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 2529

Title: Conformation and Dynamics of an Fab'-Bound Peptide by Isotope-Edited NMR Spectroscopy

Deposition date: 1995-07-31 Original release date: 1999-06-14

Authors: Tsang, P.; Rance, Mark; Fieser, T.; Ostresh, J.; Houghten, R.; Lerner, Richard; Wright, Peter

Citation: Tsang, P.; Rance, Mark; Fieser, T.; Ostresh, J.; Houghten, R.; Lerner, Richard; Wright, Peter. "Conformation and Dynamics of an Fab'-Bound Peptide by Isotope-Edited NMR Spectroscopy"  Biochemistry 31, 3862-3871 (1992).

Assembly members:
myohemerythrin, polymer, 12 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: not available

Entity Sequences (FASTA):
myohemerythrin: MHKDFLEKIGGL

Data sets:
Data typeCount
13C chemical shifts1
15N chemical shifts8
1H chemical shifts10

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1myohemerythrin1

Entities:

Entity 1, myohemerythrin 12 residues - Formula weight is not available

1   METHISLYSASPPHELEUGLULYSILEGLY
2   GLYLEU

Samples:

sample_one:

sample_condition_set_one: pH: 5 na; temperature: 308 K

Experiments:

NameSampleSample stateSample 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
SPARKY: Backbone or all simulated shifts