BMRB Entry 18657

Name: 1H,13C,15N assignments for an isoform of the type III antifreeze protein from notched-fin eelpout
Published: 2013-02-13

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PDB ID: 2lx2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18657
MolProbity Validation Chart

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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,13C,15N assignments for an isoform of the type III antifreeze protein from notched-fin eelpout

Deposition date:

2012-08-12

Original release date:

2013-02-13

Authors:

Kumeta, Hiroyuki; Ogura, Kenji; Nishimiya, Yoshiyuki; Miura, Ai; Inagaki, Fuyuhiko; Tsuda, Sakae

Citation:

Citation: Kumeta, Hiroyuki; Ogura, Kenji; Nishimiya, Yoshiyuki; Miura, Ai; Inagaki, Fuyuhiko; Tsuda, Sakae. "NMR structure note: a defective isoform and its activity-improved variant of a type III antifreeze protein from Zoarces elongates Kner." J. Biomol. NMR 55, 225-230 (2013).
PubMed: 23288342

Assembly members:

Assembly members:
nfeAFP11, polymer, 67 residues, 7071.434 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 291231 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Zoarces elongatus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pKK223-3UC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
nfeAFP11: MNQESVVAAQLIPINTALTL VMMTTRVVSPTGIPAEDIPR LISMQVNQVVPMGTTLMPDM VKGYAPA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	292
15N chemical shifts	67
1H chemical shifts	511

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	nfeAFP11	1

Entities:

Entity 1, nfeAFP11 67 residues - 7071.434 Da.

1

MET

ASN

GLN

GLU

SER

VAL

ALA

GLN

2

LEU

ILE

PRO

ILE

ASN

THR

ALA

LEU

THR

LEU

3

VAL

MET

THR

ARG

VAL

SER

PRO

4

THR

GLY

ILE

PRO

ALA

GLU

ASP

ILE

PRO

ARG

5

LEU

ILE

SER

MET

GLN

VAL

ASN

GLN

VAL

6

PRO

MET

GLY

THR

LEU

MET

PRO

ASP

MET

7

VAL

LYS

GLY

TYR

ALA

PRO

ALA

Samples:

sample_1: nfeAFP11, [U-100% 13C; U-100% 15N], 2 mM; potassium chloride 20 mM; DSS 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

Varian INOVA 600 MHz