BMRB Entry 30696

Name: Solution NMR structure of Dictyostelium discoideum Skp1A (truncated) dimer
Published: 2020-04-13

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PDB ID: 6v88
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30696
MolProbity Validation Chart

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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:

Solution NMR structure of Dictyostelium discoideum Skp1A (truncated) dimer

Deposition date:

2019-12-10

Original release date:

2020-04-13

Authors:

Kim, H.; Eletsky, A.; West, C.

Citation:

Citation: Kim, H.; Eletsky, A.; Gonzalez, K.; van der Wel, H.; Strauch, E.; Prestegard, J.; West, C.. "Skp1 Dimerization Conceals Its F-Box Protein Binding Site" Biochemistry 59, 1527-1536 (2020).
PubMed: 32227851

Assembly members:

Assembly members:
entity_1, polymer, 116 residues, 12998.891 Da.

Natural source:

Natural source: Common Name: Slime mold Taxonomy ID: 44689 Superkingdom: Eukaryota Kingdom: not available Genus/species: Dictyostelium discoideum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SLVKLESSDEKVFEIEKEIA CMSVTIKNMIEDIGESDSPI PLPNVTSTILEKVLDYCRHH HQHPGGSGLDDIPPYDRDFC KVDQPTLFELILAANYLDIK PLLDVTCKTVANMIRG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	531
15N chemical shifts	124
1H chemical shifts	851

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

Entity 1, entity_1, 1 116 residues - 12998.891 Da.

1

SER

LEU

VAL

LYS

LEU

GLU

SER

ASP

GLU

2

LYS

VAL

PHE

GLU

ILE

GLU

LYS

GLU

ILE

ALA

3

CYS

MET

SER

VAL

THR

ILE

LYS

ASN

MET

ILE

4

GLU

ASP

ILE

GLY

GLU

SER

ASP

SER

PRO

ILE

5

PRO

LEU

PRO

ASN

VAL

THR

SER

THR

ILE

LEU

6

GLU

LYS

VAL

LEU

ASP

TYR

CYS

ARG

HIS

7

HIS

GLN

HIS

PRO

GLY

SER

GLY

LEU

ASP

8

ASP

ILE

PRO

TYR

ASP

ARG

ASP

PHE

CYS

9

LYS

VAL

ASP

GLN

PRO

THR

LEU

PHE

GLU

LEU

10

ILE

LEU

ALA

ASN

TYR

LEU

ASP

ILE

LYS

11

PRO

LEU

ASP

VAL

THR

CYS

LYS

THR

VAL

12

ALA

ASN

MET

ILE

ARG

GLY

Name	Sample	Sample state	Sample conditions
2D [15N, 1H]-HSQC	sample_1	isotropic	sample_conditions_1
2D [13C, 1H] CT-HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D [13C, 1H] CT-HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 13C/15N-edited [1H,1H] NOESY	sample_1	isotropic	sample_conditions_1
3D TROSY-HNCACB	sample_1	isotropic	sample_conditions_1
3D (H)CCH-COSY aromatic	sample_1	isotropic	sample_conditions_1
3D (H)CCH-COSY aliphatic	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY aliphatic	sample_1	isotropic	sample_conditions_1
3D 13C/15N-filtered 13C/15N-edited [1H,1H] NOESY	sample_1	isotropic	sample_conditions_1
2D long-range [15N, 1H]-HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (HCA)CONH	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 30696

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: