BMRB Entry 27691

Name: Backbone assignment of the periplasmic glycoside hydrolase BoMan26A
Published: 2019-02-22

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27691

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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 periplasmic glycoside hydrolase BoMan26A

Deposition date:

2018-11-15

Original release date:

2019-02-22

Authors:

Persson, Cecilia; Akke, Mikael

Citation:

Citation: Wernersson, Sven; Bagenholm, Viktoria; Persson, Cecilia; Upadhyay, Santosh; Stalbrand, Henrik; Akke, Mikael. "Backbone 1H, 13C, and 15N resonance assignments of BoMan26A, a beta-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus" Biomol. NMR Assign. 13, 213-218 (2019).
PubMed: 30734154

Assembly members:

Assembly members:
BoMan26A, polymer, 356 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacteroides ovatus Taxonomy ID: 28116 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides ovatus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: no

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BoMan26A: MGHHHHHHLVPRGSGETGEK TPETVALLQNLKQAERKGIL FGHHDDTAYGIGWEGDKGRS DVKSVCGAYPGVMSFDLGEI ELGGTHNLDKVSFAHLREYI IEQYARGGMISLSWHVRNPK TGGDSWDVTDSTVVASVMQG GENHVKMLEWIDRVADFLLS LKTKEGVLIPVVFRPWHEHT GSWFWWGKDLCSSEQYKTLW RMTNDRLRLKGVNNVLLAYS PGMESDTVEEYLERYPGDDI IDVLGTDVYQFERSQYIKQL NKMLTILTEAGKKHDKPIAL TETGLEGIPDSLWWTGTLLP VIEKYPLSYVLVWRNAREKS THYYAPYPGQVSADDFVKFS RSPKILFVGDNFELYK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	953
15N chemical shifts	316
1H chemical shifts	315

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BoMan26A	1

Entities:

Entity 1, BoMan26A 356 residues - Formula weight is not available

1

MET

GLY

HIS

LEU

VAL

2

PRO

ARG

GLY

SER

GLY

GLU

THR

GLY

GLU

LYS

3

THR

PRO

GLU

THR

VAL

ALA

LEU

GLN

ASN

4

LEU

LYS

GLN

ALA

GLU

ARG

LYS

GLY

ILE

LEU

5

PHE

GLY

HIS

ASP

THR

ALA

TYR

GLY

6

ILE

GLY

TRP

GLU

GLY

ASP

LYS

GLY

ARG

SER

7

ASP

VAL

LYS

SER

VAL

CYS

GLY

ALA

TYR

PRO

8

GLY

VAL

MET

SER

PHE

ASP

LEU

GLY

GLU

ILE

9

GLU

LEU

GLY

THR

HIS

ASN

LEU

ASP

LYS

10

VAL

SER

PHE

ALA

HIS

LEU

ARG

GLU

TYR

ILE

11

ILE

GLU

GLN

TYR

ALA

ARG

GLY

MET

ILE

12

SER

LEU

SER

TRP

HIS

VAL

ARG

ASN

PRO

LYS

13

THR

GLY

ASP

SER

TRP

ASP

VAL

THR

ASP

14

SER

THR

VAL

ALA

SER

VAL

MET

GLN

GLY

15

GLY

GLU

ASN

HIS

VAL

LYS

MET

LEU

GLU

TRP

16

ILE

ASP

ARG

VAL

ALA

ASP

PHE

LEU

SER

17

LEU

LYS

THR

LYS

GLU

GLY

VAL

LEU

ILE

PRO

18

VAL

PHE

ARG

PRO

TRP

HIS

GLU

HIS

THR

19

GLY

SER

TRP

PHE

TRP

GLY

LYS

ASP

LEU

20

CYS

SER

GLU

GLN

TYR

LYS

THR

LEU

TRP

21

ARG

MET

THR

ASN

ASP

ARG

LEU

ARG

LEU

LYS

22

GLY

VAL

ASN

VAL

LEU

ALA

TYR

SER

23

PRO

GLY

MET

GLU

SER

ASP

THR

VAL

GLU

24

TYR

LEU

GLU

ARG

TYR

PRO

GLY

ASP

ILE

25

ILE

ASP

VAL

LEU

GLY

THR

ASP

VAL

TYR

GLN

26

PHE

GLU

ARG

SER

GLN

TYR

ILE

LYS

GLN

LEU

27

ASN

LYS

MET

LEU

THR

ILE

LEU

THR

GLU

ALA

28

GLY

LYS

HIS

ASP

LYS

PRO

ILE

ALA

LEU

29

THR

GLU

THR

GLY

LEU

GLU

GLY

ILE

PRO

ASP

30

SER

LEU

TRP

THR

GLY

THR

LEU

PRO

31

VAL

ILE

GLU

LYS

TYR

PRO

LEU

SER

TYR

VAL

32

LEU

VAL

TRP

ARG

ASN

ALA

ARG

GLU

LYS

SER

33

THR

HIS

TYR

ALA

PRO

TYR

PRO

GLY

GLN

34

VAL

SER

ALA

ASP

PHE

VAL

LYS

PHE

SER

35

ARG

SER

PRO

LYS

ILE

LEU

PHE

VAL

GLY

ASP

36

ASN

PHE

GLU

LEU

TYR

LYS

Samples:

sample_1: BoMan26A, [U-99% 13C; U-99% 15N], 0.21 mM

sample_conditions_1: ionic strength: 0 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 15N-TROSY	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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5pl7, Bruker Biospin - collection, processing

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

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

NMR spectrometers:

Oxford Avance 800 MHz

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