BMRB Entry 15161

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15161

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Title:
The MYND domain from human AML1-ETO
Deposition date:
2007-03-06
Original release date:
2007-10-24
Authors:
Liu, Yizhou; Chen, Wei; Gaudet, Justin; Cheney, Matthew; Roudaia, Liya; Cierpicki, Tomasz; Klet, Rachel; Hartman, Kari; Laue, Thomas; Speck, Nancy; Bushweller, John
Citation:

Citation: Liu, Yizhou; Chen, Wei; Gaudet, Justin; Cheney, Matthew; Roudaia, Liya; Cierpicki, Tomasz; Klet, Rachel; Hartman, Kari; Laue, Thomas; Speck, Nancy; Bushweller, John. "Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity"  Cancer Cell 11, 483-497 (2007).
PubMed: 17560331

Assembly members:

Assembly members:
ETO_MYND, polymer, 50 residues, Formula weight is not available
ZN, non-polymer, 65.409 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: pGEX4T3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ETO_MYND: DSSESCWNCGRKASETCSGC NTARYCGSFCQHKDWEKHHH ICGQTLQAQQ

Data sets:
Data typeCount
13C chemical shifts202
15N chemical shifts59
1H chemical shifts269

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ETO MYND1
2ZINC ION, 12
3ZINC ION, 22

Entities:

Entity 1, ETO MYND 50 residues - Formula weight is not available

1   ASPSERSERGLUSERCYSTRPASNCYSGLY
2   ARGLYSALASERGLUTHRCYSSERGLYCYS
3   ASNTHRALAARGTYRCYSGLYSERPHECYS
4   GLNHISLYSASPTRPGLULYSHISHISHIS
5   ILECYSGLYGLNTHRLEUGLNALAGLNGLN

Entity 2, ZINC ION, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: ETO MYND, [U-99% 13C; U-99% 15N], 1 mM; ZINC ION 1 mM; Bis-Tris 25 mM; NaCl 100 mM; DTT 5 mM; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian Unity 600 MHz

Related Database Links:

BMRB 15173
PDB
DBJ BAA03089 BAA03247 BAA03558 BAA06774 BAA07755
EMBL CAA56311 CAF99400 CAG33073
GB AAB34819 AAC28931 AAC28932 AAF72198 AAF72199
REF NP_001070244 NP_001089065 NP_001102127 NP_001104496 NP_001104497
SP Q06455 Q61909
AlphaFold Q06455 Q61909

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