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 17534

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17534
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633   PubMed: 21643970

Deposition date: 2011-03-18 Original release date: 2012-05-10

Authors: Christ, Nina Alexandra; Duchardt-Ferner, Elke; Duesterhus, Stefanie; Koetter, Peter; Entian, Karl-Dieter; Woehnert, Jens

Citation: Christ, Nina Alexandra; Duchardt-Ferner, Elke; Dusterhus, Stefanie; Kotter, Peter; Entian, Karl-Dieter; Wohnert, Jens. "NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633."  Biomol. NMR Assignments 6, 9-13 (2012).

Assembly members:
SpaI, polymer, 128 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
SpaI: GSTMHFTDDNENDTSETMES LIDKGKLDQVVYDDQLYHLK EKVDEDKKGKVIGAIGQTFF VDGDGKRWSEEELKEPYISN NPDEIREKKPLRYGKVYSTN EDSDAKDEIIVEFNREYYRA VLIKNEKE

Data sets:
Data typeCount
13C chemical shifts564
15N chemical shifts137
1H chemical shifts893

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SpaI monomer1

Entities:

Entity 1, SpaI monomer 128 residues - Formula weight is not available

1   GLYSERTHRMETHISPHETHRASPASPASN
2   GLUASNASPTHRSERGLUTHRMETGLUSER
3   LEUILEASPLYSGLYLYSLEUASPGLNVAL
4   VALTYRASPASPGLNLEUTYRHISLEULYS
5   GLULYSVALASPGLUASPLYSLYSGLYLYS
6   VALILEGLYALAILEGLYGLNTHRPHEPHE
7   VALASPGLYASPGLYLYSARGTRPSERGLU
8   GLUGLULEULYSGLUPROTYRILESERASN
9   ASNPROASPGLUILEARGGLULYSLYSPRO
10   LEUARGTYRGLYLYSVALTYRSERTHRASN
11   GLUASPSERASPALALYSASPGLUILEILE
12   VALGLUPHEASNARGGLUTYRTYRARGALA
13   VALLEUILELYSASNGLULYSGLU

Samples:

15N: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 10 uM; SpaI, [U-15N], 300 – 400 uM; H2O 90%; D2O 10%

2H15N13C: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 10 uM; SpaI, [U-13C; U-15N; U-2H], 420 uM; H2O 90%; D2O 10%

15N13C: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 10 uM; SpaI, [U-13C; U-15N], 300 – 400 uM; H2O 90%; D2O 10%

15N13C_D2O: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 10 uM; SpaI, [U-13C; U-15N], 300 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic15N13C_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aromatic15N13Cisotropicsample_conditions_1
3D CBCA(CO)NH15N13Cisotropicsample_conditions_1
3D HNCO2H15N13Cisotropicsample_conditions_1
3D HNCA2H15N13Cisotropicsample_conditions_1
3D HNCACB2H15N13Cisotropicsample_conditions_1
3D HBHA(CO)NH15N13Cisotropicsample_conditions_1
3D H(CCO)NH15N13Cisotropicsample_conditions_1
3D C(CO)NH15N13Cisotropicsample_conditions_1
3D HCCH-TOCSY15N13C_D2Oisotropicsample_conditions_1
3D HCCH-COSY15N13C_D2Oisotropicsample_conditions_1
3D HNHA15Nisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic15N13Cisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic15N13C_D2Oisotropicsample_conditions_1
3D 1H-13C NOESY aromatic15N13Cisotropicsample_conditions_1
3D HNCACO2H15N13Cisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN_Analysis, CCPN - chemical shift assignment, data analysis

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
GB AAB91598 ADM39343 AJD37803 AJW87462 EFG93306
REF WP_003220043 WP_041905979 WP_044445585 WP_045385074

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