BMRB Entry 18753

Title:
Structure of the biofilm matrix promoter AbbA from B. subtilis
Deposition date:
2012-10-02
Original release date:
2013-09-10
Authors:
Bobay, Benjamin; Tucker, Ashley; Losick, Richard; Cavanagh, John
Citation:

Citation: Tucker, Ashley; Bobay, Benjamin; Banse, Allison; Olson, Andrew; Thompson, Richele; Varney, Kristen; Losick, Richard; Cavanagh, John. "Structure of the biofilm matrix promoter AbbA from B. subtilis"  .

Assembly members:

Assembly members:
entity, polymer, 68 residues, 7989.087 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts274
15N chemical shifts68
1H chemical shifts443

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1biofilm matrix promoter AbbA from B. subtilis, 11
2biofilm matrix promoter AbbA from B. subtilis, 21

Entities:

Entity 1, biofilm matrix promoter AbbA from B. subtilis, 1 68 residues - 7989.087 Da.

Residues 1-3 represent a non-native sequence left after cleavage of affinity tag

1   GLYSERHISMETARGMETSERLEUILEGLY
2   GLUARGPHETHRGLUGLUGLUGLNLYSLEU
3   LEULEUASNILELEUILEASNHISGLUTYR
4   ALAILEGLULEULEUSERSERGLUILEASN
5   ASPILEGLUTHRGLYTHRLYSASNVALASP
6   GLYTHRTHRTYRLYSLYSLEUVALTHRLEU
7   TYRASPARGPHEARGPHEGLUASN

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 – 1.0 mM; DTT 1 mM; TRIS 20 mM; sodium chloride 200 mM; EDTA 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 0.5 – 1.0 mM; DTT 1 mM; TRIS 20 mM; sodium chloride 200 mM; EDTA 1 mM; sodium azide 0.02%; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 13C-12C isotope filtered NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQC RDCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC RDCsample_1anisotropicsample_conditions_1

Software:

NMRPipe vVersion 7.5 Rev 2012.204.11.07, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw vVersion 7.5 Rev 2012.204.11.07, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v8a, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

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

AMBER v11, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 950 MHz

Related Database Links:

PDB
DBJ BAI85022 BAM52057 BAM57634 GAK78528
EMBL CAB13285 CCU57976 CEI56592 CEJ76998 CJS26336
GB ADM37499 ADP31919 ADV96430 AEP86387 AEP90557
REF NP_389295 WP_003218673 WP_003327264 WP_010886502 WP_046160339
SP O31697
AlphaFold O31697

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