BMRB Entry 15639

Name: 1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris
Published: 2008-05-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15639

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:

1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris

Deposition date:

2008-01-25

Original release date:

2008-05-28

Authors:

Kumaki, Yasuhiro; Kawano, Keiichi; Hikichi, Kunio; Matsumoto, Takeshi; Matsushima, Norio

Citation:

Citation: Kumaki, Yasuhiro; Kawano, Keiichi; Hikichi, Kunio; Matsumoto, Takeshi; Matsushima, Norio. "A circular loop of the sixteen-residue repeating unit in ice nucleation protein" Biochem. Biophys. Res. Commun. 371, 5-9 (2008).
PubMed: 18361918

Assembly members:

Assembly members:
model_peptide_for_INP, polymer, 17 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Xanthomonas campestris Taxonomy ID: 339 Superkingdom: Bacteria Kingdom: not available Genus/species: Xanthomonas campestris

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
model_peptide_for_INP: XTARKGSDLTTGYGSTX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
coupling_constants
- coupling_constant_list_1

Data type	Count
1H chemical shifts	103
coupling constants	10

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	polymer chains	1

Entities:

Entity 1, polymer chains 17 residues - Formula weight is not available

1

NLQ

THR

ALA

ARG

LYS

GLY

SER

ASP

LEU

THR

2

THR

GLY

TYR

GLY

SER

THR

SET

Samples:

sample_1: model peptide for INP 3 mM; DSS 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 4.4; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

Delta v4.3.2, JEOL - processing

NMR spectrometers:

JEOL ALPHA 500 MHz