BMRB Entry 52655

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52655

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for CBP-TAZ4
Deposition date:
2024-10-24
Original release date:
2026-02-03
Authors:
Bracaglia, Lorenzo; Oliveti, Silvia; Felli, Isabella; Pierattelli, Roberta
Citation:

Citation: Bracaglia, Lorenzo; Oliveti, Silvia; Felli, Isabella; Pierattelli, Roberta. "Decoding Order and Disorder in Proteins by NMR Spectroscopy"  J. Am. Chem. Soc. 147, 13146-13157 (2025).
PubMed: 40223218

Assembly members:

Assembly members:
entity_1, polymer, 306 residues, 33297 Da.
entity_ZN, non-polymer, 65.409 Da.

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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSPQESRRLSIQRAIQSLV HAAQCRNANCSLPSCQKMKR VVQHTKGCKRKTNGGCPVCK QLIALAAYHAKHCQENKCPV PFCLNIKHKLRQQQIQHRLQ QAQLMRRRMATMNTRNVPQQ SLPSPTSAPPGTPTQQPSTP QTPQPPAQPQPSPVSMSPAG FPSVARTQPPTTVSTGKPTS QVPAPPPPAQPPPAAVEAAR QIEREAQQQQHLYRVNINNS MPPGRTGMGTPGSQMAPVSL NVPRPNQVSGPVMPSMPPGQ WQQAPLPQQQPMPGLPRPVI SMQAQAAVAGPRMPSVQQLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts803
15N chemical shifts272
1H chemical shifts227

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TAZ41
2Zinc ions, 12
3Zinc ions, 22
4Zinc ions, 32

Entities:

Entity 1, TAZ4 306 residues - 33297 Da.

Residues 1-2 are not native. Residues 298-306 are a non-native histidine tag. The sequence 3-297 corresponds to the 1763-2057 human CREB Binding Protein (CBP) region.

1   METGLYSERPROGLNGLUSERARGARGLEU
2   SERILEGLNARGALAILEGLNSERLEUVAL
3   HISALAALAGLNCYSARGASNALAASNCYS
4   SERLEUPROSERCYSGLNLYSMETLYSARG
5   VALVALGLNHISTHRLYSGLYCYSLYSARG
6   LYSTHRASNGLYGLYCYSPROVALCYSLYS
7   GLNLEUILEALALEUALAALATYRHISALA
8   LYSHISCYSGLNGLUASNLYSCYSPROVAL
9   PROPHECYSLEUASNILELYSHISLYSLEU
10   ARGGLNGLNGLNILEGLNHISARGLEUGLN
11   GLNALAGLNLEUMETARGARGARGMETALA
12   THRMETASNTHRARGASNVALPROGLNGLN
13   SERLEUPROSERPROTHRSERALAPROPRO
14   GLYTHRPROTHRGLNGLNPROSERTHRPRO
15   GLNTHRPROGLNPROPROALAGLNPROGLN
16   PROSERPROVALSERMETSERPROALAGLY
17   PHEPROSERVALALAARGTHRGLNPROPRO
18   THRTHRVALSERTHRGLYLYSPROTHRSER
19   GLNVALPROALAPROPROPROPROALAGLN
20   PROPROPROALAALAVALGLUALAALAARG
21   GLNILEGLUARGGLUALAGLNGLNGLNGLN
22   HISLEUTYRARGVALASNILEASNASNSER
23   METPROPROGLYARGTHRGLYMETGLYTHR
24   PROGLYSERGLNMETALAPROVALSERLEU
25   ASNVALPROARGPROASNGLNVALSERGLY
26   PROVALMETPROSERMETPROPROGLYGLN
27   TRPGLNGLNALAPROLEUPROGLNGLNGLN
28   PROMETPROGLYLEUPROARGPROVALILE
29   SERMETGLNALAGLNALAALAVALALAGLY
30   PROARGMETPROSERVALGLNGLNLEUGLU
31   HISHISHISHISHISHIS

Entity 2, Zinc ions, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: CBP-TAZ4, [U-100% 13C; U-100% 15N], 250 uM; sodium acetate 25 mM; sodium chloride 50 mM; TCEP 2 mM; zinc chloride 0.1 mM

sample_2: CBP-TAZ4, [U-100% 15N], 300 uM; sodium acetate 25 mM; sodium chloride 50 mM; TCEP 2 mM; zinc chloride 0.1 mM

sample_conditions_1: pH: 5.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D IR HNCOsample_1isotropicsample_conditions_1
3D IR HNCAsample_1isotropicsample_conditions_1
2D CCCOsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
2D CBCACOsample_1isotropicsample_conditions_1
3D (H)N(CA)NNHsample_1isotropicsample_conditions_1
3D (H)N(COCA)NNHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D 1H-13C TROSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection, processing

NEASY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 1200 MHz
  • Bruker AVANCE NEO 900 MHz
  • Bruke AVANCE NEO 700 MHz

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