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 4065

Title: Sequence-Specific Resonance Assignments for a Designed Four-Alpha-Helix-Bundle Protein

Deposition date: 1997-10-03 Original release date: 2002-08-12

Authors: Skalicky, Jack; Bieber, Ramona; Gibney, Brian; Rabanal, Francesc; Dutton, Leslie; Wand, Joshua

Citation: Skalicky, Jack; Bieber, Ramona; Gibney, Brian; Rabanal, Francesc; Dutton, Leslie; Wand, Joshua. "Sequence-Specific Resonance Assignments for a Designed Four-Alpha-Helix-Bundle Protein"  J. Biomol. NMR 11, 227-228 (1998).

Assembly members:
H10H24-L6I,L13F, polymer, 31 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
H10H24-L6I,L13F: CGGGEIWKLHEEFLKKFEEL LKLHEERLKKL

Data typeCount
13C chemical shifts263
15N chemical shifts60
1H chemical shifts391

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1chain_A1
2chain_B1
3chain_C1
4chain_D1

Entities:

Entity 1, chain_A 31 residues - Formula weight is not available

1   CYSGLYGLYGLYGLUILETRPLYSLEUHIS
2   GLUGLUPHELEULYSLYSPHEGLUGLULEU
3   LEULYSLEUHISGLUGLUARGLEULYSLYS
4   LEU

Samples:

sample_one: H10H24-L6I,L13F 1.5 mM

sample_conditions: ionic strength: 0.150 mu; pH: 6.60; pressure: 760 mm Hg; temperature: 305.5 K

Experiments:

NameSampleSample stateSample conditions
not availablesample_onenot availablesample_conditions

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
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