Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53615

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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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Name: NMR backbone chemical shift assignments of the carbohydrate-binding module family 92 (CBM92A) from Chitinophaga pinensis
Published: 2026-03-23

Title:

NMR backbone chemical shift assignments of the carbohydrate-binding module family 92 (CBM92A) from Chitinophaga pinensis

Deposition date:

2026-03-11

Original release date:

2026-03-23

Authors:

Trooyen, Susanne; Courtade, Gaston

Citation:

Citation: Trooyen, Susanne; Ruoff, Marina; McKee, Lauren; Courtade, Gaston. "Molecular basis of protein-glycan cross-linking by CpCBM92A revealed by NMR spectroscopy" .

Assembly members:

Assembly members:
entity_1, polymer, 151 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Chitinophaga pinensis Taxonomy ID: 79329 Superkingdom: Bacteria Kingdom: not available Genus/species: Chitinophaga pinensis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MASMTGGQQMGRGSVGKTIW LQGFNNKYVNSKNGQGAMWC DSDAPQAWELFTVVDAGNGK IALRGNNGMYVSSENGEQAI TCNRPAIQGWEAFDWLETAD GKVSLRGSNGLFISSENGAA AMTCTRPTASGWEAFGYSVV GNALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	304
15N chemical shifts	119
1H chemical shifts	119

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CBM92A	1

Entities:

Entity 1, CBM92A 151 residues - Formula weight is not available

1

MET

ALA

SER

MET

THR

GLY

GLN

MET

2

GLY

ARG

GLY

SER

VAL

GLY

LYS

THR

ILE

TRP

3

LEU

GLN

GLY

PHE

ASN

LYS

TYR

VAL

ASN

4

SER

LYS

ASN

GLY

GLN

GLY

ALA

MET

TRP

CYS

5

ASP

SER

ASP

ALA

PRO

GLN

ALA

TRP

GLU

LEU

6

PHE

THR

VAL

ASP

ALA

GLY

ASN

GLY

LYS

7

ILE

ALA

LEU

ARG

GLY

ASN

GLY

MET

TYR

8

VAL

SER

GLU

ASN

GLY

GLU

GLN

ALA

ILE

9

THR

CYS

ASN

ARG

PRO

ALA

ILE

GLN

GLY

TRP

10

GLU

ALA

PHE

ASP

TRP

LEU

GLU

THR

ALA

ASP

11

GLY

LYS

VAL

SER

LEU

ARG

GLY

SER

ASN

GLY

12

LEU

PHE

ILE

SER

GLU

ASN

GLY

ALA

13

ALA

MET

THR

CYS

THR

ARG

PRO

THR

ALA

SER

14

GLY

TRP

GLU

ALA

PHE

GLY

TYR

SER

VAL

15

GLY

ASN

ALA

LEU

GLU

HIS

16

HIS

Samples:

sample_1: CBM92A, [U-98% 13C; U-98% 15N], 70 uM; MES 20 mM; sodium chloride 10 mM

sample_conditions_1: ionic strength: 30 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 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 53615