BMRB Entry 34519

Name: NMR solution structure of the carbohydrate-binding module family 5 (CBM5) from Cellvibrio japonicus CjLPMO10A
Published: 2021-04-26

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PDB ID: 6z40
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34519
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR solution structure of the carbohydrate-binding module family 5 (CBM5) from Cellvibrio japonicus CjLPMO10A PubMed: 34411561

Deposition date: 2020-05-22 Original release date: 2021-04-26

Authors: Madland, E.; Aachmann, F.; Courtade, G.

Citation: Madland, E.; Forsberg, Z.; Wang, Y.; Lindorff-Larsen, K.; Niebisch, A.; Modregger, J.; Eijsink, V.; Aachmann, F.; Courtade, G.. "Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus" J. Biol. Chem. 297, 101084-101084 (2021).

Assembly members:
entity_1, polymer, 67 residues, 7630.195 Da.

Natural source: Common Name: Cellvibrio japonicus Taxonomy ID: 498211 Superkingdom: Bacteria Kingdom: not available Genus/species: Cellvibrio japonicus

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pNIC-CH

Entity Sequences (FASTA):
entity_1: MDTCATLPSWDASTVYTNPQ QVKHNSKRYQANYWTQNQNP STNSGQYGPWLDLGNCVTSG AHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	212
15N chemical shifts	70
1H chemical shifts	349

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 67 residues - 7630.195 Da.

1

MET

ASP

THR

CYS

ALA

THR

LEU

PRO

SER

TRP

2

ASP

ALA

SER

THR

VAL

TYR

THR

ASN

PRO

GLN

3

GLN

VAL

LYS

HIS

ASN

SER

LYS

ARG

TYR

GLN

4

ALA

ASN

TYR

TRP

THR

GLN

ASN

GLN

ASN

PRO

5

SER

THR

ASN

SER

GLY

GLN

TYR

GLY

PRO

TRP

6

LEU

ASP

LEU

GLY

ASN

CYS

VAL

THR

SER

GLY

7

ALA

HIS

Samples:

sample_1: CBM5, [U-15N], 0.1 ± 0.05 mM; sodium phosphate 25 mM; sodium chloride 10 mM

sample_2: CBM5, [U-13C; U-15N], 0.1 ± 0.05 mM; sodium phosphate 25 mM; sodium chloride 10 mM

sample_3: CBM5 0.1 ± 0.05 mM; sodium phosphate 25 mM; sodium chloride 10 mM

sample_conditions_1: ionic strength: 55 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1

Software:

TopSpin v3.5, Bruker Biospin - processing

CARA v1.5.5, Keller and Wuthrich - chemical shift assignment

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA v14.6.23, YASARA - refinement

NMR spectrometers:

Bruker AVANCE III 800 MHz

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