BMRB Entry 52153

Name: Endo-b-1,4-xylanase (Xylanase A) D11F/R122D mutant from Bacillus subtilis
Published: 2023-10-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52153

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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:

Endo-b-1,4-xylanase (Xylanase A) D11F/R122D mutant from Bacillus subtilis

Deposition date:

2023-09-28

Original release date:

2023-10-18

Authors:

MacDonald, Meagan

Citation:

Citation: MacDonald, Meagan; Wells, Nicholas; Hassan, Bakar; Dudley, Joshua; Walters, Kylie; Korzhnev, Dmitry; Aramini, James; Smith, Colin. "Effects of Xylanase A double mutation on substrate specificity and structural dynamics" J. Struct. Biol. 216, 108082-108082 (2024).
PubMed: 38438058

Assembly members:

Assembly members:
entity_1, polymer, 189 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMASTDYWQNWTFGGGIV NAVNGSGGNYSVNWSNTGNF VVGKGWTTGSPFRTINYNAG VWAPNGNGYLTLYGWTRSPL IEYYVVDSWGTYRPTGTYKG TVKSDGGTYDIYTTTRYNAP SIDGDDTTFTQYWSVRQSKR PTGSNATITFSNHVNAWKSH GMNLGSNWAYQVMATEGYQS SGSSNVTVW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	338
15N chemical shifts	160
1H chemical shifts	160

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Xylanase A, D11F/R122D	1

Entities:

Entity 1, Xylanase A, D11F/R122D 189 residues - Formula weight is not available

His-tag scar GSHM included in the sequence

1

GLY

SER

HIS

MET

ALA

SER

THR

ASP

TYR

TRP

2

GLN

ASN

TRP

THR

PHE

GLY

ILE

VAL

3

ASN

ALA

VAL

ASN

GLY

SER

GLY

ASN

TYR

4

SER

VAL

ASN

TRP

SER

ASN

THR

GLY

ASN

PHE

5

VAL

GLY

LYS

GLY

TRP

THR

GLY

SER

6

PRO

PHE

ARG

THR

ILE

ASN

TYR

ASN

ALA

GLY

7

VAL

TRP

ALA

PRO

ASN

GLY

ASN

GLY

TYR

LEU

8

THR

LEU

TYR

GLY

TRP

THR

ARG

SER

PRO

LEU

9

ILE

GLU

TYR

VAL

ASP

SER

TRP

GLY

10

THR

TYR

ARG

PRO

THR

GLY

THR

TYR

LYS

GLY

11

THR

VAL

LYS

SER

ASP

GLY

THR

TYR

ASP

12

ILE

TYR

THR

ARG

TYR

ASN

ALA

PRO

13

SER

ILE

ASP

GLY

ASP

THR

PHE

THR

14

GLN

TYR

TRP

SER

VAL

ARG

GLN

SER

LYS

ARG

15

PRO

THR

GLY

SER

ASN

ALA

THR

ILE

THR

PHE

16

SER

ASN

HIS

VAL

ASN

ALA

TRP

LYS

SER

HIS

17

GLY

MET

ASN

LEU

GLY

SER

ASN

TRP

ALA

TYR

18

GLN

VAL

MET

ALA

THR

GLU

GLY

TYR

GLN

SER

19

SER

GLY

SER

ASN

VAL

THR

VAL

TRP

Samples:

sample_1: XylA D11F/R122D, [U-100% 13C; U-100% 15N], 0.20 mM; sodium acetate 25 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 10%; sodium azide 0.03%

sample_conditions_1: ionic strength: 0.05 M; pH: 5.7; pressure: 1 atm; temperature: 295.83 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5 - collection

NMRPipe - processing

CcpNMR v3.0.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 700 MHz

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