BMRB Entry 34229

Name: Solution NMR structure of CBM64 from S.thermophila using 20% 13C, 100% 15N
Published: 2019-01-28

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PDB ID: 6ffu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34229
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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:

Solution NMR structure of CBM64 from S.thermophila using 20% 13C, 100% 15N

Deposition date:

2018-01-09

Original release date:

2019-01-28

Authors:

Heikkinen, Harri; Iwai, Hideo

Citation:

Citation: Heikkinen, Harri; Backlund, Sofia; Iwai, Hideo. "NMR Structure Determinations of Small Proteins Using only One Fractionally 20% 13C- and Uniformly 100% 15N-Labeled Sample" Molecules 26, 747-747 (2021).
PubMed: 33535444

Assembly members:

Assembly members:
Glycosyl hydrolase family 5 cellulase CBM64, polymer, 86 residues, 10025.756 Da.

Natural source:

Natural source: Common Name: Spirochaeta thermophila Taxonomy ID: 154 Superkingdom: Bacteria Kingdom: not available Genus/species: Spirochaeta thermophila

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Glycosyl hydrolase family 5 cellulase CBM64: SGEYTEIALPFSYDGAGEYY WKTDQFSTDPNDWSRYVNSW NLDLLEINGTDYTNVWVAQH QIPAASDGYWYIHYKSGVSW GHVEIK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	368
15N chemical shifts	93
1H chemical shifts	569

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 86 residues - 10025.756 Da.

1

SER

GLY

GLU

TYR

THR

GLU

ILE

ALA

LEU

PRO

2

PHE

SER

TYR

ASP

GLY

ALA

GLY

GLU

TYR

3

TRP

LYS

THR

ASP

GLN

PHE

SER

THR

ASP

PRO

4

ASN

ASP

TRP

SER

ARG

TYR

VAL

ASN

SER

TRP

5

ASN

LEU

ASP

LEU

GLU

ILE

ASN

GLY

THR

6

ASP

TYR

THR

ASN

VAL

TRP

VAL

ALA

GLN

HIS

7

GLN

ILE

PRO

ALA

SER

ASP

GLY

TYR

TRP

8

TYR

ILE

HIS

TYR

LYS

SER

GLY

VAL

SER

TRP

9

GLY

HIS

VAL

GLU

ILE

LYS

Samples:

sample_1: CBM64_20C13, 20% 13C, 100% 15N, 9.85 ± 0.1 mg/mL

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 bar; temperature: 303 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection

CcpNMR v2.4.2, CCPN - chemical shift assignment, peak picking

AMBER v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

PSVS v1.5, Bhattacharya and Montelione - data analysis

NMR spectrometers:

Bruker Avance III 850 MHz

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