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 27184

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27184

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Title: Backbone 1H, 13C and 15N resonance assignments of the OB domain of the single stranded DNA-binding protein hSSB2 (NABP1/OBFC1B) and chemical shift mapping of the DNA-binding interface   PubMed: 29063999

Deposition date: 2017-07-19 Original release date: 2017-10-27

Authors: Kariawasam, Ruvini; Knight, Maddison; Gamsjaeger, Roland; Cubeddu, Liza

Citation: Kariawasam, Ruvini; Knight, Maddison; Gamsjaeger, Roland; Cubeddu, Liza. "Backbone 1H, 13C and 15N resonance assignments of the OB domain of the single stranded DNA-binding protein hSSB2 (NABP1/OBFC1B) and chemical shift mapping of the DNA-binding interface"  Biomol. NMR Assignments 12, 107-111 (2018).

Assembly members:
hSSB2, polymer, 130 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   Vector: pGex6-P

Entity Sequences (FASTA):
hSSB2: GPLGSMNRVNDPLIFIRDIK PGLKNLNVVFIVLEIGRVTK TKDGHEVRSCKVADKTGSIT ISVWDEIGGLIQPGDIIRLT RGYASMWKGCLTLYTGRGGE LQKIGEFCMVYSEVPNFSEP NPDYRGQQNK

Data sets:
Data typeCount
13C chemical shifts361
15N chemical shifts118
1H chemical shifts118

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hSSB21

Entities:

Entity 1, hSSB2 130 residues - Formula weight is not available

1   GLYPROLEUGLYSERMETASNARGVALASN
2   ASPPROLEUILEPHEILEARGASPILELYS
3   PROGLYLEULYSASNLEUASNVALVALPHE
4   ILEVALLEUGLUILEGLYARGVALTHRLYS
5   THRLYSASPGLYHISGLUVALARGSERCYS
6   LYSVALALAASPLYSTHRGLYSERILETHR
7   ILESERVALTRPASPGLUILEGLYGLYLEU
8   ILEGLNPROGLYASPILEILEARGLEUTHR
9   ARGGLYTYRALASERMETTRPLYSGLYCYS
10   LEUTHRLEUTYRTHRGLYARGGLYGLYGLU
11   LEUGLNLYSILEGLYGLUPHECYSMETVAL
12   TYRSERGLUVALPROASNPHESERGLUPRO
13   ASNPROASPTYRARGGLYGLNGLNASNLYS

Samples:

sample_1: hSSB2 0.5 mM; MES 10 mM; sodium chloride 50 mM; TCEP 3 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker AMX 800 MHz
  • Bruker AMX 600 MHz

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