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Biological Magnetic Resonance Data Bank


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BMRB Entry 11252

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11252
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Title: Resonance assignments of HRDC domain from Bloom syndrome protein

Deposition date: 2010-08-05 Original release date: 2010-09-28

Authors: Sato, Akiko; Mishima, Masaki; Nagai, Aki; Kim, Sun-Yong; Ito, Yutaka; Hakoshima, Toshio; Jee, Jun-Goo; Kitano, Ken

Citation: Sato, Akiko; Mishima, Masaki; Nagai, Aki; Kim, Sun-Yong; Ito, Yutaka; Hakoshima, Toshio; Jee, Jun-Goo; Kitano, Ken. "Resonance assignments of HRDC domain from Bloom syndrome protein"  J. Biochem. ., .-..

Assembly members:
BLM HRDC domain, polymer, 101 residues, 11282.033 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 HRDC domain: GIPEFKQKALVAKVSQREEM VKKCLGELTEVCKSLGKVFG VHYFNIFNTVTLKKLAESLS SDPEVLLQIDGVTEDKLEKY GAEVISVLQKYSEWTSPAED S

Data sets:
Data typeCount
13C chemical shifts295
15N chemical shifts88
1H chemical shifts590

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 101 residues - 11282.033 Da.

Residues 1-5 represent a non-native expression tag

1   GLYILEPROGLUPHELYSGLNLYSALALEU
2   VALALALYSVALSERGLNARGGLUGLUMET
3   VALLYSLYSCYSLEUGLYGLULEUTHRGLU
4   VALCYSLYSSERLEUGLYLYSVALPHEGLY
5   VALHISTYRPHEASNILEPHEASNTHRVAL
6   THRLEULYSLYSLEUALAGLUSERLEUSER
7   SERASPPROGLUVALLEULEUGLNILEASP
8   GLYVALTHRGLUASPLYSLEUGLULYSTYR
9   GLYALAGLUVALILESERVALLEUGLNLYS
10   TYRSERGLUTRPTHRSERPROALAGLUASP
11   SER

Samples:

sample_1: BLM HRDC domain, [U-98% 13C; U-98% 15N], 0.5 mM; TRIS 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: BLM HRDC domain, [U-100% 15N], 1 mM; d11-TRIS 50 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_3: BLM HRDC domain, [U-98% 13C; U-98% 15N], 1 mM; d11-TRIS 50 mM; sodium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
4D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D HN(CO)HBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

NMRPipe v5.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16766
PDB
DBJ BAG36927 BAH12008 BAH13907
GB AAA87850 AAH93622 AAI01568 AAI15031 AAI15033
REF NP_000048 NP_001274175 NP_001274177 XP_001097543 XP_002749167
SP P54132

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