Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53343

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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 and 15N backbone resonance assignments of the exonuclease protein CNase.

Deposition date:

2025-09-10

Original release date:

2026-08-03

Authors:

Koduru, Tejaswi

Citation:

Citation: Koduru, Tejaswi; Barthe, Philippe; Hantman, Noam; De Guillen, Karine; McCallum, Scott; Morgan, Joel; Yee, Estella; Leonardi, Pierce; Foland, Jack; Roumestand, Christian; Royer, Catherine. "Adaptation of Folding and Function of a Nuclease from the Cold Deep Sea " J. Mol. Biol. 438, 169602-169602 (2026).
PubMed: 41443464

Assembly members:

Assembly members:
entity_1, polymer, 144 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Carnobacterium Taxonomy ID: 2747 Superkingdom: Bacteria Kingdom: not available Genus/species: Carnobacterium not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-24a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDQVAVELERVIDGDTIVFT ENNEEKKLRLLLIDTPESST TKTGSAQPYGVEAKSFLTNF LKGKELAIEYDPSHEKVDDY ERVLAYLYADGELVQEVLVE EGLARVGYENGDELYLGRLE KAEQKASAAEVNIWSVKGYV KEYR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	367
15N chemical shifts	132
1H chemical shifts	275

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CNASE	1

Entities:

Entity 1, CNASE 144 residues - Formula weight is not available

1

MET

ASP

GLN

VAL

ALA

VAL

GLU

LEU

GLU

ARG

2

VAL

ILE

ASP

GLY

ASP

THR

ILE

VAL

PHE

THR

3

GLU

ASN

GLU

LYS

LEU

ARG

LEU

4

LEU

ILE

ASP

THR

PRO

GLU

SER

THR

5

THR

LYS

THR

GLY

SER

ALA

GLN

PRO

TYR

GLY

6

VAL

GLU

ALA

LYS

SER

PHE

LEU

THR

ASN

PHE

7

LEU

LYS

GLY

LYS

GLU

LEU

ALA

ILE

GLU

TYR

8

ASP

PRO

SER

HIS

GLU

LYS

VAL

ASP

TYR

9

GLU

ARG

VAL

LEU

ALA

TYR

LEU

TYR

ALA

ASP

10

GLY

GLU

LEU

VAL

GLN

GLU

VAL

LEU

VAL

GLU

11

GLU

GLY

LEU

ALA

ARG

VAL

GLY

TYR

GLU

ASN

12

GLY

ASP

GLU

LEU

TYR

LEU

GLY

ARG

LEU

GLU

13

LYS

ALA

GLU

GLN

LYS

ALA

SER

ALA

GLU

14

VAL

ASN

ILE

TRP

SER

VAL

LYS

GLY

TYR

VAL

15

LYS

GLU

TYR

ARG

Samples:

sample_1: CNASE, [U-100% 13C; U-100% 15N], 0.5 mM; potassium chloride 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v4.4.0 - collection

NMR spectrometers:

Bruker Avance 600 MHz

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

BMRB Entry 53343