BMRB Entry 20010

Name: Superimposed fifteen structures of 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris
Published: 2008-07-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20010

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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:

Superimposed fifteen structures of 17-residue peptide corresponding to the segment within ice nucleation protein of X. campestris pv. campestris

Deposition date:

2008-02-26

Original release date:

2008-07-15

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 16-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, 19 residues, 1964.123 Da.

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: XQTARKGSDLTTGYGSTSX

Data sets:

conformer_family_coord_set
- ensemble_coordinates

Data type	Count
conformer coordinate sets	1

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	model_peptide_for_INP	1

Entities:

Entity 1, model_peptide_for_INP 19 residues - 1964.123 Da.

1

ACE

GLN

THR

ALA

ARG

LYS

GLY

SER

ASP

LEU

2

THR

GLY

TYR

GLY

SER

THR

SER

NH2

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
2D 1H-1H ROESY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

JEOL ALPHA 500 MHz

DBJ	GAE51334 GAE56226 GAE61386
EMBL	CAP49871 CEM56732
GB	AAM39823 AAY47600 AEL08859 AKC80693 AKU51266
REF	NP_635899 WP_002804985 WP_006450271 WP_011035756 WP_014509183