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 6039

Title: NMR Structure of a D,L-Alternating Dodecamer of Norleucine   PubMed: 11373724

Authors: Navarro, E.; Celda, B.

Citation: Navarro, E.; Tejero, R.; Fenude, E.; Celda, B.. "Solution NMR Structure of a D,L-Alternating Oligonorleucine as a Model of Beta-Helix"  Biopolymers 59, 110-119 (2001).

Assembly members:
proteins_1A-1B, 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: chemical synthesis

Entity Sequences (FASTA):
proteins_1A-1B: XXXXXXXXXXXX

Data sets:
Data typeCount
13C chemical shifts12
15N chemical shifts0
1H chemical shifts72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Microtubule-associated proteins 1A/1B light chain 3B1

Entities:

Entity 1, Microtubule-associated proteins 1A/1B light chain 3B 12 residues - Formula weight is not available

1   DNENLEDNENLEDNENLEDNENLEDNMNLE
2   DNENLE

Samples:

sample_1: proteins_1A/1B 5.5 mM; chloroform-d 100%

sample_cond_1: pH: .; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D ROESYsample_1not availablesample_cond_1
2D TOCSYsample_1not availablesample_cond_1
DQF-COSYsample_1not availablesample_cond_1

Software:

DISCOVER v2.9.7 - refinement, structure solution

NMR spectrometers:

  • Varian UNITY 400 MHz

Related Database Links: