BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19866

Title: NMR assignment of the amylase-binding protein A from Streptococcus Parasanguinis   PubMed: 25016927

Deposition date: 2014-03-18 Original release date: 2014-10-08

Authors: Liu, Bing; Zhou, Fan; Wu, Hui; Matthews, Stephen

Citation: Liu, Bing; Zhou, Fan; Wu, Hui; Matthews, Stephen. "NMR assignment of the amylase-binding protein A from Streptococcus parasanguinis"  Biomol. NMR Assignments ., .-. (2014).

Assembly members:
AbpA, polymer, 186 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
AbpA: SEFELRRQACGRQGENPSAS NQLIQKKYVSWRDAADEANT QVAAHEAEIKEETLRQPGVV AAQQALDKANAIVGHDHEQA VKRAQEDYNTAYNEAYNTVR NRYIQVLQQKYIEAAKAQGN YYDETAVEANRTNEQRIADD IKAQTGKDVTVTKDENGNYV VKDEKGNVVATVDKDGKTVK ADAKAG

Data sets:
Data typeCount
13C chemical shifts687
15N chemical shifts170
1H chemical shifts1070

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AbpA1

Entities:

Entity 1, AbpA 186 residues - Formula weight is not available

1   SERGLUPHEGLULEUARGARGGLNALACYS
2   GLYARGGLNGLYGLUASNPROSERALASER
3   ASNGLNLEUILEGLNLYSLYSTYRVALSER
4   TRPARGASPALAALAASPGLUALAASNTHR
5   GLNVALALAALAHISGLUALAGLUILELYS
6   GLUGLUTHRLEUARGGLNPROGLYVALVAL
7   ALAALAGLNGLNALALEUASPLYSALAASN
8   ALAILEVALGLYHISASPHISGLUGLNALA
9   VALLYSARGALAGLNGLUASPTYRASNTHR
10   ALATYRASNGLUALATYRASNTHRVALARG
11   ASNARGTYRILEGLNVALLEUGLNGLNLYS
12   TYRILEGLUALAALALYSALAGLNGLYASN
13   TYRTYRASPGLUTHRALAVALGLUALAASN
14   ARGTHRASNGLUGLNARGILEALAASPASP
15   ILELYSALAGLNTHRGLYLYSASPVALTHR
16   VALTHRLYSASPGLUASNGLYASNTYRVAL
17   VALLYSASPGLULYSGLYASNVALVALALA
18   THRVALASPLYSASPGLYLYSTHRVALLYS
19   ALAASPALALYSALAGLY

Samples:

sample_1: H2O 4.8 na; sodium chloride 50 mM; potassium phosphate 50 mM; AbpA, [U-13C; U-15N], mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5; pressure: 1 atm; temperature: 310 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 HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

GB AEH56528 AFJ25054 KJU96617
REF WP_013904381 WP_049489234 WP_049498793 WP_049518287

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