BMRB Entry 27984

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Cezanne UBA domain (residues 2-55)
Published: 2020-01-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27984

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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: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Cezanne UBA domain (residues 2-55) PubMed: 31937588

Deposition date: 2019-07-23 Original release date: 2020-01-15

Authors: Rogov, Vladimir; Huber, Jessica; Doetsch, Volker; Mader, Julia; Bremm, Anja

Citation: Mader, Julia; Huber, Jessica; Bonn, Florian; Doetsch, Volker; Rogov, Vladimir; Bremm, Anja. "Oxygen-dependent asparagine hydroxylation of the ubiquitin-associated (UBA) domain in Cezanne regulates ubiquitin binding" J. Biol. Chem. 295, 2160-2174 (2020).

Assembly members:
Cezanne_UBA_domain, polymer, 55 residues, Formula weight is not available

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 Vector: pOPINK

Entity Sequences (FASTA):
Cezanne_UBA_domain: MTLDMDAVLSDFVRSTGAEP GLARDLLEGKNWDVNAALSD FEQLRQVHAGNLPPS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	102
15N chemical shifts	52
1H chemical shifts	52

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cezanne UBA domain	1

Entities:

Entity 1, Cezanne UBA domain 55 residues - Formula weight is not available

1

MET

THR

LEU

ASP

MET

ASP

ALA

VAL

LEU

SER

2

ASP

PHE

VAL

ARG

SER

THR

GLY

ALA

GLU

PRO

3

GLY

LEU

ALA

ARG

ASP

LEU

GLU

GLY

LYS

4

ASN

TRP

ASP

VAL

ASN

ALA

LEU

SER

ASP

5

PHE

GLU

GLN

LEU

ARG

GLN

VAL

HIS

ALA

GLY

6

ASN

LEU

PRO

SER

Samples:

sample_1: Cezanne UBA domain, [U-98% 13C; U-98% 15N], 0.8 mM; HEPES 25 mM; sodium chloride 50 mM; D2O 5%; DSS 1 mM; protease inhibitors cocktail 5 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin, Goddard - chemical shift assignment, collection, data analysis

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz

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