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Biological Magnetic Resonance Data Bank


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BMRB Entry 11591

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11591
MolProbity Validation Chart

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Title: Solution structure of chitosan-binding module 1 derived from chitosanase/glucanase from Paenibacillus sp. IK-5   PubMed: 26936968

Deposition date: 2015-05-12 Original release date: 2016-04-04

Authors: Shinya, Shoko; Nishimura, Shigenori; Fukamizo, Tamo

Citation: Shinya, Shoko; Nishimura, Shigenori; Kitaoku, Yoshihito; Ohnuma, Takayuki; Numata, Tomoyuki; Kimoto, Hisashi; Kusaoke, Hideo; Fukamizo, Tamo. "Mechanism of chitosan recognition by CBM32 carbohydrate-binding modules from a Paenibacillus sp. IK-5 chitosanase/glucanase"  Biochem. J. ., .-. (2016).

Assembly members:
DD1, polymer, 130 residues, 14093.350 Da.

Natural source:   Common Name: Paenibacillus sp.   Taxonomy ID: 44249   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Paenibacillus sp.

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

Entity Sequences (FASTA):
DD1: NLALNKTATASSIEGAGFEA SRAFDGSSTTRWASAEGVDP QWIYVNLGSSQTVNRVKLNW EAAYASSYTIQVSNDSGTPT NWTTVYTTTTGDGGIDDITF TARTAKYVRVHGTVRGTPYG YSLWEFEVYG

Data sets:
Data typeCount
13C chemical shifts457
15N chemical shifts140
1H chemical shifts677

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 130 residues - 14093.350 Da.

1   ASNLEUALALEUASNLYSTHRALATHRALA
2   SERSERILEGLUGLYALAGLYPHEGLUALA
3   SERARGALAPHEASPGLYSERSERTHRTHR
4   ARGTRPALASERALAGLUGLYVALASPPRO
5   GLNTRPILETYRVALASNLEUGLYSERSER
6   GLNTHRVALASNARGVALLYSLEUASNTRP
7   GLUALAALATYRALASERSERTYRTHRILE
8   GLNVALSERASNASPSERGLYTHRPROTHR
9   ASNTRPTHRTHRVALTYRTHRTHRTHRTHR
10   GLYASPGLYGLYILEASPASPILETHRPHE
11   THRALAARGTHRALALYSTYRVALARGVAL
12   HISGLYTHRVALARGGLYTHRPROTYRGLY
13   TYRSERLEUTRPGLUPHEGLUVALTYRGLY

Samples:

sample_1: DD1, [U-95% 13C; U-95% 15N], 0.4 mM; TRIS 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: DD1, [U-95% 13C; U-95% 15N], 0.4 mM; D2O, [U-2H], 100%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TALOS, Cornilescu, Delaglio and Bax - backbone angle prediction

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

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