BMRB Entry 18994

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18994

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 13C and 15N chemical shift assignments for the N-terminal domain of the KCNH channel from Zebrafish
Deposition date:
2013-01-31
Original release date:
2014-02-03
Authors:
Kim, Young Mee; 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:
zNTD, polymer, 147 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: pET29 b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
zNTD: MPVMRGLLAPQNTFLDTIAT RFDGTHSNFVLGNAQVQSLY PIVYCSDGFCELTGYARAEL MQKSCACHFLYGPETSDRLM AQIQGALDERREFKTELVFY KKGGTQFWCLLDIVPIKNEK GEVVLFLVSHKDITDNKKDL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts538
15N chemical shifts138
1H chemical shifts926

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zNTD1

Entities:

Entity 1, zNTD 147 residues - Formula weight is not available

Residues 140-147 represent a non-native affinity tag

1   METPROVALMETARGGLYLEULEUALAPRO
2   GLNASNTHRPHELEUASPTHRILEALATHR
3   ARGPHEASPGLYTHRHISSERASNPHEVAL
4   LEUGLYASNALAGLNVALGLNSERLEUTYR
5   PROILEVALTYRCYSSERASPGLYPHECYS
6   GLULEUTHRGLYTYRALAARGALAGLULEU
7   METGLNLYSSERCYSALACYSHISPHELEU
8   TYRGLYPROGLUTHRSERASPARGLEUMET
9   ALAGLNILEGLNGLYALALEUASPGLUARG
10   ARGGLUPHELYSTHRGLULEUVALPHETYR
11   LYSLYSGLYGLYTHRGLNPHETRPCYSLEU
12   LEUASPILEVALPROILELYSASNGLULYS
13   GLYGLUVALVALLEUPHELEUVALSERHIS
14   LYSASPILETHRASPASNLYSLYSASPLEU
15   GLUHISHISHISHISHISHIS

Samples:

sample_1: zNTD, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: zNTD, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; 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 HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

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

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

REF XP_001919436 XP_007260506 XP_008326080

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