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 15001

Title: Structures and chemical shift assignments for the ADD domain of the ATRX protein   PubMed: 17609377

Authors: Yang, Ji-Chun; Neuhaus, David

Citation: Argentaro, Anthony; Yang, Ji-Chun; Chapman, Lynda; Kowalczyk, Monika; Gibbons, Richard; Higgs, Douglas; Neuhaus, David; Rhodes, Daniela. "Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX"  Proc. Natl. Acad. Sci. U. S. A. 104, 11939-11944 (2007).

Assembly members:
ADD_domain_156-296, polymer, 142 residues, Formula weight is not available
ZN, non-polymer, 65.409 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

Entity Sequences (FASTA):
ADD_domain_156-296: GAMADKRGDGLHGIVSCTAC GQQVNHFQKDSIYRHPSLQV LICKNCFKYYMSDDISRDSD GMDEQCRWCAEGGNLICCDF CHNAFCKKCILRNLGRKELS TIMDENNQWYCYICHPEPLL DLVTACNSVFENLEQLLQQN KK

Data sets:
Data typeCount
13C chemical shifts399
15N chemical shifts139
1H chemical shifts852

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein chain1
2zinc 12
3zinc 22
4zinc 32

Entities:

Entity 1, protein chain 142 residues - Formula weight is not available

1   GLYALAMETALAASPLYSARGGLYASPGLY
2   LEUHISGLYILEVALSERCYSTHRALACYS
3   GLYGLNGLNVALASNHISPHEGLNLYSASP
4   SERILETYRARGHISPROSERLEUGLNVAL
5   LEUILECYSLYSASNCYSPHELYSTYRTYR
6   METSERASPASPILESERARGASPSERASP
7   GLYMETASPGLUGLNCYSARGTRPCYSALA
8   GLUGLYGLYASNLEUILECYSCYSASPPHE
9   CYSHISASNALAPHECYSLYSLYSCYSILE
10   LEUARGASNLEUGLYARGLYSGLULEUSER
11   THRILEMETASPGLUASNASNGLNTRPTYR
12   CYSTYRILECYSHISPROGLUPROLEULEU
13   ASPLEUVALTHRALACYSASNSERVALPHE
14   GLUASNLEUGLUGLNLEULEUGLNGLNASN
15   LYSLYS

Entity 2, zinc 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: ADD domain 156-296, [U-15N], 0.6 – 0.8 mM; TRIS, none, 20 mM; DTT, none, 1 mM; zinc chloride, none, 100 uM; sodium chloride, none, 0.5 M

sample_2: ADD domain 156-296, [U-13C; U-15N], 0.3 – 0.4 mM; TRIS, none, 20 mM; DTT, none, 1 mM; zinc chloride, none, 100 uM; sodium chloride, none, 0.5 M

sample_conditions_1: ionic strength: 0.5 M; pH: 6.7; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
HNHAHBsample_2isotropicsample_conditions_1
HN(CO)HAHBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection, processing

SPARKY, T Goddard - data analysis, peak picking

X-PLOR v3.8, AT Brunger - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 17569
PDB
DBJ BAC28096 BAC40142 BAC81110 BAC81111 BAC81112
EMBL CAB90351 CAI40710 CAI42674 CAI42675 CAI43115
GB AAB40698 AAB40699 AAB40700 AAB49969 AAB49970
REF NP_000480 NP_001009018 NP_033556 NP_612114 XP_001099671
SP P46100 Q61687 Q7YQM3 Q7YQM4
TPG DAA12976 DAA12977