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 5323

Title: Solution Structure of the Tenebrio molitor Antifreeze Protein   PubMed: 11969412

Deposition date: 2002-03-16 Original release date: 2002-05-10

Authors: Daley, M.; Spyracopoulos, L.; Jia, Z.; Davies, P.; Sykes, B.

Citation: Daley, M.; Spyracopoulos, L.; Jia, Z.; Davies, P.; Sykes, B.. "Structure and Dynamics of a beta-Helical Antifreeze Protein"  Biochemistry 41, 5515-5525 (2002).

Assembly members:
Tenebrio molitor antifreeze protein, polymer, 84 residues, Formula weight is not available

Natural source:   Common Name: yellow mealworm beetle   Taxonomy ID: 7067   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Tenebrio molitor

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Tenebrio molitor antifreeze protein: QCTGGADCTSCTGACTGCGN CPNAVTCTNSQHCVKANTCT GSTDCNTAQTCTNSKDCFEA NTCTDSTNCYKATACTNSSG CPGH

Data sets:
Data typeCount
15N chemical shifts85
1H chemical shifts420

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Thermal hysteresis protein isoform YL-1 (2-14)1

Entities:

Entity 1, Thermal hysteresis protein isoform YL-1 (2-14) 84 residues - Formula weight is not available

1   GLNCYSTHRGLYGLYALAASPCYSTHRSER
2   CYSTHRGLYALACYSTHRGLYCYSGLYASN
3   CYSPROASNALAVALTHRCYSTHRASNSER
4   GLNHISCYSVALLYSALAASNTHRCYSTHR
5   GLYSERTHRASPCYSASNTHRALAGLNTHR
6   CYSTHRASNSERLYSASPCYSPHEGLUALA
7   ASNTHRCYSTHRASPSERTHRASNCYSTYR
8   LYSALATHRALACYSTHRASNSERSERGLY
9   CYSPROGLYHIS

Samples:

sample_1: Tenebrio molitor antifreeze protein, [U-15N], 0.4 mM; H2O 90%; D2O 10%

sample_2: Tenebrio molitor antifreeze protein 1.0 mM; H2O 90%; D2O 10%

sample_3: Tenebrio molitor antifreeze protein 1.0 mM; D2O 100%

sample_cond_1: ionic strength: 0 mM; pH: 5.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-edited TOCSYnot availablenot availablenot available
HNHAnot availablenot availablenot available
HNHBnot availablenot availablenot available
3D 15N-edited NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
13C-HSQCnot availablenot availablenot available
15N-HSQCnot availablenot availablenot available

Software:

VNMR v6.1B - collection

NMRPipe vsgi6 - processing

NMRView v4.1.2 - data analysis

CNS v1.0 - structure solution

NMR spectrometers:

  • Varian Unity 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
GenBank AAB70750 ABA46869 ABB29471

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