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 34636

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34636
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Title: Structure and folding of a 600-million-year-old nuclear coactivator binding domain suggest conservation of dynamic properties   PubMed: 35354917

Deposition date: 2021-06-09 Original release date: 2022-04-15

Authors: Chi, C.

Citation: Karlsson, Elin; Sorgenfrei, Frieda; Andersson, Eva; Dogan, Jakob; Jemth, Per; Chi, Celestine. "The dynamic properties of a nuclear coactivator binding domain are evolutionarily conserved"  Commun. Biol. 5, 286-286 (2022).

Assembly members:
entity_1, polymer, 50 residues, 5655.529 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: GSIMPPALQQLLQTLKSPNS PQQQQQVLHILKSNPQLMAA FIKQRSQQQQ

Data sets:
Data typeCount
13C chemical shifts139
15N chemical shifts44
1H chemical shifts283

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 50 residues - 5655.529 Da.

1   GLYSERILEMETPROPROALALEUGLNGLN
2   LEULEUGLNTHRLEULYSSERPROASNSER
3   PROGLNGLNGLNGLNGLNVALLEUHISILE
4   LEULYSSERASNPROGLNLEUMETALAALA
5   PHEILELYSGLNARGSERGLNGLNGLNGLN

Samples:

sample_1: NCBD, [U-10% 13C; U-99% 15N], 500 uM

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

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P. - refinement

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz

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