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 50865

Title: Complex of the CBP TAZ1 domain and a CITED2-HIF-1alpha fusion peptide   PubMed: 34520739

Deposition date: 2021-03-31 Original release date: 2021-07-24

Authors: Appling, Francis; Berlow, Rebecca; Stanfield, Robyn; Dyson, H Jane; Wright, Peter

Citation: Appling, Francis; Berlow, Rebecca; Stanfield, Robyn; Dyson, H Jane; Wright, Peter. "The molecular basis of allostery in a facilitated dissociation process"  Structure 29, 1327-1338 (2021).

Assembly members:
entity_1, polymer, 100 residues, Formula weight is not available
entity_2, polymer, 67 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21d

Entity Sequences (FASTA):
entity_1: ATGPTADPEKRKLIQQQLVL LLHAHKCQRREQANGEVRAC SLPHCRTMKNVLNHMTHCQA GKACQVAHCASSRQIISHWK NCTRHDCPVCLPLKNASDKR
entity_2: GSHMSNVIDTDFIDEEVLMS LVIEMGLDRIKELPELTSYD CEVNAPIQGSRNLLQGEELL RALDQVN

Data sets:
Data typeCount
13C chemical shifts325
15N chemical shifts123
1H chemical shifts234

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TAZ11
2CITED2-HIF1alpha fusion peptide2
3zinc13
4zinc23
5zinc33

Entities:

Entity 1, TAZ1 100 residues - Formula weight is not available

1   ALATHRGLYPROTHRALAASPPROGLULYS
2   ARGLYSLEUILEGLNGLNGLNLEUVALLEU
3   LEULEUHISALAHISLYSCYSGLNARGARG
4   GLUGLNALAASNGLYGLUVALARGALACYS
5   SERLEUPROHISCYSARGTHRMETLYSASN
6   VALLEUASNHISMETTHRHISCYSGLNALA
7   GLYLYSALACYSGLNVALALAHISCYSALA
8   SERSERARGGLNILEILESERHISTRPLYS
9   ASNCYSTHRARGHISASPCYSPROVALCYS
10   LEUPROLEULYSASNALASERASPLYSARG

Entity 2, CITED2-HIF1alpha fusion peptide 67 residues - Formula weight is not available

1   GLYSERHISMETSERASNVALILEASPTHR
2   ASPPHEILEASPGLUGLUVALLEUMETSER
3   LEUVALILEGLUMETGLYLEUASPARGILE
4   LYSGLULEUPROGLULEUTHRSERTYRASP
5   CYSGLUVALASNALAPROILEGLNGLYSER
6   ARGASNLEULEUGLNGLYGLUGLULEULEU
7   ARGALALEUASPGLNVALASN

Entity 3, zinc1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: CBP TAZ1 domain, [U-100% 13C, 15N], 300 uM; CITED2-HIF-1alpha fusion peptide 360 uM; NaCl 50 mM; DTT 2 mM; TRIS 20 mM

sample_2: CBP TAZ1 domain 570 uM; CITED2-HIF-1alpha fusion peptide, [U-100% 13C, 15N], 300 uM; NaCl 50 mM; DTT 2 mM; TRIS 20 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D best-HNCOsample_1isotropicsample_conditions_1
3D best-HN(CA)COsample_1isotropicsample_conditions_1
3D best-HNCAsample_1isotropicsample_conditions_1
3D best-HN(CO)CAsample_1isotropicsample_conditions_1
3D best-HNCACBsample_1isotropicsample_conditions_1
3D best-HN(CO)CACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CACBsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

NMRbox - data analysis, processing

GNU Octave - data analysis

NMRFAM-SPARKY - data analysis

NMRPipe - processing

NMR spectrometers:

  • Bruker Avance 700 MHz

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