundance	2 (±0.2) mM
19	Pf1 phage	natural abundance	14 (±2.0) mg/mL

NMR combined restraints 6 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints, RDC restraints	combined_30569_6nx4.nef
Input source #2: Coordindates	6nx4.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

-560-----570-------580-------590-------600-------610-------620-------630-------640-------650-------6
SHMGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDG
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SHMGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDG
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100

60-------670-------680-------690-------700-------710-------720-----
MQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
MQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE
-------110-------120-------130-------140-------150-------160-------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	167	0	0	100.0

Content subtype: combined_30569_6nx4.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	1849		99.4 (chain: A, length: 167)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	OK	2094 (1)	noe	95.2 (chain: A, length: 167)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	230 (230)	.	79.0 (chain: A, length: 167)
1	RDC restraints	CNS/XPLOR_dipolar_coupling_3	OK	65 (65)	.	49.1 (chain: A, length: 167)
2	RDC restraints	CNS/XPLOR_dipolar_coupling_5	OK	70 (70)	.	41.9 (chain: A, length: 167)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 99.4%
- Total number of assignments
  - ¹³C chemical shifts: 712
  - ¹H chemical shifts: 954
  - ¹⁵N chemical shifts: 183
- Completeness of assignments
  - Entity_assemble_ID: A
- 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: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	731	712	97.4
¹H chemical shifts	987	954	96.7
¹⁵N chemical shifts	187	183	97.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	334	330	98.8
¹H chemical shifts	344	338	98.3
¹⁵N chemical shifts	163	160	98.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	397	382	96.2
¹H chemical shifts	643	616	95.8
¹⁵N chemical shifts	24	23	95.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	85	85	100.0
¹H chemical shifts	85	85	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹³C chemical shifts	74	64	86.5
¹H chemical shifts	77	67	87.0
¹⁵N chemical shifts	3	3	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 95.2%
- Total number of restraints: 2094
- Weight of restraints: 1.0 (2094)
- Potential type of restraints: square-well-parabolic (2094)
- Range of distance target values: 1.52, 7.55 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 79.0%
- Total number of restraints: 230
- Total number of restraints per polymer type: 230
- Weight of restraints: 1.0 (230)
- Potential type of restraints: square-well-parabolic (230)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

RDC restraints

Saveframe: CNS/XPLOR_dipolar_coupling_3
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 49.1%
- Total number of restraints: 65
- Potential type of restraints: undefined (65)
- Range of observed RDC values: 100.0, -100.0 (Hz)
- RDC restraints per residue
- Saveframe: CNS/XPLOR_dipolar_coupling_5
  - Status: OK
  - Experiment type: .
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 167, Sequence coverage: 41.9%
  - Total number of restraints: 70
  - Potential type of restraints: undefined (70)
  - Range of observed RDC values: 100.0, -100.0 (Hz)
  - RDC restraints per residue

Keywords SEL1, TPR, TRANSLATION, binding domain, eEF2, eEF2K, elongation, kinase, transferase

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Found 1 Document (1.374 seconds)

BMRB: 30569

Sample #1

Sample #2

Sample #3

Sample #4

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. Eukaryotic elongation factor 2 kinase (E.C.2.7.11.20), : 1 : 2 : 8 entities Detail

Interaction partners 1. Eukaryotic elongation factor 2 kinase (E.C.2.7.11.20), : 7 interactors Detail

Experiments performed 17 experiments Detail

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NMR combined restraints 6 contents Detail