BMRB Entry 11144

Click here to enlarge.

PDB ID: 2yua
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11144
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 DnaJ domain from human Williams-Beuren syndrome chromosome region 18 protein

Deposition date:

2010-03-31

Original release date:

2011-04-01

Authors:

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

Citation:

Citation: Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the DnaJ domain from human Williams-Beuren syndrome chromosome region 18 protein" .

Assembly members:

Assembly members:
DnaJ domain, polymer, 99 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: P050620-25

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DnaJ domain: GSSGSSGSQGDCSYSRTALY DLLGVPSTATQAQIKAAYYR QCFLYHPDRNSGSAEAAERF TRISQAYVVLGSATLRRKYD RGLLSDEDLRGPGSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	390
15N chemical shifts	91
1H chemical shifts	586

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DnaJ domain	1

Entities:

Entity 1, DnaJ domain 99 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

SER

GLN

GLY

2

ASP

CYS

SER

TYR

SER

ARG

THR

ALA

LEU

TYR

3

ASP

LEU

GLY

VAL

PRO

SER

THR

ALA

THR

4

GLN

ALA

GLN

ILE

LYS

ALA

TYR

ARG

5

GLN

CYS

PHE

LEU

TYR

HIS

PRO

ASP

ARG

ASN

6

SER

GLY

SER

ALA

GLU

ALA

GLU

ARG

PHE

7

THR

ARG

ILE

SER

GLN

ALA

TYR

VAL

LEU

8

GLY

SER

ALA

THR

LEU

ARG

LYS

TYR

ASP

9

ARG

GLY

LEU

SER

ASP

GLU

ASP

LEU

ARG

10

GLY

PRO

GLY

SER

GLY

PRO

SER

GLY

Samples:

sample_1: Gal-binding lectin, [U-13C; U-15N], 1.14 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 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 v3.5, Bruker - collection

NMRPipe v20060524, Delaglio, F. - processing

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

Kujira v0.9825, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2YUA
DBJ	BAB71671
GB	AAM62307 AAS07471 EAW69658
REF	NP_001181473 NP_115693 XP_001145797 XP_002817906 XP_003815619
SP	Q96LL9
AlphaFold	Q96LL9