BMRB Entry 25791

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25791
MolProbity Validation Chart

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Title:
Solution structure of kinase in complex with its regulatory protein
Deposition date:
2015-09-02
Original release date:
2016-07-13
Authors:
Veverka, Vaclav; Hexnerova, Rozalie
Citation:

Citation: Klima, Martin; Toth, Daniel; Hexnerova, Rozalie; Baumlova, Adriana; Chalupska, Dominika; Tykvart, Jan; Rezabkova, Lenka; Sengupta, Nivedita; Man, Petr; Dubankova, Anna; Humpolickova, Jana; Nencka, Radim; Veverka, Vaclav; Balla, Tamas; Boura, Evzen. "Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein"  Sci. Rep. 6, 23641-23641 (2016).
PubMed: 27009356

Assembly members:

Assembly members:
entity_1, polymer, 69 residues, 8293.291 Da.
entity_2, polymer, 80 residues, 8010.200 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: n/a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQQKQQIMAALNSQTAVQFQ QYAAQQYPGNYEQQQILIRQ LQEQHYQQYMQQLYQVQLAQ QQAALQKQQ
entity_2: GAMVEARSLAVAMGDTVVEP APLKPTSEPTSGPPGNNGGS LLSVITEGVGELSVIDPEVA QKACQEVLEKVKLLHGGVAV

Data sets:
Data typeCount
13C chemical shifts611
15N chemical shifts155
1H chemical shifts1041

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 69 residues - 8293.291 Da.

1   METGLNGLNLYSGLNGLNILEMETALAALA
2   LEUASNSERGLNTHRALAVALGLNPHEGLN
3   GLNTYRALAALAGLNGLNTYRPROGLYASN
4   TYRGLUGLNGLNGLNILELEUILEARGGLN
5   LEUGLNGLUGLNHISTYRGLNGLNTYRMET
6   GLNGLNLEUTYRGLNVALGLNLEUALAGLN
7   GLNGLNALAALALEUGLNLYSGLNGLN

Entity 2, entity_2 80 residues - 8010.200 Da.

1   GLYALAMETVALGLUALAARGSERLEUALA
2   VALALAMETGLYASPTHRVALVALGLUPRO
3   ALAPROLEULYSPROTHRSERGLUPROTHR
4   SERGLYPROPROGLYASNASNGLYGLYSER
5   LEULEUSERVALILETHRGLUGLYVALGLY
6   GLULEUSERVALILEASPPROGLUVALALA
7   GLNLYSALACYSGLNGLUVALLEUGLULYS
8   VALLYSLEULEUHISGLYGLYVALALAVAL

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.47 mM; entity_2, [U-13C; U-15N], 0.47 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

YASARA, na - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

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