BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26745

Title: Backbone 1H, 13C, and 15N assignments for Sortase C1 (SrtC1) from Streptococcus pneumoniae   PubMed: 27109553

Deposition date: 2016-02-13 Original release date: 2016-07-14

Authors: Jacobitz, Alex; Clubb, Robert

Citation: Jacobitz, Alex; Naziga, Emmanuel; Sung Wook, Yi; McConnell, Scott; Peterson, Robert; Jung, Michael; Clubb, Robert; Wereszczynski, Jeff. "The "Lid" in the Streptococcus pneumoniae SrtC1 Sortase Adopts a Rigid Structure that Regulates Substrate Access to the Active Site"  J. Phys. Chem. B 120, 8302-8312 (2016).

Assembly members:
SrtC1, polymer, 213 residues, 23812.9 Da.

Natural source:   Common Name: fermicutes   Taxonomy ID: 170187   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

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

Entity Sequences (FASTA):
SrtC1: SESNQQIADFDKEKATLDEA DIDERMKLAQAFNDSLNNVV SGDPWSEEMKKKGRAEYARM LEIHERMGHVEIPVIDVDLP VYAGTAEEVLQQGAGHLEGT SLPIGGNSTHAVITAHTGLP TAKMFTDLTKLKVGDKFYVH NIKEVMAYQVDQVKVIEPTN FDDLLIVPGHDYVTLLTCTP YMINTHRLLVRGHRIPYVAE VEEEFIAANKLSH

Data sets:
Data typeCount
13C chemical shifts310
15N chemical shifts192
1H chemical shifts339

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SrtC11

Entities:

Entity 1, SrtC1 213 residues - 23812.9 Da.

Sequence matches PDB ID 2W1J. First 15 residues in this sequence are part of a membrane anchor and were removed to generate a soluble construct. First residue, S-16, is a remnant of a cleaved purification tag.

1   SERGLUSERASNGLNGLNILEALAASPPHE
2   ASPLYSGLULYSALATHRLEUASPGLUALA
3   ASPILEASPGLUARGMETLYSLEUALAGLN
4   ALAPHEASNASPSERLEUASNASNVALVAL
5   SERGLYASPPROTRPSERGLUGLUMETLYS
6   LYSLYSGLYARGALAGLUTYRALAARGMET
7   LEUGLUILEHISGLUARGMETGLYHISVAL
8   GLUILEPROVALILEASPVALASPLEUPRO
9   VALTYRALAGLYTHRALAGLUGLUVALLEU
10   GLNGLNGLYALAGLYHISLEUGLUGLYTHR
11   SERLEUPROILEGLYGLYASNSERTHRHIS
12   ALAVALILETHRALAHISTHRGLYLEUPRO
13   THRALALYSMETPHETHRASPLEUTHRLYS
14   LEULYSVALGLYASPLYSPHETYRVALHIS
15   ASNILELYSGLUVALMETALATYRGLNVAL
16   ASPGLNVALLYSVALILEGLUPROTHRASN
17   PHEASPASPLEULEUILEVALPROGLYHIS
18   ASPTYRVALTHRLEULEUTHRCYSTHRPRO
19   TYRMETILEASNTHRHISARGLEULEUVAL
20   ARGGLYHISARGILEPROTYRVALALAGLU
21   VALGLUGLUGLUPHEILEALAALAASNLYS
22   LEUSERHIS

Samples:

sample_1: SrtC1, [U-99% 13C; U-99% 15N], 2 mM; sodium chloride 50 mM; potassium phosphate 50 mM; sodium azide 0.01%; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; 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 C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CARA v1.9.0, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB EJH14048.1

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