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 7154

Title: NMR spectroscopy of T4 Lysozyme peptide fragments   PubMed: 10801343

Authors: Najbar, L.; Craik, D.; Wade, J.; McLeish, M.

Citation: Najbar, L.; Craik, D.; Wade, J.; McLeish, M.. "Identification of initiation sites for T4 lysozyme folding using CD and NMR spectroscopy of peptide fragments"  Biochemistry 39, 5911-5920 (2000).

Assembly members:
helix E (lys 92-107), polymer, 16 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: chemical synthesis

Entity Sequences (FASTA):
helix E (lys 92-107): DAVRRAALINMVFQMG

Data sets:
Data typeCount
1H chemical shifts105

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1fragment corresponding to Lys Helix E (residues 92-107)1

Entities:

Entity 1, fragment corresponding to Lys Helix E (residues 92-107) 16 residues - Formula weight is not available

1   ASPALAVALARGARGALAALALEUILEASN
2   METVALPHEGLNMETGLY

Samples:

sample_1: helix E (lys 92-107)1 – 2 mM; TFE 50%; H2O 45%; D2O 5%

conditions_1: pH: . .; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
unknownsample_1isotropicconditions_1

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz

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