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 19905

Title: Phosphorylated 4E-BP2   PubMed: 25533957

Deposition date: 2014-04-10 Original release date: 2014-12-09

Authors: Bah, Alaji; Forman-Kay, Julie

Citation: Bah, Alaji; Vernon, Robert; Siddiqui, Zeba; Krzeminski, Mickael; Muhandiram, Ranjith; Zhao, Charlie; Sonenberg, Nahum; Kay, Lewis; Forman-Kay, Julie. "Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch"  Nature 519, 106-109 (2015).

Assembly members:
Phosphorylated_4E-BP2, polymer, 120 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
Phosphorylated_4E-BP2: MSSSAGSGHQPSQSRAIPTR TVAISDAAQLPHDYCTTPGG TLFSTTPGGTRIIYDRKFLL DRRNSPMAQTPPCHLPNIPG VTSPGTLIEDSKVEVNNLNN LNNHDRKHAVGDDAQFEMDI

Data sets:
Data typeCount
13C chemical shifts299
1H chemical shifts216

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1phosphorylated 4E-BP2 monomer1

Entities:

Entity 1, phosphorylated 4E-BP2 monomer 120 residues - Formula weight is not available

1   METSERSERSERALAGLYSERGLYHISGLN
2   PROSERGLNSERARGALAILEPROTHRARG
3   THRVALALAILESERASPALAALAGLNLEU
4   PROHISASPTYRCYSTHRTHRPROGLYGLY
5   THRLEUPHESERTHRTHRPROGLYGLYTHR
6   ARGILEILETYRASPARGLYSPHELEULEU
7   ASPARGARGASNSERPROMETALAGLNTHR
8   PROPROCYSHISLEUPROASNILEPROGLY
9   VALTHRSERPROGLYTHRLEUILEGLUASP
10   SERLYSVALGLUVALASNASNLEUASNASN
11   LEUASNASNHISASPARGLYSHISALAVAL
12   GLYASPASPALAGLNPHEGLUMETASPILE

Samples:

sample_1: Phosphorylated 4E-BP2, [U-99% 13C; U-99% 15N], 1 mM; DTT 2 mM; sodium chloride 100 mM; sodium phosphate 30 mM; EDTA 1 mM; Benzamidine 1 mM

sample_conditions_1: ionic strength: 0.150 M; pH: 6.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard, Shen, Vernon, Baker and Bax - chemical shift assignment, processing, structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Varian INOVA 500 MHz

Related Database Links:

BMRB 19114
DBJ BAG11409 BAG36466
EMBL CAG47036
GB AAA62270 AAH05057 AAH50633 AAP35981 AAX32712
PRF 2021415B
REF NP_001178078 NP_001244839 NP_004087 XP_002718482 XP_002756317
SP Q13542
TPG DAA14291