BMRB Entry 30135

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30135
MolProbity Validation Chart

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Title:
Structure of the C-terminal Helical Repeat Domain of Elongation Factor 2 Kinase
Deposition date:
2016-07-07
Original release date:
2016-09-09
Authors:
Piserchio, A.; Will, N.; Snyder, I.; Ferguson, S.; Giles, D.; Dalby, K.; Ghose, R.
Citation:

Citation: Will, N.; Piserchio, A.; Snyder, I.; Ferguson, S.; Giles, D.; Dalby, K.; Ghose, R.. "Structure of the C-terminal Helical Repeat Domain of Eukaryotic Elongation Factor 2 Kinase."  Biochemistry 55, 5377-5386 (2016).
PubMed: 27571275

Assembly members:

Assembly members:
entity_1, polymer, 103 residues, 11856.014 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: S3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMSPDRCQDWLEALHWYN TALEMTDCDEGGEYDGMQDE PRYMMLAREAEMLFTGGYGL EKDPQRSGDLYTQAAEAAME AMKGRLANQYYQKAEEAWAQ MEE

Data sets:
Data typeCount
13C chemical shifts416
15N chemical shifts109
1H chemical shifts613

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 103 residues - 11856.014 Da.

1   GLYSERHISMETSERPROASPARGCYSGLN
2   ASPTRPLEUGLUALALEUHISTRPTYRASN
3   THRALALEUGLUMETTHRASPCYSASPGLU
4   GLYGLYGLUTYRASPGLYMETGLNASPGLU
5   PROARGTYRMETMETLEUALAARGGLUALA
6   GLUMETLEUPHETHRGLYGLYTYRGLYLEU
7   GLULYSASPPROGLNARGSERGLYASPLEU
8   TYRTHRGLNALAALAGLUALAALAMETGLU
9   ALAMETLYSGLYARGLEUALAASNGLNTYR
10   TYRGLNLYSALAGLUGLUALATRPALAGLN
11   METGLUGLU

Samples:

sample_1: DTT 4 ± 0.1 mM; eEF2K_627-725, [U-99% 13C; U-99% 15N], 600 ± 30 uM; sodium phosphate 50 ± 1 mM

sample_2: DTT 4 ± 0.1 mM; eEF2K_627-725, [U-99% 13C; U-99% 15N], 300 ± 25 uM; sodium phosphate 50 ± 1 mM

sample_3: DTT 4 ± 0.1 mM; Pf1 phage (ASLA Ltd) 15 ± 1 mg/mL; eEF2K_627-725, [U-99% 13C; U-99% 1, 300 ± 30 uM; sodium phosphate 50 ± 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298.15 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.5 pH*; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
HNCOsample_1isotropicsample_conditions_1
HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
H(CC)CONHsample_1isotropicsample_conditions_1
(H)CCCONHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-15N NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
15N IPAPsample_3anisotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

WhatIF, Vriend - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 600 MHz
  • Bruker AvanceIII 700 MHz
  • Bruker Avance 800 MHz
  • Bruker AvanceIII 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks