BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15732

Title: 1H, 13C, and 15N backbone resonance assignments of the bright domain of the histone demethylase JARID 1B   PubMed: 19636953

Deposition date: 2008-04-16 Original release date: 2009-03-03

Authors: Yao, Wenming

Citation: Yao, Wenming; Peng, Yu; Chen, Qun; Lin, Donghai. "1H, 13C, 15N backbone and side-chain resonance assignments of the Bright/ARID domain from the human histone demethylase JARID1B"  Biomol. NMR Assignments 3, 85-87 (2009).

Assembly members:
bright_domain, polymer, 119 residues, Formula weight is not available

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):
bright_domain: MRLNELEAQTRVKLNFLDQI AKYWELQGSTLKIPHVERKI LDLFQLNKLVAEEGGFAVVC KDRKWTKIATKMGFAPGKAV GSHIRGHYERILNPYNLFLS GDSLRCLQKPNLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts270
15N chemical shifts92
1H chemical shifts544

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1jarid1B-bright1

Entities:

Entity 1, jarid1B-bright 119 residues - Formula weight is not available

1   METARGLEUASNGLULEUGLUALAGLNTHR
2   ARGVALLYSLEUASNPHELEUASPGLNILE
3   ALALYSTYRTRPGLULEUGLNGLYSERTHR
4   LEULYSILEPROHISVALGLUARGLYSILE
5   LEUASPLEUPHEGLNLEUASNLYSLEUVAL
6   ALAGLUGLUGLYGLYPHEALAVALVALCYS
7   LYSASPARGLYSTRPTHRLYSILEALATHR
8   LYSMETGLYPHEALAPROGLYLYSALAVAL
9   GLYSERHISILEARGGLYHISTYRGLUARG
10   ILELEUASNPROTYRASNLEUPHELEUSER
11   GLYASPSERLEUARGCYSLEUGLNLYSPRO
12   ASNLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: bright domain, [U-95% 15N], 1 mM; NaH2PO4 20 mM; NaCl 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 11388
PDB
DBJ BAC30898 BAD90482 BAE37363
EMBL CAB43532 CAB63108
GB AAD16061 AAH48180 AAH57318 AAI56050 AAI57032
REF NP_001100647 NP_001300971 NP_006609 NP_690855 XP_002717636
SP Q80Y84 Q9UGL1
TPG DAA21261

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