BMRB Entry 50124

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50124
MolProbity Validation Chart

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Title:
Complete sequential assignment of the protein K1-CanA from Pyrodictium abyssi
Deposition date:
2019-12-12
Original release date:
2020-12-14
Authors:
Munte, Claudia; Kalbitzer, Hans Robert; Kreitner, Raphael; Singer, Katrin; Stetter, Karl; Horn, Gudrun; Kremer, Werner
Citation:

Citation: Kreitner, Raphael; Munte, Claudia; Singer, Katrin; Stetter, Karl; Horn, Gudrun; Kremer, Werner; Kalbitzer, Hans Robert. "Complete sequential assignment and secondary structure prediction of the cannulae forming protein CanA from the hyperthermophilic archebacterium Pyrodictium abyssi"  Biomol. NMR Assign. 14, 141-146 (2020).
PubMed: 32052266

Assembly members:

Assembly members:
entity_1, polymer, 172 residues, 18706.21 Da.

Natural source:

Natural source:   Common Name: Pyrodictium abyssi   Taxonomy ID: 54256   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrodictium abyssi

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET17b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ATGTAQAVSEPIDVESHLGS ITPAAGAQGSDDIGYAIVWI KDQVNDVKLKVTLANAEQLK PYFKYLQIQITSGYETNSTA LGNFSETKAVISLDNPSAVI VLDKEDIAVLYPDKTGYTNT SIWVPGEPDKIIVYNETKPV AILNFKAFYEAKEGMLFDSL PVIFNFQVLQVG

Data sets:
Data typeCount
13C chemical shifts756
15N chemical shifts187
1H chemical shifts1227

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1K1-CanA monomer1

Entities:

Entity 1, K1-CanA monomer 172 residues - 18706.21 Da.

Residues 1-10 from CanA have been removed

1   ALATHRGLYTHRALAGLNALAVALSERGLU
2   PROILEASPVALGLUSERHISLEUGLYSER
3   ILETHRPROALAALAGLYALAGLNGLYSER
4   ASPASPILEGLYTYRALAILEVALTRPILE
5   LYSASPGLNVALASNASPVALLYSLEULYS
6   VALTHRLEUALAASNALAGLUGLNLEULYS
7   PROTYRPHELYSTYRLEUGLNILEGLNILE
8   THRSERGLYTYRGLUTHRASNSERTHRALA
9   LEUGLYASNPHESERGLUTHRLYSALAVAL
10   ILESERLEUASPASNPROSERALAVALILE
11   VALLEUASPLYSGLUASPILEALAVALLEU
12   TYRPROASPLYSTHRGLYTYRTHRASNTHR
13   SERILETRPVALPROGLYGLUPROASPLYS
14   ILEILEVALTYRASNGLUTHRLYSPROVAL
15   ALAILELEUASNPHELYSALAPHETYRGLU
16   ALALYSGLUGLYMETLEUPHEASPSERLEU
17   PROVALILEPHEASNPHEGLNVALLEUGLN
18   VALGLY

Samples:

sample_1: K1-CanA 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM

sample_2: K1-CanA 1.8 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM

sample_3: K1-CanA 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM

sample_4: K1-CanA, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM

sample_5: K1-CanA, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM

sample_6: K1-CanA, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 0.1 mM; sodium azide 0.4 mM; DSS 0.4 mM

sample_conditions_1: pH: 6.6; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_5isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D CBCANHsample_3isotropicsample_conditions_1
3D HCANsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_6isotropicsample_conditions_1
3D 1H-15N NOESYsample_6isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D (HB)CB(CGCC-TOCSY)Harsample_3isotropicsample_conditions_1
3D (HB)CB(CGCD)HDsample_3isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

TOPSPIN, Bruker Biospin - processing

AUREMOL, Bruker Biospin - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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