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 5157

Title: Solution structure of a hydrophobic analogue of the winter flounder antifreeze protein   PubMed: 11856360

Authors: Liepinsh, Edvards; Otting, Gottfried; Harding, Margaret; Ward, Leanne; Mackay, Joel; Haymet, A.

Citation: Liepinsh, Edvards; Otting, Gottfried; Harding, Margaret; Ward, Leanne; Mackay, Joel; Haymet, A.. "Solution Structure of a Hydrophobic Analogue of the Winter Flounder Antifreeze Protein "  Eur. J. Biochem. 269, 1259-1266 (2002).

Assembly members:
antifreeze protein type 1 mutant, polymer, 37 residues, 3464 Da.

Natural source:   Common Name: winter flounder   Taxonomy ID: 8265   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Pseudopleuronectes americanus

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
antifreeze protein type 1 mutant: DVASDAKAAAELVAANAKAA AELVAANAKAAAEAVAX

Data sets:
Data typeCount
1H chemical shifts161

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1type 1 AFP mutant1

Entities:

Entity 1, type 1 AFP mutant 37 residues - 3464 Da.

1   ASPVALALASERASPALALYSALAALAALA
2   GLULEUVALALAALAASNALALYSALAALA
3   ALAGLULEUVALALAALAASNALALYSALA
4   ALAALAGLUALAVALALAAAR

Samples:

sample_1: antifreeze protein type 1 mutant 11 mM; NaCl 100 mM

sample_2: antifreeze protein type 1 mutant 2 mM; NaCl 100 mM

ex-cond_1: pH: 4.9; temperature: 288 K; ionic strength: 0.1 M

ex-cond_2: pH: 7.0; temperature: 283 K; ionic strength: 0.1 M

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablenot available
2D ROESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
2D DQF-COSYnot availablenot availablenot available

Software:

PROSA v2.6 - spectra processing

XEASY v2.5 - spectral analysis

DYANA v2.6 - structure calculation

OPAL v2.2 - structure refinement

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Varian Unity-INOVA 800 MHz

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