BMRB Entry 17687

Title:
PARP BRCT Domain
Deposition date:
2011-06-03
Original release date:
2011-10-12
Authors:
Mueller, Geoffrey; Loeffler, Paul; Cuneo, Matthew; DeRose, Eugene; London, Robert
Citation:

Citation: Loeffler, Paul; Cuneo, Matthew; Mueller, Geoffrey; Derose, Eugene; Gabel, Scott; London, Robert. "Structural studies of the PARP-1 BRCT domain."  BMC Struct. Biol. 11, 37-37 (2011).
PubMed: 21967661

Assembly members:

Assembly members:
entity, polymer, 212 residues, 23327.365 Da.

Natural source:

Natural source:   Common Name: norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet21A

Data sets:
Data typeCount
13C chemical shifts328
15N chemical shifts98
1H chemical shifts987

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PARP-1 BRCT domain1

Entities:

Entity 1, PARP-1 BRCT domain 212 residues - 23327.365 Da.

1   METLYSPROLEUSERASNMETLYSILELEU
2   THRLEUGLYLYSLEUSERGLNASNLYSASP
3   GLUALALYSALAMETILEGLULYSLEUGLY
4   GLYLYSLEUTHRGLYSERALAASNLYSALA
5   SERLEUCYSILESERTHRLYSLYSGLUVAL
6   GLULYSMETSERLYSLYSMETGLUGLUVAL
7   LYSALAALAASNVALARGVALVALCYSGLU
8   ASPPHELEUGLNASPVALSERALASERALA
9   LYSSERLEUGLNGLULEULEUSERALAHIS
10   SERLEUSERSERTRPGLYALAGLUVALLYS
11   HISHISHISHISHISHISMETLYSPROLEU
12   SERASNMETLYSILELEUTHRLEUGLYLYS
13   LEUSERGLNASNLYSASPGLUALALYSALA
14   METILEGLULYSLEUGLYGLYLYSLEUTHR
15   GLYSERALAASNLYSALASERLEUCYSILE
16   SERTHRLYSLYSGLUVALGLULYSMETSER
17   LYSLYSMETGLUGLUVALLYSALAALAASN
18   VALARGVALVALCYSGLUASPPHELEUGLN
19   ASPVALSERALASERALALYSSERLEUGLN
20   GLULEULEUSERALAHISSERLEUSERSER
21   TRPGLYALAGLUVALLYSHISHISHISHIS
22   HISHIS

Samples:

sample_1: PARP-1_BRCT_domain, [U-100% 13C; U-100% 15N], 3 mM; sodium phosphate 40 mM; sodium chloride 140 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.18 M; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
(HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
(HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

NMRView, Johnson, One Moon Scientific - chemical shift assignment

VNMRJ, Varian - collection

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB

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