BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16345

Title: Solution structure and backbone dynamics of the permutant P54-55   PubMed: 19966220

Deposition date: 2009-06-10 Original release date: 2009-12-16

Authors: Ohman, Anders; Oliveberg, Mikael; Oman, Tommy

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).

Assembly members:
permutant P54-55, polymer, 96 residues, 11258.984 Da.

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

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

Entity Sequences (FASTA):
permutant P54-55: MDPQGYFLWYQVEMPEDRVN DLARELRIRDNVRRVMVVAS TTPGRYEVNIVLNPNLDQSQ LALEKEIIQRALENYGARVE KVEELGLRRLAYPIAK

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts104
1H chemical shifts659

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1permutant P54-551

Entities:

Entity 1, permutant P54-55 96 residues - 11258.984 Da.

1   METASPPROGLNGLYTYRPHELEUTRPTYR
2   GLNVALGLUMETPROGLUASPARGVALASN
3   ASPLEUALAARGGLULEUARGILEARGASP
4   ASNVALARGARGVALMETVALVALALASER
5   THRTHRPROGLYARGTYRGLUVALASNILE
6   VALLEUASNPROASNLEUASPGLNSERGLN
7   LEUALALEUGLULYSGLUILEILEGLNARG
8   ALALEUGLUASNTYRGLYALAARGVALGLU
9   LYSVALGLUGLULEUGLYLEUARGARGLEU
10   ALATYRPROILEALALYS

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_3: entity, [U-13C; U-15N], 0.8 – 1.2 mM; MES 20 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

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_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
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, 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

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