BMRB Entry 17212

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17212

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Title:
1H, 13C and 15N resonance assignment of Rap1 BRCT domain from Saccharomyces cerevisiae
Deposition date:
2010-09-28
Original release date:
2011-03-30
Authors:
Zhang, Wen; Zhang, Jiahai; Tu, Xiaoming
Citation:

Citation: Zhang, Wen; Zhang, Jiahai; Zhang, Xuecheng; Xu, Chao; Tu, Xiaoming. "Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold."  Biochem. Biophys. Res. Commun. 404, 1055-1059 (2011).
PubMed: 21187076

Assembly members:

Assembly members:
Rap1_BRCT_domain, polymer, 106 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet22

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rap1_BRCT_domain: MEKKEQVSGPPLSNMKFYLN RDADAHDSLNDIDQLARLIR ANGGEVLDSKPRESKENVFI VSPYNHTNLPTVTPTYIKAC CQSNSLLNMENYLVPYDNLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts344
15N chemical shifts89
1H chemical shifts487

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rap1 BRCT domain1

Entities:

Entity 1, Rap1 BRCT domain 106 residues - Formula weight is not available

1   METGLULYSLYSGLUGLNVALSERGLYPRO
2   PROLEUSERASNMETLYSPHETYRLEUASN
3   ARGASPALAASPALAHISASPSERLEUASN
4   ASPILEASPGLNLEUALAARGLEUILEARG
5   ALAASNGLYGLYGLUVALLEUASPSERLYS
6   PROARGGLUSERLYSGLUASNVALPHEILE
7   VALSERPROTYRASNHISTHRASNLEUPRO
8   THRVALTHRPROTHRTYRILELYSALACYS
9   CYSGLNSERASNSERLEULEUASNMETGLU
10   ASNTYRLEUVALPROTYRASPASNLEUGLU
11   HISHISHISHISHISHIS

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 100 mM; Rap1 BRCT domain 0.8 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, collection

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

PDB
DBJ GAA25889
EMBL CAA55491 CAA96118 CAY82390
GB AAA18404 AHY76889 AJP41127 AJT01564 AJT01934
REF NP_014183
SP P11938
TPG DAA10340
AlphaFold P11938

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