BMRB Entry 26534

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26534

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Title:
Backbone and side chain 1H, 13C, and 15N chemical shift assignments for Extracellular Loop 1 (ECL1) of FtsX in Streptococcus pneumoniae
Deposition date:
2015-03-09
Original release date:
2016-01-06
Authors:
Fu, Yue; Giedroc, David
Citation:

Citation: Fu, Yue; Bruce, Kevin; Rued, Britta; Winkler, Malcolm; Giedroc, David. "1H, 13C, 15N resonance assignments of the extracellular loop 1 domain (ECL1) of Streptococcus pneumoniae D39 FtsX, an essential cell division protein"  Biomol. NMR Assign. 10, 89-92 (2016).
PubMed: 26370567

Assembly members:

Assembly members:
FtsXECL1, polymer, 126 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 373153   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FtsXECL1: GAMATAKLATDIENNVRVVV YIRKDVEDNSQTIEKEGQTV TNNDYHKVYDSLKNMSTVKS VTFSSKEEQYEKLTEIMGDN WKIFEGDANPLYDAYIVEAN APNDVKTIAEDAKKIEGVSE VQDGGA

Data sets:
Data typeCount
13C chemical shifts540
15N chemical shifts122
1H chemical shifts786

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FtsXECL1 monomer1

Entities:

Entity 1, FtsXECL1 monomer 126 residues - Formula weight is not available

Residue 1-4 represent a cloning artefact from His6-affinity tag after TEV cleavage. This is the bigger of the two extracellular loops of a membrane protein FtsX.

1   GLYALAMETALATHRALALYSLEUALATHR
2   ASPILEGLUASNASNVALARGVALVALVAL
3   TYRILEARGLYSASPVALGLUASPASNSER
4   GLNTHRILEGLULYSGLUGLYGLNTHRVAL
5   THRASNASNASPTYRHISLYSVALTYRASP
6   SERLEULYSASNMETSERTHRVALLYSSER
7   VALTHRPHESERSERLYSGLUGLUGLNTYR
8   GLULYSLEUTHRGLUILEMETGLYASPASN
9   TRPLYSILEPHEGLUGLYASPALAASNPRO
10   LEUTYRASPALATYRILEVALGLUALAASN
11   ALAPROASNASPVALLYSTHRILEALAGLU
12   ASPALALYSLYSILEGLUGLYVALSERGLU
13   VALGLNASPGLYGLYALA

Samples:

sample_1: FtsXECL1, [U-99% 13C; U-99% 15N], 0.5 – 0.7 mM; H2O 90%; D2O, [U-99% 2H], 10%; potassium phosphate 50 mM; sodium chloride 50 mM

sample_2: FtsXECL1, [U-99% 13C; U-99% 15N], 0.5 – 0.7 mM; D2O, [U-99% 2H], 100%; potassium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_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 HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CYANA v3.96, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

VNMRJ, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

CCPNMR_analysis, CCPN - peak picking

NMR spectrometers:

  • Varian DDR 600 MHz

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