BMRB Entry 19775

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19775
MolProbity Validation Chart

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Title:
Solution structure of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in free state
Deposition date:
2014-02-07
Original release date:
2014-07-21
Authors:
Afroz, Tariq; Skrisovska, Lenka; Belloc, Eulalia; Boixet, Jordina; Mendez, Raul; Allain, Frederic
Citation:

Citation: Afroz, Tariq; Skrisovska, Lenka; Belloc, Eulalia; Boixet, Jordina; Mendez, Raul; Allain, Frederic. "A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins"  Genes Dev. 28, 1498-1514 (2014).
PubMed: 24990967

Assembly members:

Assembly members:
CPEB1RRM12, polymer, 217 residues, 23817.588 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):
CPEB1RRM12: MTWSGQLPPRNYKNPIYSCK VFLGGVPWDITEAGLVNTFR VFGSLSVEWPGKDGKHPRCP PKGYVYLVFELEKSVRSLLQ ACSHDPLSPDGLSEYYFKMS SRRMRCKEVQVIPWVLADSN FVRSPSQRLDPSRTVFVGAL HGMLNAEALAAILNDLFGGV VYAGIDTDKHKYPIGSGRVT FNNQRSYLKAVSAAFVEIKT TKFTKKVQIDPYLEDSL

Data sets:
Data typeCount
13C chemical shifts563
15N chemical shifts212
1H chemical shifts1262

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CPEB1RRM121

Entities:

Entity 1, CPEB1RRM12 217 residues - 23817.588 Da.

1   METTHRTRPSERGLYGLNLEUPROPROARG
2   ASNTYRLYSASNPROILETYRSERCYSLYS
3   VALPHELEUGLYGLYVALPROTRPASPILE
4   THRGLUALAGLYLEUVALASNTHRPHEARG
5   VALPHEGLYSERLEUSERVALGLUTRPPRO
6   GLYLYSASPGLYLYSHISPROARGCYSPRO
7   PROLYSGLYTYRVALTYRLEUVALPHEGLU
8   LEUGLULYSSERVALARGSERLEULEUGLN
9   ALACYSSERHISASPPROLEUSERPROASP
10   GLYLEUSERGLUTYRTYRPHELYSMETSER
11   SERARGARGMETARGCYSLYSGLUVALGLN
12   VALILEPROTRPVALLEUALAASPSERASN
13   PHEVALARGSERPROSERGLNARGLEUASP
14   PROSERARGTHRVALPHEVALGLYALALEU
15   HISGLYMETLEUASNALAGLUALALEUALA
16   ALAILELEUASNASPLEUPHEGLYGLYVAL
17   VALTYRALAGLYILEASPTHRASPLYSHIS
18   LYSTYRPROILEGLYSERGLYARGVALTHR
19   PHEASNASNGLNARGSERTYRLEULYSALA
20   VALSERALAALAPHEVALGLUILELYSTHR
21   THRLYSPHETHRLYSLYSVALGLNILEASP
22   PROTYRLEUGLUASPSERLEU

Samples:

sample_1: CPEB1RRM12, [U-100% 15N], 0.4 – 0.6 mM; sodium chloride 100 mM; DTT 1 mM; magnesium sulphate 1 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%

sample_2: CPEB1RRM12, [U-100% 13C; U-100% 15N], 0.4 – 0.6 mM; sodium chloride 100 mM; DTT 1 mM; magnesium sulphate 1 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%

sample_3: CPEB1RRM12, [U-100% 13C; U-100% 15N; U-100% 2H], 0.4 – 0.6 mM; sodium chloride 100 mM; DTT 1 mM; magnesium sulphate 1 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 19778
PDB
DBJ BAB14496 BAB33089 BAE87429 BAG63194 BAH11723
EMBL CAH92427
GB AAH35348 AAH50629 AAK01239 AAK01240 ADQ32841
REF NP_001073001 NP_001073002 NP_001073003 NP_001126432 NP_001239455
SP Q5R733 Q9BZB8
TPG DAA17635
AlphaFold Q5R733 Q9BZB8

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