BMRB Entry 6612

Title:
NMR structure of unliagnded MDM2
Deposition date:
2005-04-28
Original release date:
2005-10-27
Authors:
Uhrinova, S.; Uhrin, D.; Powers, H.; Watt, K.; Zheleva, D.; Fischer, P.; McInnes, C.; Barlow, P.
Citation:

Citation: Uhrinova, S.; Uhrin, D.; Powers, H.; Watt, K.; Zheleva, D.; Fischer, P.; McInnes, C.; Barlow, P.. "Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding."  J. Mol. Biol. 350, 587-598 (2005).
PubMed: 15953616

Assembly members:

Assembly members:
Ubiquitin-protein ligase E3 Mdm2 (E.C.6.3.2.-), polymer, 119 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

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts719
13C chemical shifts320
15N chemical shifts103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ubiquitin-protein ligase E3 Mdm21

Entities:

Entity 1, Ubiquitin-protein ligase E3 Mdm2 119 residues - Formula weight is not available

1   METCYSASNTHRASNMETSERVALPROTHR
2   ASPGLYALAVALTHRTHRSERGLNILEPRO
3   ALASERGLUGLNGLUTHRLEUVALARGPRO
4   LYSPROLEULEULEULYSLEULEULYSSER
5   VALGLYALAGLNLYSASPTHRTYRTHRMET
6   LYSGLUVALLEUPHETYRLEUGLYGLNTYR
7   ILEMETTHRLYSARGLEUTYRASPGLULYS
8   GLNGLNHISILEVALTYRCYSSERASNASP
9   LEULEUGLYASPLEUPHEGLYVALPROSER
10   PHESERVALLYSGLUHISARGLYSILETYR
11   THRMETILETYRARGASNLEUVALVALVAL
12   ASNGLNGLNGLUSERSERASPSERSER

Samples:

sample_1: Ubiquitin-protein ligase E3 Mdm2 (E.C.6.3.2.-), [U-13C; U-15N], 0.5 mM; sodium acetate, [U-2H], 60 mM; phosphate buffer 60 mM; H2O 90%; D2O 10%

sample_2: Ubiquitin-protein ligase E3 Mdm2 (E.C.6.3.2.-), [U-13C; U-15N], 0.5 mM; sodium acetate, [U-2H], 60 mM; phosphate buffer 60 mM; D2O 99.5%

sample_cond_1: pH: 7.3; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions

Software:

AZARA - processing

ANSIG - data analysis

CNS - structure solution, refinement

NMR spectrometers:

  • Bruker AMX 600 MHz

Related Database Links:

BMRB 18755 19230 2410
PDB
DBJ BAF83030 BAJ17752
EMBL CAA78055 CAD23251 CAD36959 CAD79457 CAH89564
GB AAA60568 AAI48523 AAI52385 AAI52391 AAI53118
PRF 1814460A
REF NP_001124685 NP_001138809 NP_001138811 NP_001253331 NP_002383
SP Q00987
AlphaFold Q00987

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