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 15847

Title: Solution NMR Structure of XF2673 from Xylella fastidiosa. Northeast Structural Genomics Consortium Target XfR39   PubMed: TBA

Authors: Tang, Yuefeng; Wang, Huang; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Tang, Yuefeng; Wang, Huang; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of XF2673 from Xylella fastidiosa. Northeast Structural Genomics Consortium Target XfR39"  Not known ., .-..

Assembly members:
XF2673, polymer, 97 residues, 10981.5 Da.

Natural source:   Common Name: Xylella fastidiosa   Taxonomy ID: 2371   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Xylella fastidiosa

Experimental source:   Production method: recombinant technology   Host organism: BL21(DE3)+magic

Entity Sequences (FASTA):
XF2673: MDRKLLHLLCSPDTRQPLSL LESKGLEALNKAIVSGTVQR ADGSIQNQSLHEALITRDRK QVFRIEDSIPVLLPEEAIAT IQIANFPDKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts91
1H chemical shifts654

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1XF26731

Entities:

Entity 1, XF2673 97 residues - 10981.5 Da.

1   METASPARGLYSLEULEUHISLEULEUCYS
2   SERPROASPTHRARGGLNPROLEUSERLEU
3   LEUGLUSERLYSGLYLEUGLUALALEUASN
4   LYSALAILEVALSERGLYTHRVALGLNARG
5   ALAASPGLYSERILEGLNASNGLNSERLEU
6   HISGLUALALEUILETHRARGASPARGLYS
7   GLNVALPHEARGILEGLUASPSERILEPRO
8   VALLEULEUPROGLUGLUALAILEALATHR
9   ILEGLNILEALAASNPHEPROASPLYSLEU
10   GLUHISHISHISHISHISHIS

Samples:

sample_1: XfR39, [U-100% 13C; U-100% 15N], 1.0 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM

sample_2: XfR39, [U-5% 13C; U-100% 15N], 1.0 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC_armaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D simutaeous NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY_aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC_high resolutionsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY v3.110, Goddard - data analysis, peak picking

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

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

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - data analysis

PDBStat v5.0, Tejero and Montelione - PDBanalysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAF85470 AAO29861 ACA13079 ACB93534 ADN62897
REF WP_004084759 WP_010895087