BMRB Entry 26783

Name: APC11 binding Ubiquitin Variant
Published: 2018-06-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26783

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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:

APC11 binding Ubiquitin Variant

Deposition date:

2016-04-21

Original release date:

2018-06-19

Authors:

Brown, Nicholas; Grace, Christy; Schulman, Brenda

Citation:

Citation: Brown, Nicholas; VanderLinden, Ryan; Watson, Edmond; Weissmann, Florian; Ordureau, Alban; Wu, Kuen-Phon; Zhang, Wei; Yu, Shanshan; Mercredi, Peter; Harrison, Joseph; Davidson, Iain; Qiao, Renping; Lu, Ying; Dube, Prakash; Brunner, Michael; Grace, Christy; Miller, Darcie; Haselbach, David; Jarvis, Marc; Yamaguchi, Masaya; Yanishevski, David; Petzold, Georg; Sidhu, Sachdev; Kuhlman, Brian; Kirschner, Marc; Harper, J Wade; Peters, Jan-Michael; Stark, Holger; Schulman, Brenda. "Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C." Cell 165, 1440-1453 (2016).
PubMed: 27259151

Assembly members:

Assembly members:
UBv, polymer, 84 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBv: GSGGSGMQILVKTPRGKTIT LEVEPSDTIENVKAKIQDKE GIPPDQQILFFAVKRLEDGR TLSDYNIQKKSSLLLAMRVP GKMK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	231
15N chemical shifts	75
1H chemical shifts	75

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBv	1

Entities:

Entity 1, UBv 84 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

GLN

ILE

LEU

2

VAL

LYS

THR

PRO

ARG

GLY

LYS

THR

ILE

THR

3

LEU

GLU

VAL

GLU

PRO

SER

ASP

THR

ILE

GLU

4

ASN

VAL

LYS

ALA

LYS

ILE

GLN

ASP

LYS

GLU

5

GLY

ILE

PRO

ASP

GLN

ILE

LEU

PHE

6

PHE

ALA

VAL

LYS

ARG

LEU

GLU

ASP

GLY

ARG

7

THR

LEU

SER

ASP

TYR

ASN

ILE

GLN

LYS

8

SER

LEU

ALA

MET

ARG

VAL

PRO

9

GLY

LYS

MET

LYS

Samples:

sample_1: UBv, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 600 MHz

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