BMRB Entry 25805

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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/BMR25805
MolProbity Validation Chart

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Title:
Structure of the cyclic nucleotide-binding homology domain of the hERG channel
Deposition date:
2015-09-10
Original release date:
2016-05-23
Authors:
Li, Yan; Ng, Hui Qi; Li, Qingxin; Kang, CongBao
Citation:

Citation: Li, Yan; Ng, Hui Qi; Li, Qingxin; Kang, CongBao. "Structure of the Cyclic Nucleotide-Binding Homology Domain of the hERG Channel and Its Insight into Type 2 Long QT Syndrom"  Sci. Rep. 6, 23712-23712 (2016).
PubMed: 27025590

Assembly members:

Assembly members:
the_cyclic_nucleotide-binding_homology_domain_of_the_hERG_channel, polymer, 154 residues, 14750.103 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: PNIC28-Bsa4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
the_cyclic_nucleotide-binding_homology_domain_of_the_hERG_channel: MHHHHHHSSGVDLGTENLYF QSMRSLLQHCKPFRGATKGC LRALAMKFKTTHAPPGDTLV HAGDLLTALYFISRGSIEIL RGDVVVAILGKNDIFGEPLN LYARPGKSNGDVRALTYCDL HKIHRDDLLEVLDMYPEFSD HFWSSLEITFNLRD

Data sets:
Data typeCount
13C chemical shifts508
15N chemical shifts125
1H chemical shifts845

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1cyclic nucleotide-binding homology domain of hERG channel1

Entities:

Entity 1, cyclic nucleotide-binding homology domain of hERG channel 154 residues - 14750.103 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   VALASPLEUGLYTHRGLUASNLEUTYRPHE
3   GLNSERMETARGSERLEULEUGLNHISCYS
4   LYSPROPHEARGGLYALATHRLYSGLYCYS
5   LEUARGALALEUALAMETLYSPHELYSTHR
6   THRHISALAPROPROGLYASPTHRLEUVAL
7   HISALAGLYASPLEULEUTHRALALEUTYR
8   PHEILESERARGGLYSERILEGLUILELEU
9   ARGGLYASPVALVALVALALAILELEUGLY
10   LYSASNASPILEPHEGLYGLUPROLEUASN
11   LEUTYRALAARGPROGLYLYSSERASNGLY
12   ASPVALARGALALEUTHRTYRCYSASPLEU
13   HISLYSILEHISARGASPASPLEULEUGLU
14   VALLEUASPMETTYRPROGLUPHESERASP
15   HISPHETRPSERSERLEUGLUILETHRPHE
16   ASNLEUARGASP

Samples:

sample_1: the cyclic nucleotide-binding homology domain of the hERG channel, [U-100% 13C; U-100% 15N], 0.4 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 170 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, processing, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

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