BMRB Entry 50256

Title:
hCPEB3
Deposition date:
2020-05-01
Original release date:
2022-04-12
Authors:
Ramirez de Mingo, Daniel; Laurents, Douglas
Citation:

Citation: Ramirez de Mingo, Daniel; Pantoja-Uceda, David; Carrion-Vazquez, Mariano; Laurents, Douglas. "Human CPEB3's Prion-Like Domain: Preferred Conformations and Implications for Memory Consolidation"  Mol. Cell ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 450 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: pLL3.7-syn

Data sets:
Data typeCount
13C chemical shifts1416
15N chemical shifts441
1H chemical shifts384

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 450 residues - Formula weight is not available

1   METGLNASPASPLEULEUMETASPLYSSER
2   LYSTHRGLNPROGLNPROGLNGLNGLNGLN
3   ARGGLNGLNGLNGLNPROGLNPROGLUSER
4   SERVALSERGLUALAPROSERTHRPROLEU
5   SERSERGLUTHRPROLYSPROGLUGLUASN
6   SERALAVALPROALALEUSERPROALAALA
7   ALAPROPROALAPROASNGLYPROASPLYS
8   METGLNMETGLUSERPROLEULEUPROGLY
9   LEUSERPHEHISGLNPROPROGLNGLNPRO
10   PROPROPROGLNGLUPROALAALAPROGLY
11   ALASERLEUSERPROSERPHEGLYSERTHR
12   TRPSERTHRGLYTHRTHRASNALAVALGLU
13   ASPSERPHEPHEGLNGLYILETHRPROVAL
14   ASNGLYTHRMETLEUPHEGLNASNPHEPRO
15   HISHISVALASNPROVALPHEGLYGLYTHR
16   PHESERPROGLNILEGLYLEUALAGLNTHR
17   GLNHISHISGLNGLNPROPROPROPROALA
18   PROALAPROGLNPROALAGLNPROALAGLN
19   PROPROGLNALAGLNPROPROGLNGLNARG
20   ARGSERPROALASERPROSERGLNALAPRO
21   TYRALAGLNARGSERALAALAALAALATYR
22   GLYHISGLNPROILEMETTHRSERLYSPRO
23   SERSERSERSERALAVALALAALAALAALA
24   ALAALAALAALAALASERSERALASERSER
25   SERTRPASNTHRHISGLNSERVALASNALA
26   ALATRPSERALAPROSERASNPROTRPGLY
27   GLYLEUGLNALAGLYARGASPPROARGARG
28   ALAVALGLYVALGLYVALGLYVALGLYVAL
29   GLYVALPROSERPROLEUASNPROILESER
30   PROLEULYSLYSPROPHESERSERASNVAL
31   ILEALAPROPROLYSPHEPROARGALAALA
32   PROLEUTHRSERLYSSERTRPMETGLUASP
33   ASNALAPHEARGTHRASPASNGLYASNASN
34   LEULEUPROPHEGLNASPARGSERARGPRO
35   TYRASPTHRPHEASNLEUHISSERLEUGLU
36   ASNSERLEUMETASPMETILEARGTHRASP
37   HISGLUPROLEULYSGLYARGMETGLYILE
38   ASNPHEHISHISPROGLYTHRASPASNILE
39   METALALEUASNSERARGSERSERLEUPHE
40   PROPHEGLUASPALAPHELEUASPASPSER
41   HISGLYASPGLNALALEUSERSERGLYLEU
42   SERSERPROTHRARGCYSGLNASNGLYGLU
43   ARGVALGLUARGTYRSERARGLYSVALPHE
44   VALGLYGLYLEUPROPROASPILEASPGLU
45   ASPGLUILETHRALASERPHEARGARGPHE

Samples:

sample_1: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 1.5 ± 0.2 mM

sample_2: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 0.4 ± 0.1 mM

sample_3: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 1.5 ± 0.2 mM

sample_4: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 1.5 ± 0.2 mM

sample_5: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 1.5 ± 0.2 mM

sample_6: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 0.6 ± 0.1 mM

sample_7: hCPEB3 IDR, [U-98% 13C; U-98% 15N], 0.6 ± 0.1 mM

sample_conditions_1: ionic strength: 0.0010 M; pH: 4.0; pressure: 0.93 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
1H-15N heteronoesample_1isotropicsample_conditions_1
T1rho/R1rho relaxationsample_1isotropicsample_conditions_1
1D 1Hsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
1H-15N heteronoesample_2isotropicsample_conditions_1
T1rho/R1rho relaxationsample_2isotropicsample_conditions_1
1D 1Hsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
1H-15N heteronoesample_3isotropicsample_conditions_1
T1rho/R1rho relaxationsample_3isotropicsample_conditions_1
1D 1Hsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
1H-15N heteronoesample_4isotropicsample_conditions_1
T1rho/R1rho relaxationsample_4isotropicsample_conditions_1
3D HNHAsample_4isotropicsample_conditions_1
1D 1Hsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
3D HNCOsample_5isotropicsample_conditions_1
3D CBCA(CO)NHsample_5isotropicsample_conditions_1
T1rho/R1rho relaxationsample_5isotropicsample_conditions_1
1H-15N heteronoesample_5isotropicsample_conditions_1
1D 1Hsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
3D HNCOsample_6isotropicsample_conditions_1
3D CBCA(CO)NHsample_6isotropicsample_conditions_1
1H-15N heteronoesample_6isotropicsample_conditions_1
T1rho/R1rho relaxationsample_6isotropicsample_conditions_1
1D 1Hsample_7isotropicsample_conditions_1
2D 1H-15N HSQCsample_7isotropicsample_conditions_1
3D HNCOsample_7isotropicsample_conditions_1
3D CBCA(CO)NHsample_7isotropicsample_conditions_1
T1rho/R1rho relaxationsample_7isotropicsample_conditions_1
1H-15N heteronoesample_7isotropicsample_conditions_1

Software:

SPARKY v3.12 - chemical shift assignment

TOPSPIN v2.1 - collection

NMRPipe - data analysis

TALOS+ - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

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