BMRB Entry 16766

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16766

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 the human BLM HRDC domain
Deposition date:
2010-03-04
Original release date:
2010-09-08
Authors:
Kim, Young Mee; Choi, Byong-Seok
Citation:

Citation: Kim, Young Mee; Choi, Byong-Seok. "Structure and function of the regulatory HRDC domain from human Bloom syndrome protein."  Nucleic Acids Res. 38, 7764-7777 (2010).
PubMed: 20639533

Assembly members:

Assembly members:
BLM HRDC domain, polymer, 85 residues, 9595.003 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BLM HRDC domain: QREEMVKKCLGELTEVCKSL GKVFGVHYFNIFNTVTLKKL AESLSSDPEVLLQIDGVTED KLEKYGAEVISVLQKYSEWT SPAED

Data sets:
Data typeCount
13C chemical shifts373
15N chemical shifts88
1H chemical shifts624

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BLM HRDC domain1

Entities:

Entity 1, BLM HRDC domain 85 residues - 9595.003 Da.

1   GLNARGGLUGLUMETVALLYSLYSCYSLEU
2   GLYGLULEUTHRGLUVALCYSLYSSERLEU
3   GLYLYSVALPHEGLYVALHISTYRPHEASN
4   ILEPHEASNTHRVALTHRLEULYSLYSLEU
5   ALAGLUSERLEUSERSERASPPROGLUVAL
6   LEULEUGLNILEASPGLYVALTHRGLUASP
7   LYSLEUGLULYSTYRGLYALAGLUVALILE
8   SERVALLEUGLNLYSTYRSERGLUTRPTHR
9   SERPROALAGLUASP

Samples:

sample_1: BLM HRDC domain, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; DTT 1 mM; HEPES 20 mM; sodium chloride 100 mM; sodium azide 0.02%

sample_2: BLM HRDC domain, [U-99% 13C; U-99% 15N], 1 mM; D2O 100%; DTT 1 mM; HEPES 20 mM; sodium chloride 100 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCCO)NHsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 11252
PDB
DBJ BAG36927 BAH12008 BAH13907
GB AAA87850 AAH93622 AAI01568 AAI15031 AAI15033
REF NP_000048 NP_001274175 NP_001274176 NP_001274177 XP_001097543
SP P54132
AlphaFold P54132

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