BMRB Entry 30063

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30063
MolProbity Validation Chart

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Title:
Structure of calmodulin in a complex with a peptide derived from a calmodulin-dependent kinase
Deposition date:
2016-04-07
Original release date:
2016-09-01
Authors:
Alphonse, S.; Lee, K.; Piserchio, A.; Tavares, C.; Giles, D.; Wellmann, R.; Dalby, K.; Ghose, R.
Citation:

Citation: Lee, K.; Alphonse, S.; Piserchio, A.; Tavares, C.; Giles, D.; Wellmann, R.; Dalby, K.; Ghose, R.. "Structural Basis for the Recognition of Eukaryotic Elongation Factor 2 Kinase by Calmodulin"  Structure 24, 1441-1451 (2016).
PubMed: 27499441

Assembly members:

Assembly members:
Calmodulin, polymer, 148 residues, 16721.350 Da.
Eukaryotic elongation factor 2 kinase, polymer, 27 residues, 3167.618 Da.
CALCIUM ION, non-polymer, 40.078 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: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
Eukaryotic elongation factor 2 kinase: SPANSFHFKEAWKHAIQKAK HMPDPWA

Data sets:
Data typeCount
13C chemical shifts737
15N chemical shifts183
1H chemical shifts1125

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3CALCIUM ION3
4CALCIUM ION3

Entities:

Entity 1, entity_1 148 residues - 16721.350 Da.

1   ALAASPGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHESERLEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEASNGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUTHR
8   METMETALAARGLYSMETLYSASPTHRASP
9   SERGLUGLUGLUILEARGGLUALAPHEARG
10   VALPHEASPLYSASPGLYASNGLYTYRILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPGLUGLU
13   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, entity_2 27 residues - 3167.618 Da.

1   SERPROALAASNSERPHEHISPHELYSGLU
2   ALATRPLYSHISALAILEGLNLYSALALYS
3   HISMETPROASPPROTRPALA

Entity 3, CALCIUM ION - 40.078 Da.

1   CA

Samples:

sample_1: Calmodulin, [U-99% 13C; U-99% 15N], 320 ± 10 uM; eEF2K_74-100 320 ± 10 uM; H2O 95%; D2O 5%; BisTris 20 mM; Potassium Chloride 150 mM; Calcium Chloride 10 mM

sample_2: Calmodulin 595 ± 10 uM; eEF2K_74-100, [U-99% 13C; U-99% 15N], 595 ± 10 uM; H2O 95%; D2O 5%; BisTris 20 mM; Potassium Chloride 150 mM; Calcium Chloride 10 mM

sample_3: Calmodulin, [U-99% 13C; U-99% 15N], 320 uM; eEF2K_74-100 320 uM; D2O 100%; BisTris 20 mM; Potassium Chloride 150 mM; Calcium Chloride 10 mM

sample_4: Calmodulin 320 uM; eEF2K_74-100, [U-99% 13C; U-99% 15N], 320 uM; D2O 100%; BisTris 20 mM; Potassium Chloride 150 mM; Calcium Chloride 10 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 308.15 K

sample_conditions_2: pH: 6.8; pressure: 1 atm; temperature: 308.15 K

sample_conditions_3: pH: 6.8 pD; pressure: 1 atm; temperature: 308.15 K

sample_conditions_4: pH: 6.8 pD; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_3
3D 1H-13C NOESY aliphatic 13C-filteredsample_3isotropicsample_conditions_3
3D HNCOsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D H(CCO)NHsample_2isotropicsample_conditions_2
3D C(CO)NHsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_4isotropicsample_conditions_4
3D 1H-13C NOESY aliphatic 13C filteredsample_4isotropicsample_conditions_4

Software:

ARIA v2.3.1, Linge, O'Donoghue and Nilges - structure calculation

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

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

TOPSPIN v3.1, Bruker Biospin - collection

VNMR, Varian - collection

Xplor_NIH v2.4, NIH; C.D. Schwieters, J.J. Kuszewski, N. Tjandra and G.M. Clore - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 500 MHz

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