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Biological Magnetic Resonance Data Bank


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BMRB Entry 26016

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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/BMR26016
MolProbity Validation Chart

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Title: Solution Structure of Ca2+-bound C2 domain from Protein Kinase C alpha in the form of complex with V5-pHM peptide   PubMed: 29642029

Deposition date: 2016-03-28 Original release date: 2017-03-24

Authors: Yang, Yuan; Igumenova, Tatyana

Citation: Yang, Yuan; Shu, Chang; Li, Pingwei; Igumenova, Tatyana. "Structural Basis of Protein Kinase Calpha Regulation by the C-Terminal Tail."  Biophys. J. 114, 1590-1603 (2018).

Assembly members:
C2, polymer, 139 residues, 16240.596 Da.
CALCIUM ION, non-polymer, 40.078 Da.

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

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

Entity Sequences (FASTA):
C2: HTEKRGRIYLKAEVTDEKLH VTVRDAKNLIPMDPNGLSDP YVKLKLIPDPKNESKQKTKT IRSTLNPQWNESFTFKLKPS DKDRRLSVEIWDWDRTTRND FMGSLSFGVSELMKMPASGW YKLLNQEEGEYYNVPIPEG

Data sets:
Data typeCount
13C chemical shifts604
15N chemical shifts148
1H chemical shifts967

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2CALCIUM ION_12
3CALCIUM ION_22

Entities:

Entity 1, entity_1 139 residues - 16240.596 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, CALCIUM ION_1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: CALCIUM ION 2.225 mM; C2, [U-13C; U-15N], 0.89 mM; MES 6.7 mM; potassium chloride 67 mM; sodium azide 0.02%; pHM peptide 2 mM; H2O 92%; D2O 8%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

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

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis

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

PSVS, Bhattacharya and Montelione - structural validation

CcpNMR, CCPN - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts