BMRB Entry 36061

Title:
Ligand induced structure of AmyP-SBD
Deposition date:
2017-02-17
Original release date:
2017-06-20
Authors:
Li, X.; Yu, J.; Sun, H.; Zhang, X.
Citation:

Citation: Li, X.; Yu, J.; Tu, X.; Sun, H.; Peng, H.; Zhang, X.. "Ligand binding induced folding of a novel CBM69 starch binding domain"  .

Assembly members:

Assembly members:
entity_1, polymer, 157 residues, 17023.881 Da.

Natural source:

Natural source:   Common Name: uncultured bacterium   Taxonomy ID: 77133   Superkingdom: Bacteria   Kingdom: not available   Genus/species: uncultured bacterium

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts530
15N chemical shifts151
1H chemical shifts944

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 157 residues - 17023.881 Da.

1   THRPROSERALASERGLYLEUTHRLYSVAL
2   ALATHRVALSERALAALASERSERLEUILE
3   GLYGLUGLYPHEMETALAGLNCYSASPASN
4   PROTHRILEGLUGLYASPGLYPROILEGLY
5   LYSTHRLEUTYRVALVALGLYASPPHEALA
6   ASPALASERTRPLYSGLNLYSPROHISARG
7   ALATYRARGTYRVALGLYGLUASNTHRTYR
8   GLNALAVALVALASPGLULYSALAGLYALA
9   PHEARGMETGLNTYRALASERLYSASPTRP
10   SERPROGLNPHETHRALAASPGLYLEUGLU
11   LEUTHRPROGLYLYSTHRALASERLEULYS
12   ARGGLYGLYTYRGLYGLNASPTHRALAVAL
13   THRLEUPROGLUALAGLYGLNTYRVALTRP
14   SERLEULYSPHETHRASPSERGLYASPPRO
15   GLUGLNILEMETVALSERLYSCYSPROLEU
16   GLUHISHISHISHISHISHIS

Samples:

sample_1: AmyP-SBD, [U-99% 15N], 0.4 mM; beta-cyclodextrin 2 mM; NaH2PO4 20 mM; NaCl 150 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: AmyP-SBD, [U-99% 13C; U-99% 15N], 0.4 mM; beta-cyclodextrin 2 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: AmyP-SBD, [U-99% 13C; U-99% 15N], 0.4 mM; beta-cyclodextrin 2 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 0.12 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCC(CO)NHsample_2isotropicsample_conditions_1
3D CC(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1

Software:

CNS, BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ - refinement, structure solution

SPARKY - structure solution

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker DMX 600 MHz

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