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Biological Magnetic Resonance Data Bank


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BMRB Entry 16988

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16988
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Title: Solution NMR Structure of a domain of adhesion exoprotein from Pediococcus pentosaceus, Northeast Structural Genomics Consortium Target PtR41O

Deposition date: 2010-06-09 Original release date: 2010-08-10

Authors: He, Yunfen; Eletsky, Alexander; Mills, Jeffrey; Wang, Huang; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation: He, Yunfen; Eletsky, Alexander; Mills, Jeffrey; Wang, Huang; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of a domain of adhesion exoprotein from Pediococcus pentosaceus, Northeast Structural Genomics Consortium Target PtR41O"  Not known ., .-..

Assembly members:
PtR41O, polymer, 87 residues, 9309.011 Da.

Natural source:   Common Name: Pediococcus pentosaceus   Taxonomy ID: 1255   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pediococcus pentosaceus

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

Entity Sequences (FASTA):
PtR41O: MDEDATITYVDDDKGGAQVG DIVTVTGKTDDSTTYTVTIP DGYEYVGTDGGVVSSDGKTV TITFAADDSDNVVIHLKHGL EHHHHHH

Data typeCount
13C chemical shifts337
15N chemical shifts87
1H chemical shifts523

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PtR41O1

Entities:

Entity 1, PtR41O 87 residues - 9309.011 Da.

the 1st residue is initiating Methionine, 2nd to 79th residues are corresponding to residues 1288-1365 in the native protein, and 80th to 87th residues belong to purification tag.

1   METASPGLUASPALATHRILETHRTYRVAL
2   ASPASPASPLYSGLYGLYALAGLNVALGLY
3   ASPILEVALTHRVALTHRGLYLYSTHRASP
4   ASPSERTHRTHRTYRTHRVALTHRILEPRO
5   ASPGLYTYRGLUTYRVALGLYTHRASPGLY
6   GLYVALVALSERSERASPGLYLYSTHRVAL
7   THRILETHRPHEALAALAASPASPSERASP
8   ASNVALVALILEHISLEULYSHISGLYLEU
9   GLUHISHISHISHISHISHIS

Samples:

sample_4: PtR41O, [U-5% 13C; U-100% 15N], 0.66 mM; sodium chloride 66 mM; calcium chloride 3.3 mM; DTT 6.6 mM; MES 13.2 mM; NaN3 0.0132 % by volume; DSS 33 uM; Pf1 phage 13.25 mg/ml; H2O 83%; D2O 17%

sample_1: PtR41O, [U-100% 13C; U-100% 15N], 1.0 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02 % by volume; DSS 50 uM; H2O 90%; D2O 10%

sample_2: PtR41O, [U-5% 13C; U-100% 15N], 1.2 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; MES 20 mM; NaN3 0.02 % by volume; DSS 50 uM; H2O 90%; D2O 10%

sample_3: PtR41O, [U-5% 13C; U-100% 15N], 0.66 mM; sodium chloride 66 mM; calcium chloride 3.3 mM; DTT 6.6 mM; MES 13.2 mM; NaN3 0.0132 % by volume; DSS 33 uM; poly ethylene glycol 4 % by volume; H2O 83%; D2O 17%

sample_conditions_1: ionic strength: 117.5 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC alisample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC arosample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
GFT CBCA(CO)NHsample_1isotropicsample_conditions_1
GFT HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSY alisample_1isotropicsample_conditions_1
13C/15N-NOESYsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC (methyl)sample_2isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCsample_2isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCsample_3anisotropicsample_conditions_1
2D J-modulation 1H-15N HSQCsample_4anisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe v2007.030.16.06, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY, Bartels et al. - data analysis

TOPSPIN, Bruker Biospin - collection

VNMRJ v2.1B, Varian - collection

Molmol, Koradi, Billeter and Wuthrich - refinement

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

TALOS+, Shen, Cornilescu, Delaglio and Bax - data analysis

PSVS v1.3, Bhattacharya and Montelione - validation

NMRDraw v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

PROSA, Guntert - processing

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 500 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

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