BMRB Entry 15534

Name: Solution Structure of the UBA domain from c-Cbl
Published: 2008-07-15

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15534

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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 Structure of the UBA domain from c-Cbl

Deposition date:

2007-10-24

Original release date:

2008-07-15

Authors:

Zhou, Zi-ren; Hong, Jing; 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:
c-Cbl, polymer, 56 residues, Formula weight is not available

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):
c-Cbl: ATASPQLSSEIENLMSQGYS YQDIQKALVIAQNNIEMAKN ILREFVSISSPAHVAT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	220
15N chemical shifts	64
1H chemical shifts	346

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	c-Cbl_UBA	1

Entities:

Entity 1, c-Cbl_UBA 56 residues - Formula weight is not available

1

ALA

THR

ALA

SER

PRO

GLN

LEU

SER

GLU

2

ILE

GLU

ASN

LEU

MET

SER

GLN

GLY

TYR

SER

3

TYR

GLN

ASP

ILE

GLN

LYS

ALA

LEU

VAL

ILE

4

ALA

GLN

ASN

ILE

GLU

MET

ALA

LYS

ASN

5

ILE

LEU

ARG

GLU

PHE

VAL

SER

ILE

SER

6

PRO

ALA

HIS

VAL

ALA

THR

Samples:

sample_1_N_H2O: c-Cbl_UBA 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; H20 90%; D2O 10%

sample_2_CN_H2O: c-Cbl_UBA 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; H20 90%; D2O 10%

sample_3_CN_D2O: c-Cbl_UBA 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2_CN_H2O	isotropic	sample_conditions_1
3D HNCACB	sample_2_CN_H2O	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2_CN_H2O	isotropic	sample_conditions_1
3D HNCO	sample_2_CN_H2O	isotropic	sample_conditions_1
3D HNHA	sample_1_N_H2O	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3_CN_D2O	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1_N_H2O	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3_CN_D2O	isotropic	sample_conditions_1

Software:

CNS, Linge, O'Donoghue and Nilges - refinement

NMR spectrometers:

Varian Unity 600 MHz

PDB	2JUJ
EMBL	CAA40393
GB	AAI32734 AAI36464 EAW67476 EHH23510 EHH56827
REF	NP_001245076 NP_005179 XP_001165648 XP_002193659 XP_002754480
SP	P22681
AlphaFold	P22681