BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17810

Title: Atomic Resolution Protein Structures using NMR Chemical Shift Tensors   PubMed: 21969532

Authors: Wylie, Benjamin; Sperling, Lindsay; Nieuwkoop, Andrew; Franks, William; Oldfield, Eric; Rienstra, Chad

Citation: Wylie, Benjamin; Sperling, Lindsay; Nieuwkoop, Andrew; Franks, W.; Oldfield, Eric; Rienstra, Chad. "Ultrahigh resolution protein structures using NMR chemical shift tensors"  Proc. Natl. Acad. Sci. U.S.A. 108, 16974-16979 (2011).

Assembly members:
entity, polymer, 56 residues, 6228.870 Da.

Natural source:   Common Name: firmicutes   Taxonomy ID: 1320   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus Streptococcus sp. 'group G'

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

Entity Sequences (FASTA):
entity: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTE

Data sets:
Data typeCount
13C chemical shifts274
15N chemical shifts68

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 56 residues - 6228.870 Da.

1   METGLNTYRLYSLEUILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRALAASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLU

Samples:

sample_1: GB1, [U-2-13C-glycerol; U-100% 15N], 20 mg; (4R)-2-Metylpentane-2,4-Diol 50%; Isopropyl alcohol 25%; GB1 25 mg/mL; sodium phosphate buffered H2O 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D-NCA-{13C CST}sample_1solidsample_conditions_1
3D-NCA-{1H-13C}sample_1solidsample_conditions_1
3D-NCA-{13C CST}:{15N-13C}sample_1solidsample_conditions_1
3D-NCA-1:1{13C CST}:{1H-13C}sample_1solidsample_conditions_1
3D-NCA-2:1{13C CST}:{1H-13C}sample_1solidsample_conditions_1
3D-NCA-3:1{13C CST}:{1H-13C}sample_1solidsample_conditions_1
3D-NCA-{15N CST}sample_1solidsample_conditions_1
3D-NCA-{1H-15N}sample_1solidsample_conditions_1
3D-NCA-1:1{15N CST}:{1H-15N}sample_1solidsample_conditions_1
3D-NCA-2:1{15N CST}:{1H-15N}sample_1solidsample_conditions_1
3D-NCA-1:2{15N CST}:{1H-15N}sample_1solidsample_conditions_1

Software:

X-PLOR NIH v2.18.(2-4), Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - data analysis

Spinevolution, M.Veshtort, R.G.Griffin - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, data analysis, peak picking, processing

Minuit, James, F; Roos, M - data analysis

NMR spectrometers:

  • Varian Infinity Plus 500 MHz

Related Database Links:

BMRB 15156 15380 16444 16627 16755 16873 16882 16958 18397 19394 26630
PDB
EMBL CAA37410
GB AAY41168