BMRB Entry 4376

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4376

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Title:
Chemical shift assignments, 3JHNHA coupling constants, secondary structure and 15N{1H} Heteronuclear NOE values of the N-domain of VAT (VCP like ATPase of Thermoplasma). A group II AAA ATPase.
Deposition date:
1999-08-13
Original release date:
1999-10-13
Authors:
Coles, Murray; Diercks, Tammo; Liermann, Jens; Groeger, Adriane; Rockel, Beate; Baumeister, Wolfgang; Koretke, Kirstin; Lupas, Andrei; Peters, Juergen; Kessler, Horst
Citation:

Citation: Coles, Murray; Diercks, Tammo; Liermann, Jens; Groeger, Adriane; Rockel, Beate; Baumeister, Wolfgang; Koretke, Kirstin; Lupas, Andrei; Peters, Juergen; Kessler, Horst. "The Solution Strucutre of VAT-N Reveals a Missing Link in the Evolution of Complex Enzymes from a Simple bbab Element."  Current Biology 9, 1158-1168 (1999).

Assembly members:

Assembly members:
VCP-like ATPase of Thermoplasma N-domain, polymer, 185 residues, 21702 Da.

Natural source:

Natural source:   Common Name: Thermoplasma acidophilum   Taxonomy ID: 2302   Superkingdom: Archaea   Kingdom: Euryarchaeota   Genus/species: Thermoplasma acididophilum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: BL21[DE3] Escherichia   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VCP-like ATPase of Thermoplasma N-domain: MESNNGIILRVAEANSTDPG MSRVRLDESSRRLLDAEIGD VVEIEKVRKTVGRVYRARPE DENKGIVRIDSVMRNNCGAS IGDKVKVRKVRTEIAKKVTL APIIRKDQRLKFGEGIEEYV QRALIRRPMLEQDNISVPGL TLAGQTGLLFKVVKTLPSKV PVEIGEETKIEIREEPASEV LEEGG

Data sets:
Data typeCount
13C chemical shifts785
15N chemical shifts183
1H chemical shifts1319
coupling constants150
heteronuclear NOE values183

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1VATN1

Entities:

Entity 1, VATN 185 residues - 21702 Da.

1   METGLUSERASNASNGLYILEILELEUARG
2   VALALAGLUALAASNSERTHRASPPROGLY
3   METSERARGVALARGLEUASPGLUSERSER
4   ARGARGLEULEUASPALAGLUILEGLYASP
5   VALVALGLUILEGLULYSVALARGLYSTHR
6   VALGLYARGVALTYRARGALAARGPROGLU
7   ASPGLUASNLYSGLYILEVALARGILEASP
8   SERVALMETARGASNASNCYSGLYALASER
9   ILEGLYASPLYSVALLYSVALARGLYSVAL
10   ARGTHRGLUILEALALYSLYSVALTHRLEU
11   ALAPROILEILEARGLYSASPGLNARGLEU
12   LYSPHEGLYGLUGLYILEGLUGLUTYRVAL
13   GLNARGALALEUILEARGARGPROMETLEU
14   GLUGLNASPASNILESERVALPROGLYLEU
15   THRLEUALAGLYGLNTHRGLYLEULEUPHE
16   LYSVALVALLYSTHRLEUPROSERLYSVAL
17   PROVALGLUILEGLYGLUGLUTHRLYSILE
18   GLUILEARGGLUGLUPROALASERGLUVAL
19   LEUGLUGLUGLYGLY

Samples:

VATN_sample_N15: VCP-like ATPase of Thermoplasma N-domain, [U-15N], 1.40 mM; phosphate buffer 40 mM; sodium chloride 80 mM; sodium azide 10 mM; D2O 10.0%; H2O 90.0%

VATN_sample_dl: VCP-like ATPase of Thermoplasma N-domain, [U-15N; U-13C], 1.20 mM; phosphate buffer 100 mM; sodium chloride 200 mM; sodium azide 10 mM; D2O 10.0%; H2O 90.0%

sample_conditions_all: pH: 5.9; temperature: 320 K

Experiments:

NameSampleSample stateSample conditions
not availablenot availablenot availablesample_conditions_all

Software:

No software information available

NMR spectrometers:

  • Bruker DMX 750 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
EMBL CAC11969
GB AAC45089
REF WP_010901251
SP O05209
AlphaFold O05209

Download HSQC peak lists in one of the following formats:
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