BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 52255

Title: Mdm2aa211-223 pS215-pT218

Deposition date: 2024-01-02 Original release date: 2024-01-08

Authors: Luo, Yingyue; Theillet, Francois-Xavier

Citation: Luo, Yingyue; Theillet, Francois-Xavier. "Structural characterization of the MDM2 NLS/NES/arrestin-binding/acidic domain in phospho- and unmodified-forms"  .

Assembly members:
entity_1, polymer, 15 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: chemical synthesis

Entity Sequences (FASTA):
entity_1: XSSSEXTGXPSNPDX

Data sets:
Data typeCount
15N chemical shifts11
1H chemical shifts49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mdm2aa211-223_pS215-pT2181

Entities:

Entity 1, Mdm2aa211-223_pS215-pT218 15 residues - Formula weight is not available

Ac-SSSEpSTGpTPSNPD-NH2

1   ACESERSERSERGLUSEPTHRGLYTPOPRO
2   SERASNPROASPNH2

Samples:

sample_1: Mdm2aa211_223_pS215_pT218 3 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DSS 0.5 mM

sample_conditions_1: ionic strength: 0.190 M; pH: 7.1; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H ROESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4 - collection

TOPSPIN v3 - collection

CcpNMR v3 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 700 MHz
  • Bruker AVANCE III 600 MHz

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