BMRB Entry 52996

Name: Random coil chemical shifts of 6-fluoro-L-tryptophan
Published: 2025-07-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52996

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Random coil chemical shifts of 6-fluoro-L-tryptophan

Deposition date:

2025-03-31

Original release date:

2025-07-08

Authors:

Reiter, David; Schubert, Mario

Citation:

Citation: Reiter, David; Mutlu, Ferhat; Ebert, Dominik; Noutio, Marceline; Heberle, Joachim; Schubert, Mario; Koksch, Beate. "Investigating the Site-Specific Impact of Fluorine Substitution on Aromatic Interactions in a Tryptophan Zipper Peptide" Chemistry ., .-. (2025).
PubMed: 40536432

Assembly members:

Assembly members:
entity_1, polymer, 6 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGXAGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	11
15N chemical shifts	2
19F chemical shifts	1
1H chemical shifts	9

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	random coil peptide GGXAGG	1

Entities:

Entity 1, random coil peptide GGXAGG 6 residues - Formula weight is not available

1

GLY

FT6

ALA

GLY

Samples:

sample_1: random coil peptide 2 mM; urea 1 M; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
1D 13C	sample_1	isotropic	sample_conditions_1
1D 19F	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

MestReNova - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz
JEOL ECZ 600 MHz

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