BMRB Entry 16900

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16900

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Title:
MDM4 binds ligands via an induced fit mechanism in which disordered regions become structured
Deposition date:
2010-04-23
Original release date:
2010-06-16
Authors:
Sanchez, Maria; Renshaw, Jonathan; Davies, Gareth; Barlow, Paul; Vogtherr, Martin
Citation:

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).
PubMed: 20515689

Assembly members:

Assembly members:
MDM4_N-terminal_domain, polymer, 102 residues, Formula weight is not available
p53_peptide, polymer, 11 residues, Formula weight is not available

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: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MDM4_N-terminal_domain: GSHMDSASRISPGQINQVRP KLPLLKILHAAGAQGEMFTV KEVMHYLGQYIMVKQLYDQQ EQHMVYCGGDLLGELLGRQS FSVKDPSPLYDMLRKNLVTL AT
p53_peptide: ETFSDLWKLLP

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts93
1H chemical shifts93

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MDM41
2p53 peptide2

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

Entity 2, p53 peptide 11 residues - Formula weight is not available

1   GLUTHRPHESERASPLEUTRPLYSLEULEU
2   PRO

Samples:

sample_1: MDM4 N-terminal domain, [U-100% 13C; U-100% 15N], 0.1 mM; p53 peptide 0.2 ± 0.1 mM; potassium chloride 100 mM; sodium azide 0.1%; BisTris 50 mM; TCEP 2 mM; EDTA 0.1 mM; H20 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
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CC(CO)NH TOCSYsample_1isotropicsample_conditions_1
3D H(CC)(CO)NH TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.5.5, Keller and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16893 16894
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
AlphaFold O15151

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