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Solution structure of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in free state
Authors
Afroz, T., Skrisovska, L., Belloc, E., Boixet, J.G., Mendez, R., Allain, F.H.-T.
Assembly
CPEB1RRM12
Entity
1. CPEB1RRM12 (polymer, Thiol state: all free), 217 monomers, 24343.72 Da Detail

MTWSGQLPPR NYKNPIYSCK VFLGGVPWDI TEAGLVNTFR VFGSLSVEWP GKDGKHPRCP PKGYVYLVFE LEKSVRSLLQ ACSHDPLSPD GLSEYYFKMS SRRMRCKEVQ VIPWVLADSN FVRSPSQRLD PSRTVFVGAL HGMLNAEALA AILNDLFGGV VYAGIDTDKH KYPIGSGRVT FNNQRSYLKA VSAAFVEIKT TKFTKKVQID PYLEDSL


Formula weight
24343.72 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.2 %, Completeness: 74.1 %, Completeness (bb): 73.3 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All74.1 % (1903 of 2569)79.3 % (1060 of 1336)62.2 % (630 of 1013)96.8 % (213 of 220)
Backbone73.3 % (933 of 1272)85.5 % (372 of 435)57.5 % (365 of 635)97.0 % (196 of 202)
Sidechain76.2 % (1142 of 1498)76.4 % (688 of 901)75.5 % (437 of 579)94.4 % (17 of 18)
Aromatic73.6 % (187 of 254)88.2 % (112 of 127)57.7 % (71 of 123)100.0 % (4 of 4)
Methyl91.5 % (214 of 234)90.6 % (106 of 117)92.3 % (108 of 117)

1. CPEB1RRM12

MTWSGQLPPR NYKNPIYSCK VFLGGVPWDI TEAGLVNTFR VFGSLSVEWP GKDGKHPRCP PKGYVYLVFE LEKSVRSLLQ ACSHDPLSPD GLSEYYFKMS SRRMRCKEVQ VIPWVLADSN FVRSPSQRLD PSRTVFVGAL HGMLNAEALA AILNDLFGGV VYAGIDTDKH KYPIGSGRVT FNNQRSYLKA VSAAFVEIKT TKFTKKVQID PYLEDSL

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.5


#NameIsotope labelingTypeConcentration
1CPEB1RRM12[U-100% 15N]0.4 ~ 0.6 mM
2sodium chloridenatural abundance100 mM
3DTTnatural abundance1 mM
4magnesium sulphatenatural abundance1 mM
5sodium phosphatenatural abundance50 mM
6H2Onatural abundance90 %
7D2Onatural abundance10 %
Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.5


#NameIsotope labelingTypeConcentration
8CPEB1RRM12[U-100% 13C; U-100% 15N]0.4 ~ 0.6 mM
9sodium chloridenatural abundance100 mM
10DTTnatural abundance1 mM
11magnesium sulphatenatural abundance1 mM
12sodium phosphatenatural abundance50 mM
13H2Onatural abundance90 %
14D2Onatural abundance10 %
Sample #3

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 303 K, pH 6.5


#NameIsotope labelingTypeConcentration
15CPEB1RRM12[U-100% 13C; U-100% 15N; U-100% 2H]0.4 ~ 0.6 mM
16sodium chloridenatural abundance100 mM
17DTTnatural abundance1 mM
18magnesium sulphatenatural abundance1 mM
19sodium phosphatenatural abundance50 mM
20H2Onatural abundance90 %
21D2Onatural abundance10 %

LACS Plot; CA
Referencing offset: 3.17 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: 3.17 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.08 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2MKH, Strand ID: A Detail


Release date
2014-07-20
Citation
A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins
Afroz, T., Skrisovska, L., Belloc, E., Boixet, J.G., Mendez, R., Allain, F.H.-T.
Genes. Dev. (2014), 28, 1498-1514, PubMed 24990967 , DOI 10.1101/gad.241133.114 ,
Entries sharing articles BMRB: 4 entries Detail
  BMRB: 19771 released on 2014-07-20
    Title Solution structure of CPEB1 ZZ domain in the free state
  BMRB: 19776 released on 2014-07-20
    Title Solution structure of tandem RRM domains of cytoplasmic polyadenylation element binding protein 4 (CPEB4) in complex with RNA
  BMRB: 19777 released on 2014-07-20
    Title Solution structure of tandem RRM domains of cytoplasmic polyadenylation element binding protein 4 (CPEB4) in free state
  BMRB: 19778 released on 2014-07-20
    Title Structural model of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in complex with RNA
Related entities 1. CPEB1RRM12, : 1 : 1 : 77 entities Detail
Interaction partners 1. CPEB1RRM12, : 4 interactors Detail
Experiments performed 15 experiments Detail
nullKeywords CPEB1, Cytoplasmic polyadenylation, RNA recognition motif (RRM), Translational regulation