BMRB Entry 6997

Title:
Structural Insights of the Specificity and Catalysis of a Dimeric Viral SET Domain Histone H3 Lysine-27 Methyltransferase
Deposition date:
2006-02-21
Original release date:
2007-02-07
Authors:
Qian, Chengmin
Citation:

Citation: Qian, Chengmin; Wang, Xueqi; Manzur, Karishma; Sachchidanand, .; Farooq, Amjad; Zeng, Lei; Wang, Rong; Zhou, Ming-Ming. "Structural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferase."  J. Mol. Biol. 359, 86-89 (2006).
PubMed: 16603186

Assembly members:

Assembly members:
13C/15N vSET complex, polymer, 119 residues, Formula weight is not available
me_K27_H3_Peptide, polymer, 21 residues, Formula weight is not available
SAH, non-polymer, 384.411 Da.

Natural source:

Natural source:   Common Name: Paramecium bursaria   Taxonomy ID: 74790   Superkingdom: Viruses   Kingdom: not available   Genus/species: Paramecium bursaria

Experimental source:

Experimental source:   Production method: recombinant technology

Data sets:
Data typeCount
13C chemical shifts364
15N chemical shifts110
1H chemical shifts829

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1vSET1
2me_K27_H3_Peptide2
3SAH3

Entities:

Entity 1, vSET 119 residues - Formula weight is not available

1   METPHEASNASPARGVALILEVALLYSLYS
2   SERPROLEUGLYGLYTYRGLYVALPHEALA
3   ARGLYSSERPHEGLULYSGLYGLULEUVAL
4   GLUGLUCYSLEUCYSILEVALARGHISASN
5   ASPASPTRPGLYTHRALALEUGLUASPTYR
6   LEUPHESERARGLYSASNMETSERALAMET
7   ALALEUGLYPHEGLYALAILEPHEASNHIS
8   SERLYSASPPROASNALAARGHISGLULEU
9   THRALAGLYLEULYSARGMETARGILEPHE
10   THRILELYSPROILEALAILEGLYGLUGLU
11   ILETHRILESERTYRGLYASPASPTYRTRP
12   LEUSERARGPROARGLEUTHRGLNASN

Entity 2, me_K27_H3_Peptide 21 residues - Formula weight is not available

1   GLYLYSALAPROARGLYSGLNLEUALATHR
2   LYSALAALAARGMEKSERALAPROALATHR
3   GLY

Entity 3, SAH - C14 H20 N6 O5 S - 384.411 Da.

1   SAH

Samples:

sample_1: 13C/15N vSET complex, [U-13C; U-15N], 5.0 mM

conditions_1: pH: 6.5; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
HNCAsample_1not availableconditions_1
HN(CO)CAsample_1not availableconditions_1
HNCACBsample_1not availableconditions_1
HN(CO)CACBsample_1not availableconditions_1
(H)C(CO)NH-TOCSYsample_1not availableconditions_1
HCCH-COSYsample_1not availableconditions_1
2D ROESY and TOCSYsample_1not availableconditions_1
15N or 13C-edited 3D NOESY or 2D homonuclear NOESYsample_1not availableconditions_1
3D 13C-F1 editedsample_1not availableconditions_1
13C/15N-F3 filtered NOESYsample_1not availableconditions_1

Software:

No software information available

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAM62356
GB AAY18719 ABB83163 ABL95239 ABL95241 ABN80289

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