BMRB Entry 11032

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11032
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

Title:
Solution structure of the knotted tudor domain of the yeast histone acetyltransferase protein, Esa1
Deposition date:
2008-03-01
Original release date:
2008-04-16
Authors:
Shimojo, Hideaki; Sano, Norihiko; Moriwaki, Yoshihito; Okuda, Masahiko; Horikoshi, Masami; Nishimura, Yoshifumi
Citation:

Citation: Shimojo, Hideaki; Sano, Norihiko; Moriwaki, Yoshihito; Okuda, Masahiko; Horikoshi, Masami; Nishimura, Yoshifumi. "Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain"  J. Mol. Biol. 378, 987-1001 (2008).
PubMed: 18407291

Assembly members:

Assembly members:
Residues 1-89, polymer, 92 residues, 10791.321 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Residues 1-89: GSHMSHDGKEEPGIAKKINS VDDIIIKCQCWVQKNDEERL AEILSINTRKAPPKFYVHYV NYNKRLDEWITTDRINLDKE VLYPKLKATDED

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts96
1H chemical shifts676

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Residues 1-891

Entities:

Entity 1, Residues 1-89 92 residues - 10791.321 Da.

1   GLYSERHISMETSERHISASPGLYLYSGLU
2   GLUPROGLYILEALALYSLYSILEASNSER
3   VALASPASPILEILEILELYSCYSGLNCYS
4   TRPVALGLNLYSASNASPGLUGLUARGLEU
5   ALAGLUILELEUSERILEASNTHRARGLYS
6   ALAPROPROLYSPHETYRVALHISTYRVAL
7   ASNTYRASNLYSARGLEUASPGLUTRPILE
8   THRTHRASPARGILEASNLEUASPLYSGLU
9   VALLEUTYRPROLYSLEULYSALATHRASP
10   GLUASP

Samples:

sample_1: Residues 1-89, [U-99% 13C; U-99% 15N], 0.35 mM; potassium phosphate 200 mM; H2O 95%; D2O 5%

sample_2: Residues 1-89 0.35 mM; potassium phosphate 200 mM; D2O 100%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement

Olivia, Yokochi, M., Sekiguchi, S. and Inagaki, F. - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

BMRB 11033
PDB
DBJ GAA26555
EMBL CAA99465 CAY86525
GB AHY77525 AJP41755 AJT71177 AJT71665 AJT72155
REF NP_014887
SP Q08649
TPG DAA11012
AlphaFold Q08649

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks