BMRB Entry 15641

Name: 1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 24-residue peptide corresponding to the segment within ice nucleation protein of Erwinia uredovora, Erwinia herbicola
Published: 2008-05-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15641

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

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Title:

1H-NMR Chemical shifts and vicinal coupling constants (3JHNHa) for 24-residue peptide corresponding to the segment within ice nucleation protein of Erwinia uredovora, Erwinia herbicola

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, 24 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Erwinia herbicola Taxonomy ID: 553 Superkingdom: Bacteria Kingdom: not available Genus/species: Pantoea ananatis

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
model_peptide_for_INP: SGLRSVLTAGYGSSLISGRR SSLT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
coupling_constants
- coupling_constant_list_1

Data type	Count
1H chemical shifts	151
coupling constants	12

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	polymer chains	1

Entities:

Entity 1, polymer chains 24 residues - Formula weight is not available

1

SER

GLY

LEU

ARG

SER

VAL

LEU

THR

ALA

GLY

2

TYR

GLY

SER

LEU

ILE

SER

GLY

ARG

3

SER

LEU

THR

Samples:

sample_1: model peptide for INP 6 mM; acetic acid 50 mM; TSP 1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 4.0; 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