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 16893

Title: MDM4 binds ligands via an induced fit mechanism in which disordered regions become structured   PubMed: 20515689

Deposition date: 2010-04-22 Original release date: 2010-06-16

Authors: Sanchez, Maria; Renshaw, Jonathan; Davies, Gareth; Barlow, Paul; Vogtherr, Martin

Citation: Sanchez, Maria; Renshaw, Jonathan; Davies, Gareth; Barlow, Paul; Vogtherr, Martin. "MDM4 binds ligands via a mechanism in which disordered regions become structured."  FEBS Lett. 584, 3035-3041 (2010).

Assembly members:
MDM4 N-terminal domain, polymer, 102 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):
MDM4 N-terminal domain: GSHMDSASRISPGQINQVRP KLPLLKILHAAGAQGEMFTV KEVMHYLGQYIMVKQLYDQQ EQHMVYCGGDLLGELLGRQS FSVKDPSPLYDMLRKNLVTL AT

Data sets:
Data typeCount
13C chemical shifts215
15N chemical shifts66
1H chemical shifts66

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MDM41

Entities:

Entity 1, MDM4 102 residues - Formula weight is not available

1   GLYSERHISMETASPSERALASERARGILE
2   SERPROGLYGLNILEASNGLNVALARGPRO
3   LYSLEUPROLEULEULYSILELEUHISALA
4   ALAGLYALAGLNGLYGLUMETPHETHRVAL
5   LYSGLUVALMETHISTYRLEUGLYGLNTYR
6   ILEMETVALLYSGLNLEUTYRASPGLNGLN
7   GLUGLNHISMETVALTYRCYSGLYGLYASP
8   LEULEUGLYGLULEULEUGLYARGGLNSER
9   PHESERVALLYSASPPROSERPROLEUTYR
10   ASPMETLEUARGLYSASNLEUVALTHRLEU
11   ALATHR

Samples:

sample_1: MDM4 N-terminal domain, [U-100% 13C; U-100% 15N], 0.1 mM; sodium chloride 100 mM; TCEP 2 mM; EDTA 0.1 mM; BisTris 50 mM; sodium azide 0.1%; H2O 99%; DMSO 1%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.5.5, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16894 16900
PDB
DBJ BAD96948 BAG64634 BAG65468 BAK62829
EMBL CAE45961 CAH18300
GB AAH67299 AAI05107 AAO13494 AGJ70143 AGZ93683
REF NP_001191100 NP_001265445 NP_001265447 NP_001267305 NP_002384
SP O15151

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