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 34033

Title: Engineering protein stability with atomic precision in a monomeric miniprotein   PubMed: 28530710

Authors: Baker, E.; Williams, C.; Hudson, K.; Bartlett, G.; Heal, J.; Sessions, R.; Crump, M.; Woolfson, D.

Citation: Baker, E.; Williams, C.; Hudson, K.; Bartlett, G.; Heal, J.; Porter Goff, K.; Sessions, R.; Crump, M.; Woolfson, D.. "Engineering protein stability with atomic precision in a monomeric miniprotein"  Nat. Chem. Biol. 13, 764-770 (2017).

Assembly members:
entity_1, polymer, 36 residues, 3801.367 Da.

Natural source:   Common Name: Streptococcus mutans   Taxonomy ID: 1309   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus mutans

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: XPPTKPTKPGDNATPEKLAK XQADLAKXQKDLADXX

Data sets:
Data typeCount
13C chemical shifts38
15N chemical shifts32
1H chemical shifts227

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 36 residues - 3801.367 Da.

1   ACEPROPROTHRLYSPROTHRLYSPROGLY
2   ASPASNALATHRPROGLULYSLEUALALYS
3   4PHGLNALAASPLEUALALYS4PHGLNLYS
4   ASPLEUALAASP4PHNH2

Samples:

sample_1: KH2PO4 1.8 mM; Na2HPO4 8.2 mM; NaCl 137 mM; NaOH 13.7 mM; PPa-CH3 1 mM

sample_conditions_1: ionic strength: 0.1698 M; pH: 7.4; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement

Analysis, CCPN - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 700 MHz
  • Bruker AvanceIII 900 MHz

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