BMRB Entry 16344

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16344
MolProbity Validation Chart

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Title:
Solution structure and backbone dynamics of the ribosomal protein S6wt.
Deposition date:
2009-06-10
Original release date:
2009-12-16
Authors:
Ohman, Anders; Oliveberg, Mikael; Oman, Tommy
Citation:

Citation: Haglund, Ellinor; Lind, Jesper; Oman, Tommy; Ohman, Anders; Maler, Lena; Oliveberg, Mikael. "The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway."  Proc. Natl. Acad. Sci. U.S.A. 106, 21619-21624 (2009).
PubMed: 19966220

Assembly members:

Assembly members:
S6wt, polymer, 101 residues, 11972.7 Da.

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S6wt: MRRYEVNIVLNPNLDQSQLA LEKEIIQRALENYGARVEKV EELGLRRLAYPIAKDPQGYF LWYQVEMPEDRVNDLARELR IRDNVRRVMVVKSQEPFLAN A

Data sets:
Data typeCount
15N chemical shifts106
1H chemical shifts659

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1S6wt1

Entities:

Entity 1, S6wt 101 residues - 11972.7 Da.

1   METARGARGTYRGLUVALASNILEVALLEU
2   ASNPROASNLEUASPGLNSERGLNLEUALA
3   LEUGLULYSGLUILEILEGLNARGALALEU
4   GLUASNTYRGLYALAARGVALGLULYSVAL
5   GLUGLULEUGLYLEUARGARGLEUALATYR
6   PROILEALALYSASPPROGLNGLYTYRPHE
7   LEUTRPTYRGLNVALGLUMETPROGLUASP
8   ARGVALASNASPLEUALAARGGLULEUARG
9   ILEARGASPASNVALARGARGVALMETVAL
10   VALLYSSERGLNGLUPROPHELEUALAASN
11   ALA

Samples:

sample_1: entity, [U-15N], 0.8 – 1.2 mM; MES 20 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

sample_2: entity0.8 – 1.2 mM; sodium chloride 50 mM; D2O 100%

sample_conditions_1: ionic strength: 0.06 M; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

xwinnmr/TOPSPIN, Bruker Biospin - collection

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

ANSIG, Kraulis - chemical shift assignment, data analysis, peak picking

X-PLOR, Brunger - geometry optimization, refinement, structure solution

AQUA, Rullmann, Doreleijers and Kaptein - data analysis

ProcheckNMR, Laskowski and MacArthur - structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

Molmol, Koradi, Billeter and Wuthrich - structure solution

Mulder, P. Padrta & V. Sklenar - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAD70068
GB AAF27295 AAS82082 AEG32576 AFH38067 EIA40156
PIR S43389
REF WP_011174099 WP_038034932 YP_143511
SP P23370 P62666 Q5SLP8
AlphaFold P23370 P62666 Q5SLP8

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