BMRB Entry 16089

Title:
Solution NMR structure of ribosomal protein sso0164 from Sulfolobus solfataricus. NortheastStructural Genomics Consortium (NESG) target SsT4
Deposition date:
2008-12-23
Original release date:
2010-09-24
Authors:
Lemak, Alexander; Gutmanas, Aleksandras; Yee, Adelinda; Fares, Christophe; Garcia, Maite; Montelione, Gaetano; Arrowsmith, Cheryl
Citation:

Citation: Lemak, Alexander; Gutmanas, Aleksandras; Yee, Adelinda; Fares, Christophe; Garcia, Maite; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution NMR Structure of ribosomal protein sso0164 from Sulfolobus solfataricus"  .

Assembly members:

Assembly members:
sso0164, polymer, 133 residues, 14686.104 Da.

Natural source:

Natural source:   Common Name: Sulfolobus solfataricus   Taxonomy ID: 2287   Superkingdom: Archaea   Kingdom: not available   Genus/species: Sulfolobus solfataricus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: P11

Experimental source:

Natural source:   Common Name: Sulfolobus solfataricus   Taxonomy ID: 2287   Superkingdom: Archaea   Kingdom: not available   Genus/species: Sulfolobus solfataricus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: P11

Data sets:
Data typeCount
13C chemical shifts478
15N chemical shifts112
1H chemical shifts817
residual dipolar couplings30

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sso01641

Entities:

Entity 1, sso0164 133 residues - 14686.104 Da.

1   METGLYPHETYRGLNGLYPROASPASNARG
2   LYSILETHRGLYGLYLEULYSGLYLYSHIS
3   ARGASPLYSARGLYSTYRGLUILEGLYASN
4   PROPROTHRPHETHRTHRLEUSERALAGLU
5   ASPILEARGILELYSASPARGTHRLEUGLY
6   GLYASNPHELYSVALARGLEULYSTYRTHR
7   THRTHRALAASNVALLEUASPPROALATHR
8   ASNTHRALALYSLYSVALLYSILELEUGLU
9   ILELEUGLUTHRPROALAASNLYSGLULEU
10   ALAARGARGGLYILEILEILEARGGLYALA
11   LYSILEARGTHRGLUALAGLYLEUALAVAL
12   VALTHRSERARGPROGLYGLNASPGLYVAL
13   ILEASNALAVALLEULEULYSASNGLUSER
14   GLNARGSER

Samples:

sample_1: sso0164, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 500 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM

sample_conditions_1: ionic strength: 500 mM; pH: 7.7; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C_arom NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC(IPAP)sample_1anisotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

FMC, Lemak, Steren, Llinas, Arrowsmith - resonanmce assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAK40509 ACP36129 ACP46351 ACP47944 ACP55921
REF WP_009990388 WP_012714112
SP C3MJ42 C3MZT9 C3N864 C3NF48 C4KJ22
AlphaFold C3MZT9

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts