BMRB Entry 53509

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53509

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for CITED2 CTAD
Deposition date:
2026-01-15
Original release date:
2026-07-14
Authors:
Do, To Uyen; Kraft, Emma; Chappell, Garrett; Parnham, Stuart; Berlow, Rebecca
Citation:

Citation: Do, To Uyen; Kraft, Emma; Chappell, Garrett; Parnham, Stuart; Berlow, Rebecca. "Sequence-encoded differences in the conformational ensembles of CITED transcriptional activation domains impact coactivator binding "  Protein Sci. 35, e70693-e70693 (2026).
PubMed: 42332380

Assembly members:

Assembly members:
entity_1, polymer, 60 residues, Formula weight is not available

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: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMSNVIDTDFIDEEVLMS LVIEMGLDRIKELPELWLGQ NEFDFMTDFVCKQQPSRVSC

Data sets:
Data typeCount
13C chemical shifts168
15N chemical shifts54
1H chemical shifts54

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CITED2 CTAD1

Entities:

Entity 1, CITED2 CTAD 60 residues - Formula weight is not available

Residues 1-5 represent a nonnative cloning artifact.

1   GLYSERHISMETSERASNVALILEASPTHR
2   ASPPHEILEASPGLUGLUVALLEUMETSER
3   LEUVALILEGLUMETGLYLEUASPARGILE
4   LYSGLULEUPROGLULEUTRPLEUGLYGLN
5   ASNGLUPHEASPPHEMETTHRASPPHEVAL
6   CYSLYSGLNGLNPROSERARGVALSERCYS

Samples:

sample_1: CITED2 C-terminal activation domain, [U-100% 13C; U-100% 15N], 100 uM; D2O, [U-100% 2H], 1%; TRIS 20 mM; sodium chloride 50 mM; DTT 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

SMILE - processing

NMRPipe - processing

NMRbox - data analysis, processing

NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 850 MHz

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