BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26765

Title: NMR backbone 1H, 13C and 15N chemical shift assignments of human S-phase kinase-associated protein 1 (Skp1)   PubMed: 27394725

Deposition date: 2016-03-22 Original release date: 2017-03-02

Authors: Kachariya, Nitin Nathubhai; Kumar, Ashutosh

Citation: Kachariya, Nitin; Dantu, Sarath; Kumar, Ashutosh. "Backbone and side chain assignments of human cell cycle regulatory protein S-phase kinase-associated protein 1"  J. Biomol. NMR 10, 351-355 (2016).

Assembly members:
Skp1, polymer, 168 residues, 19289 Da.

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

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

Entity Sequences (FASTA):
Skp1: GPLGSMPSIKLQSSDGEIFE VDVEIAKQSVTIKTMLEDLG MDDEGDDDPVPLPNVNAAIL KKVIQWCTHHKDDPPPPEDD ENKEKRTDDIPVWDQEFLKV DQGTLFELILAANYLDIKGL LDVTCKTVANMIKGKTPEEI RKTFNIKNDFTEEEEAQVRK ENQWCEEK

Data sets:
Data typeCount
13C chemical shifts583
15N chemical shifts137
1H chemical shifts840

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Skp11

Entities:

Entity 1, Skp1 168 residues - 19289 Da.

"GPLGS" five extra residues are present at N terminal of Skp1

1   GLYPROLEUGLYSERMETPROSERILELYS
2   LEUGLNSERSERASPGLYGLUILEPHEGLU
3   VALASPVALGLUILEALALYSGLNSERVAL
4   THRILELYSTHRMETLEUGLUASPLEUGLY
5   METASPASPGLUGLYASPASPASPPROVAL
6   PROLEUPROASNVALASNALAALAILELEU
7   LYSLYSVALILEGLNTRPCYSTHRHISHIS
8   LYSASPASPPROPROPROPROGLUASPASP
9   GLUASNLYSGLULYSARGTHRASPASPILE
10   PROVALTRPASPGLNGLUPHELEULYSVAL
11   ASPGLNGLYTHRLEUPHEGLULEUILELEU
12   ALAALAASNTYRLEUASPILELYSGLYLEU
13   LEUASPVALTHRCYSLYSTHRVALALAASN
14   METILELYSGLYLYSTHRPROGLUGLUILE
15   ARGLYSTHRPHEASNILELYSASNASPPHE
16   THRGLUGLUGLUGLUALAGLNVALARGLYS
17   GLUASNGLNTRPCYSGLUGLULYS

Samples:

Skp1_sample: Skp1, [U-15N], 0.7 mM; Skp1, [U-13C; U-15N], 1.2 mM; Sodium Phosphate 25 mM; NaCl 100 mM; Beta mercaptoethanol 1 mM

Skp1_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSkp1_sampleisotropicSkp1_conditions_1
3D HNCOSkp1_sampleisotropicSkp1_conditions_1
3D HN(CA)COSkp1_sampleisotropicSkp1_conditions_1
3D HN(CO)CACBSkp1_sampleisotropicSkp1_conditions_1
3D HNCACBSkp1_sampleisotropicSkp1_conditions_1
3D H(CCO)NHSkp1_sampleisotropicSkp1_conditions_1
3D CC(CO)NHSkp1_sampleisotropicSkp1_conditions_1
3D 1H-15N NOESYSkp1_sampleisotropicSkp1_conditions_1
3D TOCSY-HSQCSkp1_sampleisotropicSkp1_conditions_1

Software:

CcpNmr_Analysis v2.4.1, CCPN - chemical shift assignment

TOPSPIN v3.2, Bruker Biospin - processing

TALOS vTALOS+, Cornilescu, Delaglio and Bax - Secondary structure prediction

NMR spectrometers:

  • Bruker Ascend 750 MHz

Related Database Links:

NCBI NP_733779.1

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