BMRB Entry 11260

Name: Solution Structure of UBA domain of Human Ubiquitin Associated Protein 1 (UBAP1)
Published: 2011-08-17

Click here to enlarge.

PDB ID: 1wgn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11260
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution Structure of UBA domain of Human Ubiquitin Associated Protein 1 (UBAP1)

Deposition date:

2010-08-09

Original release date:

2011-08-17

Authors:

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

Citation:

Citation: Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of UBA domain of Human Ubiquitin Associated Protein 1 (UBAP1)" .

Assembly members:

Assembly members:
UBA domain, polymer, 63 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: E. coli - cell free Vector: P040301-63

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBA domain: GSSGSSGAYSELQMLSPSER QCVETVVNMGYSYECVLRAM KKKGENIEQILDYLFAHSGP SSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	245
15N chemical shifts	57
1H chemical shifts	387

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBA domain	1

Entities:

Entity 1, UBA domain 63 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ALA

TYR

SER

2

GLU

LEU

GLN

MET

LEU

SER

PRO

SER

GLU

ARG

3

GLN

CYS

VAL

GLU

THR

VAL

ASN

MET

GLY

4

TYR

SER

TYR

GLU

CYS

VAL

LEU

ARG

ALA

MET

5

LYS

GLY

GLU

ASN

ILE

GLU

GLN

ILE

6

LEU

ASP

TYR

LEU

PHE

ALA

HIS

SER

GLY

PRO

7

SER

GLY

Samples:

sample_1: UBA domain mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298.0 K

Experiments:

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

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.8996, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WGN
DBJ	BAC11162 BAC11176 BAC11224 BAC11323 BAC11342
EMBL	CAB66667 CAG38582 CAL38740
GB	AAF37827 AAH20950 AAH98141 AAH98316 AAH99726
REF	NP_001164672 NP_001164673 NP_001164674 NP_001164675 NP_001253443
SP	Q9NZ09
AlphaFold	Q9NZ09