BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26761

Title: Backbone assignment of the Xylanase B2 from Streptomyces lividans   PubMed: 27387012

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: 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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts446
15N chemical shifts147
1H chemical shifts146

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1XlnB21

Entities:

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

1   ASPTHRVALVALTHRTHRASNGLNGLUGLY
2   THRASNASNGLYTYRTYRTYRSERPHETRP
3   THRASPSERGLNGLYTHRVALSERMETASN
4   METGLYSERGLYGLYGLNTYRSERTHRSER
5   TRPARGASNTHRGLYASNPHEVALALAGLY
6   LYSGLYTRPALAASNGLYGLYARGARGTHR
7   VALGLNTYRSERGLYSERPHEASNPROSER
8   GLYASNALATYRLEUALALEUTYRGLYTRP
9   THRSERASNPROLEUVALGLUTYRTYRILE
10   VALASPASNTRPGLYTHRTYRARGPROTHR
11   GLYGLUTYRLYSGLYTHRVALTHRSERASP
12   GLYGLYTHRTYRASPILETYRLYSTHRTHR
13   ARGVALASNLYSPROSERVALGLUGLYTHR
14   ARGTHRPHEASPGLNTYRTRPSERVALARG
15   GLNSERLYSARGTHRGLYGLYTHRILETHR
16   THRGLYASNHISPHEASPALATRPALAARG
17   ALAGLYMETPROLEUGLYASNPHESERTYR
18   TYRMETILEMETALATHRGLUGLYTYRGLN
19   SERSERGLYSERSERSERILEASNVALGLY
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts