BMRB Entry 10338

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10338

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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 First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)

Deposition date:

2011-01-13

Original release date:

2019-09-04

Authors:

Zhao, C.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation:

Citation: Zhao, C.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)" .

Assembly members:

Assembly members:
UBA domain, polymer, 54 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: cell free synthesis Host organism: Escherichia coli Vector: P050613-08

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBA domain: GLDESVIIQLVEMGFPMDAC RKAVYYTGNSGAEAAMNWVM SHMDDPDFANPLIL

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	235
15N chemical shifts	53
1H chemical shifts	368

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBA domain	1

Entities:

Entity 1, UBA domain 54 residues - Formula weight is not available

1

GLY

LEU

ASP

GLU

SER

VAL

ILE

GLN

LEU

2

VAL

GLU

MET

GLY

PHE

PRO

MET

ASP

ALA

CYS

3

ARG

LYS

ALA

VAL

TYR

THR

GLY

ASN

SER

4

GLY

ALA

GLU

ALA

MET

ASN

TRP

VAL

MET

5

SER

HIS

MET

ASP

PRO

ASP

PHE

ALA

ASN

6

PRO

LEU

ILE

LEU

Samples:

sample_1: UBA domain, [U-13C; U-15N], 1.05 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296.0 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

TOPSPIN v2.1, Bruker - collection

NMRPipe, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.9843, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - structure solution

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