BMRB Entry 25347

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25347
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution structure of 53BP1 tandem Tudor domains in complex with a p53K370me2 peptide
Deposition date:
2014-11-15
Original release date:
2014-12-08
Authors:
Cui, Gaofeng; Botuyan, Maria Victoria; Mer, Georges
Citation:

Citation: Tong, Qiong; Cui, Gaofeng; Botuyan, Maria Victoria; Rothbart, Scott; Hayashi, Ryo; Musselman, Catherine; Singh, Namit; Appela, Ettore; Strahl, Brian; Mer, Georges; Kutateladze, Tatiana. "Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1."  Structure 23, 312-321 (2015).
PubMed: 25579814

Assembly members:

Assembly members:
entity_1, polymer, 123 residues, 13944.895 Da.
entity_2, polymer, 15 residues, 1540.761 Da.

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: pTEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMNSFVGLRVVAKWSSNGY FYSGKITRDVGAGKYKLLFD DGYECDVLGKDILLCDPIPL DTEVTALSEDEYFSAGVVKG HRKESGELYYSIEKEGQRKW YKRMAVILSLEQGNRLREQY GLG
entity_2: RAHSSHLXSKKGQST

Data sets:
Data typeCount
13C chemical shifts585
15N chemical shifts116
1H chemical shifts940

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 123 residues - 13944.895 Da.

1   GLYHISMETASNSERPHEVALGLYLEUARG
2   VALVALALALYSTRPSERSERASNGLYTYR
3   PHETYRSERGLYLYSILETHRARGASPVAL
4   GLYALAGLYLYSTYRLYSLEULEUPHEASP
5   ASPGLYTYRGLUCYSASPVALLEUGLYLYS
6   ASPILELEULEUCYSASPPROILEPROLEU
7   ASPTHRGLUVALTHRALALEUSERGLUASP
8   GLUTYRPHESERALAGLYVALVALLYSGLY
9   HISARGLYSGLUSERGLYGLULEUTYRTYR
10   SERILEGLULYSGLUGLYGLNARGLYSTRP
11   TYRLYSARGMETALAVALILELEUSERLEU
12   GLUGLNGLYASNARGLEUARGGLUGLNTYR
13   GLYLEUGLY

Entity 2, entity_2 15 residues - 1540.761 Da.

1   ARGALAHISSERSERHISLEUMLYSERLYS
2   LYSGLYGLNSERTHR

Samples:

sample_1: sodium phosphate 25 mM; sodium azide 1.5 mM; 53BP1-Tudor, [U-100% 13C; U-100% 15N], 2.0 mM; p53K370me2 6.0 mM; D2O 10%; H2O 90%

sample_2: sodium phosphate 25 mM; sodium azide 1.5 mM; 53BP1-Tudor, [U-100% 13C; U-100% 15N], 2.0 mM; p53K370me2 6.0 mM; D2O 100%

sample_3: sodium phosphate 25 mM; sodium azide 1.5 mM; 53BP1-Tudor 5.0 mM; p53Kc370me2, [U-100% 13C; U-100% 15N], 2.0 mM; D2O 10%; H2O 90%

sample_4: sodium phosphate 25 mM; sodium azide 1.5 mM; 53BP1-Tudor 5.0 mM; p53Kc370me2, [U-100% 13C; U-100% 15N], 2.0 mM; D2O 100%

sample_5: sodium phosphate 25 mM; sodium azide 1.5 mM; 53BP1-Tudor, [U-100% 15N], 2.0 mM; p53K370me2 6.0 mM; D2O 10%; H2O 90%

sample_6: sodium phosphate 35 mM; sodium azide 1.5 mM; p53K370me2 2.0 mM; D2O 100%

sample_7: sodium phosphate 25 mM; sodium azide 1.5 mM; p53Kc370me2, [U-100% 13C; U-100% 15N], 2.0 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 25 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
3D 1H-15N TOCSYsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_5isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D Filtered (15N/13C)-Edited (13C)sample_2isotropicsample_conditions_1
3D Filtered (15N/13C)-Edited (13C)sample_4isotropicsample_conditions_1
3D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_6isotropicsample_conditions_1
2D 1H-13C HSQCsample_7isotropicsample_conditions_1
2D 1H-15N HSQCsample_7isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - processing

SANE, Duggan, Legge, Dyson & Wright - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance III 700 MHz

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