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 15339

Title: Solution NMR Structure of Ribosome Modulation Factor VP1593 from Vibrio parahaemolyticus. Northeast Structural Genomics Target VpR55   PubMed: TBA

Authors: Tang, Yuefeng; Rossi, Paolo; Swapna, G.V.T; Wang, Huang; Jiang, Mei; Cunningham, Kellie; Owens, Leah; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Tang, Yuefeng; Rossi, Paolo; Swapna, G.V.T; Wang, Huang; Jiang, Mei; Cunningham, Kellie; Owens, Leah; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of Ribosome Modulation Factor VP1593 from Vibrio parahaemolyticus"  Not known ., .-..

Assembly members:
VpR55, polymer, 65 residues, 7115.986 Da.

Natural source:   Common Name: vibrio parahaemolyticus   Taxonomy ID: 670   Superkingdom: Bacteria   Kingdom: not available   Genus/species: vibrio parahaemolyticus

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

Entity Sequences (FASTA):
VpR55: MKRQKRDRLERAQSQGYKAG LNGRSQEACPYQQVDARSYW LGGWRDARDEKQSGLYKLEH HHHHH

Data typeCount
13C chemical shifts258
15N chemical shifts71
1H chemical shifts407

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ribosome Modulation Factor1

Entities:

Entity 1, Ribosome Modulation Factor 65 residues - 7115.986 Da.

Residue 58-65 represent a non-native affinity purification tag (LEHHHHHH)

1   METLYSARGGLNLYSARGASPARGLEUGLU
2   ARGALAGLNSERGLNGLYTYRLYSALAGLY
3   LEUASNGLYARGSERGLNGLUALACYSPRO
4   TYRGLNGLNVALASPALAARGSERTYRTRP
5   LEUGLYGLYTRPARGASPALAARGASPGLU
6   LYSGLNSERGLYLEUTYRLYSLEUGLUHIS
7   HISHISHISHISHIS

Samples:

sample_1: VpR55, [U-100% 13C; U-100% 15N], 1.1 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%

sample_2: VpR55, [U-5% 13C; U-100% 15N], 1.1 mM; MES 20 mM; NaCl 100 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 393 K

Experiments:

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

Software:

TOPSPIN v1.3, Bruker Biospin - collection

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

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

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

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

X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

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

PSVS v1.3, Bhattacharya and Montelione - data analysis

PDBStat v4.0, Tejero and Montelione - PDB analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

SWS Q87PC4_VIBPA
PDB
DBJ BAC59856 GAD73629 GAJ70766 GAJ75149 GAK18004
GB ABU71295 ACY51602 AEX22003 AGQ92134 AGR00117
REF NP_797972 WP_005377453 WP_005494976 WP_005532367 WP_014231881