BMRB Entry 19860

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19860
MolProbity Validation Chart

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Title:
Solution structure of a ribosomal protein
Deposition date:
2014-03-17
Original release date:
2014-06-09
Authors:
Feng, Yingang
Citation:

Citation: Feng, Yingang; Song, Xiaxia; Lin, Jinzhong; Xuan, Jinsong; Cui, Qiu; Wang, Jinfeng. "Structure determination of archaea-specific ribosomal protein L46a reveals a novel protein fold."  Biochem. Biophys. Res. Commun. 450, 67-72 (2014).
PubMed: 24875358

Assembly members:

Assembly members:
rib_prot, polymer, 77 residues, 9223.893 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rib_prot: MLKHGKYVYIDLNNGKYVKV RILKSRDDNSVEKYVLTSHV SKNRPKNAIVIKMDNLPIEV KDKLTRFFLLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts83
1H chemical shifts579

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1rib_prot1

Entities:

Entity 1, rib_prot 77 residues - 9223.893 Da.

1   METLEULYSHISGLYLYSTYRVALTYRILE
2   ASPLEUASNASNGLYLYSTYRVALLYSVAL
3   ARGILELEULYSSERARGASPASPASNSER
4   VALGLULYSTYRVALLEUTHRSERHISVAL
5   SERLYSASNARGPROLYSASNALAILEVAL
6   ILELYSMETASPASNLEUPROILEGLUVAL
7   LYSASPLYSLEUTHRARGPHEPHELEULEU
8   GLUHISHISHISHISHISHIS

Samples:

sample_1: rib_prot, [U-13C; U-15N], 0.5 – 1.0 mM; potassium phosphate 50 mM; potassium chloride 50 mM; EDTA 2 mM; DSS 0.02%; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

Felix, Accelrys Software Inc. - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SANE, Duggan, Legge, Dyson & Wright - refinement

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

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
GB ACX92136 AKA74176 AKA76874 AKA79567
REF WP_009992386

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