BMRB Entry 19206

Title:
1H, 13C and 15N backbone and side-chain resonance assignments of a family 36 carbohydrate binding module of Xylanase from Paenibacillus campinasensis
Deposition date:
2013-04-30
Original release date:
2014-02-13
Authors:
Wang, Yu-Sheng; Ko, Chun-Han; Chang, Hao-Ting; Yang, Kai-Jay; Chen, Yu-Jen; Huang, Shing-Jong; Chang, Chi-Fon; Fang, Pei-Ju; Tzou, Der-Lii M.
Citation:

Citation: Wang, Yu-Sheng; Ko, Chun-Han; Chang, Hao-Ting; Yang, Kai-Jay; Chen, Yu-Jen; Huang, Shing-Jong; Fang, Pei-Ju; Chang, Chi-Fon; Tzou, Der-Lii. "(1)H, (13)C and (15)N backbone and side-chain resonance assignments of a family 36 carbohydrate binding module of xylanase from Paenibacillus campinasensis."  Biomol. NMR Assignments ., .-. (2013).
PubMed: 23835623

Assembly members:

Assembly members:
PcCBM36, polymer, 145 residues, Formula weight is not available
CALCIUM ION, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: Penibacillus campinasensis   Taxonomy ID: 66347   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Penibacillus campinasensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a(+)

Data sets:
Data typeCount
13C chemical shifts544
15N chemical shifts131
1H chemical shifts813

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PcCBM361
2Calcium ion2

Entities:

Entity 1, PcCBM36 145 residues - Formula weight is not available

1   METALASERMETTHRGLYGLYGLNGLNMET
2   GLYARGGLYSERTHRARGVALGLUALAGLU
3   ASNMETTHRLYSSERGLYGLNTYRTHRGLY
4   ASNILESERSERPROPHEASNGLYVALALA
5   LEUTYRALAASNASNASPSERVALLYSTYR
6   THRGLNTYRPHESERTHRSERTHRHISSER
7   PHESERLEUARGGLYALASERASNASNALA
8   ASNMETALAARGVALASPLEULYSILEGLY
9   GLYGLNTHRLYSGLYTHRPHETYRPHEGLY
10   GLYSERSERPROALAVALTYRTHRLEUASN
11   ASNVALSERHISGLYTHRGLYASNGLNGLU
12   ILEGLULEUILEVALTHRALAASPASPGLY
13   THRTRPASPALATYRILEASPTYRLEUGLU
14   ILEARGLYSLEUALAALAALALEUGLUHIS
15   HISHISHISHISHIS

Entity 2, Calcium ion - Ca - 40.078 Da.

1   CA

Samples:

sample_1: Recombinatant PcCBM36, [U-99% 13C; U-99% 15N], 0.6 mM; MES 20 mM; Calcium ion 10 mM; H2O 95%; D2O 5%

sample_2: Recombinatant PcCBM36, [U-99% 13C; U-99% 15N], 0.6 mM; MES 20 mM; Calcium ion 10 mM; D2O 100%

sample_conditions_1: ionic strength: 0.03 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D HBCBCGCDHDsample_2isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_2isotropicsample_conditions_1

Software:

CARA vV1.9.0 Beta, Keller and Wuthrich - chemical shift assignment, data analysis

TOPSPIN vV3.1, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

GB ABB77852 ACJ67894 ACJ67896 ADR03137 AEP19213

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