BMRB Entry 5878

Title:
1H, 13C and 15N NMR assignment of the region 1463-1617 of mouse p53 Binding Protein 1 (53BP1)
Deposition date:
2003-07-22
Original release date:
2004-02-11
Authors:
Charier, Gaelle; Alpha-Bazin, Beatrice; Couprie, Joel; Callebaut, Isabelle; Berenguer, Frederic; Quemeneur, Eric; Gilquin, Bernard; Zinn-Justin, Sophie
Citation:

Citation: Charier, Gaelle; Alpha-Bazin, Beatrice; Couprie, Joel; Callebaut, Isabelle; Berenguer, Frederic; Quemeneur, Eric; Gilquin, Bernard; Zinn-Justin, Sophie. "Letter to the Editor: 1H, 13C and 15N resonance assignments of the region 1463-1617 of the mouse p53 Binding Protein 1 (53BP1) "  J. Biomol. NMR 28, 303-304 (2004).
PubMed: 14752266

Assembly members:

Assembly members:
p53 Binding Protein 1, polymer, 155 residues, 17345 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDEST15

Data sets:
Data typeCount
1H chemical shifts1023
13C chemical shifts676
15N chemical shifts162

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
153BP1 subunit 11

Entities:

Entity 1, 53BP1 subunit 1 155 residues - 17345 Da.

1   ASPSERSERSERSERGLYASNSERPHEVAL
2   GLYLEUARGVALVALALALYSTRPSERSER
3   ASNGLYTYRPHETYRSERGLYLYSILETHR
4   ARGASPVALGLYALAGLYLYSTYRLYSLEU
5   LEUPHEASPASPGLYTYRGLUCYSASPVAL
6   LEUGLYLYSASPILELEULEUCYSASPPRO
7   ILEPROLEUASPTHRGLUVALTHRALALEU
8   SERGLUASPGLUTYRPHESERALAGLYVAL
9   VALLYSGLYHISARGLYSGLUSERGLYGLU
10   LEUTYRTYRSERILEGLULYSGLUGLYGLN
11   ARGLYSTRPTYRLYSARGMETALAVALILE
12   LEUSERLEUGLUGLNGLYASNARGLEUARG
13   GLUGLNTYRGLYLEUGLYPROTYRGLUALA
14   VALTHRPROLEUTHRLYSALAALAASPILE
15   SERLEUASPASNLEUVALGLUGLYLYSARG
16   LYSARGARGSERASN

Samples:

sample_1: p53 Binding Protein 1, [U-95% 13C; U-95% 15N], 0.8 mM; Tris-HCl 50 mM; NaCl 150 mM; D2O 100%

sample_2: p53 Binding Protein 1, [U-95% 13C; U-95% 15N], 0.8 mM; Tris-HCl 50 mM; NaCl 150 mM; H2O 90%; D2O 10%

sample_3: p53 Binding Protein 1, [U-95% 15N], 0.7 mM; Tris-HCl 50 mM; NaCl 150 mM; H2O 90%; D2O 10%

condition_1: pH: 7.1; temperature: 300 K; ionic strength: 0.2 M

condition_2: pH*: 7.0; temperature: 300 K; ionic strength: 0.2 M

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availablenot available
HNCOnot availablenot availablenot available
HNCAnot availablenot availablenot available
HN(CO)CAnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
CBCANHnot availablenot availablenot available
CBCACOHAnot availablenot availablenot available
HNHAnot availablenot availablenot available
(HCA)CO(CA)NHnot availablenot availablenot available
15N HSQC NOESYnot availablenot availablenot available
HBHA(CO)NHnot availablenot availablenot available
HCCH TOSCYnot availablenot availablenot available
HCCH COSYnot availablenot availablenot available
13C HSQC NOESYnot availablenot availablenot available

Software:

NMRPipe v2.0 - data processing

FELIX v2000 - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

BMRB 18579 25347 25348
PDB
DBJ BAC26637 BAC29383 BAE06107 BAE21103 BAG10235
EMBL CAC94013 CAD97660
GB AAA21596 AAC62018 AAH35206 AAH79906 AAI12162
REF NP_001135451 NP_001135452 NP_001162434 NP_001193326 NP_001277759
SP P70399 Q12888
AlphaFold P70399 Q12888

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