BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27691

Title: Backbone assignment of the periplasmic glycoside hydrolase BoMan26A   PubMed: 30734154

Deposition date: 2018-11-15 Original release date: 2019-02-22

Authors: Persson, Cecilia; Akke, Mikael

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts953
15N chemical shifts316
1H chemical shifts315

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1BoMan26A1

Entities:

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

1   METGLYHISHISHISHISHISHISLEUVAL
2   PROARGGLYSERGLYGLUTHRGLYGLULYS
3   THRPROGLUTHRVALALALEULEUGLNASN
4   LEULYSGLNALAGLUARGLYSGLYILELEU
5   PHEGLYHISHISASPASPTHRALATYRGLY
6   ILEGLYTRPGLUGLYASPLYSGLYARGSER
7   ASPVALLYSSERVALCYSGLYALATYRPRO
8   GLYVALMETSERPHEASPLEUGLYGLUILE
9   GLULEUGLYGLYTHRHISASNLEUASPLYS
10   VALSERPHEALAHISLEUARGGLUTYRILE
11   ILEGLUGLNTYRALAARGGLYGLYMETILE
12   SERLEUSERTRPHISVALARGASNPROLYS
13   THRGLYGLYASPSERTRPASPVALTHRASP
14   SERTHRVALVALALASERVALMETGLNGLY
15   GLYGLUASNHISVALLYSMETLEUGLUTRP
16   ILEASPARGVALALAASPPHELEULEUSER
17   LEULYSTHRLYSGLUGLYVALLEUILEPRO
18   VALVALPHEARGPROTRPHISGLUHISTHR
19   GLYSERTRPPHETRPTRPGLYLYSASPLEU
20   CYSSERSERGLUGLNTYRLYSTHRLEUTRP
21   ARGMETTHRASNASPARGLEUARGLEULYS
22   GLYVALASNASNVALLEULEUALATYRSER
23   PROGLYMETGLUSERASPTHRVALGLUGLU
24   TYRLEUGLUARGTYRPROGLYASPASPILE
25   ILEASPVALLEUGLYTHRASPVALTYRGLN
26   PHEGLUARGSERGLNTYRILELYSGLNLEU
27   ASNLYSMETLEUTHRILELEUTHRGLUALA
28   GLYLYSLYSHISASPLYSPROILEALALEU
29   THRGLUTHRGLYLEUGLUGLYILEPROASP
30   SERLEUTRPTRPTHRGLYTHRLEULEUPRO
31   VALILEGLULYSTYRPROLEUSERTYRVAL
32   LEUVALTRPARGASNALAARGGLULYSSER
33   THRHISTYRTYRALAPROTYRPROGLYGLN
34   VALSERALAASPASPPHEVALLYSPHESER
35   ARGSERPROLYSILELEUPHEVALGLYASP
36   ASNPHEGLULEUTYRLYS

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:

NameSampleSample stateSample conditions
2D 15N-TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts