BMRB Entry 19621

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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/BMR19621
MolProbity Validation Chart

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Title:
1H, 13C and 15N chemical shift assignments for the cyclic-nucleotide binding homology domain of the KCNH channel from Zebrafish
Deposition date:
2013-11-19
Original release date:
2014-02-11
Authors:
Li, Qingxin; Ng, Hui Qi; Kang, Congbao
Citation:

Citation: Li, Qingxin; Ng, Hui Qi; Kang, Congbao. "(1)H, (13)C and (15)N chemical shift assignments for the cyclic-nucleotide binding homology domain of a KCNH channel."  Biomol. NMR Assignments ., .-. (2014).
PubMed: 24414223

Assembly members:

Assembly members:
CNBHD, polymer, 143 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: zebrafish   Taxonomy ID: 7955   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Danio rerio

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CNBHD: MNKELLQLPLFESASRGCLR SLSLIIKTSFCAPGEFLIRQ GDALQAIYFVCSGSMEVLKD NTVLAILGKGDLIGSDSLTK EQVIKTNANVKALTYCDLQY ISLKGLREVLRLYPEYAQKF VSEIQHDLTYNLREGLEHHH HHH

Data sets:
Data typeCount
13C chemical shifts554
15N chemical shifts137
1H chemical shifts833

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CNBHD1

Entities:

Entity 1, CNBHD 143 residues - Formula weight is not available

1   METASNLYSGLULEULEUGLNLEUPROLEU
2   PHEGLUSERALASERARGGLYCYSLEUARG
3   SERLEUSERLEUILEILELYSTHRSERPHE
4   CYSALAPROGLYGLUPHELEUILEARGGLN
5   GLYASPALALEUGLNALAILETYRPHEVAL
6   CYSSERGLYSERMETGLUVALLEULYSASP
7   ASNTHRVALLEUALAILELEUGLYLYSGLY
8   ASPLEUILEGLYSERASPSERLEUTHRLYS
9   GLUGLNVALILELYSTHRASNALAASNVAL
10   LYSALALEUTHRTYRCYSASPLEUGLNTYR
11   ILESERLEULYSGLYLEUARGGLUVALLEU
12   ARGLEUTYRPROGLUTYRALAGLNLYSPHE
13   VALSERGLUILEGLNHISASPLEUTHRTYR
14   ASNLEUARGGLUGLYLEUGLUHISHISHIS
15   HISHISHIS

Samples:

sample_1: CNBHD, [U-100% 15N], 0.2 – 0.8 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_2: CNBHD, [U-100% 13C; U-100% 15N], 0.3 – 0.8 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_3-D2O: CNBHD, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; 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 CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3-D2Oisotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3-D2Oisotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3DCCONHsample_2isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
REF XP_001919436 XP_005475215 XP_005933423 XP_006636461 XP_006805904

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