BMRB Entry 15902

Title:
Solution NMR structure of the OB domain of Ta0387 from Thermoplasma acidophilum. Northeast Structural Genomics Consortium target TaR80b.
Deposition date:
2008-08-01
Original release date:
2008-08-13
Authors:
Ramelot, Theresa; Ding, Keyang; Lee, Dan; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Ramelot, Theresa; Ding, Keyang; Lee, Dan; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the OB domain of Ta0387 from Thermoplasma acidophilum."  .

Assembly members:

Assembly members:
Ta0387, polymer, 106 residues, 11896.298 Da.

Natural source:

Natural source:   Common Name: Thermoplasma acidophilum   Taxonomy ID: 2303   Superkingdom: Archaea   Kingdom: not available   Genus/species: Thermoplasma acidophilum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-23C

Data typeCount
13C chemical shifts467
15N chemical shifts117
1H chemical shifts733

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ta03871

Entities:

Entity 1, Ta0387 106 residues - 11896.298 Da.

residues 105-202 of Ta0387

1   SERASPLEUVALLYSILEARGASPVALSER
2   LEUSERTHRPROTYRVALSERVALILEGLY
3   LYSILETHRGLYILEHISLYSLYSGLUTYR
4   GLUSERASPGLYTHRTHRLYSSERVALTYR
5   GLNGLYTYRILEGLUASPASPTHRALAARG
6   ILEARGILESERSERPHEGLYLYSGLNLEU
7   GLNASPSERASPVALVALARGILEASPASN
8   ALAARGVALALAGLNPHEASNGLYTYRLEU
9   SERLEUSERVALGLYASPSERSERARGILE
10   GLUSERVALASNVALASNILEPROLEUGLU
11   HISHISHISHISHISHIS

Samples:

NC_sample: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.05 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; D2O 5%; H2O 95%

NC5_sample: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.05 mM; sodium azide 0.02 ± 0.001 %; protein, [U-5% 13C; U-100% 15N], 1.3 ± .1 mM; D2O 5%; H2O 95%

NC_sample_in_D2O: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 10 ± 0.5 mM; calcium chloride 5 ± 0.05 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC (1 hr)NC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC_sample_in_D2Oisotropicsample_conditions_1
3D 1H-13C NOESYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC (1 day)NC_sample_in_D2Oisotropicsample_conditions_1

Software:

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20.0, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

SWS Q9HL44
UNP Q9HL44
PDB
AlphaFold Q9HL44

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