BMRB Entry 10041

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PDB ID: 1wgs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10041
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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 Tudor Domain from Mouse Hypothetical Protein Homologous to Histone Acetyltransferase

Deposition date:

2006-11-09

Original release date:

2008-08-13

Authors:

Li, H.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Li, H.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to Histone Acetyltransferase" .

Assembly members:

Assembly members:
Tudor domain, polymer, 133 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: P031110-09

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Tudor domain: GSSGSSGEPEVTVEIGETYL CRRPDSTWHSAEVIQSRVND QEGREEFYVHYVGFNRRLDE WVDKNRLALTKTVKDAVQKN SEKYLSELAEQPERKITRNQ KRKHDEINHVQKTYAEMDPT TAALEKESGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	506
15N chemical shifts	116
1H chemical shifts	777

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MYST histone acetyltransferase 1	1

Entities:

Entity 1, MYST histone acetyltransferase 1 133 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLU

PRO

GLU

2

VAL

THR

VAL

GLU

ILE

GLY

GLU

THR

TYR

LEU

3

CYS

ARG

PRO

ASP

SER

THR

TRP

HIS

SER

4

ALA

GLU

VAL

ILE

GLN

SER

ARG

VAL

ASN

ASP

5

GLN

GLU

GLY

ARG

GLU

PHE

TYR

VAL

HIS

6

TYR

VAL

GLY

PHE

ASN

ARG

LEU

ASP

GLU

7

TRP

VAL

ASP

LYS

ASN

ARG

LEU

ALA

LEU

THR

8

LYS

THR

VAL

LYS

ASP

ALA

VAL

GLN

LYS

ASN

9

SER

GLU

LYS

TYR

LEU

SER

GLU

LEU

ALA

GLU

10

GLN

PRO

GLU

ARG

LYS

ILE

THR

ARG

ASN

GLN

11

LYS

ARG

LYS

HIS

ASP

GLU

ILE

ASN

HIS

VAL

12

GLN

LYS

THR

TYR

ALA

GLU

MET

ASP

PRO

THR

13

THR

ALA

LEU

GLU

LYS

GLU

SER

GLY

PRO

14

SER

GLY

Samples:

sample_1: Tudor domain, [U-13C, U-15N], 1.06 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: 298 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 v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.897, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WGS
DBJ	BAB13924 BAB14827 BAB22680 BAC25539 BAC26411
GB	AAF72665 AAH36284 AAH37773 AAH83891 AAI33612
REF	NP_001017378 NP_001098953 NP_001271295 NP_080646 NP_115564
SP	Q5XI06 Q9D1P2 Q9H7Z6
TPG	DAA15349
AlphaFold	Q5XI06 Q9D1P2 Q9H7Z6