BMRB Entry 11323

Title:
Solution structure of the MYND domain of the human zinc finger MYND domain-containing protein 10
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Miyamoto, K.; Kigawa, T.; Tomizawa, T.; Tochio, N.; Sasagawa, A.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation:

Citation: Miyamoto, K.; Kigawa, T.; Tomizawa, T.; Tochio, N.; Sasagawa, A.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the MYND domain of the human zinc finger MYND domain-containing protein 10"  .

Assembly members:

Assembly members:
zf-MYND, polymer, 70 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: cell free synthesis   Host organism: E. coli - cell free   Vector: P040816-10

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts262
15N chemical shifts63
1H chemical shifts395

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zf-MYND1
2ZINC ION no.12
3ZINC ION no.22

Entities:

Entity 1, zf-MYND 70 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEUGLUALA
2   VALALAPROGLUARGPROARGCYSALATYR
3   CYSSERALAGLUALASERLYSARGCYSSER
4   ARGCYSGLNASNGLUTRPTYRCYSCYSARG
5   GLUCYSGLNVALLYSHISTRPGLULYSHIS
6   GLYLYSTHRCYSVALLEUALAALAGLNGLY
7   ASPARGALALYSSERGLYPROSERSERGLY

Entity 2, ZINC ION no.1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: zf-MYND, [U-13C; U-15N], 0.3 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.9321, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAD97063 BAG53316 BAG73936 BAK63946
EMBL CAD38688 CAL37695 CAL38065
GB AAC24726 AAC24728 AAH33732 AIC56440 EAW65104
REF NP_001233432 NP_001295308 NP_056980 XP_001090964 XP_003257157
SP O75800
AlphaFold O75800

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