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 30676

Title: NMR structure of biofilm-related EbsA from Synechococcus elongatus

Deposition date: 2019-09-23 Original release date: 2020-09-28

Authors: Zhang, N.; LiWang, A.

Citation: Zhang, N.; LiWang, A.. "NMR structure of biofilm-related EbsA from Synechococcus elongatus"  . ., .-..

Assembly members:
entity_1, polymer, 125 residues, 14425.336 Da.

Natural source:   Common Name: Synechococcus elongatus   Taxonomy ID: 1140   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechococcus elongatus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
entity_1: MRIDELVPADPRAVSLYTPY YSQANRRRYLPYALSLYQGS SIEGSRAVEGGAPISFVATW TVTPLPADMTRCHLQFNNDA ELTYEILLPNHEFLEYLIDM LMGYQRMQKTDFPGAFYRRL LGYDS

Data sets:
Data typeCount
13C chemical shifts302
15N chemical shifts112
1H chemical shifts657

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 125 residues - 14425.336 Da.

1   METARGILEASPGLULEUVALPROALAASP
2   PROARGALAVALSERLEUTYRTHRPROTYR
3   TYRSERGLNALAASNARGARGARGTYRLEU
4   PROTYRALALEUSERLEUTYRGLNGLYSER
5   SERILEGLUGLYSERARGALAVALGLUGLY
6   GLYALAPROILESERPHEVALALATHRTRP
7   THRVALTHRPROLEUPROALAASPMETTHR
8   ARGCYSHISLEUGLNPHEASNASNASPALA
9   GLULEUTHRTYRGLUILELEULEUPROASN
10   HISGLUPHELEUGLUTYRLEUILEASPMET
11   LEUMETGLYTYRGLNARGMETGLNLYSTHR
12   ASPPHEPROGLYALAPHETYRARGARGLEU
13   LEUGLYTYRASPSER

Samples:

sample_1: EbsA, [U-99% 13C; U-99% 15N], 0.6 mM

sample_conditions_1: ionic strength: 125 mM; pH: 7; pressure: 1013.25 mbar; temperature: 295 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D IPAP-HNCOsample_1isotropicsample_conditions_1
2D (HB)CB(CDCGCE)HEsample_1isotropicsample_conditions_1
2D (HB)CB(CDCG)HGsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HCCH(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
4D 13C-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.51, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMRFAM-SPARKY v1.414, Woonghee Lee, Marco Tonelli, and John L. Markley - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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