BMRB Entry 36675

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36675
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title:
NMR solution structures of ASH1L BRD-PHD domain in complex with H3K4me2 peptide
Deposition date:
2024-06-14
Original release date:
2025-11-04
Authors:
Zeng, L.; Zhou, M.-M., M.
Citation:

Citation: Zeng, L.; Zhou, M.-M., M.. "NMR solution structures of ASH1L BRD-PHD domain in complex with H3K4me2 peptide"  .

Assembly members:

Assembly members:
ASH1L bromodomain and PHD domain, polymer, 205 residues, 23309.365 Da.
Histone H3.3C, polymer, 12 residues, 1335.534 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: not available   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Homo sapiens

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ASH1L bromodomain and PHD domain: SMNIEVARAARLAQIFKEIC DGIISYRDSSQQTLAAPLLN LPPKKKNADYYEKISDPLDL STIEKQILIGYYKTVEAFDA DMLKVFRNAEKYYGRKSPIG RDVCRLRKAYYSARHEASAQ IDEIVGETASEADSSETSVS EKESGHEKDDDVIRCICGLY KDEGLMIQCDKCMVWQHCDC MGVNTDVEHYLCEQCDPRPV DREVP
Histone H3.3C: ARTXQTARKSTG

Data sets:
Data typeCount
13C chemical shifts682
15N chemical shifts212
1H chemical shifts1328

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_ZN3

Entities:

Entity 1, entity_1 205 residues - 23309.365 Da.

1   SERMETASNILEGLUVALALAARGALAALA
2   ARGLEUALAGLNILEPHELYSGLUILECYS
3   ASPGLYILEILESERTYRARGASPSERSER
4   GLNGLNTHRLEUALAALAPROLEULEUASN
5   LEUPROPROLYSLYSLYSASNALAASPTYR
6   TYRGLULYSILESERASPPROLEUASPLEU
7   SERTHRILEGLULYSGLNILELEUILEGLY
8   TYRTYRLYSTHRVALGLUALAPHEASPALA
9   ASPMETLEULYSVALPHEARGASNALAGLU
10   LYSTYRTYRGLYARGLYSSERPROILEGLY
11   ARGASPVALCYSARGLEUARGLYSALATYR
12   TYRSERALAARGHISGLUALASERALAGLN
13   ILEASPGLUILEVALGLYGLUTHRALASER
14   GLUALAASPSERSERGLUTHRSERVALSER
15   GLULYSGLUSERGLYHISGLULYSASPASP
16   ASPVALILEARGCYSILECYSGLYLEUTYR
17   LYSASPGLUGLYLEUMETILEGLNCYSASP
18   LYSCYSMETVALTRPGLNHISCYSASPCYS
19   METGLYVALASNTHRASPVALGLUHISTYR
20   LEUCYSGLUGLNCYSASPPROARGPROVAL
21   ASPARGGLUVALPRO

Entity 2, entity_2 12 residues - 1335.534 Da.

1   ALAARGTHRMLYGLNTHRALAARGLYSSER
2   THRGLY

Entity 3, entity_ZN - Zn - 65.409 Da.

1   ZNZN

Samples:

sample_1: ASH1L bromodomain and PHD domain, [U-13C; U-15N], mM; Histone H3.3C mM; DTT 2 mM; potassium chloride 50 mM; sodium phosphate 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: ASH1L bromodomain and PHD domain, [U-13C; U-15N], mM; Histone H3.3C mM; DTT 2 mM; potassium chloride 50 mM; sodium phosphate 100 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: . Not defined; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

ARIA, Linge, O'Donoghue and Nilges - refinement

NMRView, Johnson, One Moon Scientific - peak picking

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

NMR spectrometers:

  • Bruker AVANCE 900 MHz
  • Bruker AVANCE 800 MHz

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