BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27131

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for 98-243   PubMed: 28860187

Authors: Sugitani, Norie; Voehler, Markus; Roh, Michelle; Topolska-Wo, Agnieszka; Chazin, Walter

Citation: Sugitani, Norie; Voehler, Markus; Roh, Michelle; Topolska-Wo, Agnieszka; Chazin, Walter. "Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates"  J. Biol. Chem. ., .-. (2017).

Assembly members:
XPA98-239, polymer, 146 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
XPA98-239: GPGSMEFDYVICEECGKEFM DSYLMNHFDLPTCDNCRDAD DKHKLITKTEAKQEYLLKDC DLEKREPPLKFIVKKNPHHS QWGDMKLYLKLQIVKRSLEV WGSQEALEEAKEVRQENREK MKQKKFDKKVKELRRAVRSS VWKRET

Data sets:
Data typeCount
13C chemical shifts415
15N chemical shifts137
1H chemical shifts137

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1XPA98-2391

Entities:

Entity 1, XPA98-239 146 residues - Formula weight is not available

1   GLYPROGLYSERMETGLUPHEASPTYRVAL
2   ILECYSGLUGLUCYSGLYLYSGLUPHEMET
3   ASPSERTYRLEUMETASNHISPHEASPLEU
4   PROTHRCYSASPASNCYSARGASPALAASP
5   ASPLYSHISLYSLEUILETHRLYSTHRGLU
6   ALALYSGLNGLUTYRLEULEULYSASPCYS
7   ASPLEUGLULYSARGGLUPROPROLEULYS
8   PHEILEVALLYSLYSASNPROHISHISSER
9   GLNTRPGLYASPMETLYSLEUTYRLEULYS
10   LEUGLNILEVALLYSARGSERLEUGLUVAL
11   TRPGLYSERGLNGLUALALEUGLUGLUALA
12   LYSGLUVALARGGLNGLUASNARGGLULYS
13   METLYSGLNLYSLYSPHEASPLYSLYSVAL
14   LYSGLULEUARGARGALAVALARGSERSER
15   VALTRPLYSARGGLUTHR

Samples:

sample_1: XPA, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 500 mM; TCEP 1 mM; DSS .5 mM

sample_conditions_1: ionic strength: 500 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

PINE v2.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMRView v9.2.0-b2, Johnson, One Moon Scientific - data analysis

TALOS v3.80F1 Rev 2012.080.14.41, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - data analysis

TOPSPIN v3.5, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links: