BMRB Entry 30305

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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/BMR30305
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Title:
Solution structure of C2 domain from protein kinase C alpha in ternary complex with calcium and V5-pHM peptide
Deposition date:
2017-06-12
Original release date:
2018-04-20
Authors:
Yang, Y.; Igumenova, T.
Citation:

Citation: Yang, Yuan; Shu, Chang; Li, Pingwei; Igumenova, Tatyana. "Structural basis of protein kinase C alpha regulation by the C-terminal tail"  Biophys. J. 114, 1590-1603 (2018).
PubMed: 29642029

Assembly members:

Assembly members:
Protein kinase C alpha type, polymer, 139 residues, 16240.451 Da.
V5-pHM peptide, polymer, 12 residues, 1298.187 Da.
CALCIUM ION, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein kinase C alpha type: HTEKRGRIYLKAEVTDEKLH VTVRDAKNLIPMDPNGLSDP YVKLKLIPDPKNESKQKTKT IRSTLNPQWNESFTFKLKPS DKDRRLSVEIWDWDRTTRND FMGSLSFGVSELMKMPASGW YKLLNQEEGEYYNVPIPEG
V5-pHM peptide: XDQSDFEGFXYX

Data sets:
Data typeCount
1H chemical shifts59

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_3, 13
4entity_3, 23

Entities:

Entity 1, entity_1 139 residues - 16240.451 Da.

1   HISTHRGLULYSARGGLYARGILETYRLEU
2   LYSALAGLUVALTHRASPGLULYSLEUHIS
3   VALTHRVALARGASPALALYSASNLEUILE
4   PROMETASPPROASNGLYLEUSERASPPRO
5   TYRVALLYSLEULYSLEUILEPROASPPRO
6   LYSASNGLUSERLYSGLNLYSTHRLYSTHR
7   ILEARGSERTHRLEUASNPROGLNTRPASN
8   GLUSERPHETHRPHELYSLEULYSPROSER
9   ASPLYSASPARGARGLEUSERVALGLUILE
10   TRPASPTRPASPARGTHRTHRARGASNASP
11   PHEMETGLYSERLEUSERPHEGLYVALSER
12   GLULEUMETLYSMETPROALASERGLYTRP
13   TYRLYSLEULEUASNGLNGLUGLUGLYGLU
14   TYRTYRASNVALPROILEPROGLUGLY

Entity 2, entity_2 12 residues - 1298.187 Da.

1   ACEASPGLNSERASPPHEGLUGLYPHESEP
2   TYRNH2

Entity 3, entity_3, 1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: C2 domain of protein kinase C alpha, [U-13C; U-15N], 0.89 mM; CALCIUM ION 2.225 mM; MES 6.7 mM; V5-pHM peptide 2 mM; potassium chloride 67 mM; sodium azide 0.2 mg/mL

sample_2: C2 domain of protein kinase C alpha, [U-13C; U-15N], 1.47 mM; CALCIUM ION 3.75 mM; MES 6.7 mM; V5-pHM peptide 0.6 mM; potassium chloride 67 mM; sodium azide 0.2 mg/mL

sample_3: C2 domain of protein kinase C alpha, [U-13C; U-15N], 0.89 mM; CALCIUM ION 2.225 mM; MES 6.7 mM; V5-pHM peptide 2 mM; potassium chloride 67 mM; sodium azide 0.2 mg/mL

sample_conditions_1: ionic strength: 0.076 M; pH: 6.0; pressure: 1 atm; temperature: 296.15 K

sample_conditions_2: ionic strength: 0.077 M; pH: 6.0; pressure: 1 atm; temperature: 296.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D aromatic HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D [F2-15N,13C filtered] NOESYsample_1isotropicsample_conditions_1
2D [F2-15N,13C filtered] NOESYsample_3isotropicsample_conditions_1
2D [F1,F2-15N,13C filtered] NOESYsample_1isotropicsample_conditions_1
2D [F1,F2-15N,13C filtered] NOESYsample_2isotropicsample_conditions_2
2D [F1,F2-15N,13C filtered] TOCSYsample_1isotropicsample_conditions_1
2D [F1,F2-15N,13C filtered] TOCSYsample_2isotropicsample_conditions_2
3D [F1-15N,13C filtered] 1H-15N NOESYsample_1isotropicsample_conditions_1
3D [F1-15N,13C filtered] 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

HADDOCK, Bonvin - structure calculation

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

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 800 MHz
  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 500 MHz