BMRB Entry 26765

Name: NMR backbone 1H, 13C and 15N chemical shift assignments of human S-phase kinase-associated protein 1 (Skp1)
Published: 2017-03-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26765

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2016-03-22

Original release date:

2017-03-02

Authors:

Kachariya, Nitin Nathubhai; Kumar, Ashutosh

Citation:

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).
PubMed: 27394725

Assembly members:

Assembly members:
Skp1, polymer, 168 residues, 19289 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: pGEX-6P-1

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	607
15N chemical shifts	149
1H chemical shifts	964

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Skp1	1

Entities:

Entity 1, Skp1 168 residues - 19289 Da.

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

1

GLY

PRO

LEU

GLY

SER

MET

PRO

SER

ILE

LYS

2

LEU

GLN

SER

ASP

GLY

GLU

ILE

PHE

GLU

3

VAL

ASP

VAL

GLU

ILE

ALA

LYS

GLN

SER

VAL

4

THR

ILE

LYS

THR

MET

LEU

GLU

ASP

LEU

GLY

5

MET

ASP

GLU

GLY

ASP

PRO

VAL

6

PRO

LEU

PRO

ASN

VAL

ASN

ALA

ILE

LEU

7

LYS

VAL

ILE

GLN

TRP

CYS

THR

HIS

8

LYS

ASP

PRO

GLU

ASP

9

GLU

ASN

LYS

GLU

LYS

ARG

THR

ASP

ILE

10

PRO

VAL

TRP

ASP

GLN

GLU

PHE

LEU

LYS

VAL

11

ASP

GLN

GLY

THR

LEU

PHE

GLU

LEU

ILE

LEU

12

ALA

ASN

TYR

LEU

ASP

ILE

LYS

GLY

LEU

13

LEU

ASP

VAL

THR

CYS

LYS

THR

VAL

ALA

ASN

14

MET

ILE

LYS

GLY

LYS

THR

PRO

GLU

ILE

15

ARG

LYS

THR

PHE

ASN

ILE

LYS

ASN

ASP

PHE

16

THR

GLU

ALA

GLN

VAL

ARG

LYS

17

GLU

ASN

GLN

TRP

CYS

GLU

LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	Skp1_sample	isotropic	Skp1_conditions_1
3D HNCO	Skp1_sample	isotropic	Skp1_conditions_1
3D HN(CA)CO	Skp1_sample	isotropic	Skp1_conditions_1
3D HN(CO)CACB	Skp1_sample	isotropic	Skp1_conditions_1
3D HNCACB	Skp1_sample	isotropic	Skp1_conditions_1
3D H(CCO)NH	Skp1_sample	isotropic	Skp1_conditions_1
3D CC(CO)NH	Skp1_sample	isotropic	Skp1_conditions_1
3D 1H-15N NOESY	Skp1_sample	isotropic	Skp1_conditions_1
3D TOCSY-HSQC	Skp1_sample	isotropic	Skp1_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