BMRB Entry 15673

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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/BMR15673
MolProbity Validation Chart

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Title:
NMR solution structure of PisI
Deposition date:
2008-02-25
Original release date:
2008-06-27
Authors:
Martin-Visscher, Leah; Sprules, Tara; Gursky, Lucas; Vederas, John
Citation:

Citation: Martin-Visscher, Leah; Sprules, Tara; Gursky, Lucas; Vederas, John. "Nuclear magnetic resonance solution structure of PisI, a group B immunity protein that provides protection against the type IIa bacteriocin piscicolin 126, PisA."  Biochemistry 47, 6427-6436 (2008).
PubMed: 18500825

Assembly members:

Assembly members:
PisI, polymer, 98 residues, 11197.856 Da.

Natural source:

Natural source:   Common Name: Carnibacterium piscicola   Taxonomy ID: 2751   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Carnobacterium maltaromaticum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PisI: MGKLKWFSGGKERSNQAENI ITDLLDDLKTDLDNESLKKV LENYLEELKQKSASVPLILS RMNLDISKAIRNDGVTLSDY QSKKLKELTSISNIRYGY

Data sets:
Data typeCount
13C chemical shifts342
15N chemical shifts106
1H chemical shifts674

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PisI1

Entities:

Entity 1, PisI 98 residues - 11197.856 Da.

1   METGLYLYSLEULYSTRPPHESERGLYGLY
2   LYSGLUARGSERASNGLNALAGLUASNILE
3   ILETHRASPLEULEUASPASPLEULYSTHR
4   ASPLEUASPASNGLUSERLEULYSLYSVAL
5   LEUGLUASNTYRLEUGLUGLULEULYSGLN
6   LYSSERALASERVALPROLEUILELEUSER
7   ARGMETASNLEUASPILESERLYSALAILE
8   ARGASNASPGLYVALTHRLEUSERASPTYR
9   GLNSERLYSLYSLEULYSGLULEUTHRSER
10   ILESERASNILEARGTYRGLYTYR

Samples:

sample_1: PisI, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 1 mM; sodium azide 1 mM; DSS .05 mM

sample_2: PisI, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 1 mM; sodium azide 1 mM; DSS .05 mM

sample_3: PisI, [U-99% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 1 mM; sodium azide 1 mM; DSS .05 mM

sample_conditions_1: pH: 5.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
2D NNOEsample_1isotropicsample_conditions_1

Software:

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

VNMRJ v1.1D, Varian - collection

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

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
EMBL CCO10376
GB AAK69418 AAX21353 KRN60250 KRN73764 KRN85081
REF WP_010050956 WP_056999692

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