BMRB Entry 25435

Title:
Structure of Amylase binding Protein A of Streptococcous gordonii: a potential receptor for human salivary amylase enzyme
Deposition date:
2015-01-18
Original release date:
2015-05-11
Authors:
Sethi, Ashish; Mohanty, Biswaranjan; Ramasubbu, Narayanan; Gooley, Paul
Citation:

Citation: Sethi, Ashish; Mohanty, Biswaranjan; Ramasubbu, Narayanan; Gooley, Paul. "Structure of amylase-binding protein A of Streptococcus gordonii: A potential receptor for human salivary alpha-amylase enzyme"  Protein Sci. 24, 1013-1018 (2015).
PubMed: 25739638

Assembly members:

Assembly members:
entity, polymer, 179 residues, 19170.961 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 29390   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus gordonii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: E. coli BL21 (DE3) bacteria   Vector: pET29b

Data sets:
Data typeCount
13C chemical shifts640
15N chemical shifts177
1H chemical shifts991

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 179 residues - 19170.961 Da.

1   METALAASPGLUALATHRASPALAALAARG
2   ASNASNASPGLYALATYRTYRLEUGLNTHR
3   GLNPHETHRASNALAASPLYSVALASNGLU
4   TYRLEUALAGLNHISASPGLYGLUILEARG
5   ALAGLUALAALAALAASPPROALAVALVAL
6   ALAALALYSALAALALEUASPALAVALGLU
7   GLYGLYSERHISASNTYRGLYGLUVALLYS
8   ALAALATYRGLUALAALAPHEASNASNALA
9   PHEASNALAVALARGASNLYSTYRVALGLN
10   ARGPHEGLNALATHRTYRASNASNALATHR
11   GLUGLNGLUGLYLYSTHRTYRILEGLNGLY
12   GLUTHRPROGLUGLNALAASNALAARGTYR
13   LEULYSARGVALGLYALAALAASNASNGLN
14   ASNPROALAALAGLUASPLYSGLYALATHR
15   THRPROALASERLYSGLUGLUALALYSLYS
16   SERGLUALAALAALALYSASNALAGLYLYS
17   ALAALAGLYLYSALALEUPROLYSTHRSER
18   ALAVALLYSHISHISHISHISHISHIS

Samples:

sample_1: AbpA, U-98% 13C; U-98% 15N, 325 uM; Sodium phosphate 50 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 5.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D CccoNHsample_1isotropicsample_conditions_1
3D HcccoNHsample_1isotropicsample_conditions_1
3D 15N resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
3D 13Cali resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
3D 13Caro resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
2D 15N{1H}-NOEsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - data collection, processing

CARA v1.5.3, Keller and Wuthrich - chemical shift assignment, peak picking

UNIO v2.0.1, Herrmann and Wuthrich - NOE assignment, peak picking, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

OPALp v1.2, Koradi,Billeter and Guntert - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

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