BMRB Entry 15111

Name: Solution Structure of the UBA Domain from Cbl-b
Published: 2008-07-08

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PDB ID: 2jnh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15111
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of the UBA Domain from Cbl-b

Deposition date:

2007-01-24

Original release date:

2008-07-08

Authors:

Zhou, Chen-Jie; Zhou, Zi-Ren; Lin, Dong-Hai; Hu, Hong-Yu

Citation:

Citation: Zhou, Zi-Ren; Gao, Hong-Chang; Zhou, Chen-Jie; Chang, Yong-Gang; Hong, Jing; Song, Ai-Xin; Lin, Dong-Hai; Hu, Hong-Yu. "Differential Ubiquitin Binding of the UBA Domains from Human c-Cbl and Cbl-b: NMR Structural and Biochemical Insights" Protein Sci. 17, 1805-1814 (2008).
PubMed: 18596201

Assembly members:

Assembly members:
UBA domain of Cbl-b, polymer, 46 residues, 5113.846 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: pET-32M

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBA domain of Cbl-b: EAALENVDAKIAKLMGEGYA FEEVKRALEIAQNNVEVARS ILREFA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	113
15N chemical shifts	42
1H chemical shifts	258

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBA domain of Cbl-b	1

Entities:

Entity 1, UBA domain of Cbl-b 46 residues - 5113.846 Da.

1

GLU

ALA

LEU

GLU

ASN

VAL

ASP

ALA

LYS

2

ILE

ALA

LYS

LEU

MET

GLY

GLU

GLY

TYR

ALA

3

PHE

GLU

VAL

LYS

ARG

ALA

LEU

GLU

ILE

4

ALA

GLN

ASN

VAL

GLU

VAL

ALA

ARG

SER

5

ILE

LEU

ARG

GLU

PHE

ALA

Samples:

sample_1: entity, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%

sample_conditions_1: pH: 6.5; 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-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRDraw v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - chemical shift assignment, peak picking

ARIA v2.0, Linge, O'Donoghue and Nilges - data analysis, refinement, structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2DO6 2JNH 2OOA 2OOB
DBJ	BAC05498 BAE36418 BAF85481 BAG52839 BAG53874
EMBL	CAH18449 CAH56175
GB	AAB09291 AAF13271 AAH32851 AAI50935 AAI50939
REF	NP_001028410 NP_001192852 NP_598285 NP_733762 XP_001503404
SP	Q13191 Q3TTA7 Q8K4S7
TPG	DAA33541
AlphaFold	Q13191 Q3TTA7 Q8K4S7