BMRB Entry 27120

Name: Backbone chemical shifts of a circularized type III antifreeze protein from Macrozoarces americanus
Published: 2017-07-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27120

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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:

Backbone chemical shifts of a circularized type III antifreeze protein from Macrozoarces americanus

Deposition date:

2017-05-31

Original release date:

2017-07-06

Authors:

Stevens, Corey; Langelaan, David; Allingham, John; Davies, Peter

Citation:

Citation: Stevens, Corey; Semrau, Joanna; Chiriac, Dragos; Litschko, Morgan; Campbell, Robert; Langelaan, David; Smith, Steven; Davies, Peter; Allingham, John. "Peptide backbone circularization enhances antifreeze protein thermostability." Protein Sci. 26, 1932-1941 (2017).
PubMed: 28691252

Assembly members:

Assembly members:
circAFP, polymer, 74 residues, Formula weight is not available

Natural source:

Natural source: Common Name: ocean pout Taxonomy ID: 8199 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Macrozoarces americanus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
circAFP: CWEGAANQASVVANQLIPIN TALTLVMMRSEVVTPVGIPA EDIPRLVSMQVNRAVPLGTT LMPDMVKGYAARGK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	216
15N chemical shifts	69
1H chemical shifts	69

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	circAFP	1

Entities:

Entity 1, circAFP 74 residues - Formula weight is not available

This is a circularized protein.

1

CYS

TRP

GLU

GLY

ALA

ASN

GLN

ALA

SER

2

VAL

ALA

ASN

GLN

LEU

ILE

PRO

ILE

ASN

3

THR

ALA

LEU

THR

LEU

VAL

MET

ARG

SER

4

GLU

VAL

THR

PRO

VAL

GLY

ILE

PRO

ALA

5

GLU

ASP

ILE

PRO

ARG

LEU

VAL

SER

MET

GLN

6

VAL

ASN

ARG

ALA

VAL

PRO

LEU

GLY

THR

7

LEU

MET

PRO

ASP

MET

VAL

LYS

GLY

TYR

ALA

8

ALA

ARG

GLY

LYS

Samples:

sample_1: circAFP, [U-100% 13C; U-100% 15N], 3 mM; TRIS 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNmr_Analysis v2.4, CCPN, Varian - chemical shift assignment, collection, data analysis

NMR spectrometers:

Varian INOVA 600 MHz

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