BMRB Entry 10091

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PDB ID: 1wjn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10091
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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 C-terminal ubiquitin-like domain of mouse tubulin-specific chaperone e

Deposition date:

2007-01-24

Original release date:

2008-08-14

Authors:

Sato, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Sato, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the C-terminal ubiquitin-like domain of mouse tubulin-specific chaperone e" .

Assembly members:

Assembly members:
ubiquitin like-domain, polymer, 97 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: cell free synthesis Vector: P040301-91

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin like-domain: GSSGSSGQLLTLKIKCSNQP ERQILEKQLPDSMTVQKVKG LLSRLLKVPVSELLLSYESS KMPGREIELENDLQPLQFYS VENGDCLLVRWSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	422
15N chemical shifts	96
1H chemical shifts	689

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tubulin-folding protein TBCE	1

Entities:

Entity 1, Tubulin-folding protein TBCE 97 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLN

LEU

2

THR

LEU

LYS

ILE

LYS

CYS

SER

ASN

GLN

PRO

3

GLU

ARG

GLN

ILE

LEU

GLU

LYS

GLN

LEU

PRO

4

ASP

SER

MET

THR

VAL

GLN

LYS

VAL

LYS

GLY

5

LEU

SER

ARG

LEU

LYS

VAL

PRO

VAL

6

SER

GLU

LEU

SER

TYR

GLU

SER

7

LYS

MET

PRO

GLY

ARG

GLU

ILE

GLU

LEU

GLU

8

ASN

ASP

LEU

GLN

PRO

LEU

GLN

PHE

TYR

SER

9

VAL

GLU

ASN

GLY

ASP

CYS

LEU

VAL

ARG

10

TRP

SER

GLY

PRO

SER

GLY

Samples:

sample_1: ubiquitin-like domain, [U-13C; U-15N], 1.1 mM; d-Tris-HCl 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 220 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	condition_1
3D 15N-separated NOESY	sample_1	not available	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.8994, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 700 MHz

PDB	1WJN
DBJ	BAE39475
GB	AAH50206 AAL92570 EDL32750 EDL32752 EDL32753
REF	NP_848027 XP_006516836 XP_006516838
SP	Q8CIV8
AlphaFold	Q8CIV8