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 18142

Title: MOZ   PubMed: 22713874

Deposition date: 2011-12-15 Original release date: 2012-06-26

Authors: Qiu, Yu

Citation: Qiu, Yu; Liu, Lei; Zhao, Chen; Han, Chuanchun; Li, Fudong; Zhang, Jiahai; Wu, Mian; Wu, Jihui; Shi, Yunyu. "Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription"  Genes Dev. 26, 1376-1391 (2012).

Assembly members:
entity_1, polymer, 110 residues, 12510.658 Da.
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):
entity_1: EPIPICSFCLGTKEQNREKK PEELISCADCGNSGHPSCLK FSPELTVRVKALRWQCIECK TCSSCRDQGKNADNMLFCDS CDRGFHMECCDPPLTRMPKG MWICQICRPR

Data sets:
Data typeCount
13C chemical shifts392
15N chemical shifts105
1H chemical shifts677

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PHD zinc finger1
2ZINC ION_12
3ZINC ION_22
4ZINC ION_32
5ZINC ION_42

Entities:

Entity 1, PHD zinc finger 110 residues - 12510.658 Da.

1   GLUPROILEPROILECYSSERPHECYSLEU
2   GLYTHRLYSGLUGLNASNARGGLULYSLYS
3   PROGLUGLULEUILESERCYSALAASPCYS
4   GLYASNSERGLYHISPROSERCYSLEULYS
5   PHESERPROGLULEUTHRVALARGVALLYS
6   ALALEUARGTRPGLNCYSILEGLUCYSLYS
7   THRCYSSERSERCYSARGASPGLNGLYLYS
8   ASNALAASPASNMETLEUPHECYSASPSER
9   CYSASPARGGLYPHEHISMETGLUCYSCYS
10   ASPPROPROLEUTHRARGMETPROLYSGLY
11   METTRPILECYSGLNILECYSARGPROARG

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: HEPES 50 mM; sodium chloride 100 mM; entity_1, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_2: HEPES 50 mM; sodium chloride 100 mM; entity_1, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC25728 BAC29621 BAC30401 BAC35729 BAD00088
EMBL CAH89880
GB AAC50662 AAI42660 AAI42960 AAI63677 AAI72379
REF NP_001074618 NP_001094040 NP_001116784 NP_001292807 NP_006757
SP Q5TKR9 Q8BZ21 Q92794
TPG DAA14459

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts