BMRB Entry 18813

Title:
The solution structure of human PHF1 in complex with H3K36me3
Deposition date:
2012-10-30
Original release date:
2012-01-15
Authors:
Song, Jikui; Patel, Dinshaw
Citation:

Citation: Cai, Ling; Rothbart, Scott; Lu, Rui; Xu, Bowen; Chen, Wei-Yi; Tripathy, Ashutosh; Rockowitz, Shira; Zheng, Deyou; Patel, Dinshaw; Allis, C. David; Strahl, Brian; Song, Jikui; Wang, Gang Greg. "An H3K36 Methylation-Engaging Tudor Motif of Polycomb-like Proteins Mediates PRC2 Complex Targeting."  Mol. Cell 49, 571-582 (2013).
PubMed: 23273982

Assembly members:

Assembly members:
entity_1, polymer, 79 residues, 8737.930 Da.
entity_2, polymer, 11 residues, 1259.513 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PRSF-Duet

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts61
1H chemical shifts428

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human PHF11
2H3K36me32

Entities:

Entity 1, human PHF1 79 residues - 8737.930 Da.

1   SERARGLEUSERARGSERGLYALASERSER
2   LEUTRPASPPROALASERPROALAPROTHR
3   SERGLYPROARGPROARGLEUTRPGLUGLY
4   GLNASPVALLEUALAARGTRPTHRASPGLY
5   LEULEUTYRLEUGLYTHRILELYSLYSVAL
6   ASPSERALAARGGLUVALCYSLEUVALGLN
7   PHEGLUASPASPSERGLNPHELEUVALLEU
8   TRPLYSASPILESERPROALAALALEU

Entity 2, H3K36me3 11 residues - 1259.513 Da.

1   ALATHRGLYGLYVALM3LLYSPROHISARG
2   TYR

Samples:

sample_1: human PHF1, [U-100% 13C; U-100% 15N], 0.3 – 0.5 mM; H3K36me30.6 – 1.0 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker DMX 900 MHz
  • Bruker DMX 700 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAA25074 BAE00455 BAG58363 BAH14870 BAK62078
EMBL CAA16158 CAA16159 CAC38366 CAC38367 CAE83917
GB AAC13273 AAC52062 AAD00518 AAH08834 AAH83843
REF NP_001092384 NP_001244355 NP_001267246 NP_001289326 NP_002627
SP O43189 Q9Z1B8
TPG DAA16680
AlphaFold Q93081 O43189 Q9Z1B8

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