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 17518

Title: Solution Strucuture of CBM25-1 of beta/alpha-amylase from Paenibacillus polymyxa

Deposition date: 2011-03-09 Original release date: 2012-08-07

Authors: Horibe, Ippei; Takahashi, Ryosuke; Yoshida, Takuya; Ohkubo, Tadayasu; Sumitani, Jun-ichi; Nishimura, Shigenori

Citation: Takahashi, Ryosuke; Horibe, Ippei; Fukada, Harumi; Yoshida, Takuya; Ohkubo, Tadayasu; Inui, Takashi; Nishimura, Shigenori; Sumitani, Jun-ichi. "A functional and structural analysis of tundem family 25 carbohydrate-binding modules from Paenibacillus polymyxa beta/alpha-amylase"  Protein Sci. ., .-..

Assembly members:
entity, polymer, 104 residues, 10745.604 Da.

Natural source:   Common Name: Bacillus polymyxa   Taxonomy ID: 1406   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus polymyxa

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Entity Sequences (FASTA):
entity: GGTGNKVTIYYKKGFNSPYI HYRPAGGSWTAAPGVKMQDA EISGYAKITVDIGSASQLEA AFNDGNNNWDSNNTKNYSFS TGTSTYTPGNSGNAGTITSG APAG

Data sets:
Data typeCount
13C chemical shifts420
15N chemical shifts112
1H chemical shifts599

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CBM25-1 of beta/alpha-amylase1

Entities:

Entity 1, CBM25-1 of beta/alpha-amylase 104 residues - 10745.604 Da.

1   GLYGLYTHRGLYASNLYSVALTHRILETYR
2   TYRLYSLYSGLYPHEASNSERPROTYRILE
3   HISTYRARGPROALAGLYGLYSERTRPTHR
4   ALAALAPROGLYVALLYSMETGLNASPALA
5   GLUILESERGLYTYRALALYSILETHRVAL
6   ASPILEGLYSERALASERGLNLEUGLUALA
7   ALAPHEASNASPGLYASNASNASNTRPASP
8   SERASNASNTHRLYSASNTYRSERPHESER
9   THRGLYTHRSERTHRTYRTHRPROGLYASN
10   SERGLYASNALAGLYTHRILETHRSERGLY
11   ALAPROALAGLY

Samples:

sample_1: sodium acetate, [U-100% 15N], 0.5-1.2 mM; sodium acetate, [U-99% 13C; U-99% 15N], 0.5-1.2 mM

sample_2: sodium acetate, [U-100% 15N], 0.6 mM

sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

SPARKY, Guntert, Braun and Wuthrich - chemical shift assignment

DYANA, Guntert, Braun and Wuthrich - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

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