BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 10041

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: 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:
Tudor domain, polymer, 133 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis

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

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts116
1H chemical shifts777

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MYST histone acetyltransferase 11

Entities:

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

1   GLYSERSERGLYSERSERGLYGLUPROGLU
2   VALTHRVALGLUILEGLYGLUTHRTYRLEU
3   CYSARGARGPROASPSERTHRTRPHISSER
4   ALAGLUVALILEGLNSERARGVALASNASP
5   GLNGLUGLYARGGLUGLUPHETYRVALHIS
6   TYRVALGLYPHEASNARGARGLEUASPGLU
7   TRPVALASPLYSASNARGLEUALALEUTHR
8   LYSTHRVALLYSASPALAVALGLNLYSASN
9   SERGLULYSTYRLEUSERGLULEUALAGLU
10   GLNPROGLUARGLYSILETHRARGASNGLN
11   LYSARGLYSHISASPGLUILEASNHISVAL
12   GLNLYSTHRTYRALAGLUMETASPPROTHR
13   THRALAALALEUGLULYSGLUSERGLYPRO
14   SERSERGLY

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:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_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

Related Database Links:

PDB
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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts