BMRB Entry 11256

Click here to enlarge.

PDB ID: 1wgg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11256
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 the N-terminal Ubiquitin-like Domain of Mouse Ubiquitin Specific Protease 14 (USP14)

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 the N-terminal Ubiquitin-like Domain of Mouse Ubiquitin Specific Protease 14 (USP14)" .

Assembly members:

Assembly members:
ubiquitin-like domain, polymer, 96 residues, Formula weight is not available

Natural source:

Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: P0302212-91

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin-like domain: GSSGSSGYSVTVKWGKEKFE GVELNTDEPPMVFKAQLFAL TGVQPARQKVMVKGGTLKDD DWGNIKMKNGMTVLMMGSAD ALPEEPSAKTSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	408
15N chemical shifts	96
1H chemical shifts	634

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ubiquitin-like domain	1

Entities:

Entity 1, ubiquitin-like domain 96 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

TYR

SER

VAL

2

THR

VAL

LYS

TRP

GLY

LYS

GLU

LYS

PHE

GLU

3

GLY

VAL

GLU

LEU

ASN

THR

ASP

GLU

PRO

4

MET

VAL

PHE

LYS

ALA

GLN

LEU

PHE

ALA

LEU

5

THR

GLY

VAL

GLN

PRO

ALA

ARG

GLN

LYS

VAL

6

MET

VAL

LYS

GLY

THR

LEU

LYS

ASP

7

ASP

TRP

GLY

ASN

ILE

LYS

MET

LYS

ASN

GLY

8

MET

THR

VAL

LEU

MET

GLY

SER

ALA

ASP

9

ALA

LEU

PRO

GLU

PRO

SER

ALA

LYS

THR

10

SER

GLY

PRO

SER

GLY

Samples:

sample_1: ubiquitin-like domain mM; PiNa 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; 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	1WGG
DBJ	BAA93551 BAB27544 BAC26713 BAC32528 BAE89403
GB	AAB60365 AAH03556 AAH05571 AAH50197 AAH85947
REF	NP_001008302 NP_001032411 NP_001033678 NP_001038961 NP_001068657
SP	P54578 P60051 Q0IIF7 Q9JMA1
TPG	DAA15782
AlphaFold	P54578 P60051 Q0IIF7 Q9JMA1