BMRB Entry 11268

Click here to enlarge.

PDB ID: 1x1m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11268
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 in Mouse Ubiquitin-like Protein SB132

Deposition date:

2010-08-09

Original release date:

2011-08-18

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 in Mouse Ubiquitin-like Protein SB132" .

Assembly members:

Assembly members:
ubiquitin-like domain, polymer, 107 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: P050111-20

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin-like domain: GSSGSSGMSLSDWHLAVKLA DQPLAPKSILQLPETELGEY SLGGYSISFLKQLIAGKLQE SVPDPELIDLIYCGRKLKDD QTLDFYGIQPGSTVHVLRKS WSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	461
15N chemical shifts	99
1H chemical shifts	723

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 107 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

MET

SER

LEU

2

SER

ASP

TRP

HIS

LEU

ALA

VAL

LYS

LEU

ALA

3

ASP

GLN

PRO

LEU

ALA

PRO

LYS

SER

ILE

LEU

4

GLN

LEU

PRO

GLU

THR

GLU

LEU

GLY

GLU

TYR

5

SER

LEU

GLY

TYR

SER

ILE

SER

PHE

LEU

6

LYS

GLN

LEU

ILE

ALA

GLY

LYS

LEU

GLN

GLU

7

SER

VAL

PRO

ASP

PRO

GLU

LEU

ILE

ASP

LEU

8

ILE

TYR

CYS

GLY

ARG

LYS

LEU

LYS

ASP

9

GLN

THR

LEU

ASP

PHE

TYR

GLY

ILE

GLN

PRO

10

GLY

SER

THR

VAL

HIS

VAL

LEU

ARG

LYS

SER

11

TRP

SER

GLY

PRO

SER

GLY

Samples:

sample_1: ubiquitin-like domain, [U-13C; U-15N], 1.35 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 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-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 v0.921, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1X1M
DBJ	BAB26033 BAE32627
GB	AAH16456 AAH79221 AAH94047 AAI12530 AAX08728
REF	NP_001004247 NP_001015573 NP_001116345 NP_081362 XP_001135544
SP	Q2KIS3 Q91W67
TPG	DAA17515
AlphaFold	Q2KIS3 Q91W67