BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26059

Title: Solution NMR structures of AF9 yeats domain in complex with histon H3 acetylation at K18   PubMed: 27545619

Deposition date: 2016-05-19 Original release date: 2016-09-01

Authors: Zeng, Lei; ZHOU, MING-MING

Citation: Zhang, Qiang; Zeng, Lei; Zhao, Chengcheng; Ju, Ying; Konuma, Tsuyoshi; ZHOU, MING-MING. "Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain"  Structure 24, 1606-1612 (2016).

Assembly members:
entity_1, polymer, 141 residues, 16611.314 Da.
entity_2, polymer, 13 residues, 1370.634 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21(DE3)

Entity Sequences (FASTA):
entity_1: GSHMASSCAVQVKLELGHRA QVRKKPTVEGFTHDWMVFVR GPEHSNIQHFVEKVVFHLHE SFPRPKRVCKDPPYKVEESG YAGFILPIEVYFKNKEEPRK VRFDYDLFLHLEGHPPVNHL RCEKLTFNNPTEDFRRKLLK A
entity_2: GGKAPRXQLATKA

Data sets:
Data typeCount
13C chemical shifts666
15N chemical shifts123
1H chemical shifts1014

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 141 residues - 16611.314 Da.

1   GLYSERHISMETALASERSERCYSALAVAL
2   GLNVALLYSLEUGLULEUGLYHISARGALA
3   GLNVALARGLYSLYSPROTHRVALGLUGLY
4   PHETHRHISASPTRPMETVALPHEVALARG
5   GLYPROGLUHISSERASNILEGLNHISPHE
6   VALGLULYSVALVALPHEHISLEUHISGLU
7   SERPHEPROARGPROLYSARGVALCYSLYS
8   ASPPROPROTYRLYSVALGLUGLUSERGLY
9   TYRALAGLYPHEILELEUPROILEGLUVAL
10   TYRPHELYSASNLYSGLUGLUPROARGLYS
11   VALARGPHEASPTYRASPLEUPHELEUHIS
12   LEUGLUGLYHISPROPROVALASNHISLEU
13   ARGCYSGLULYSLEUTHRPHEASNASNPRO
14   THRGLUASPPHEARGARGLYSLEULEULYS
15   ALA

Entity 2, entity_2 13 residues - 1370.634 Da.

1   GLYGLYLYSALAPROARGALYGLNLEUALA
2   THRLYSALA

Samples:

sample_1: sodium phosphate 10 mM; sodium chloride 500 mM; EDTA 2 mM; DTT, [U-100% 2H], 2 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 10 mM; sodium chloride 500 mM; EDTA 2 mM; DTT, [U-100% 2H], 2 mM; D2O 100%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D filtered 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D filtered 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement

NMRPipe v7.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift calculation, processing

NMRView v5.04 C-version, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

TALOS vtalosn, talosplus, Cornilescu, Delaglio and Bax - refinement

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

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