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 10117

Title: The Confirmation of the Denatured Structure of Pyrrolidone carboxyl Peptidase under Non denaturing Conditions: Deference in Helix Propensity of Two Synthetic Peptides with Single Amino Acid Substitution   PubMed: 17979195

Deposition date: 2007-02-16 Original release date: 2008-06-27

Authors: Umezaki, Taro; Iimura, Satoshi; Noda, Yasuo; Segawa, Shin-ichi; Yutani, Katsuhide

Citation: Umezaki, Taro; Iimura, Satoshi; Noda, Yasuo; Segawa, Shin-ichi; Yutani, Katsuhide. "The confirmation of the denatured structure of pyrrolidone carboxyl peptidase under nondenaturing conditions: difference in helix propensity of two synthetic peptides with single amino acid substitution."  Proteins 71, 737-742 (2008).

Assembly members:
mutant H6-peptide, polymer, 18 residues, 2049 Da.

Natural source:   Common Name: Pyrococcus furiosus   Taxonomy ID: 2261   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrococcus furiosus

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
mutant H6-peptide: SYEMELEAVKVPIEVALE

Data sets:
Data typeCount
1H chemical shifts117

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1subunit 11
2subunit 21
3subunit 31
4subunit 41

Entities:

Entity 1, subunit 1 18 residues - 2049 Da.

1   SERTYRGLUMETGLULEUGLUALAVALLYS
2   VALPROILEGLUVALALALEUGLU

Samples:

sample_1: mutant H6-peptide 0.7 mM; 2.2.2 trifluoroethanol-d2 30%

condition_1: pH: 7.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-1H NOESYsample_1not availablecondition_1
HOHAHAsample_1not availablecondition_1
DQF-COSYsample_1not availablecondition_1

Software:

xwinnmr - collection

SPARKY v3.110 - peak assignments

NMR spectrometers:

  • Bruker DRX 600 MHz

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