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 19530

Title: Resonance assignment of RQC domain of human Bloom syndrome protein   PubMed: 24435566

Deposition date: 2013-09-25 Original release date: 2014-04-16

Authors: Ko, Junsang; Ryu, Kyoung-Seok; Choi, Byong-Seok

Citation: Park, Chin-Ju; Ko, Junsang; Ryu, Kyoung-Seok; Choi, Byong-Seok. "Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein."  J. Biomol. NMR 58, 141-147 (2014).

Assembly members:
BLM_RQC, polymer, 144 residues, 16089.5 Da.

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):
BLM_RQC: CKTKDYKTRDVTDDVKSIVR FVQEHSSSQGMRNIKHVGPS GRFTMNMLVDIFLGSKSAKI QSGIFGKGSAYSRHNAERLF KKLILDKILDEDLYINANDQ AIAYVMLGNKAQTVLNGNLK VDFMETENSSSVKKQKALVA KVSQ

Data sets:
Data typeCount
1H chemical shifts796
13C chemical shifts324
15N chemical shifts120

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BLM RQC1

Entities:

Entity 1, BLM RQC 144 residues - 16089.5 Da.

1   CYSLYSTHRLYSASPTYRLYSTHRARGASP
2   VALTHRASPASPVALLYSSERILEVALARG
3   PHEVALGLNGLUHISSERSERSERGLNGLY
4   METARGASNILELYSHISVALGLYPROSER
5   GLYARGPHETHRMETASNMETLEUVALASP
6   ILEPHELEUGLYSERLYSSERALALYSILE
7   GLNSERGLYILEPHEGLYLYSGLYSERALA
8   TYRSERARGHISASNALAGLUARGLEUPHE
9   LYSLYSLEUILELEUASPLYSILELEUASP
10   GLUASPLEUTYRILEASNALAASNASPGLN
11   ALAILEALATYRVALMETLEUGLYASNLYS
12   ALAGLNTHRVALLEUASNGLYASNLEULYS
13   VALASPPHEMETGLUTHRGLUASNSERSER
14   SERVALLYSLYSGLNLYSALALEUVALALA
15   LYSVALSERGLN

Samples:

sample_1: BLM RQC, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%; DTT 1 mM; Tris 20 mM; Sodium Chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

GB NP_000048 .1 AAA87850 AAH93622 AAI01568 AAI15031 AAI15033
PDB
DBJ BAG36927 BAH12008 BAH13907
REF NP_000048 NP_001274175 NP_001274177 XP_001097543 XP_003268551
SP P54132

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