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 34295

Title: Stabilising and Understanding a Miniprotein by Rational Design.   PubMed: 31251570

Deposition date: 2018-06-26 Original release date: 2019-07-02

Authors: Porter Goff, K.; Williams, C.; Baker, E.; Nicol, D.; Samphire, J.; Zieleniewski, F.; Crump, M.; Woolfson, D.

Citation: Porter Goff, K.; Nicol, D.; Williams, C.; Crump, M.; Zieleniewski, F.; Samphire, J.; Baker, E.; Woolfson, D.. "Stabilizing and Understanding a Miniprotein by Rational Redesign."  Biochemistry 58, 3060-3064 (2019).

Assembly members:
entity_1, polymer, 36 residues, 3791.348 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: XPPKKPKKPGDNATPEKLAA YEKELAAYEKELAAYX

Data sets:
Data typeCount
13C chemical shifts35
15N chemical shifts30
1H chemical shifts241

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 36 residues - 3791.348 Da.

1   ACEPROPROLYSLYSPROLYSLYSPROGLY
2   ASPASNALATHRPROGLULYSLEUALAALA
3   TYRGLULYSGLULEUALAALATYRGLULYS
4   GLULEUALAALATYRNH2

Samples:

sample_1: Optimised PPa-TYR 1 ± 0.1 mM; Na2HPO4 8.2 ± 0.1 mM; KH2PO4 1.8 ± 0.1 mM; KCL 2.7 ± 0.1 mM; NaCl 137 ± 0.1 mM; D2O, [U-99% 2H], 10 ± 0.1 %

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

Experiments:

NameSampleSample stateSample conditions
2D 100ms NOESYsample_1isotropicsample_conditions_1
2D 100ms NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H 250ms NOESYsample_1isotropicsample_conditions_1
2D 1H-1H 250ms NOESYsample_1isotropicsample_conditions_1
1H-13N HSQCsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

ARIA v2.3.1, Linge, O'Donoghue and Nilges - structure calculation

CcpNmr Analysis v2.4.1, CCPN - chemical shift assignment, peak picking

TopSpin v3.5, Bruker Biospin - collection

VNMR v4, Varian - collection

NMRDraw v9.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe v9.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker AvanceIII 700 MHz
  • Varian VNMRS 600 MHz

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