BMRB Entry 26761

Name: Backbone assignment of the Xylanase B2 from Streptomyces lividans
Published: 2016-04-22

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26761

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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:

Backbone assignment of the Xylanase B2 from Streptomyces lividans

Deposition date:

2016-03-19

Original release date:

2016-04-22

Authors:

Gagne, Donald; Nguyen Thi, Nhung; Narayanan, Chitra; Roux, Louise; Brunzelle, Joseph; Couture, Jean-Francois; Agarwal, Pratul; Doucet, Nicolas

Citation:

Citation: Gagne, Donald; Nguyen Thi, Nhung; Narayanan, Chitra; Roux, Louise; Brunzelle, Joseph; Couture, Jean-Francois; Agarwal, Pratul; Doucet, Nicolas. "Ligand Binding Enhances Millisecond Conformational Exchange in Xylanase B2 from Streptomyces lividans" Biochemistry 55, 4184-4196 (2016).
PubMed: 27387012

Assembly members:

Assembly members:
XlnB2, polymer, 191 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptomyces lividans Taxonomy ID: 1916 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces lividans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Streptomyces lividans Vector: pIAF935

Entity Sequences (FASTA):

Entity Sequences (FASTA):
XlnB2: DTVVTTNQEGTNNGYYYSFW TDSQGTVSMNMGSGGQYSTS WRNTGNFVAGKGWANGGRRT VQYSGSFNPSGNAYLALYGW TSNPLVEYYIVDNWGTYRPT GEYKGTVTSDGGTYDIYKTT RVNKPSVEGTRTFDQYWSVR QSKRTGGTITTGNHFDAWAR AGMPLGNFSYYMIMATEGYQ SSGSSSINVGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	446
15N chemical shifts	147
1H chemical shifts	146

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	XlnB2	1

Entities:

Entity 1, XlnB2 191 residues - Formula weight is not available

1

ASP

THR

VAL

THR

ASN

GLN

GLU

GLY

2

THR

ASN

GLY

TYR

SER

PHE

TRP

3

THR

ASP

SER

GLN

GLY

THR

VAL

SER

MET

ASN

4

MET

GLY

SER

GLY

GLN

TYR

SER

THR

SER

5

TRP

ARG

ASN

THR

GLY

ASN

PHE

VAL

ALA

GLY

6

LYS

GLY

TRP

ALA

ASN

GLY

ARG

THR

7

VAL

GLN

TYR

SER

GLY

SER

PHE

ASN

PRO

SER

8

GLY

ASN

ALA

TYR

LEU

ALA

LEU

TYR

GLY

TRP

9

THR

SER

ASN

PRO

LEU

VAL

GLU

TYR

ILE

10

VAL

ASP

ASN

TRP

GLY

THR

TYR

ARG

PRO

THR

11

GLY

GLU

TYR

LYS

GLY

THR

VAL

THR

SER

ASP

12

GLY

THR

TYR

ASP

ILE

TYR

LYS

THR

13

ARG

VAL

ASN

LYS

PRO

SER

VAL

GLU

GLY

THR

14

ARG

THR

PHE

ASP

GLN

TYR

TRP

SER

VAL

ARG

15

GLN

SER

LYS

ARG

THR

GLY

THR

ILE

THR

16

THR

GLY

ASN

HIS

PHE

ASP

ALA

TRP

ALA

ARG

17

ALA

GLY

MET

PRO

LEU

GLY

ASN

PHE

SER

TYR

18

TYR

MET

ILE

MET

ALA

THR

GLU

GLY

TYR

GLN

19

SER

GLY

SER

ILE

ASN

VAL

GLY

20

GLY

Samples:

sample_1: XlnB2, [U-100% 15N], 3 g/L; XlnB2, [U-100% 13C], 2 g/L

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 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
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Varian INOVA 800 MHz
Varian INOVA 600 MHz

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